Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7MU50 (PDXH_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidase

EC=1.4.3.5
Alternative name(s):
PNP/PMP oxidase
Short name=PNPOx
Pyridoxal 5'-phosphate synthase
Gene names
Name:pdxH
Ordered Locus Names:PG_1714
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity. HAMAP-Rule MF_01629

Catalytic activity

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule MF_01629

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_01629

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP-Rule MF_01629

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167733

Regions

Nucleotide binding77 – 782FMN By similarity
Nucleotide binding141 – 1422FMN By similarity
Region9 – 124Substrate binding By similarity
Region192 – 1943Substrate binding By similarity

Sites

Binding site621FMN By similarity
Binding site651FMN; via amide nitrogen By similarity
Binding site671Substrate By similarity
Binding site841FMN By similarity
Binding site1241Substrate By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MU50 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D348FC7BA1808305

FASTA21424,912
        10         20         30         40         50         60 
MDLHFENIRR EYDKRSLSAS DLTPTPFDLV TRWLQDAVEA KTYEPTAVIV GTATPDGHPS 

        70         80         90        100        110        120 
TRTVLLKEFM NNEFIFYSNY ESRKGQQMAA NPHVCLTFLW HELERQIHVE GDVRILEPEL 

       130        140        150        160        170        180 
SDAYFATRPY KSRVGARISP QSRPIPGRSF IVQEFMKESL KYAGRTVPRP DTWGGFAVKP 

       190        200        210 
VRIEFWQGRE SRLHDRFLYE LRPDASWSVH RLAP 

« Hide

References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ66723.1.
RefSeqNP_905824.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ7MU50.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242619.PG1714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ66723; AAQ66723; PG_1714.
GeneID2552531.
KEGGpgi:PG1714.
PATRIC22980426. VBIPorGin134034_1589.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
KOK00275.
OMAFTNRESR.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycPGIN242619:GHX8-1546-MONOMER.
UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_PORGI
AccessionPrimary (citable) accession number: Q7MU50
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways