Reviewed, UniProtKB/Swiss-Prot Q0VSU8 (PDXH_ALCBS)

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:	ABO_0302

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	209 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 – 209	209	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255849
Regions
	Nucleotide binding	73 – 74	2	FMN By similarity
	Nucleotide binding	137 – 138	2	FMN By similarity
	Region	5 – 8	4	Substrate binding By similarity
	Region	187 – 189	3	Substrate binding By similarity
Sites
	Binding site	58	1	FMN By similarity
	Binding site	61	1	FMN; via amide nitrogen By similarity
	Binding site	63	1	Substrate By similarity
	Binding site	80	1	FMN By similarity
	Binding site	120	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VSU8-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: A8DB30E2821CFB2C	FASTA	209	24,002
	10 20 30 40 50 60 MKDVREEYHA DGLIEATLHD DPLEQARRWV DEAIEAELPL PNAITLATVS ANGQPSSRVV 70 80 90 100 110 120 LLKGIENQGF TFFTHYDSRK GEEIAANPKV SFTMFWQPFD RQMIVIGEAQ KVDQEESDSY 130 140 150 160 170 180 FASRPYASQV SAAISPQSRP ASREWLEAEV SRLEQEFPSA PVPRPEQWGG YRIIPTEIQF 190 200 WHGRPSRLHD RFRYVKQGDG CWQRERLAP

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL15750.1.
RefSeq	YP_692022.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4212450.
GenomeReviews	Gene locus ABO_0302 in contig AM286690_GR.
KEGG	abo:ABO_0302.
NMPDR	fig|393595.12.peg.299.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VSU8.
OMA	Q0VSU8. FTFFTNY.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_0302-MON.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR011576. PNPOx_rel_FMN_bd_core. IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_ALCBS

Accession

Primary (citable) accession number: Q0VSU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	September 5, 2006
Last modified:	June 16, 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)