ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5LFJ5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PDXH_BACFN
Primary accession number Q5LFJ5
Secondary accession numbers None
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on June 21, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 27)
Name and origin of the protein
Protein name Pyridoxine/pyridoxamine 5'-phosphate oxidase
Synonyms EC 1.4.3.5
PNP/PMP oxidase
PNPOx
Pyridoxal 5'-phosphate synthase
Gene name
Name: pdxH
OrderedLocusNames: BF1385
From
Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [TaxID: 272559] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1107008; PubMed=15746427 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Extensive DNA inversions in the B. fragilis genome control variable gene expression.";
Science 307:1463-1465(2005).
Comments
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
CR626927; CAH07098.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_211043.1; -.
3D structure databases
ModBase Q5LFJ5.
Enzyme and pathway databases
BioCyc BFRA272559:BF1385-MON; -.
Ontologies
GO
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.
BLOCKS Q5LFJ5.
ProtoNet Q5LFJ5.
Genome annotation databases
GeneID 3289209; -.
GenomeReviews CR626927_GR; BF1385.
KEGG bfs:BF1385; -.
Phylogenomic databases
HOGENOM Q5LFJ5; -.
Genome annotation databases
CMR Q5LFJ5; BF1385.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   235  235     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167682
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
Q5LFJ5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!