ID   T0CIN3_ALIAG            Unreviewed;       342 AA.
AC   T0CIN3; A0A9E6ZEX3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Alcohol dehydrogenase catalytic domain-containing protein {ECO:0000313|EMBL:UNO48612.1};
GN   ORFNames=K1I37_18425 {ECO:0000313|EMBL:UNO48612.1};
OS   Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS   / NCIMB 13137 / GD3B).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO48612.1, ECO:0000313|Proteomes:UP000829401};
RN   [1] {ECO:0000313|Proteomes:UP000829401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX   PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA   Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT   "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT   DSM 3922T, a taint-producing strain.";
RL   G3 (Bethesda) 12:0-0(2022).
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; CP080467; UNO48612.1; -; Genomic_DNA.
DR   RefSeq; WP_021295188.1; NZ_AURB01000047.1.
DR   STRING; 1356854.N007_19920; -.
DR   KEGG; aaco:K1I37_18425; -.
DR   Proteomes; UP000829401; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43401; 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   Reference proteome {ECO:0000313|Proteomes:UP000829401};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
SQ   SEQUENCE   342 AA;  35817 MW;  A2EFF934DF1FD9ED CRC64;
     MKAVTYTPHH GFALVEAETP QLGPDEVLLQ VEACGVCGSD RQVVAGESVP TGTAFPLVMG
     HEIAGRIAAL GETVTDWHVG DSVIVHPFVA CGTCAPCVHG QPNLCVRQVC IGYQRPGGFA
     EQVAVPARQL VRRPAELAPA AAALLVDAFA TPYHAMRAAG VESGQTVLVI GTGGLGLSAL
     MLAMGFQVGR LGAVTRRQEG IAIAEAHGAQ MVVVTDQDER TIARQLRRWS GASGIDVVID
     TVATADTIAL AAESVRPGGT IAIVGMSEDT ALYPVAKTVR RGLTFVASYG SVREDVEQLV
     SWVAEGRLDP ARLVAGALPL HEAQRAFAPD RRAGRWVIVP SE
//