MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene nox (MPN394)
Name 
nox
Stable ID 
MPN394
Location 
471476 - 472915 -
Sequence 
    1  ATGAAGAAAG TGATTGTTAT CGGTGTCAAT CACGCCGGCA CCAGTTTTAT CAGAACCCTT
   61  TTAAGCAAGA GCAAAGACTT TCAGGTCAAC GCTTATGATC GCAATACCAA CATCTCCTTT
  121  TTGGGTTGTG GAATTGCCTT GGCAGTTAGT GGTGTAGTTA AAAACACCGA AGACCTGTTC
  181  TACTCCACCC CTGAAGAGCT AAAAGCTATG GGTGCTAATG TCTTTATGGC TCATGATGTA
  241  GTTGGTCTTG ATCTAGACAA AAAACAAGTA ATCGTGAAGG ACTTGGCCAC TGGTAAGGAA
  301  ACTGTGGACC ACTATGATCA ATTGGTAGTA GCCTCTGGAG CTTGACCGAT TTGTATGAAT
  361  GTGGAAAACG AAGTAACCCA CACCCAATTG CAATTCAACC ACACTGATAA GTACTGTGGC
  421  AATATTAAGA ACTTAATTAG TTGTAAGTTG TACCAACACG CCCTTACCTT AATTGACAGC
  481  TTCCGTCATG ACAAGTCAAT TAAATCAGTA GCCATTGTGG GCTCGGGTTA CATTGGTTTA
  541  GAGTTAGCAG AAGCGGCTTG ACAGTGTGGT AAACAGGTGA CTGTGATTGA CATGTTGGAC
  601  AAACCAGCTG GCAATAACTT TGATGAAGAG TTTACCAACG AGTTGGAAAA AGCCATGAAG
  661  AAAGCGGGCA TTAACCTAAT GATGGGTAGT GCCGTTAAGG GCTTTATTGT TGATGCGGAC
  721  AAAAATGTCG TTAAAGGTGT TGAAACCGAT AAGGGTCGGG TGGATGCTGA CCTTGTCATC
  781  CAATCGATTG GGTTCCGCCC AAACACCCAG TTTGTCCCTA AAGACAGGCA GTTTGAGTTT
  841  AACCGTAACG GTTCGATTAA GGTTAATGAA TACCTCCAAG CCTTAAATCA TGAAAATGTG
  901  TATGTTATTG GTGGGGCTGC TGCCATTTAT GATGCAGCTA GTGAACAATA CGAAAACATT
  961  GACTTAGCTA CCAACGCTGT GAAAAGTGGT TTAGTCGCTG CTATGCACAT GATTGGTAGC
 1021  AAGGCTGTAA AGTTAGAGTC CATTGTTGGT ACCAATGCGC TGCACGTATT TGGTTTAAAT
 1081  CTAGCAGCTA CTGGTTTAAC CGAAAAACGT GCCAAAATGA ACGGTTTTGA TGTGGGAGTG
 1141  AGCATTGTTG ATGACAACGA CCGTCCCGAA TTTATGGGGA CCTTTGACAA GGTGCGCTTT
 1201  AAGTTAATTT ACGACAAGAA GACGCTCCGT TTGTTGGGTG CCCAATTACT TTCGTGAAAC
 1261  ACCAACCACA GTGAAATTAT CTTCTATATT GCTTTAGCAG TACAGAAGAA AATGTTGATC
 1321  AGTGAACTGG GTTTAGTAGA CGTTTACTTT CTTCCCCACT ACAATAAGCC GTTCAACTTT
 1381  GTGTTAGCAG CCGTGTTGCA AGCGCTTGGT TTTAGTTACT ATACCCCTAA AAATAAATAA
Download Sequence
Operon 
OP437
Operon location 
469365 - 472927
Protein (mpn394)
Name 
Probable NADH oxidase (NOXase) (EC 1.6.99.3)
Stable ID 
Mpn394
Molecular Weight 
52690
Isoelectric Point 
7
Localization 
Cytoplasm
Comment -
Sequence 
