Q8G2A9 (PDXH_BRUSU) Reviewed, UniProtKB/Swiss-Prot

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:	BR0416, BS1330_I0417

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	208 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	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 208	208	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167694
Regions
	Nucleotide binding	70 – 71	2	FMN By similarity
	Nucleotide binding	134 – 135	2	FMN By similarity
	Region	185 – 187	3	Substrate binding By similarity
Sites
	Binding site	55	1	FMN By similarity
	Binding site	58	1	FMN; via amide nitrogen By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	77	1	FMN By similarity
	Binding site	117	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G2A9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: CB1F50BC9612DE28	FASTA	208	23,866
	10 20 30 40 50 60 MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 70 80 90 100 110 120 DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEADAYYAS 130 140 150 160 170 180 RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 190 200 DRPFRLHDRV LFTRPTPEGD WNKDRLYP

References

[1]	"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.
[2]	"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29361.1. CP002997 Genomic DNA. Translation: AEM17774.1.
PIR	AG3441.
RefSeq	NP_697446.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8G2A9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1166077.
GenomeReviews	Gene locus BR0416 in contig AE014291_GR.
KEGG	bms:BR0416.
PATRIC	17789128. VBIBruSui107850_0432.
TIGR	BR0416.
Phylogenomic databases
HOGENOM	HBG327559.
OMA	HWSGFRI.
PhylomeDB	Q8G2A9.
ProtClustDB	PRK05679.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0416-MONOMER.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. 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]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KO	K00275.
PANTHER	PTHR10851. Pyridox_oxidase. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
PIRSF	PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAM	SSF50475. FMN_binding. 1 hit.
TIGRFAMs	TIGR00558. PdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_BRUSU

Accession

Primary (citable) accession number: Q8G2A9
Secondary accession number(s): G0K6N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program