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B0CKA2 (PDXH_BRUSI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BSUIS_A0442
OrganismBrucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]
Taxonomic identifier470137 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length203 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 MF_01629

Catalytic activity

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

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_01629

Pathway

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   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: InterPro

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_0000335782

Regions

Nucleotide binding65 – 662FMN By similarity
Nucleotide binding129 – 1302FMN By similarity
Region180 – 1823Substrate binding By similarity

Sites

Binding site501FMN By similarity
Binding site531FMN; via amide nitrogen By similarity
Binding site551Substrate By similarity
Binding site721FMN By similarity
Binding site1121Substrate By similarity
Binding site1161Substrate By similarity
Binding site1201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CKA2 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: A89D1595AC42D511

FASTA20323,281
        10         20         30         40         50         60 
MTNSSDDFTQ SAEPFKLFAE WLADAAKSEP NDPNAVALAT VDPDGLPNVR MVLLKDFDET 

        70         80         90        100        110        120 
GFVFYTNYES KKGQEILSAE KAAMCFHWKS LRRQVRVRGP VEKVSDAEAD AYYASRPRGS 

       130        140        150        160        170        180 
RIGAWASKQS RPLESRFALE KAVAEYTAKY AIGDIPRPPY WSGFRIRPVS IEFWHDRPFR 

       190        200 
LHDRVLFTRP TPEGDWNKDR LYP

« Hide

References

[1]"Brucella suis ATCC 23445 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23445 / NCTC 10510.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000911 Genomic DNA. Translation: ABY37532.1.
RefSeqYP_001627102.1. NC_010169.1.

3D structure databases

ProteinModelPortalB0CKA2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CKA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5839269.
GenomeReviewsGene locus BSUIS_A0442 in contig CP000911_GR.
KEGGbmt:BSUIS_A0442.
PATRIC17868396. VBIBruSui83806_1999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327559.
OMAHWSGFRI.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycBSUI470137:BSUIS_A0442-MONOMER.

Family and domain databases

HAMAPMF_01629. PdxH.
[Tree]
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
IPR009002. Split_barrel_FMN-bd-related.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KOK00275.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. PdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_BRUSI
AccessionPrimary (citable) accession number: B0CKA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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