ADH1_GEOAT
ID ADH1_GEOAT Reviewed; 375 AA.
AC Q9Z2M2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase A subunit;
GN Name=ADH1;
OS Geomys attwateri (Attwater's pocket gopher) (Geomys bursarius attwateri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Geomyidae;
OC Geomys.
OX NCBI_TaxID=72447;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9615452; DOI=10.1093/oxfordjournals.molbev.a025974;
RA Bradley R.D., Adkins R.M., Honeycutt R.L., McDonald J.H.;
RT "Nucleotide polymorphism at the alcohol dehydrogenase locus of pocket
RT gophers, genus Geomys.";
RL Mol. Biol. Evol. 15:709-717(1998).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR EMBL; AF044730; AAC98959.1; -; mRNA.
DR AlphaFoldDB; Q9Z2M2; -.
DR SMR; Q9Z2M2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06757"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000254949"
FT BINDING 47
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 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P06757"
FT MOD_RES 234
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00329"
FT MOD_RES 340
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00329"
SQ SEQUENCE 375 AA; 39841 MW; 6A01A35C159C1122 CRC64;
MSTAGKVIKC RAAVLWEKNK PFSIEEVEVA PPKAYEVRIK IVATGICRSD DHVVNGSIIT
PLPAILGHEA GGIVESIGEG VTTVKPGDKV IPLFVPQCGK CRACKHPESN LCTHGDLGRA
QGTLMDGTSR FTCKGKPIHH FLGVTTFSEY TVVSEISVTK IDAASPLEKV CLIGCGFSTG
YGSAVKVGKV ARGSICACVW SGRVGLSAII GCKAAGAARI IAVDINKDKF AKAKELGATE
CVNPQDYDKP IYEVLQEMTD GGVDFSFEVI GRLDTKVSAL MCCQESHGVS VIVGVPPNAQ
SLTIDPKVLL SGRSWKGAVF GGYKGKDDVP KLVADFMAKK FPLEPLITNV FPLAKINEGF
DLLRAGKSIR TVLTF
