ADH1_RABIT
ID ADH1_RABIT Reviewed; 375 AA.
AC Q03505;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase subunit alpha;
GN Name=ADH1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8477702; DOI=10.1111/j.1432-1033.1993.tb17731.x;
RA Hoeoeg J.-O., Vagelopoulos N., Yip P.-K., Keung W.M., Joernvall H.;
RT "Isozyme developments in mammalian class-I alcohol dehydrogenase. cDNA
RT cloning, functional correlations, and lack of evidence for genetic isozymes
RT in rabbit.";
RL Eur. J. Biochem. 213:31-38(1993).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X69799; CAA49458.1; -; mRNA.
DR PIR; S30353; S29343.
DR RefSeq; NP_001095174.1; NM_001101704.1.
DR AlphaFoldDB; Q03505; -.
DR SMR; Q03505; -.
DR STRING; 9986.ENSOCUP00000024666; -.
DR Ensembl; ENSOCUT00000030164; ENSOCUP00000024666; ENSOCUG00000033073.
DR GeneID; 100009283; -.
DR KEGG; ocu:100009283; -.
DR CTD; 124; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000163645; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q03505; -.
DR OMA; RVKMIAT; -.
DR OrthoDB; 664798at2759; -.
DR TreeFam; TF300429; -.
DR Proteomes; UP000001811; Chromosome 15.
DR Bgee; ENSOCUG00000033073; Expressed in liver and 16 other tissues.
DR ExpressionAtlas; Q03505; baseline.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; 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_0000160668"
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; 39588 MW; 47F03877C54E5B69 CRC64;
MSTAGKVIKC KAAVLWQLNK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHAVTGSIAV
PLPVILGHEA AGIVESIGEG VTTVKPGDKV IPLFTPQCGK CRICKHPESN FCLINDLGKP
KGMLLDGTSR FTCKGKPIHH FIGTSTFSQY TVVDEIAVAK IDAAAPLEKV CLIGCGFSTG
YGSAVKVAKV TPGSTCAVFG LGGVGLSVIM GCKAAGASRI IAVDINKDKF PKAKEVGATE
CINPQDYKKP IQEVIQEISD GGVDFSFEVI GRLDTVVAAL LSCHGACGTS VIVGVPPDSQ
SLTVNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FSLDPLITNV LPFEKINEGF
DLLRSGKSIR TILTF
