NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).

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.
CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O₂ = pyridoxal 5'-phosphate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1 .
PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AP006841; BAD48204.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_098738.1; -.

3D structure databases

ModBase

Q64WC2.

Enzyme and pathway databases

BioCyc

BFRA295405:BF1453-MON; -.

Ontologies

GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from HAMAP).
GO:0004733;	Molecular function: pyridoxamine-phosphate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01629; -; 1.
PBIL [Tree]

InterPro

IPR011576; PNPOx_rel_FMN_bd_core.
IPR000659; Pyridox_oxidase.
IPR012349; Split_barrel_FMN_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.110.10; PNPOx_FMN_bd; 1.

PANTHER

PTHR10851; Pyridox_oxidase; 1.

Pfam

PF01243; Pyridox_oxidase; 1.
Pfam graphical view of domain structure.

ProDom

PD006312; Pyridox_oxidase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00558; pdxH; 1.

PROSITE

PS01064; PYRIDOX_OXIDASE; 1.

Genome annotation databases

GeneID

3082379; -.

GenomeReviews

AP006841_GR; BF1453.

KEGG

bfr:BF1453; -.

Phylogenomic databases

HOGENOM

Q64WC2; -.

Genome annotation databases

CMR

Q64WC2; BF1453.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 235`	`235`	`Pyridoxine/pyridoxamine 5'-phosphate oxidase.`	`PRO_0000167681`
`NP_BIND`	`98 99`	`2`	`FMN (By similarity).`
`NP_BIND`	`162 163`	`2`	`FMN (By similarity).`
`REGION`	`30 33`	`4`	`Substrate binding (By similarity).`
`REGION`	`213 215`	`3`	`Substrate binding (By similarity).`
`BINDING`	`83 83`		`FMN (By similarity).`
`BINDING`	`86 86`		`FMN; via amide nitrogen (By similarity).`
`BINDING`	`88 88`		`Substrate (By similarity).`
`BINDING`	`105 105`		`FMN (By similarity).`
`BINDING`	`145 145`		`Substrate (By similarity).`
`BINDING`	`149 149`		`Substrate (By similarity).`
`BINDING`	`153 153`		`Substrate (By similarity).`

Sequence information

Length: 235 AA [This is the length of the unprocessed precursor]

Molecular weight: 26673 Da [This is the MW of the unprocessed precursor]

CRC64: 6C6C85CC8E160374 [This is a checksum on the sequence]

        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

Q64WC2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools