ID   ADH_SULSR               Reviewed;         347 AA.
AC   P50381;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=NAD-dependent alcohol dehydrogenase;
DE            EC=1.1.1.1;
GN   Name=adh;
OS   Sulfolobus sp. (strain RC3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus; unclassified Sulfolobus.
OX   NCBI_TaxID=165757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8550434; DOI=10.1128/jb.178.1.301-305.1996;
RA   Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S.;
RT   "Cloning and overexpression in Escherichia coli of the genes encoding NAD-
RT   dependent alcohol dehydrogenase from two Sulfolobus species.";
RL   J. Bacteriol. 178:301-305(1996).
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   -!- 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; Z47543; CAA87591.1; -; Genomic_DNA.
DR   PIR; S51120; S51120.
DR   AlphaFoldDB; P50381; -.
DR   SMR; P50381; -.
DR   BRENDA; 1.1.1.1; 6164.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Methylation; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..347
FT                   /note="NAD-dependent alcohol dehydrogenase"
FT                   /id="PRO_0000160754"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         213
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  37584 MW;  55D3C003792DE60D CRC64;
     MRAVRLVEIG KPLVLKDIDI PKPKGAQVLI KVEAAGVCHS DVHMRQGRFG NLRIVEDLGV
     KLPVTLGHEI AGKIEEMGDE VVGYSKGDLV AVNPWQGEGN CYYCRIGEEH LCDSPRWLGI
     NFDGAYAEYV LNPHYKYMYK LRRLNAVEAS PLTCSGITTY RAVRKASLDP TKTLVVVGAG
     GGLGTMAVQI AKAVGGATII GVDVREEAVE TAKRAGADYV INASVQDPLA EIRRITEGKG
     VDAVIDLNNS EKTLSVYPKA LAKQGKYIMV GLFGADLHFH APLITLSEIQ FVGSLVGNQS
     DFLGIMRLAE AGKVKPMITK TMKLEEANEA IDNLENFKAV GRQVLIP