ADH1S_HORSE
ID ADH1S_HORSE Reviewed; 374 AA.
AC P00328;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Alcohol dehydrogenase S chain;
DE EC=1.1.1.1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1712777; DOI=10.1016/s0021-9258(18)98838-1;
RA Park D.H., Plapp B.V.;
RT "Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and
RT steroids. cDNA cloning, expression, and comparison of active sites.";
RL J. Biol. Chem. 266:13296-13302(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-374, AND ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX PubMed=5466062; DOI=10.1111/j.1432-1033.1970.tb01050.x;
RA Joernvall H.;
RT "Horse liver alcohol dehydrogenase. On the primary structures of the
RT isoenzymes.";
RL Eur. J. Biochem. 16:41-49(1970).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=178875; DOI=10.1016/0022-2836(76)90072-3;
RA Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I.,
RA Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A.;
RT "Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A
RT resolution.";
RL J. Mol. Biol. 102:27-59(1976).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=6098306; DOI=10.1021/bi00320a014;
RA Eklund H., Samama J.-P., Jones T.A.;
RT "Crystallographic investigations of nicotinamide adenine dinucleotide
RT binding to horse liver alcohol dehydrogenase.";
RL Biochemistry 23:5982-5996(1984).
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;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Dimer of identical or non-identical chains of two types (E and
CC S) coded by 2 separate genes at different loci.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR EMBL; M64865; AAA30932.1; -; mRNA.
DR PIR; B39872; DEHOAS.
DR RefSeq; NP_001075414.1; NM_001081945.1.
DR PDB; 1EE2; X-ray; 1.54 A; A/B=2-374.
DR PDBsum; 1EE2; -.
DR AlphaFoldDB; P00328; -.
DR SMR; P00328; -.
DR STRING; 9796.ENSECAP00000032068; -.
DR BindingDB; P00328; -.
DR ChEMBL; CHEMBL2111372; -.
DR DrugCentral; P00328; -.
DR iPTMnet; P00328; -.
DR PeptideAtlas; P00328; -.
DR GeneID; 100034175; -.
DR KEGG; ecb:100034175; -.
DR OrthoDB; 664798at2759; -.
DR SABIO-RK; P00328; -.
DR EvolutionaryTrace; P00328; -.
DR PRO; PR:P00328; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006069; P:ethanol oxidation; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
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; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5466062"
FT CHAIN 2..374
FT /note="Alcohol dehydrogenase S chain"
FT /id="PRO_0000160657"
FT BINDING 47
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 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 199..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 292..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:5466062"
FT CONFLICT 44
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> SL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="V -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1EE2"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1EE2"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:1EE2"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1EE2"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:1EE2"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:1EE2"
SQ SEQUENCE 374 AA; 39623 MW; 2B15710A038DA013 CRC64;
MSTAGKVIKC KAAVLWEQKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD DHVVSGTLVA
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFIPQCGK CSVCKHPEGN LCLKNLSMPR
GTMQDGTSRF TCRGKPIHHF LGTSTFSQYT VVDEISVAKI DAASPLEKVC LVGCGFSTGY
GSAVKVAKVT QGSTCAVFGL GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC
VNPQDYKKPI QEVLTEMSNG GVDFSFEVIG RLDTMVAALS CCQEAYGVSV IVGVPPDSQN
LSMNPMLLLS GRTWKGAIFG GFKSKDSVPK LVADFMAKKF ALDPLITHVL PFEKINEGFD
LLRSGKSIRT ILTF
