MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene pdhD (MPN390)
Name 
pdhD
Stable ID 
MPN390
Location 
466473 - 467846 -
Sequence 
    1  ATGAATTACG ATCTCATTAT TATAGGGGCT GGTCCCGCTG GGTATGTGGC CGCTGAGTAC
   61  GCGGGTAAGC ATAAACTTAA AACACTCGTT GTCGAAAAGG AATACTTTGG TGGCGTGTGT
  121  TTAAATGTTG GTTGTATTCC AACGAAAACA CTGTTAAAAC GGGCCAAGAT TGTCGATTAC
  181  CTCCGCCATG CGCAGGACTA TGGTATTTCA ATTAATGGTC AAGTAGCACT TAACTGAAAC
  241  CAATTGCTGG AGCAAAAAGG TAAGGTAGTG AGTAAGTTAG TTGGTGGGGT TAAAGCGATT
  301  ATTGCTTCCG CTAAAGCTGA AACGGTAATG GGAGAAGCCA AGGTTTTGGA TCCCAACACC
  361  GTGGAGGTAG CGGGTAAAAC TTACACCACC AAAAGCATTG TGGTCGCAAC TGGTTCACGA
  421  CCCCGTTACT TAACGCTTCC GGGTTTTGCA GAAGCGCGTC AAAACGGTTT TGTAATTGAC
  481  TCGACCCAAG CGCTCTCTTT GGAAGGGGTA CCACGCAAGT TAGTTGTTGT TGGTGGTGGA
  541  GTGATTGGTA TTGAATTTGC CTTTCTCTAC GCTTCATTGG GTAGTGAAGT GACTATCTTA
  601  CAAGGGGTGG ATAGGATCTT GGAAATCTTT GACACTGAGG TATCAGATTT AGTCGCTAAA
  661  CTCTTGCAAA CCAAGAATGT CAAGATTATT ACCAACGCAC AGGTAACCCG TGCTAACAAT
  721  AATGAAGTCT TTTATTCGCA AAACGGGCAG GAAGGCAGTG TGGTTGGTGA TCGCATTTTG
  781  GTCTCGATTG GTCGCATTCC CAACACGGAA TGTCTTGATG GGTTGAACTT ACAACGTGAT
  841  GAGCGCAACC GGATTGTGCT CAATCAAGAT CTCCAAACCT CAATTCCCAA CATCTACATA
  901  GTTGGCGATG CCAATGCCCA GTTAATGTTG GCCCACTTTG CCTACCAACA AGGGCGGTAT
  961  GCGGTGAACC ATATCTTAAA CAAGAAGCAG GTCAAACCAG CGCAAAAGTT AACTTGCCCT
 1021  TCCTGTATTT ACACCAATCC GGAAGTAGCA TCGGTGGGTT ACACCGAAAT GGAGTTGAAA
 1081  AAACAGGGCA TTCCTTATGT CAAAACCAAT CTTGTTTTAG CGCACTGTGG AAAAGCAATC
 1141  GCTGACAATG AAACCAACGG TTTTGTCAAA ATGATGTTTG ACCCACAAAC CGGTAAGATC
 1201  TTGGGTTGCT GTATTATTGC TGCTACTGCT AGTGACATGA TTGCCGAGCT AGCGTTGGCT
 1261  ATGGGTGCAG GTTTGACAGT ATTTGACATT GCCAACTCCA TTTCACCACA TCCTACCATC
 1321  AACGAAATGA TCGCTGATGT GTGCAAAAAA GCTCTTTTTG ATCACTTTAA ATAG
Download Sequence
Operon 
OP439
Operon location 
464000 - 469068
Protein (mpn390)
Name 
Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate complex)
Stable ID 
Mpn390
Molecular Weight 
50270
Isoelectric Point 
8
Localization 
Cytoplasm
Comment -
Sequence 
MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALNWN
QLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGFVID
STQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANN
NEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHFAYQQGRY
AVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKI
LGCCIIAATASDMIAELALAMGAGLTVFDIANSISPHPTINEMIADVCKKALFDHFK
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation mNYDLIIIGAGPAGYVAAEYAGK 1 24 M
Oxidation mNYDLIIIGAGPAGYVAAEYAGKHK 1 26 M
Oxidation AIIASAKAETVmGEAK 99 115 M
Oxidation AETVmGEAk 106 115 M
Oxidation AETVmGEAK 106 115 M
Oxidation IVLNQDLQTSIPNIYIVGDANAQLmLAHFAYQQGR 285 320 M
Oxidation LTcPScIYTNPEVASVGYTEmELk 337 361 M
Oxidation LTcPScIYTNPEVASVGYTEmELK 337 361 M
Oxidation LTcPScIYTNPEVASVGYTEmELKk 337 362 M
Oxidation LTcPScIYTNPEVASVGYTEmELKK 337 362 M
Oxidation LTcPScIYTNPEVASVGYTEmELkk 337 362 M
Oxidation LTcPScIYTNPEVASVGYTEmELkK 337 362 M
Oxidation mMFDPQTGk 391 400 M
Oxidation MmFDPQTGk 391 400 M
Oxidation MmFDPQTGK 391 400 M
Oxidation mmFDPQTGK 391 400 M
Oxidation mMFDPQTGK 391 400 M
Oxidation mmFDPQTGk 391 400 M
GENE/PROTEIN pdhD (Domains Overview)
Click on the features to jump to domain info

