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Database: UniProt
Entry: Q735A4_BACC1
LinkDB: Q735A4_BACC1
Original site: Q735A4_BACC1 
ID   Q735A4_BACC1            Unreviewed;       340 AA.
AC   Q735A4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:AAS42158.1};
DE            EC=1.1.1.4 {ECO:0000313|EMBL:AAS42158.1};
GN   Name=gutB {ECO:0000313|EMBL:AAS42158.1};
GN   OrderedLocusNames=BCE_3248 {ECO:0000313|EMBL:AAS42158.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS42158.1, ECO:0000313|Proteomes:UP000002527};
RN   [1] {ECO:0000313|EMBL:AAS42158.1, ECO:0000313|Proteomes:UP000002527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA   Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AE017194; AAS42158.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q735A4; -.
DR   KEGG; bca:BCE_3248; -.
DR   HOGENOM; CLU_026673_11_0_9; -.
DR   OMA; MVISFHT; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08233; butanediol_DH_like; 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; IPR002328; ADH_Zn_CS.
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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAS42158.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   340 AA;  36818 MW;  1FBF11F2C8A23A90 CRC64;
     MKAAVWYGER DIRIEERETK ELQPNDVKVK VAWAGICGSD LHAYLHPGSV PINMNTVMGH
     EFSGEIAEVG SHVTKFKKGD RVCIYPMMLK DPSNAEIERF ITLDAVGAQI DGGFAEYVIL
     PQKTIFKIPD HLPLELAAMV EPAAVSFQSI KDSNVREGDT VVVYGAGPIG LFAVLGAKAA
     GASNIIVIDL FDSRLDKATE MGATHVFNAK EVNPVEEIRK LFPGGADVAI EAAGVESTFN
     QAIQSTKVRG TMMVISFHTQ DIQFNVPASL IFSGAKLMGS VGYSNETYNE VIELFANGRL
     PAQSIITSKI DIDNIAEQGF EALIHDKSQA KILVKLSGAH
//
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