Reviewed, UniProtKB/Swiss-Prot A4YQ21 (PDXH_BRASO)

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:	BRADO2146

Organism

Bradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]

Taxonomic identifier

114615 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	216 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 – 216	216	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_1000069682
Regions
	Nucleotide binding	78 – 79	2	FMN By similarity
	Nucleotide binding	142 – 143	2	FMN By similarity
	Region	193 – 195	3	Substrate binding By similarity
Sites
	Binding site	63	1	FMN By similarity
	Binding site	66	1	FMN; via amide nitrogen By similarity
	Binding site	68	1	Substrate By similarity
	Binding site	85	1	FMN By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	129	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4YQ21-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 4108D54342535456	FASTA	216	24,373
	10 20 30 40 50 60 MTDPTSIKHQ TTLTSGTSAD FTQAGEPFAL FAEWFAEASK SEPNDPNAMA LSTVDADGLP 70 80 90 100 110 120 DVRMVLMKGY DADGFVFYSH KASQKGQELA ANPKAALLFH WKSLRRQVRI RGLVTPVTDA 130 140 150 160 170 180 EADAYFATRP KQAQLGAWAS KQSQPLESRF AFEQAIAKVA TQYIIGEVPR PPGWSGWRIT 190 200 210 PVRMEFWHDR PFRLHDRIEF RREAAGQPWT KVRMYP

References

[1]

"Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia." Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z. , Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., Sadowsky M. Science 316:1307-1312(2007) [PubMed: 17540897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU234118 Genomic DNA. Translation: CAL75997.1.
RefSeq	YP_001204234.1.
3D structure databases
SMR	A4YQ21. Positions 25-216.
ModBase	Search...
Protein-protein interaction databases
STRING	A4YQ21.
Genome annotation databases
GeneID	5120050.
GenomeReviews	Gene locus BRADO2146 in contig CU234118_GR.
KEGG	bra:BRADO2146.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
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_BRASO

Accession

Primary (citable) accession number: A4YQ21

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 29, 2007
Last modified:	February 9, 2010
This is version 27 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)