Reviewed, UniProtKB/Swiss-Prot Q8YFK3 (PDXH_BRUME)

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:	BMEI1517

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	208 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 – 208	208	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167693
Regions
	Nucleotide binding	70 – 71	2	FMN By similarity
	Nucleotide binding	134 – 135	2	FMN By similarity
	Region	185 – 187	3	Substrate binding By similarity
Sites
	Binding site	55	1	FMN By similarity
	Binding site	58	1	FMN; via amide nitrogen By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	77	1	FMN By similarity
	Binding site	117	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YFK3-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: CB1F50BC9612DE28	FASTA	208	23,866
	10 20 30 40 50 60 MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 70 80 90 100 110 120 DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEADAYYAS 130 140 150 160 170 180 RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 190 200 DRPFRLHDRV LFTRPTPEGD WNKDRLYP

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008917 Genomic DNA. Translation: AAL52698.1.
PIR	AG3441.
RefSeq	NP_540434.1.
3D structure databases
HSSP	HSSP built from PDB template 1DNL based on UniProtKB P28225.
ModBase	Search...
Genome annotation databases
GeneID	1197228.
GenomeReviews	Gene locus BMEI1517 in contig AE008917_GR.
KEGG	bme:BMEI1517.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8YFK3.
OMA	EPFALFA.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI1517-MON.
BRENDA	1.4.3.5. 277959.
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_BRUME

Accession

Primary (citable) accession number: Q8YFK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 53 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)