Q1MKJ4 (PDXH_RHIL3) 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:	RL1014

Organism

Rhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]

Taxonomic identifier

216596 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium › Rhizobium leguminosarum › Rhizobium leguminosarum bv. viciae

Protein attributes

Sequence length	206 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. HAMAP-Rule MF_01629
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. HAMAP-Rule 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	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 – 206	206	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629		PRO_0000255880
Regions
	Nucleotide binding	68 – 69	2	FMN By similarity
	Nucleotide binding	132 – 133	2	FMN By similarity
	Region	183 – 185	3	Substrate binding By similarity
Sites
	Binding site	53	1	FMN By similarity
	Binding site	56	1	FMN; via amide nitrogen By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	75	1	FMN By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	123	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1MKJ4 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: F58C43BBECABE559	FASTA	206	23,766
	10 20 30 40 50 60 MSANELTSGD FTESGEPFKL FAEWLKEAEV SEPNDPNAVA LATVDEDGLP NVRMVLLKGF 70 80 90 100 110 120 DDDGFVFYTN FESQKGREIL GQKKAAMCFH WKSLRRQVRL RGPVEIVTDA EADAYFKTRA 130 140 150 160 170 180 RGSRIGAWAS RQSRPLESRF ALEKAVAEYT ARYAIGEIPR PAHWSGFRIR PTSIEFWKDQ 190 200 KFRLHDRVEF RRPSPEGEWD KVRMYP

References

[1]

"The genome of Rhizobium leguminosarum has recognizable core and accessory components." Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I., Chillingworth T., Clarke K. , Cronin A., Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J. Genome Biol. 7:R34.1-R34.20(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 3841.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM236080 Genomic DNA. Translation: CAK06511.1.
RefSeq	YP_766625.1. NC_008380.1.
3D structure databases
ProteinModelPortal	Q1MKJ4.
ModBase	Search...
Protein-protein interaction databases
STRING	216596.RL1014.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAK06511; CAK06511; RL1014.
GeneID	4401646.
KEGG	rle:RL1014.
PATRIC	23138471. VBIRhiLeg32091_2180.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HOG000242755.
KO	K00275.
OMA	HWSGFRI.
ProtClustDB	PRK05679.
Enzyme and pathway databases
BioCyc	RLEG216596:GKE5-1043-MONOMER.
UniPathway	UPA00190; UER00304. UPA00190; UER00305.
Family and domain databases
Gene3D	2.30.110.10. 1 hit.
HAMAP	MF_01629. PdxH.
InterPro	IPR000659. Pyridox_Oxase. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_RHIL3

Accession

Primary (citable) accession number: Q1MKJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 30, 2006
Last modified:	May 29, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program