Reviewed, UniProtKB/Swiss-Prot Q5LFJ5 (PDXH_BACFN)

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:	BF1385

Organism

Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]

Taxonomic identifier

272559 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	235 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 – 235	235	Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629		PRO_0000167682
Regions
	Nucleotide binding	98 – 99	2	FMN By similarity
	Nucleotide binding	162 – 163	2	FMN By similarity
	Region	30 – 33	4	Substrate binding By similarity
	Region	213 – 215	3	Substrate binding By similarity
Sites
	Binding site	83	1	FMN By similarity
	Binding site	86	1	FMN; via amide nitrogen By similarity
	Binding site	88	1	Substrate By similarity
	Binding site	105	1	FMN By similarity
	Binding site	145	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LFJ5-1 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: 6C6C85CC8E160374	FASTA	235	26,673
	10 20 30 40 50 60 MSTDHVSTHP DSPLHGNGIG SEAINLAAIR QEYTKGGLKE GDLPDNPLSL FNRWLHEAID 70 80 90 100 110 120 AQVDEPTAML VGTVSPEGQP STRTVLLKDL HDGKFIFYTN YESRKGTHLA KNPYISLSFV 130 140 150 160 170 180 WHALERQVHI EGIASKVPAG ESDTYFRQRP YKSRIGARIS PQSRPLKSRM QLIRNFVAEA 190 200 210 220 230 ARWVGREVER PAHWGGYAVT PHRIEFWQGR ANRLHDRFLY SLQPDGSWQK ERLAP

References

[1]

"Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A. , Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J. Science 307:1463-1465(2005) [PubMed: 15746427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR626927 Genomic DNA. Translation: CAH07098.1.
RefSeq	YP_211043.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3289209.
GenomeReviews	Gene locus BF1385 in contig CR626927_GR.
KEGG	bfs:BF1385.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LFJ5.
OMA	Q5LFJ5. FTFFTNY.
Enzyme and pathway databases
BioCyc	BFRA272559:BF1385-MON.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR011576. PNPOx_rel_FMN_bd_core. IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. 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_BACFN

Accession

Primary (citable) accession number: Q5LFJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	June 21, 2005
Last modified:	June 16, 2009
This is version 30 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)