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UniProtKB/Swiss-Prot entry Q8A7E7

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

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Entry information
Entry name PDXH_BACTN
Primary accession number Q8A7E7
Secondary accession numbers None
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
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: BT_1577
From
Bacteroides thetaiotaomicron [TaxID: 818] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
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
AE015928; AAO76684.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_810490.1; -.
3D structure databases
HSSP P28225; 1JNW. [HSSP ENTRY / PDB]
ModBase Q8A7E7.
Enzyme and pathway databases
BioCyc BTHE226186:BT_1577-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).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from InterPro).
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 1076053; -.
GenomeReviews AE015928_GR; BT_1577.
KEGG bth:BT_1577; -.
NMPDR fig|226186.1.peg.1577; -.
Phylogenomic databases
HOGENOM Q8A7E7; -.
Genome annotation databases
CMR Q8A7E7; BT_1577.
Other
ProtoNet Q8A7E7.
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   213  213     Pyridoxine/pyridoxamine 5'-phosphate oxidase. PRO_0000167683
NP_BIND   76    77  2     FMN (By similarity). 
NP_BIND   140   141  2     FMN (By similarity). 
REGION   8    11  4     Substrate binding (By similarity). 
REGION   191   193  3     Substrate binding (By similarity). 
BINDING   61    61        FMN (By similarity). 
BINDING   64    64        FMN; via amide nitrogen (By similarity). 
BINDING   66    66        Substrate (By similarity). 
BINDING   83    83        FMN (By similarity). 
BINDING   123   123        Substrate (By similarity). 
BINDING   127   127        Substrate (By similarity). 
BINDING   131   131        Substrate (By similarity). 
Sequence information
Length: 213 AA [This is the length of the unprocessed precursor] Molecular weight: 24724 Da [This is the MW of the unprocessed precursor] CRC64: 23BDBEC862F22E28 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNIADIRQE YTKSGLRESE LPCDPLSLFS RWLQEAIDAN VEEPTAIIVG TVSPEGRPST 

        70         80         90        100        110        120 
RTVLLKGLHD GKFIFYTNYE SRKGRQLAQN PYISLSFVWH ELERQVHIEG TAAKVSPEES 

       130        140        150        160        170        180 
DEYFRKRPYK SRIGARISPQ SQPIASRMQL IRAFVKEAAR WLGKEVERPD NWGGYAVTPT 

       190        200        210 
RMEFWQGRPN RLHDRFLYTL KTDGKWEINR LSP
Q8A7E7 in FASTA format

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