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Q3SV02 (PDXH_NITWN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:Nwi_0622
OrganismNitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]
Taxonomic identifier323098 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length213 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 – 213213Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167728

Regions

Nucleotide binding75 – 762FMN By similarity
Nucleotide binding139 – 1402FMN By similarity
Region190 – 1923Substrate binding By similarity

Sites

Binding site601FMN By similarity
Binding site631FMN; via amide nitrogen By similarity
Binding site651Substrate By similarity
Binding site821FMN By similarity
Binding site1221Substrate By similarity
Binding site1261Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SV02 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 1D1C0E1CFDCD89A1

FASTA21324,054
        10         20         30         40         50         60 
MNDTTDIKHT SQLTSGDFTE AREPFALFEA WLAEATASEP NDPDAMALAT ADADGLPDLR 

        70         80         90        100        110        120 
MVLMKGFDAR GFVFYSHIAS AKGRELAANP KAALLFHWKS LRRQVRVRGP VTPVTDAEAD 

       130        140        150        160        170        180 
AYFATRPRQA QIGAWASRQS RPLESRLAFE QAIAKEAAKY AIGAVPRPPG WSGWRITPLQ 

       190        200        210 
FEFWHDRPFR LHDRIEFRRS ALDVPWTKTR LYP 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nb-255 / ATCC 25391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000115 Genomic DNA. Translation: ABA03889.1.
RefSeqYP_317241.1. NC_007406.1.

3D structure databases

ProteinModelPortalQ3SV02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323098.Nwi_0622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA03889; ABA03889; Nwi_0622.
GeneID3676051.
KEGGnwi:Nwi_0622.
PATRIC22697690. VBINitWin102302_0684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMASIEFWCD.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycNWIN323098:GJEG-640-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_NITWN
AccessionPrimary (citable) accession number: Q3SV02
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 11, 2005
Last modified: May 14, 2014
This is version 63 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