Reviewed, UniProtKB/Swiss-Prot A5EEN4 (PDXH_BRASB)

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:	BBta_2463

Organism

Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]

Taxonomic identifier

288000 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	216 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 + 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.
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.
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_1000069681
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)
	A5EEN4-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: E2367921CB0B40CC	FASTA	216	24,520
	10 20 30 40 50 60 MTDPTSIKHQ TTLTSGTSAD FTQASEPFAL FAEWFSEANK SELNDPNAMA LATVDDSGLP 70 80 90 100 110 120 DVRMVLMKGY DEDGFVFYSH KASQKGQELA GNPKAALLFH WKSLRRQVRI RGLVTPVTDE 130 140 150 160 170 180 EADAYFATRP KQAQLGAWAS KQSQPLESRF AFEQAIAKVA AQYIIGEVPR PPGWSGWRIT 190 200 210 PVRMEFWHDR PFRLHDRIEF RRDAAGQPWT 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
EMBLGenBankDDBJ	CP000494 Genomic DNA. Translation: ABQ34628.1.
RefSeq	YP_001238534.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5EEN4.
Genome annotation databases
GeneID	5152098.
GenomeReviews	Gene locus BBta_2463 in contig CP000494_GR.
KEGG	bbt:BBta_2463.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	EPFALFA.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. 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]
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_BRASB

Accession

Primary (citable) accession number: A5EEN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 23 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)