Reviewed, UniProtKB/Swiss-Prot B0BU37 (PDXH_ACTPJ)

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:	APJL_2059

Organism

Actinobacillus pleuropneumoniae serotype 3 (strain JL03) [Complete proteome] [HAMAP]

Taxonomic identifier

434271 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

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_0000335777
Regions
	Nucleotide binding	74 – 75	2	FMN By similarity
	Nucleotide binding	138 – 139	2	FMN By similarity
	Region	7 – 10	4	Substrate binding By similarity
	Region	188 – 190	3	Substrate binding By similarity
Sites
	Binding site	59	1	FMN By similarity
	Binding site	62	1	FMN; via amide nitrogen By similarity
	Binding site	64	1	Substrate By similarity
	Binding site	81	1	FMN By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	129	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0BU37-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 54E1B3808FFEE653	FASTA	209	24,022
	10 20 30 40 50 60 MDLHNIREDY SKQELSQAHC HADPIQQFEQ WLEEAITAKA NEPTAMNVAT VLDGKPTSRI 70 80 90 100 110 120 VLLKEVNPNG FVFFTNYQSR KGQAIEQNPY AALTFFWAEL ERSVRIEGRI EKISAEESDR 130 140 150 160 170 180 YFASRPYTSR VGAWASNQSQ VLSGKSELVA KAALIAAKHP LHVPRPPHWG GYIVLPERIE 190 200 FWQGRPSRLH DRICYRLVEG KWHKERLSP

References

[1]

"Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of serotype 3 prevalent in China." Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T. , Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., Zhao G.-P., Chen H. PLoS ONE 3:E1450-E1450(2008) [PubMed: 18197260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000687 Genomic DNA. Translation: ABY70604.1.
RefSeq	YP_001653048.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5851698.
GenomeReviews	Gene locus APJL_2059 in contig CP000687_GR.
KEGG	apj:APJL_2059.
Organism-specific databases
CMR	Search...
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_ACTPJ

Accession

Primary (citable) accession number: B0BU37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	November 3, 2009
This is version 14 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)