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
//