ADH1_CHICK
ID ADH1_CHICK Reviewed; 376 AA.
AC P23991;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alcohol dehydrogenase 1;
DE Short=ADH-1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I;
GN Name=ADH1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2269284; DOI=10.1111/j.1432-1033.1990.tb15657.x;
RA Estonius M., Karlsson C., Fox E.A., Hoeoeg J.-O., Holmquist B.,
RA Vallee B.L., Davidson W.S., Joernvall H.;
RT "Avian alcohol dehydrogenase: the chicken liver enzyme. Primary structure,
RT cDNA-cloning, and relationships to other alcohol dehydrogenases.";
RL Eur. J. Biochem. 194:593-602(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-17 AND 360-376, AND ACETYLATION AT SER-2.
RX PubMed=2387402; DOI=10.1016/0014-5793(90)81152-e;
RA Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E.,
RA Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.;
RT "Fast atom bombardment mass spectrometry and chemical analysis in
RT determinations of acyl-blocked protein structures.";
RL FEBS Lett. 269:194-196(1990).
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: Homodimer.
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; X54612; CAA38433.1; ALT_SEQ; mRNA.
DR PIR; S13851; DECHA1.
DR RefSeq; NP_001292112.1; NM_001305183.1.
DR AlphaFoldDB; P23991; -.
DR SMR; P23991; -.
DR STRING; 9031.ENSGALP00000019979; -.
DR iPTMnet; P23991; -.
DR PaxDb; P23991; -.
DR GeneID; 771920; -.
DR KEGG; gga:771920; -.
DR CTD; 126; -.
DR VEuPathDB; HostDB:geneid_771920; -.
DR eggNOG; KOG0022; Eukaryota.
DR InParanoid; P23991; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P23991; -.
DR PRO; PR:P23991; -.
DR Proteomes; UP000000539; 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 Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2387402"
FT CHAIN 2..376
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160672"
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 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 201..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 294..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2387402"
SQ SEQUENCE 376 AA; 39808 MW; CCD03989E53273DE CRC64;
MSTVGKVIKC KAAVLWEANK PFSLEEVEVA PPKAHEVRIK IVATGICRSD DHVVTGALAM
PFPIILGHEA AGVIESVGEK VTSLKPGDAV IPLFVPQCGE CRSCLSTKGN LCIKNDLSSS
PTGLMADGTT RFTCKGKAIH HFVGTSTFTE YTVVHETAAA KIDSAAPLEK VCLIGCGFST
GYGAVLQTAK VEAGSTCAVF GLGGVGLSVV MGCKAAGASR IIAVDINKDK FAKAKELGAT
ECINPKDFKK PIHEVLTEMT GQGVDYSFEV IGRIETMTAA LASCHNNYGV SVIVGVPPAA
QKISFDPMLI FSGRTWKGSV FGGWKSKDAV PKLVADYMKK KFVLDPLITH TLPFTKINEG
FDLLRTGKSI RSVLVL
