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Q0VSU8 (PDXH_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:ABO_0302
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length209 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 – 209209Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000255849

Regions

Nucleotide binding73 – 742FMN By similarity
Nucleotide binding137 – 1382FMN By similarity
Region5 – 84Substrate binding By similarity
Region187 – 1893Substrate binding By similarity

Sites

Binding site581FMN By similarity
Binding site611FMN; via amide nitrogen By similarity
Binding site631Substrate By similarity
Binding site801FMN By similarity
Binding site1201Substrate By similarity
Binding site1241Substrate By similarity
Binding site1281Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VSU8 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A8DB30E2821CFB2C

FASTA20924,002
        10         20         30         40         50         60 
MKDVREEYHA DGLIEATLHD DPLEQARRWV DEAIEAELPL PNAITLATVS ANGQPSSRVV 

        70         80         90        100        110        120 
LLKGIENQGF TFFTHYDSRK GEEIAANPKV SFTMFWQPFD RQMIVIGEAQ KVDQEESDSY 

       130        140        150        160        170        180 
FASRPYASQV SAAISPQSRP ASREWLEAEV SRLEQEFPSA PVPRPEQWGG YRIIPTEIQF 

       190        200 
WHGRPSRLHD RFRYVKQGDG CWQRERLAP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL15750.1.
RefSeqYP_692022.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VSU8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393595.ABO_0302.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL15750; CAL15750; ABO_0302.
GeneID4212450.
KEGGabo:ABO_0302.
PATRIC20838207. VBIAlcBor124741_0321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMARAVTTIS.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycABOR393595:GHRI-302-MONOMER.
UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
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.
ProtoNetSearch...

Entry information

Entry namePDXH_ALCBS
AccessionPrimary (citable) accession number: Q0VSU8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 60 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