ADH_SACS2
ID ADH_SACS2 Reviewed; 347 AA.
AC P39462; O74076;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=NAD-dependent alcohol dehydrogenase;
DE EC=1.1.1.1;
GN Name=adh; OrderedLocusNames=SSO2536;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], METHYLATION AT LYS-11 AND LYS-213, AND
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=1463738; DOI=10.1021/bi00164a031;
RA Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., de Rosa M.,
RA Rossi M.;
RT "Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus
RT solfataricus: gene and protein sequence determination and relationship to
RT other alcohol dehydrogenases.";
RL Biochemistry 31:12514-12523(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RA Aravalli R.N.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=12051852; DOI=10.1016/s0022-2836(02)00088-8;
RA Esposito L., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L.,
RA Zagari A.;
RT "Crystal structure of the alcohol dehydrogenase from the hyperthermophilic
RT archaeon Sulfolobus solfataricus at 1.85 A resolution.";
RL J. Mol. Biol. 318:463-477(2002).
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.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; S51211; AAB24546.1; -; Genomic_DNA.
DR EMBL; AJ010590; CAA09258.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42665.1; -; Genomic_DNA.
DR PIR; A44245; A44245.
DR RefSeq; WP_009990984.1; NC_002754.1.
DR PDB; 1JVB; X-ray; 1.85 A; A=1-347.
DR PDB; 1NTO; X-ray; 1.94 A; A/B/C/D/E/H=1-347.
DR PDB; 1NVG; X-ray; 2.50 A; A=1-347.
DR PDB; 1R37; X-ray; 2.30 A; A/B=1-347.
DR PDB; 3I4C; X-ray; 2.00 A; A/B/C/D/E/H=1-347.
DR PDBsum; 1JVB; -.
DR PDBsum; 1NTO; -.
DR PDBsum; 1NVG; -.
DR PDBsum; 1R37; -.
DR PDBsum; 3I4C; -.
DR AlphaFoldDB; P39462; -.
DR SMR; P39462; -.
DR STRING; 273057.SSO2536; -.
DR iPTMnet; P39462; -.
DR EnsemblBacteria; AAK42665; AAK42665; SSO2536.
DR GeneID; 44128259; -.
DR KEGG; sso:SSO2536; -.
DR PATRIC; fig|273057.12.peg.2612; -.
DR eggNOG; arCOG01455; Archaea.
DR HOGENOM; CLU_026673_11_2_2; -.
DR InParanoid; P39462; -.
DR OMA; QYAHNVF; -.
DR PhylomeDB; P39462; -.
DR BRENDA; 1.1.1.1; 6163.
DR SABIO-RK; P39462; -.
DR EvolutionaryTrace; P39462; -.
DR Proteomes; UP000001974; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Methylation; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..347
FT /note="NAD-dependent alcohol dehydrogenase"
FT /id="PRO_0000160753"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT MOD_RES 11
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:1463738"
FT MOD_RES 213
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:1463738"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1NTO"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1JVB"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1NVG"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1NTO"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1JVB"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1JVB"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1JVB"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1JVB"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1NTO"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1JVB"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:1JVB"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:1JVB"
SQ SEQUENCE 347 AA; 37569 MW; 755848A249D4F4A2 CRC64;
MRAVRLVEIG KPLSLQEIGV PKPKGPQVLI KVEAAGVCHS DVHMRQGRFG NLRIVEDLGV
KLPVTLGHEI AGKIEEVGDE VVGYSKGDLV AVNPWQGEGN CYYCRIGEEH LCDSPRWLGI
NFDGAYAEYV IVPHYKYMYK LRRLNAVEAA PLTCSGITTY RAVRKASLDP TKTLLVVGAG
GGLGTMAVQI AKAVSGATII GVDVREEAVE AAKRAGADYV INASMQDPLA EIRRITESKG
VDAVIDLNNS EKTLSVYPKA LAKQGKYVMV GLFGADLHYH APLITLSEIQ FVGSLVGNQS
DFLGIMRLAE AGKVKPMITK TMKLEEANEA IDNLENFKAI GRQVLIP