MKKVIVIGVNHAGTSFIRTLLSKSKDFQVNAYDRNTNISFLGCGIALAVSGVVKNTEDLFYSTPEELKAMGANVFMAHDV
VGLDLDKKQVIVKDLATGKETVDHYDQLVVASGAWPICMNVENEVTHTQLQFNHTDKYCGNIKNLISCKLYQHALTLIDS
FRHDKSIKSVAIVGSGYIGLELAEAAWQCGKQVTVIDMLDKPAGNNFDEEFTNELEKAMKKAGINLMMGSAVKGFIVDAD
KNVVKGVETDKGRVDADLVIQSIGFRPNTQFVPKDRQFEFNRNGSIKVNEYLQALNHENVYVIGGAAAIYDAASEQYENI
DLATNAVKSGLVAAMHMIGSKAVKLESIVGTNALHVFGLNLAATGLTEKRAKMNGFDVGVSIVDDNDRPEFMGTFDKVRF
KLIYDKKTLRLLGAQLLSWNTNHSEIIFYIALAVQKKMLISELGLVDVYFLPHYNKPFNFVLAAVLQALGFSYYTPKNK
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation mKKVIVIGVNHAGTSFIR 1 19 M
Oxidation AmGANVFMAHDVVGLDLDKK 69 89 M
Oxidation AmGANVFmAHDVVGLDLDKK 69 89 M
Oxidation AMGANVFmAHDVVGLDLDkk 69 89 M
Oxidation AmGANVFMAHDVVGLDLDkk 69 89 M
Oxidation AMGANVFmAHDVVGLDLDkK 69 89 M
Oxidation AmGANVFmAHDVVGLDLDkk 69 89 M
Oxidation AmGANVFMAHDVVGLDLDkK 69 89 M
Oxidation AMGANVFmAHDVVGLDLDKk 69 89 M
Oxidation AmGANVFmAHDVVGLDLDkK 69 89 M
Oxidation AmGANVFMAHDVVGLDLDKk 69 89 M
Oxidation AMGANVFmAHDVVGLDLDKK 69 89 M
Oxidation AmGANVFmAHDVVGLDLDKk 69 89 M
Oxidation QVTVIDmLDkPAGNNFDEEFTNELEk 192 218 M
Oxidation QVTVIDmLDkPAGNNFDEEFTNELEK 192 218 M
Oxidation QVTVIDmLDKPAGNNFDEEFTNELEk 192 218 M
Oxidation QVTVIDmLDKPAGNNFDEEFTNELEK 192 218 M
Oxidation KAGINLmMGSAVK 221 234 M
Oxidation kAGINLmmGSAVk 221 234 M
Oxidation KAGINLMmGSAVK 221 234 M
Oxidation kAGINLMmGSAVk 221 234 M
Oxidation KAGINLmmGSAVK 221 234 M
Oxidation kAGINLmMGSAVk 221 234 M
Oxidation AGINLmMGSAVK 222 234 M
Oxidation AGINLmmGSAVk 222 234 M
Oxidation AGINLMmGSAVk 222 234 M
Oxidation AGINLMmGSAVK 222 234 M
Oxidation AGINLmmGSAVK 222 234 M
Oxidation AGINLmMGSAVk 222 234 M
Oxidation AGINLmmGSAVKGFIVDADKNVVK 222 246 M
Methylation VDADLVIQSIGFRPNTQFVPk 254 275 K
Oxidation SGLVAAmHMIGSk 329 342 M
Oxidation SGLVAAmHMIGSK 329 342 M
Oxidation SGLVAAMHmIGSk 329 342 M
Oxidation SGLVAAmHmIGSk 329 342 M
Oxidation SGLVAAMHmIGSK 329 342 M
Oxidation SGLVAAmHmIGSK 329 342 M
Methylation MNGFDVGVSIVDDNDRPEFMGTFDk 373 398 K
Oxidation mNGFDVGVSIVDDNDrPEFMGTFDk 373 398 M
Oxidation mNGFDVGVSIVDDNDRPEFMGTFDK 373 398 M
Oxidation mNGFDVGVSIVDDNDRPEFMGTFDk 373 398 M
GENE/PROTEIN nox (Domains Overview)
Click on the features to jump to domain info

