Reviewed, UniProtKB/Swiss-Prot Q39DH2 (PDXH_BURS3)

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:	Bcep18194_A5900

Organism

Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]

Taxonomic identifier

269483 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	214 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 MF_01629
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. HAMAP MF_01629
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. HAMAP 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	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 – 214	214	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000255859
Regions
	Nucleotide binding	76 – 77	2	FMN By similarity
	Nucleotide binding	140 – 141	2	FMN By similarity
	Region	8 – 11	4	Substrate binding By similarity
	Region	190 – 192	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)
	Q39DH2-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 301B29752B17D938	FASTA	214	24,312
	10 20 30 40 50 60 MTTLADLRIN YSRASLDEAD VAHDPFAQFD RWFKEALAAK LPEPNTMTLA TVGDDGRPSA 70 80 90 100 110 120 RIVLIKGVDE RGFVFFTNYE SRKGRDLAAH PQAALLFYWI ELERQVRIEG RIEKTSAEES 130 140 150 160 170 180 DRYFASRPLG SRIGAWASEQ SAVIDSRATL EAQEQAVSER YGDNPPRPPH WGGYRLVPDS 190 200 210 IEFWQGRPSR LHDRLLYTRD ADTSPSWSIS RLSP

References

[1]

"Complete sequence of chromosome 1 of Burkholderia sp. 383." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000151 Genomic DNA. Translation: ABB09494.1.
RefSeq	YP_370138.1.
3D structure databases
HSSP	HSSP built from PDB template 2A2J based on UniProtKB P65682.
SMR	Q39DH2. Positions 15-214.
ModBase	Search...
Protein-protein interaction databases
STRING	Q39DH2.
Genome annotation databases
GeneID	3751131.
GenomeReviews	Gene locus Bcep18194_A5900 in contig CP000151_GR.
KEGG	bur:Bcep18194_A5900.
NMPDR	fig|269483.3.peg.7378.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0259.
HOGENOM	HBG327559.
OMA	FTFFTNY.
Enzyme and pathway databases
BioCyc	BSP36773:BCEP18194_A5900-MONOMER.
Family and domain databases
HAMAP	MF_01629. PdxH. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR009002. Split_barrel_FMN-bd_related. 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]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH_BURS3

Accession

Primary (citable) accession number: Q39DH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 22, 2005
Last modified:	February 9, 2010
This is version 35 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)