 ExportIMG
Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-133 G3DSA:3.50.50.60 (n.a.) NULL 0
1-330 SSF51905 (n.a.) NULL 0
2-456 TIGR01350 (IPR006258) Dihydrolipoamide dehydrogenase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0004148'>'dihydrolipoyl' == '' ? '': 'dihydrolipoyl'; 'dehydrogenase' == '' ? '': 'dehydrogenase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004148) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0
4-26 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.2e-34
4-26 PR00411 (n.a.) NULL 0
4-305 PF07992 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.26117e-44
6-452 PTHR22912 (n.a.) NULL 0
6-452 PTHR22912:SF20 (IPR006258) Dihydrolipoamide dehydrogenase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0004148'>'dihydrolipoyl' == '' ? '': 'dihydrolipoyl'; 'dehydrogenase' == '' ? '': 'dehydrogenase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004148) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0
36-51 PR00411 (n.a.) NULL 0
37-47 PS00076 (IPR012999) Pyridine nucleotide-disulphide oxidoreductase, cla 0
49-68 PR00945 (IPR000815) Mercuric reductase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0.0000000000056
133-142 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.2e-34
133-142 PR00411 (n.a.) NULL 0
134-327 G3DSA:3.50.50.60 (n.a.) NULL 0
173-190 PR00945 (IPR000815) Mercuric reductase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0.0000000000056
173-198 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.2e-34
173-198 PR00411 (n.a.) NULL 0
173-242 PF00070 (IPR001327) Pyridine nucleotide-disulphide oxidoreductase, NAD Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0.0000000000000035
193-208 PR00945 (IPR000815) Mercuric reductase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0.0000000000056
257-271 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.2e-34
257-271 PR00411 (n.a.) NULL 0
298-305 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.2e-34
298-305 PR00411 (n.a.) NULL 0
335-356 PR00411 (n.a.) NULL 0
336-457 SSF55424 (IPR016156) FAD/NAD-linked reductase, dimerisation Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

3.4e-31
337-451 G3DSA:3.30.390.30 (IPR004099) Pyridine nucleotide-disulphide oxidoreductase, dim Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0045454'>'cell' == '' ? '': 'cell'; 'redox' == '' ? '': 'redox'; 'homeostasis' == '' ? '': 'homeostasis'; ('GO' == '' ? '': 'GO';:0045454) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Cellular Component:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0005737'>'cytoplasm' == '' ? '': 'cytoplasm'; ('GO' == '' ? '': 'GO';:0005737)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

1.8e-38
340-445 PF02852 (IPR004099) Pyridine nucleotide-disulphide oxidoreductase, dim Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0045454'>'cell' == '' ? '': 'cell'; 'redox' == '' ? '': 'redox'; 'homeostasis' == '' ? '': 'homeostasis'; ('GO' == '' ? '': 'GO';:0045454) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Cellular Component:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0005737'>'cytoplasm' == '' ? '': 'cytoplasm'; ('GO' == '' ? '': 'GO';:0005737)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

