Q6NAI9 (PDXH_RHOPA) 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:	RPA1196

Organism

Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]

Taxonomic identifier

258594 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas › Rhodopseudomonas palustris

Protein attributes

Sequence length	212 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-Rule MF_01629
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule 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-Rule 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	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: GOC 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 – 212	212	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000167749
Regions
	Nucleotide binding	74 – 75	2	FMN By similarity
	Nucleotide binding	138 – 139	2	FMN By similarity
	Region	189 – 191	3	Substrate binding By similarity
Sites
	Binding site	59	1	FMN By similarity
	Binding site	62	1	FMN; via amide nitrogen By similarity
	Binding site	64	1	Substrate By similarity
	Binding site	81	1	FMN By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6NAI9 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A53B9DB2CD1F1140	FASTA	212	24,203
	10 20 30 40 50 60 MSDPTIRPQS ELTPGDFTAA ENPFALFAEW LAEANKSEPN DPNAMALATV DPDGLPDVRM 70 80 90 100 110 120 VLMKGYDEHG FVFYSHIASQ KGRELAANPK AALLFHWKSL RRQIRIRGTV TPVTDTEADA 130 140 150 160 170 180 YFATRPKQAQ IGAWASKQSQ PLESRFAFEQ AIAKVTARHL IGDVPRPPGW SGWRITPSRI 190 200 210 EFWHDRPFRL HDRIEFRRDT PDHPWTKTRL YP

References

[1]

"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris." Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S. Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX572596 Genomic DNA. Translation: CAE26639.1.
RefSeq	NP_946547.1. NC_005296.1.
3D structure databases
ProteinModelPortal	Q6NAI9.
ModBase	Search...
Protein-protein interaction databases
STRING	258594.RPA1196.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE26639; CAE26639; RPA1196.
GeneID	2691450.
KEGG	rpa:RPA1196.
PATRIC	23286617. VBIRhoPal84835_1249.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	HWSGFRI.
ProtClustDB	PRK05679.
Enzyme and pathway databases
UniPathway	UPA00190; UER00304. UPA00190; UER00305.
Family and domain databases
Gene3D	2.30.110.10. 1 hit.
HAMAP	MF_01629. PdxH.
InterPro	IPR000659. Pyridox_Oxase. IPR019740. Pyridox_Oxase_CS. IPR011576. Pyridox_Oxase_FMN-bd. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR012349. Split_barrel_FMN-bd. [Graphical view]
PANTHER	PTHR10851. PTHR10851. 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_RHOPA

Accession

Primary (citable) accession number: Q6NAI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program