Reviewed, UniProtKB/Swiss-Prot Q7VU72 (PDXH_BORPE)

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:	BP3251

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	210 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 – 210	210	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167691
Regions
	Nucleotide binding	75 – 76	2	FMN By similarity
	Nucleotide binding	139 – 140	2	FMN By similarity
	Region	7 – 10	4	Substrate binding By similarity
	Region	188 – 190	3	Substrate binding By similarity
Sites
	Binding site	60	1	FMN By similarity
	Binding site	63	1	FMN; via amide nitrogen By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	82	1	FMN By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	130	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VU72-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: C4A38C5D60706E6C	FASTA	210	24,281
	10 20 30 40 50 60 MSVSDLRQSY EKGVLVEEQA AASPFQQFAR WFDEAVAARV PEPNAMTLAT VNAEGQPSAR 70 80 90 100 110 120 IVLIKGYDDA GFVFFTNYES RKGLDLDANP RASLLFFWQP LERQVRIEGV IEKVSAAESD 130 140 150 160 170 180 EYFHSRPLGS RLGAWASRQS QPITRDELEA REREFRDRYG EHPPRPPHWG GYRLKPNRFE 190 200 210 FWQGRPSRLH DRLRYEPDGK QGWTIDRLSP

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640420 Genomic DNA. Translation: CAE43518.1.
RefSeq	NP_881799.1.
3D structure databases
SMR	Q7VU72. Positions 13-210.
ModBase	Search...
Genome annotation databases
GeneID	2667670.
KEGG	bpe:BP3251.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG327559.
OMA	FTFFTNY.
PhylomeDB	Q7VU72.
Enzyme and pathway databases
BioCyc	BPER257313:BP3251-MONOMER.
BRENDA	1.4.3.5. 21511.
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_BORPE

Accession

Primary (citable) accession number: Q7VU72

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 44 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)