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Database: UniProt
Entry: Q669E9_YERPS
LinkDB: Q669E9_YERPS
Original site: Q669E9_YERPS 
ID   Q669E9_YERPS            Unreviewed;       408 AA.
AC   Q669E9;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   SubName: Full=Putative sorbitol dehydrogenase {ECO:0000313|EMBL:CAH21776.1};
DE            EC=1.1.1.14 {ECO:0000313|EMBL:CAH21776.1};
GN   Name=gutB {ECO:0000313|EMBL:CAH21776.1};
GN   OrderedLocusNames=YPTB2538 {ECO:0000313|EMBL:CAH21776.1};
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH21776.1, ECO:0000313|Proteomes:UP000001011};
RN   [1] {ECO:0000313|EMBL:CAH21776.1, ECO:0000313|Proteomes:UP000001011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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DR   EMBL; BX936398; CAH21776.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q669E9; -.
DR   KEGG; yps:YPTB2538; -.
DR   OMA; IRYTTGC; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd08256; Zn_ADH2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CAH21776.1}.
FT   DOMAIN          68..406
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   408 AA;  45042 MW;  6698C868621D8AFA CRC64;
     MILNVYVVIS IFIMNAMSLL SVEVSNFTFV DLFKNDNVNI VSIHRVLLLL EELMSQLPEK
     MSAVVCHGPQ DYRLEHVPTP VPKAKELVIK VKGCGICAGD CKCKNGAKMF WGETPWVKPP
     VVPGHEFYGH IVALGEGTES KYKIGERVIA EQIVPCWDCR YCNSGSYWMC ETHNIYGFQK
     DVAEGGMAEY MRFSENAIVH KIPESLSHED AVLIEPMACA IHTVARGDIQ LDDVVVLAGA
     GPLGLCMVQV ARLKTPKKLI VIDTIEERLA LAKAFGADVV INPLKEDADK IVKSLTGGYG
     CDVYIEATGA PIGVTQGLQM IRKLGRFVEF SVFGQETTVD WSIIGDRKEL DIRGAHLAPY
     SYEIATDLFE RGLVTSKGIV THSYSLDDWE KAFELADSTN SIKVILVP
//
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