Reviewed, UniProtKB/Swiss-Prot Q487G8 (PDXH_COLP3)

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:	CPS_1053

Organism

Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]

Taxonomic identifier

167879 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Colwelliaceae › Colwellia

Protein attributes

Sequence length	217 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 – 217	217	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167699
Regions
	Nucleotide binding	81 – 82	2	FMN By similarity
	Nucleotide binding	145 – 146	2	FMN By similarity
	Region	196 – 198	3	Substrate binding By similarity
Sites
	Binding site	66	1	FMN By similarity
	Binding site	69	1	FMN; via amide nitrogen By similarity
	Binding site	71	1	Substrate By similarity
	Binding site	88	1	FMN By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	136	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q487G8-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 34BCDD1E98C24F38	FASTA	217	25,231
	10 20 30 40 50 60 MTLFEKLRCL FTFGQGVALP LPELSSNTTP DQIFEQWFAD ANKSGILLPE AMSVSSCNSD 70 80 90 100 110 120 GQPSSRMVLL KDYDKEGFVF FTNYESRKSH ELAENNKVAL LFHWNVLQRQ IRIEGTVEKV 130 140 150 160 170 180 SIQESADYFH SRDRGSQVGA WASKQSQKLK YDDELKERMS HYQDKFSEGE VPHPEFWGGW 190 200 210 RVKPHAIEFW QGRANRLHDR LCFEKDGETW LNHKLNP

References

[1]

"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses." Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000083 Genomic DNA. Translation: AAZ28207.1.
RefSeq	YP_267797.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q487G8.
Genome annotation databases
GeneID	3522466.
GenomeReviews	Gene locus CPS_1053 in contig CP000083_GR.
KEGG	cps:CPS_1053.
NMPDR	fig|167879.3.peg.1015.
TIGR	CPS_1053.
Phylogenomic databases
HOGENOM	Q487G8.
OMA	EPFALFA.
Enzyme and pathway databases
BioCyc	CPSY167879:CPS_1053-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_COLP3

Accession

Primary (citable) accession number: Q487G8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	September 13, 2005
Last modified:	November 3, 2009
This is version 31 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)