ADH1_MAIZE
ID ADH1_MAIZE Reviewed; 379 AA.
AC P00333;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN Name=ADH1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6328449; DOI=10.1093/nar/12.9.3983;
RA Dennis E.S., Gerlach W.L., Pryor A.J., Bennetzen J.L., Inglis A.,
RA Llewellyn D.J., Sachs M.M., Ferl R.J., Peacock W.J.;
RT "Molecular analysis of the alcohol dehydrogenase (Adh1) gene of maize.";
RL Nucleic Acids Res. 12:3983-4000(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2987807; DOI=10.1093/nar/13.3.727;
RA Dennis E.S., Sachs M.M., Gerlach W.L., Finnegan E.J., Peacock W.J.;
RT "Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize.";
RL Nucleic Acids Res. 13:727-743(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6378620; DOI=10.1002/j.1460-2075.1984.tb01967.x;
RA Braenden C.-I., Eklund H., Cambillau C., Pryor A.J.;
RT "Correlation of exons with structural domains in alcohol dehydrogenase.";
RL EMBO J. 3:1307-1310(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE (ALLELE ADH1-F), AND POLYMORPHISM.
RC STRAIN=cv. Berkeley Fast;
RX PubMed=17246333; DOI=10.1093/genetics/113.2.449;
RA Sachs M.M., Dennis E.S., Gerlach W.L., Peacock W.J.;
RT "Two alleles of maize alcohol dehydrogenase 1 have 3'-structural and
RT poly(A) addition polymorphisms.";
RL Genetics 113:449-467(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE (ALLELE ADH1-CM).
RX PubMed=2577507; DOI=10.1007/bf00016138;
RA Osterman J.C., Dennis E.S.;
RT "Molecular analysis of the ADH1-Cm allele of maize.";
RL Plant Mol. Biol. 13:203-212(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 212-379.
RX PubMed=16593188; DOI=10.1073/pnas.79.9.2981;
RA Gerlach W.L., Pryor A.J., Dennis E.S., Ferl R.J., Sachs M.M., Peacock W.J.;
RT "cDNA cloning and induction of the alcohol dehydrogenase gene (Adh1) of
RT maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2981-2985(1982).
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:0000250|UniProtKB:P06525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}.
CC -!- POLYMORPHISM: The sequence shown is that of allele ADH1-F.
CC {ECO:0000269|PubMed:17246333}.
CC -!- MISCELLANEOUS: In maize there are two isozymes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X04049; CAA27681.1; -; Genomic_DNA.
DR EMBL; X00580; CAA25239.1; -; mRNA.
DR EMBL; X04050; CAA27682.1; -; Genomic_DNA.
DR EMBL; M32984; AAA33434.1; -; Genomic_DNA.
DR PIR; S04571; S04571.
DR RefSeq; NP_001105409.1; NM_001111939.1.
DR RefSeq; XP_008648693.1; XM_008650471.1.
DR AlphaFoldDB; P00333; -.
DR SMR; P00333; -.
DR STRING; 4577.GRMZM2G442658_P06; -.
DR PaxDb; P00333; -.
DR PRIDE; P00333; -.
DR GeneID; 542363; -.
DR KEGG; zma:542363; -.
DR MaizeGDB; 13844; -.
DR eggNOG; KOG0022; Eukaryota.
DR OrthoDB; 664798at2759; -.
DR BioCyc; MetaCyc:MON-15098; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P00333; baseline and differential.
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:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic 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 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; Reference proteome; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160703"
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 VARIANT 52
FT /note="Y -> D (in allele ADH1-Cm)"
FT VARIANT 127
FT /note="A -> G (in allele ADH1-S)"
FT VARIANT 179
FT /note="Y -> I (in allele ADH1-Cm and allele ADH1-S)"
FT VARIANT 363
FT /note="D -> N (in allele ADH1-S)"
SQ SEQUENCE 379 AA; 40981 MW; 5E0618F7E1A4B973 CRC64;
MATAGKVIKC KAAVAWEAGK PLSIEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQT
PVFPRIFGHE AGGIIESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT
DRGVMIADGK SRFSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPQAPLD KVCVLSCGYS
TGLGASINVA KPPKGSTVAV FGLGAVGLAA AEGARIAGAS RIIGVDLNPS RFEEARKFGC
TEFVNPKDHN KPVQEVLAEM TNGGVDRSVE CTGNINAMIQ AFECVHDGWG VAVLVGVPHK
DAEFKTHPMN FLNERTLKGT FFGNYKPRTD LPNVVELYMK KELEVEKFIT HSVPFAEINK
AFDLMAKGEG IRCIIRMEN