 ExportIMG
Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-110 G3DSA:3.50.50.60 (n.a.) NULL 1e-37
1-339 SSF51905 (n.a.) NULL 3.9e-37
3-25 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.0000000000027
3-310 PF07992 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 1.9e-32
5-472 PTHR22912:SF2 (n.a.) NULL 0
5-472 PTHR22912 (n.a.) NULL 0
111-339 G3DSA:3.50.50.60 (n.a.) NULL 1.7e-38
169-194 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.0000000000027
169-247 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)

2.4e-16
257-271 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.0000000000027
300-307 PR00368 (IPR013027) FAD-dependent pyridine nucleotide-disulphide oxido 0.0000000000027
347-473 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)

7.2e-28
357-455 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)

0.0000000000046
359-469 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)

1.6e-28
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
104 388 284 - b2711 Escherichia coli 99 354 0.0000000002 26.3699 145
100 435 335 - b0116 Escherichia coli 133 430 0.000000009 25.9259 132
59 271 212 - b2542 Escherichia coli 52 245 0.0000001 23.6111 122
3 473 470 - MAG2630 Mycoplasma agalactiae 2 452 <1e-50 48.3122 1088
3 454 451 - MAG2460 Mycoplasma agalactiae 2 429 3e-38 28.4141 380
3 473 470 - MCJ_003020 Mycoplasma conjunctivae 2 455 <1e-50 44.3038 979
105 443 338 - MCJ_005300 Mycoplasma conjunctivae 129 426 0.000000000005 24.3478 154
155 417 262 - MCJ_000700 Mycoplasma conjunctivae 323 569 0.0000000003 28.0303 138
3 474 471 - MCAP_0223 Mycoplasma capricolum subsp. capricolum 2 450 <1e-50 41.3136 929
3 465 462 - MCAP_0858 Mycoplasma capricolum subsp. capricolum 2 441 2e-39 26.5659 390
2 418 416 - MCAP_0541 Mycoplasma capricolum subsp. capricolum 3 431 0.0000007 19.8218 110
159 443 284 - MCAP_0427 Mycoplasma capricolum subsp. capricolum 162 427 0.000009 23.1034 101
3 474 471 - MYCGA4860 Mycoplasma gallisepticum 2 466 <1e-50 50.6276 1280
181 443 262 - MYCGA4820 Mycoplasma gallisepticum 193 437 0.00000006 24.6269 119
1 477 476 - MG275 Mycoplasma genitalium 1 477 <1e-50 83.2285 2164
3 473 470 - MHP7448_0082 Mycoplasma hyopneumoniae 7448 2 455 <1e-50 46.4135 1018
2 473 471 - MMOB6200 Mycoplasma mobile 5 459 <1e-50 45.0526 1019
3 474 471 - MSC_0263 Mycoplasma mycoides subsp. mycoides SC 2 450 <1e-50 41.5254 931
3 465 462 - MSC_1044 Mycoplasma mycoides subsp. mycoides SC 26 465 3e-39 26.5659 389
3 465 462 - MSC_1019 Mycoplasma mycoides subsp. mycoides SC 26 465 3e-39 26.5659 389
169 443 274 - MSC_0544 Mycoplasma mycoides subsp. mycoides SC 173 426 0.000000005 23.0216 129
3 473 470 - MYPE1690 Mycoplasma penetrans 2 452 <1e-50 50.1057 1145
172 327 155 - MYPE5110 Mycoplasma penetrans 179 328 0.000001 23.7179 109
170 304 134 - Lactococcus lactis subsp. lactis KF147 165 295 0.00000003 33.0986 124
118 304 186 - Lactococcus lactis subsp. lactis KF147 131 318 0.0000000003 29.5337 142
1 454 453 - Lactococcus lactis subsp. lactis KF147 2 426 2e-22 23.4783 247
3 467 464 - Lactococcus lactis subsp. lactis KF147 2 439 5e-40 25.9023 399
3 468 465 - Lactococcus lactis subsp. lactis KF147 2 445 <1e-50 34.0471 701
