ID B7H525_BACC4 Unreviewed; 345 AA.
AC B7H525;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00016352};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN OrderedLocusNames=BCB4264_A2248 {ECO:0000313|EMBL:ACK61719.1};
OS Bacillus cereus (strain B4264).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK61719.1, ECO:0000313|Proteomes:UP000007096};
RN [1] {ECO:0000313|EMBL:ACK61719.1, ECO:0000313|Proteomes:UP000007096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4264 {ECO:0000313|EMBL:ACK61719.1,
RC ECO:0000313|Proteomes:UP000007096};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus B4264.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001176; ACK61719.1; -; Genomic_DNA.
DR RefSeq; WP_000649119.1; NZ_VEHB01000001.1.
DR AlphaFoldDB; B7H525; -.
DR KEGG; bcb:BCB4264_A2248; -.
DR HOGENOM; CLU_026673_20_1_9; -.
DR OMA; GLKMTDT; -.
DR Proteomes; UP000007096; 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; 36804 MW; 2E5D70554E3B478C CRC64;
MKAVVVNKNS KANIEVIEKE LRPLHSGEAL VDVEYCGVCH TDLHVANHDF GNTDGRILGH
EGVGIVTKIA DDVTSLKIGD RVSIAWMFQS CGRCEYCVTG RETFCREVKN AGYSVDGGMA
EQCIVTADYA VKVPEGLDPA QASSITCAGV TTYKAIKVSD IKPSQPIVIY GCGGLGNLAI
QYAKNVFGAK VIAVDINDDK LALAKEVGAD MTINPISQGP ADKIVQEEFG GAYAAVVTAV
SKVAFNSAVD AVRACGKVVA VGLPVETMDL NIPRLVLDGI EVVGSLVGTR KDLEEAFMFG
AEGKVVPVVQ TCSLDKVQNV FEEMEQGRIQ GRMVIDFKKH NCDCK
//