ADH1_HORVU
ID ADH1_HORVU Reviewed; 379 AA.
AC P05336; Q40011; Q40012; Q40013; Q40014;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN Name=ADH1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Himalaya;
RX PubMed=3405765; DOI=10.1093/nar/16.14.7182;
RA Good A., Pelcher L.E., Crosby W.L.;
RT "Nucleotide sequence of a complete barley alcohol dehydrogenase 1 cDNA.";
RL Nucleic Acids Res. 16:7182-7182(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-304, AND HOMODIMER.
RC STRAIN=cv. Proctor;
RX AGRICOLA=IND92000066; DOI=10.1007/BF00015667;
RA Trick M., Dennis E.S., Edwards K.J.R., Peacock W.J.;
RT "Molecular analysis of the alcohol dehydrogenase gene family of barley.";
RL Plant Mol. Biol. 11:147-160(1988).
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 Evidence={ECO:0000250|UniProtKB:P06525};
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 Evidence={ECO:0000250|UniProtKB:P06525};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X07774; CAA30600.1; -; mRNA.
DR EMBL; X12732; CAB51640.1; -; Genomic_DNA.
DR PIR; S01893; S01893.
DR AlphaFoldDB; P05336; -.
DR SMR; P05336; -.
DR ExpressionAtlas; P05336; baseline and differential.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160699"
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|UniProtKB:P06525"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 202..207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 295..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 372
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT CONFLICT 74
FT /note="I -> T (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> A (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..127
FT /note="IG -> NR (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> F (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="A -> S (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> T (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="V -> I (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="V -> F (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="D -> A (in Ref. 2; CAB51640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 40884 MW; 3A94ABDD2967FCB7 CRC64;
MATAGKVIKC KAAVAWEAGK PLTMEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQI
PMFPRIFGHE AGGIVESVGE GVTDVAPGDH VLPVFTGECK ECPHCKSAES NMCDLLRINT
DRGVMIGDGK SRFSIGGKPI YHFVGTSTFS EYTVMHVGCV AKINPEAPLD KVCVLSCGIS
TGLGASINVA KPPKGSTVAI FGLGAVGLAA AEGARIAGAS RIIGVDLNAV RFEEARKFGC
TEFVNPKDHT KPVQQVLADM TNGGVDRSVE CTGNVNAMIQ AFECVHDGWG VAVLVGVPHK
DAEFKTHPMN FLNERTLKGT FFGNFKPRTD LPNVVEMYMK KELEVEKFIT HSVPFSEINT
AFDLMAKGEG IRCIIRMDN
