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A4W9V9 (PDXH_ENT38) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Ent638_1810
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Protein attributes

Sequence length218 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 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000069693

Regions

Nucleotide binding82 – 832FMN By similarity
Nucleotide binding146 – 1472FMN By similarity
Region14 – 174Substrate binding By similarity
Region197 – 1993Substrate binding By similarity

Sites

Binding site671FMN By similarity
Binding site701FMN; via amide nitrogen By similarity
Binding site721Substrate By similarity
Binding site891FMN By similarity
Binding site1291Substrate By similarity
Binding site1331Substrate By similarity
Binding site1371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4W9V9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 22BCB556E02F190F

FASTA21825,530
        10         20         30         40         50         60 
MSDNDELQQI AHLRREYTKG GLRRQDLPAE PLDLFERWLK QACEAKLADP TAMVVATVDE 

        70         80         90        100        110        120 
NSQPYQRIVL LKHYDEKGLV FYTNLGSRKA HHLENNPRIS LLFPWHMLER QVMVTGKAER 

       130        140        150        160        170        180 
LSTLEVLKYF HSRPRDSQIG AWVSKQSSRI SARGVLESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSVEQMEF WQGGEHRLHD RFLYQRDNAA WKIDRLAP 

« Hide

References

[1]"Genome sequence of the plant growth promoting endophytic bacterium Enterobacter sp. 638."
Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., Vangronsveld J., Newman L., Monchy S.
PLoS Genet. 6:E1000943-E1000943(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000653 Genomic DNA. Translation: ABP60489.1.
RefSeqYP_001176540.1. NC_009436.1.

3D structure databases

ProteinModelPortalA4W9V9.
SMRA4W9V9. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399742.Ent638_1810.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP60489; ABP60489; Ent638_1810.
GeneID5113333.
KEGGent:Ent638_1810.
PATRIC20413255. VBIEntSp101211_1957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANMGSRKA.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycESP399742:GJ0E-1856-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_ENT38
AccessionPrimary (citable) accession number: A4W9V9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 55 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