2.8e-30
371-391 PR00945 (IPR000815) Mercuric reductase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0050660'>'FAD' == '' ? '': 'FAD'; 'or' == '' ? '': 'or'; 'FADH' == '' ? '': 'FADH';2 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0050660)

0.0000000000056
400-415 PR00411 (n.a.) NULL 0
422-442 PR00411 (n.a.) NULL 0
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
3 327 324 - MAG0910 Mycoplasma agalactiae 7 304 0.0000000003 24.4838 138
2 452 450 - MAG0960 Mycoplasma agalactiae 68 527 <1e-50 35.4978 762
133 411 278 - MAG2460 Mycoplasma agalactiae 105 397 0.00000005 26.8212 119
194 431 237 - MAG2630 Mycoplasma agalactiae 173 423 0.0000004 25 112
2 444 442 - Caulobacter crescentus NA1000 4 452 <1e-50 30.989 611
2 450 448 - Caulobacter crescentus NA1000 5 456 2e-33 23.9829 343
2 444 442 - Caulobacter crescentus NA1000 12 461 <1e-50 34.3545 546
125 304 179 - Caulobacter crescentus NA1000 309 489 0.000004 24.6073 108
2 451 449 - MCJ_000700 Mycoplasma conjunctivae 166 614 <1e-50 40.5765 937
190 437 247 - MCJ_003020 Mycoplasma conjunctivae 168 435 0.000000001 24.8227 134
3 307 304 - MCJ_005260 Mycoplasma conjunctivae 5 281 0.0000008 27.0186 109
3 455 452 - MCJ_005300 Mycoplasma conjunctivae 4 451 <1e-50 31.0573 617
4 451 447 - Lactococcus lactis subsp. lactis KF147 11 465 <1e-50 33.1183 597
6 449 443 - Lactococcus lactis subsp. lactis KF147 9 436 4e-38 26.9737 382
133 430 297 - Lactococcus lactis subsp. lactis KF147 107 413 0.000001 21.7391 111
197 430 233 - Lactococcus lactis subsp. lactis KF147 177 415 4e-17 29.5082 201
30 440 410 - Lactococcus lactis subsp. lactis KF147 29 427 2e-29 26.0766 308
125 303 178 - Bacillus subtilis subsp. subtilis 302 479 0.00000003 26.3441 129
2 448 446 - Bacillus subtilis subsp. subtilis 4 464 <1e-50 32.839 597
4 452 448 - Bacillus subtilis subsp. subtilis 11 462 <1e-50 36.1472 710
29 446 417 - Bacillus subtilis subsp. subtilis 27 446 <1e-50 29.1375 509
126 325 199 - Bacillus subtilis subsp. subtilis 98 303 0.0000009 26.9767 116
29 444 415 - Bacillus subtilis subsp. subtilis 27 444 <1e-50 29.274 510
125 303 178 - Bacillus subtilis subsp. subtilis 302 479 0.00000003 26.3441 128
4 452 448 - Bacillus subtilis subsp. subtilis 11 462 <1e-50 36.1472 710
2 448 446 - Bacillus subtilis subsp. subtilis 4 464 <1e-50 32.839 599
126 325 199 - Bacillus subtilis subsp. subtilis 98 303 0.0000003 27.4419 120
2 444 442 - Rv2855 Mycobacterium tuberculosis 3 451 2e-32 24.4541 335
1 450 449 - Rv3303c Mycobacterium tuberculosis 1 463 3e-31 25.0531 325
27 442 415 - b3500 Escherichia coli 29 444 4e-33 24.2424 341
5 445 440 - b0116 Escherichia coli 9 453 <1e-50 30.9735 575
2 442 440 - b3962 Escherichia coli 6 452 3e-35 26.4192 360
3 303 300 - b0606 Escherichia coli 213 488 0.000005 24.127 108
1 456 455 - MG271 Mycoplasma genitalium 1 456 <1e-50 68.8596 1692
2 456 454 - Rv0462 Mycobacterium tuberculosis 3 461 <1e-50 29.3362 497
2 442 440 - Rv2713 Mycobacterium tuberculosis 3 447 8.99998e-41 27.6923 407
3 447 444 - b0304 Escherichia coli 4 436 9.99995e-41 26.7699 406
