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Database: UniProt
Entry: C2NH94_BACCE
LinkDB: C2NH94_BACCE
Original site: C2NH94_BACCE 
ID   C2NH94_BACCE            Unreviewed;       345 AA.
AC   C2NH94;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00016352};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=bcere0004_20570 {ECO:0000313|EMBL:EEK56611.1};
OS   Bacillus cereus BGSC 6E1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK56611.1};
RN   [1] {ECO:0000313|EMBL:EEK56611.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK56611.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEK56611.1}.
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DR   EMBL; ACLU01000051; EEK56611.1; -; Genomic_DNA.
DR   RefSeq; WP_000649134.1; NZ_CM000716.1.
DR   AlphaFoldDB; C2NH94; -.
DR   HOGENOM; CLU_026673_20_1_9; -.
DR   Proteomes; UP000000284; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          9..335
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   345 AA;  36740 MW;  F5203769BF8C9E72 CRC64;
     MKAVVVNKNS KANIEVVEKE LRPLHSGEAL VDVEYCGVCH TDLHVANHDF GNTDGRILGH
     EGVGIVMKIA DDVTSLKVGD RVSIAWMFQS CGRCEYCVTG RETFCREVKN AGYSVDGGMA
     EQCIVTADYA VKVPEGLDPA QASSITCAGV TTYKAIKVSD IKPGQPIVIY GCGGLGNLAI
     QYAKNVFGAK VIAVDINDDK LALAKEVGAD MTINPISQGP ADKIIQEEFG GAYAAVVTAV
     SKVAFNSAVD AVRACGKVVA VGLPVETMDL NIPRLVLDGI EVVGSLVGTR KDLEEAFMFG
     AEGKVVPVVQ TCSLDTVQNV FEEMEQGRIQ GRMVIDFKQN NCDCK
//
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