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Database: UniProt/TrEMBL
Entry: Q2FDQ9_STAA3
LinkDB: Q2FDQ9_STAA3
Original site: Q2FDQ9_STAA3 
ID   Q2FDQ9_STAA3            Unreviewed;       286 AA.
AC   Q2FDQ9;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   01-OCT-2014, entry version 58.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU003776};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU003776};
GN   Name=panE {ECO:0000313|EMBL:ABD20450.1};
GN   OrderedLocusNames=SAUSA300_2535 {ECO:0000313|EMBL:ABD20450.1};
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830 {ECO:0000313|Proteomes:UP000001939};
RN   [1] {ECO:0000313|EMBL:ABD20450.1, ECO:0000313|Proteomes:UP000001939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 {ECO:0000313|Proteomes:UP000001939};
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate
CC       into pantoic acid. {ECO:0000256|RuleBase:RU003776}.
CC   -!- CATALYTIC ACTIVITY: (R)-pantoate + NADP(+) = 2-dehydropantoate +
CC       NADPH. {ECO:0000256|RuleBase:RU003776}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|RuleBase:RU003776}.
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DR   EMBL; CP000255; ABD20450.1; -; Genomic_DNA.
DR   RefSeq; YP_495169.1; NC_007793.1.
DR   ProteinModelPortal; Q2FDQ9; -.
DR   STRING; 451515.SAUSA300_2535; -.
DR   EnsemblBacteria; ABD20450; ABD20450; SAUSA300_2535.
DR   GeneID; 3913849; -.
DR   KEGG; saa:SAUSA300_2535; -.
DR   PATRIC; 19594673; VBIStaAur129981_2712.
DR   HOGENOM; HOG000280297; -.
DR   KO; K00077; -.
DR   OMA; KSPHIES; -.
DR   OrthoDB; EOG6V7BJJ; -.
DR   BioCyc; SAUR451515:GH3C-2535-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   TIGRFAMs; TIGR00745; apbA_panE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001939};
KW   NADP {ECO:0000256|RuleBase:RU003776};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003776,
KW   ECO:0000313|EMBL:ABD20450.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU003776}.
SQ   SEQUENCE   286 AA;  32358 MW;  833DB4AD9F5AF254 CRC64;
     MLSVAIIGPG AVGTTIAYEL QQSLPHTTLI GRHAKTITYY TVPHAPAQDI VVKGYEDVTN
     TFDVIIIAVK THQLDAVIPH LTHLAHEDTL IILAQNGYGQ LEHISFKNVC QAVVYISGQK
     KGDVVTHFRD YQLRIQDNAL TRQFRDLVQD SQIDIVLEAN IQQAIWYKLL VNLGINSITA
     LGRQTVAIMH NPEIRTLCRQ LLLDGCRVAQ AEGLNFSEQT VDTIMTIYQG YPDEMGTSMY
     YDIAHQQPLE VEAIQGFIYR RAREHNLDTP YLDTIYSFLR AYQQNM
//
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