MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene trxB (MPN240)
Name 
trxB
Stable ID 
MPN240
Location 
292328 - 293275 +
Sequence 
    1  ATGCTTAAAG TAAAGTCAGA TTTTTTAACT AAAGATCAGG TTATTTACGA TGTAGCGATA
   61  GTGGGTGCTG GGCCAGCTGG CATAGCAGCG GGTATTTATG GCAAACGCGC TAACCTCAAT
  121  CTAGCCATTA TTGAAGGTAG TACTCCCGGC GGTAAGGTTG TCAAAACCAA CATTGTCGAG
  181  AACTATCCGG GTTACAAGTC AATTACCGGA CCTGACTTGG GGTTGGAAAT GTACAACCAC
  241  CTAATTGATT TAGAGCCCAC CTTTTTCTAT GCTAACCTAA TTAAGTTAGA TAAGGCAGCA
  301  GATACCTTTA TCTTGTACCT CGATGACAAA ACTGTGGTGT TTGCCAAAAC CGTTATTTAC
  361  GCTACGGGAA TGTTGGAGCG TAAACTGGGC GTAGCCAAAG AAGACCACTT TTACGGTAAG
  421  GGAATTAGTT ACTGTGCCAT TTGTGATGGG TCCTTGTACA AAGACCAGGT GGTGGGTGTT
  481  GTTGGTGGGG GGAACTCTGC CATTCAGGAA GCGTTGTATT TAGCTAGCAT GGCTAAAACG
  541  GTGCACTTAA TCCACCGCCG TGAGGGCTTT CGTGCTGATG AAACGGCGTT AAATAAACTG
  601  AGAAACTTAC CGAATGTTGT TTTTCACTTG AACTATACCG TAAAAGAATT GTTGGGTAAC
  661  AATACCCTAA ACGGCATAGT GCTTCAAAAC ACGCTCGATC ATTCAACAAA ACAGATAGAT
  721  CTCAATTGTG TCTTTCCCTA TATTGGTTTT GAAAGTATTA CCAAACCGGT GGAACACCTC
  781  AACTTAAAGT TAGATCCCCA GGGTTTTTTA ATTACCAATG AACAGATGGA AACAAGTTTA
  841  AAGGGTCTGT TTGCAGCAGG TGATTGTCGT TCTAAGCACT TCCGTCAAAT TGGTACTGCC
  901  ATTAATGACG GCATTATCGC GGTGTTAACG ATCCGTGATG TCCTTTAG
Download Sequence
Operon 
OP98
Operon location 
291652 - 294075
Protein (mpn240)
Name 
Thioredoxin reductase (TRXR) (EC 1.8.1.9)
Stable ID 
Mpn240
Molecular Weight 
34650
Isoelectric Point 
7
Localization 
Cytoplasm
Comment -
Sequence 
MLKVKSDFLTKDQVIYDVAIVGAGPAGIAAGIYGKRANLNLAIIEGSTPGGKVVKTNIVENYPGYKSITGPDLGLEMYNH
LIDLEPTFFYANLIKLDKAADTFILYLDDKTVVFAKTVIYATGMLERKLGVAKEDHFYGKGISYCAICDGSLYKDQVVGV
VGGGNSAIQEALYLASMAKTVHLIHRREGFRADETALNKLRNLPNVVFHLNYTVKELLGNNTLNGIVLQNTLDHSTKQID
LNCVFPYIGFESITKPVEHLNLKLDPQGFLITNEQMETSLKGLFAAGDCRSKHFRQIGTAINDGIIAVLTIRDVL
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation TVIYATGmLER 117 128 M
GENE/PROTEIN trxB (Domains Overview)
Click on the features to jump to domain info

 ExportIMG
Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-315 SSF51905 (n.a.) NULL 0
16-129 G3DSA:3.50.50.60 (n.a.) NULL 1.4e-35
16-315 TIGR01292 (IPR005982) Thioredoxin 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';:0019430'>'removal' == '' ? '': 'removal'; 'of' == '' ? '': 'of'; 'superoxide' == '' ? '': 'superoxide'; 'radicals' == '' ? '': 'radicals'; ('GO' == '' ? '': 'GO';:0019430) <'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';:0004791'>'thioredoxin' == '' ? '': 'thioredoxin';-'disulfide' == '' ? '': 'disulfide'; 'reductase' == '' ? '': 'reductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004791)

0
17-39 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.000000000000027
17-39 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
17-291 PF07992 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1e-29
19-311 PTHR22912 (n.a.) NULL 0.0000000000006
50-65 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
70-80 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
116-124 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
118-127 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.000000000000027
130-249 G3DSA:3.50.50.60 (n.a.) NULL 4.1e-37
138-150 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
145-165 PS00573 (IPR008255) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
153-177 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
157-182 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.000000000000027
159-228 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)

0.000000098
205-221 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
250-314 G3DSA:3.50.50.60 (n.a.) NULL 1.4e-35
278-296 PR00469 (IPR000103) Pyridine nucleotide-disulphide oxidoreductase, cla 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)