3 444 441 - MCAP_0427 Mycoplasma capricolum subsp. capricolum 4 441 <1e-50 32.2148 632
3 449 446 - MCAP_0228 Mycoplasma capricolum subsp. capricolum 164 619 <1e-50 37.5 816
105 427 322 - MCAP_0223 Mycoplasma capricolum subsp. capricolum 85 416 0.000000000002 24.4253 157
2 451 449 - MS53_0275 Mycoplasma synoviae 157 611 <1e-50 36.9231 806
3 447 444 - MS53_0152 Mycoplasma synoviae 4 459 5e-36 27.0386 360
3 457 454 - MHP7448_0571 Mycoplasma hyopneumoniae 7448 4 453 <1e-50 31.1404 591
2 452 450 - MHP7448_0507 Mycoplasma hyopneumoniae 7448 160 619 <1e-50 36.7965 871
2 303 301 - MHP7448_0098 Mycoplasma hyopneumoniae 7448 3 277 0.00000002 27.619 122
2 451 449 - MMOB5800 Mycoplasma mobile 144 593 <1e-50 40.3548 944
1 455 454 - MMOB1750 Mycoplasma mobile 5 451 0.00000000007 18.7633 143
3 444 441 - MSC_0544 Mycoplasma mycoides subsp. mycoides SC 4 440 <1e-50 31.982 682
3 449 446 - MSC_0268 Mycoplasma mycoides subsp. mycoides SC 130 585 <1e-50 37.5 833
105 427 322 - MSC_0263 Mycoplasma mycoides subsp. mycoides SC 85 416 0.000000000004 24.7839 155
2 448 446 - LIC_12475 Leptospira interrogans serovar Copenhage 4 457 <1e-50 33.1897 545
3 451 448 - LIC_11803 Leptospira interrogans serovar Copenhage 4 452 <1e-50 28.5088 486
2 452 450 - LIC_11159 Leptospira interrogans serovar Copenhage 22 484 <1e-50 30.5732 555
2 443 441 - Rv0794c Mycobacterium tuberculosis 21 483 1e-28 24.5902 302
247 457 210 - MYCGA4860 Mycoplasma gallisepticum 243 467 0.00000003 24.569 122
2 456 454 - MYCGA4820 Mycoplasma gallisepticum 7 463 <1e-50 49.1266 1186
3 456 453 - MYPE5110 Mycoplasma penetrans 4 457 <1e-50 44.1048 1004
185 431 246 - MYPE1690 Mycoplasma penetrans 163 423 0.000000000004 25.8555 156
3 449 446 - Mycoplasma pulmonis 161 614 <1e-50 37.8261 815
3 444 441 - Mycoplasma pulmonis 4 445 <1e-50 31.0962 640
External IDs
COG 
COG1249C
EC number 
1.8.1.4
Gene ID 
877059
GI 
13508129
GO 
Energy production and conversion
Home COG 
C
InterPro 
IPR013027|FAD-dependent pyridine nucleotide-disulphide oxidoreductase
InterPro 
IPR006258|Dihydrolipoamide dehydrogenase
InterPro 
IPR012999|Pyridine nucleotide-disulphide oxidoreductase, class I, active site
InterPro 
IPR001327|Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
InterPro 
IPR000815|Mercuric reductase
InterPro 
IPR004099|Pyridine nucleotide-disulphide oxidoreductase dimerisation region
InterPro 
IPR001100|Pyridine nucleotide-disulphide oxidoreductase, class I
Old MP number 
MP448
Pathway 
Metabolism energy
PDB homologs 
1ebd_A
PDB homologs 
1dxl_A
PDB homologs 
1lpf_A
Pfam 
PF07992
Pfam 
PF02852
Pfam 
PF00070
Pfam 
PF00890
Pfam 
PF03486
Pfam 
PF01946
Pfam 
PF01134
Pfam 
PF01266
Pfam 
PF05834
PID 
g1674136
RefSeq 
NP_110078.1
Swiss-Prot protein ID 
DLDH_MYCPN
phylomeDB tree 
DLDH_MYCPN
UniProt 
P75393
Transcription
IMAGE BROWSERS

OPERON OP439 (Genomic Overview)
Region:464000-469068

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STRING image

STRING of Mpn390STRING legend

PDB image(s)

1ebd

PDB 1ebd

1dxl

PDB 1dxl

1lpf

PDB 1lpf
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