Reviewed, UniProtKB/Swiss-Prot Q6F718 (PDXH_ACIAD)

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:	ACIAD3501

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	218 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 – 218	218	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167677
Regions
	Nucleotide binding	80 – 81	2	FMN By similarity
	Nucleotide binding	145 – 146	2	FMN By similarity
	Region	12 – 15	4	Substrate binding By similarity
	Region	197 – 199	3	Substrate binding By similarity
Sites
	Binding site	65	1	FMN By similarity
	Binding site	68	1	FMN; via amide nitrogen By similarity
	Binding site	70	1	Substrate By similarity
	Binding site	87	1	FMN By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6F718-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: E3356830AFD6AC0E	FASTA	218	25,705
	10 20 30 40 50 60 MKDVIKDLSE LRMSYEKGEL HEAQVDTHPH EQFLQWFNHA LQSNLHEPYA MSLATCNRQG 70 80 90 100 110 120 RPHVRTVLLR GATAQGYDFY TNYDSQKGID LAENPYAELL FYWPSLERQV RIGGIVNKIS 130 140 150 160 170 180 EHESTDYYHK RPRDSQIAAH ISTPQSGIIA NREELQQRFN RLYEQVGQQT VLSKPEFWGG 190 200 210 YRLQADYYEF WQGRPNRLHD RLSYQNTDGT WVVQRLMP

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR543861 Genomic DNA. Translation: CAG70147.1.
RefSeq	YP_047969.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6F718.
Genome annotation databases
GeneID	2878299.
GenomeReviews	Gene locus ACIAD3501 in contig CR543861_GR.
KEGG	aci:ACIAD3501.
NMPDR	fig|62977.3.peg.3162.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6F718.
OMA	FTFFTNY.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD3501-MON.
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_ACIAD

Accession

Primary (citable) accession number: Q6F718

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 43 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)