Reviewed, UniProtKB/Swiss-Prot Q57EU9 (PDXH_BRUAB)

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:	BruAb1_0439

Organism

Brucella abortus [Complete proteome] [HAMAP]

Taxonomic identifier

235 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2).
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit structure	Homodimer By similarity.
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: InterPro
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 – 208	208	Pyridoxine/pyridoxamine 5'-phosphate oxidase		PRO_0000255855
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)
	Q57EU9-1 [UniParc]. Last modified May 10, 2005. 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]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017223 Genomic DNA. Translation: AAX73835.1.
RefSeq	YP_221196.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3339404.
GenomeReviews	Gene locus BruAb1_0439 in contig AE017223_GR.
KEGG	bmb:BruAb1_0439.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q57EU9.
Enzyme and pathway databases
BioCyc	BABO262698:BRUAB1_0439-MON.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR011576. PNPOx_rel_FMN_bd_core. IPR000659. Pyridox_oxidase. 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	PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
ProDom	PD006312. Pyridox_oxidase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_BRUAB

Accession

Primary (citable) accession number: Q57EU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 10, 2005
Last modified:	November 25, 2008
This is version 28 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)