163 443 280 - LIC_11159 Leptospira interrogans serovar Copenhage 185 462 0.0000000000002 27.3333 170
4 435 431 - LIC_12475 Leptospira interrogans serovar Copenhage 7 431 0.0000000001 23.871 147
2 308 306 - LIC_20028 Leptospira interrogans serovar Copenhage 7 305 0.0000001 22.3565 121
155 310 155 - LIC_11803 Leptospira interrogans serovar Copenhage 156 309 0.000001 25.1534 112
2 473 471 - MS53_0522 Mycoplasma synoviae 4 456 <1e-50 47.5789 1086
155 456 301 - MS53_0275 Mycoplasma synoviae 318 602 0.00000008 24.7557 117
168 459 291 - MS53_0152 Mycoplasma synoviae 177 457 0.0000003 25.2525 113
190 443 253 - Rv0462 Mycobacterium tuberculosis 194 436 0.0000000000004 27.907 169
168 435 267 - Lactococcus lactis subsp. lactis KF147 161 409 0.0000000006 24.8227 140
168 422 254 - Caulobacter crescentus NA1000 184 428 0.000000001 29.1667 138
3 304 301 - Caulobacter crescentus NA1000 9 282 0.000000006 21.7105 133
156 417 261 - Caulobacter crescentus NA1000 167 414 0.00000005 26.0223 125
154 435 281 - Caulobacter crescentus NA1000 161 428 0.00001 22.4914 105
2 377 375 - Bacillus subtilis subsp. subtilis 4 346 0.0000000000008 22.3377 168
2 377 375 - Bacillus subtilis subsp. subtilis 4 346 0.000000000002 22.0779 166
168 445 277 - Bacillus subtilis subsp. subtilis 177 442 0.00000000007 25.9649 151
168 445 277 - Bacillus subtilis subsp. subtilis 177 442 0.00000000007 25.9649 151
71 378 307 - Bacillus subtilis subsp. subtilis 73 344 0.0000000002 20.6897 148
71 388 317 - Bacillus subtilis subsp. subtilis 73 350 0.0000000007 20.6687 143
1 316 315 - Bacillus subtilis subsp. subtilis 1 282 0.00000007 22.4924 126
1 316 315 - Bacillus subtilis subsp. subtilis 1 282 0.00000007 22.4924 126
98 372 274 - Bacillus subtilis subsp. subtilis 127 360 0.0000002 26.4085 122
98 372 274 - Bacillus subtilis subsp. subtilis 127 360 0.0000003 26.4085 120
190 417 227 - Bacillus subtilis subsp. subtilis 204 422 0.000002 24.7899 113
190 417 227 - Bacillus subtilis subsp. subtilis 204 422 0.000002 24.7899 113
3 473 470 - Mycoplasma pulmonis 24 477 <1e-50 44.4444 999
168 471 303 - Mycoplasma pulmonis 172 454 0.00000000003 26.1981 148
168 456 288 - Mycoplasma pulmonis 337 607 0.00000003 24.7492 122
External IDs
COG 
COG0446R
EC number 
1.6.99.3
Gene ID 
877135
GI 
13508133
GO 
Energy production and conversion
Home COG 
C
InterPro 
IPR013027|FAD-dependent pyridine nucleotide-disulphide oxidoreductase
InterPro 
IPR004099|Pyridine nucleotide-disulphide oxidoreductase dimerisation region
InterPro 
IPR001327|Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
Old MP number 
MP444
Pathway 
Metabolism energy, Aerobic
PDB homologs 
1lpf_A
PDB homologs 
1BHY
PDB homologs 
1dxl_A
PDB homologs 
1ebd_A
Pfam 
PF02852
Pfam 
PF01266
Pfam 
PF01118
Pfam 
PF00070
Pfam 
PF07992
PID 
g1674132
RefSeq 
NP_110082.1
Swiss-Prot protein ID 
NAOX_MYCPN
phylomeDB tree 
NAOX_MYCPN
UniProt 
P75389
Transcription
IMAGE BROWSERS

OPERON OP437 (Genomic Overview)
Region:469365-472927

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STRING image

STRING of Mpn394STRING legend

PDB image(s)

1lpf

PDB 1lpf

1BHY

PDB 1BHY

1dxl

PDB 1dxl

1ebd

PDB 1ebd
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