0
283-290 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.000000000000027
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
36 309 273 - b0888 Escherichia coli 27 308 1.99993e-41 36.1404 412
46 315 269 - b0606 Escherichia coli 242 515 2e-29 30.5455 308
36 311 275 - MARTH_orf510 Mycoplasma arthritidis 24 296 1.96182e-44 35.4386 431
12 315 303 - MAG0910 Mycoplasma agalactiae 3 306 1.96182e-44 34.202 432
13 312 299 - MCJ_005260 Mycoplasma conjunctivae 2 303 <1e-50 37.1711 492
15 307 292 - MCAP_0779 Mycoplasma capricolum subsp. capricolum 8 298 <1e-50 41.4966 584
35 313 278 - MYCGA4610 Mycoplasma gallisepticum 31 307 <1e-50 48.3871 699
103 315 212 - MYCGA3300 Mycoplasma gallisepticum 102 315 0.000003 26.009 103
1 313 312 - MG102 Mycoplasma genitalium 1 313 <1e-50 65.8147 1062
36 312 276 - MHP7448_0098 Mycoplasma hyopneumoniae 7448 24 303 9.99967e-42 35.4386 408
36 313 277 - MHO_3400 Mycoplasma hominis 27 304 <1e-50 38.0783 485
12 307 295 - MMOB1840 Mycoplasma mobile 3 298 <1e-50 38.796 540
15 307 292 - MSC_0938 Mycoplasma mycoides subsp. mycoides SC 8 298 <1e-50 41.8367 588
2 312 310 - MYPE9330 Mycoplasma penetrans 1 311 <1e-50 42.6282 695
105 311 206 - MYPE1390 Mycoplasma penetrans 106 315 0.0000000004 26.8182 137
118 311 193 - MYPE1690 Mycoplasma penetrans 107 314 0.0000002 29.2793 113
160 311 151 - MYPE5110 Mycoplasma penetrans 179 328 0.0000003 28.0255 112
39 289 250 - Lactococcus lactis subsp. lactis KF147 27 278 2e-21 30.2682 236
50 315 265 - Lactococcus lactis subsp. lactis KF147 242 506 2e-31 31.7343 322
36 309 273 - LIC_11470 Leptospira interrogans serovar Copenhage 23 304 6e-38 33.8028 380
68 315 247 - MS53_0596 Mycoplasma synoviae 2 249 <1e-50 41.0359 452
36 309 273 - Rv3913 Mycobacterium tuberculosis 35 309 4.99983e-42 36.0424 416
16 308 292 - Lactococcus lactis subsp. lactis KF147 6 297 <1e-50 32.6531 449
36 309 273 - Caulobacter crescentus NA1000 42 319 6e-35 33.3333 355
50 315 265 - Caulobacter crescentus NA1000 245 515 2e-32 30.9963 333
12 312 300 - Bacillus subtilis subsp. subtilis 3 302 <1e-50 35.7616 497
12 312 300 - Bacillus subtilis subsp. subtilis 3 302 <1e-50 35.4305 495
50 315 265 - Bacillus subtilis subsp. subtilis 242 506 2e-36 33.4586 370
50 315 265 - Bacillus subtilis subsp. subtilis 242 506 2e-36 33.4586 370
96 288 192 - Bacillus subtilis subsp. subtilis 93 285 2e-17 28.5714 207
96 288 192 - Bacillus subtilis subsp. subtilis 93 285 3e-17 28.5714 204
50 308 258 - Bacillus subtilis subsp. subtilis 43 309 0.000000000004 24.5487 161
50 308 258 - Bacillus subtilis subsp. subtilis 43 309 0.00000000003 24.9097 153
15 312 297 - Mycoplasma pulmonis 6 304 <1e-50 35.1974 453
111 292 181 - Mycoplasma pulmonis 126 307 0.000001 23.8342 106
External IDs
COG 
COG0492O
EC number 
1.8.1.9
Gene ID 
877259
GI 
13507979
GO 
Post-translational modification, protein turnover, chaperones/ Nucleotide transport and metabolism
Home COG 
OF
InterPro 
IPR001327|Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
InterPro 
IPR005982|Thioredoxin reductase
InterPro 
IPR008255|Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
InterPro 
IPR013027|FAD-dependent pyridine nucleotide-disulphide oxidoreductase
InterPro 
IPR000759|Adrenodoxin reductase
InterPro 
IPR000103|Pyridine nucleotide-disulphide oxidoreductase, class-II
Old MP number 
MP591
Pathway 
Biosynthesis of cofactors, prosthetic groups
Pathway 
Metabolism
PDB homologs 
1tde_
PDB homologs 
1f6m_A
PDB homologs 
1BHY
PDB homologs 
1cl0_A
Pfam 
PF01946
Pfam 
PF03486
Pfam 
PF05834
Pfam 
PF07992
Pfam 
PF01494
Pfam 
PF01266
Pfam 
PF00890
Pfam 
PF00070
PID 
g1674293
RefSeq 
NP_109928.1
Swiss-Prot protein ID 
TRXB_MYCPN
phylomeDB tree 
TRXB_MYCPN
UniProt 
P75531
Transcription
IMAGE BROWSERS

OPERON OP98 (Genomic Overview)
Region:291652-294075

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STRING image

STRING of Mpn240STRING legend

PDB image(s)

1tde

PDB 1tde

1f6m

PDB 1f6m

1BHY

PDB 1BHY

1cl0

PDB 1cl0
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