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A9QZ96 (PDXH_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:YpAngola_A2555
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length217 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 – 217217Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000186347

Regions

Nucleotide binding81 – 822FMN By similarity
Nucleotide binding145 – 1462FMN By similarity
Region13 – 164Substrate binding By similarity
Region196 – 1983Substrate binding By similarity

Sites

Binding site661FMN By similarity
Binding site691FMN; via amide nitrogen By similarity
Binding site711Substrate By similarity
Binding site881FMN By similarity
Binding site1281Substrate By similarity
Binding site1321Substrate By similarity
Binding site1361Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9QZ96 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0CB7B6F07CB1DA86

FASTA21725,383
        10         20         30         40         50         60 
MTENNEFDVA DLRREYIRGG LRRSDLTENP LELFERWLKQ ACEARLPDPT AMCVATVDTN 

        70         80         90        100        110        120 
GQPYQRIVLL KHYDDQGLVF YTNLGSRKAQ QLAENPHISL LFPWHMLDRQ VIFLGKAERL 

       130        140        150        160        170        180 
STLEVLKYFH SRPKDSQIGA WVSQQSSRIS ARGVLESKFL ELKQKFQQGD VPLPSFWGGF 

       190        200        210 
RVKFDSVEFW QGGEHRLHDR FIYQREADAW KIDRLAP 

« Hide

References

[1]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000901 Genomic DNA. Translation: ABX87086.1.
RefSeqYP_001606966.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9QZ96.
SMRA9QZ96. Positions 9-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A2555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX87086; ABX87086; YpAngola_A2555.
GeneID5801026.
KEGGypg:YpAngola_A2555.
PATRIC18574537. VBIYerPes97331_3042.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycYPES349746:GHPB-2560-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_YERPG
AccessionPrimary (citable) accession number: A9QZ96
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 52 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