Reviewed, UniProtKB/Swiss-Prot B0CKA2 (PDXH_BRUSI)

Names and origin

Protein names

Recommended 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

Organism

Brucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]

Taxonomic identifier

470137 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Pyridoxine biosynthesis
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: HAMAP pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 203	203	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000335782
Regions
	Nucleotide binding	65 – 66	2	FMN By similarity
	Nucleotide binding	129 – 130	2	FMN By similarity
	Region	180 – 182	3	Substrate binding By similarity
Sites
	Binding site	50	1	FMN By similarity
	Binding site	53	1	FMN; via amide nitrogen By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	72	1	FMN By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0CKA2-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: A89D1595AC42D511	FASTA	203	23,281
	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

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. , 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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000911 Genomic DNA. Translation: ABY37532.1.
RefSeq	YP_001627102.1.
3D structure databases
SMR	B0CKA2. Positions 12-203.
ModBase	Search...
Genome annotation databases
GeneID	5839269.
GenomeReviews	Gene locus BSUIS_A0442 in contig CP000911_GR.
KEGG	bmt:BSUIS_A0442.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG327559.
OMA	HWSGFRI.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR009002. Split_barrel_FMN-bd_related. IPR012349. Split_barrel_FMN_bd. [Graphical view]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHER	PTHR10851. Pyridox_oxidase. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_BRUSI

Accession

Primary (citable) accession number: B0CKA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	February 9, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)