Reviewed, UniProtKB/Swiss-Prot A5EXX0 (PDXH_DICNV)

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:	DNO_1023

Organism

Dichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]

Taxonomic identifier

246195 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Cardiobacteriales › Cardiobacteriaceae › Dichelobacter

Protein attributes

Sequence length	212 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 – 212	212	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000335783
Regions
	Nucleotide binding	76 – 77	2	FMN By similarity
	Nucleotide binding	140 – 141	2	FMN By similarity
	Region	191 – 193	3	Substrate binding By similarity
Sites
	Binding site	61	1	FMN By similarity
	Binding site	64	1	FMN; via amide nitrogen By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	83	1	FMN By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5EXX0-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: C8C9F5F3B890DFE5	FASTA	212	24,570
	10 20 30 40 50 60 MDIGSIRHDF TEHPPLLEQD LAADPIEQFA AWFQYAVDSG ISEPNGFVLA TVAADGQPSQ 70 80 90 100 110 120 RSVLLKLFDE EGFVFYTNYS SQKAEEIEKN AQVSMSFPWY ALQRQIHVYG RAEKIPREQS 130 140 150 160 170 180 LAYFLTRPQG SQIGAWASPQ SKIIESRDFL MLKWQNMKAK FHEGKIPLPD FWGGYRVRPH 190 200 210 KIEFWQGQPS RLHDRFLYEK TENGWTVSRR AP

References

[1]

"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus." Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T. Nat. Biotechnol. 25:569-575(2007) [PubMed: 17468768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000513 Genomic DNA. Translation: ABQ13205.1.
RefSeq	YP_001209911.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5EXX0.
Genome annotation databases
GeneID	5122950.
GenomeReviews	Gene locus DNO_1023 in contig CP000513_GR.
KEGG	dno:DNO_1023.
TIGR	DNO_1023.
Phylogenomic databases
OMA	FTFFTNY.
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_DICNV

Accession

Primary (citable) accession number: A5EXX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 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)