ADH1_ORYSI
ID ADH1_ORYSI Reviewed; 379 AA.
AC Q75ZX4; P20306;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN Name=ADH1; ORFNames=OsI_034290;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND HOMODIMER.
RC STRAIN=cv. IR26; TISSUE=Seedling;
RX PubMed=2562760; DOI=10.1007/bf00027335;
RA Xie Y., Wu R.;
RT "Rice alcohol dehydrogenase genes: anaerobic induction, organ specific
RT expression and characterization of cDNA clones.";
RL Plant Mol. Biol. 13:53-68(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15480535; DOI=10.1007/s00122-004-1752-3;
RA Yoshida K., Miyashita N.T., Ishii T.;
RT "Nucleotide polymorphism in the Adh1 locus region of the wild rice Oryza
RT rufipogon.";
RL Theor. Appl. Genet. 109:1406-1416(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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|PubMed:2562760}.
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; X16296; CAA34363.1; -; mRNA.
DR EMBL; AB118962; BAC87776.1; -; Genomic_DNA.
DR EMBL; CM000136; EAY80331.1; -; Genomic_DNA.
DR PIR; JQ0474; JQ0474.
DR AlphaFoldDB; Q75ZX4; -.
DR SMR; Q75ZX4; -.
DR STRING; 39946.Q75ZX4; -.
DR PRIDE; Q75ZX4; -.
DR EnsemblPlants; BGIOSGA034312-TA; BGIOSGA034312-PA; BGIOSGA034312.
DR Gramene; BGIOSGA034312-TA; BGIOSGA034312-PA; BGIOSGA034312.
DR HOGENOM; CLU_026673_14_0_1; -.
DR OMA; VCEMSGH; -.
DR Proteomes; UP000007015; Chromosome 11.
DR ExpressionAtlas; Q75ZX4; 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; Reference proteome; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000291461"
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 19
FT /note="A -> G (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="V -> S (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..34
FT /note="PPQA -> KE (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="V -> I (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Missing (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> R (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="V -> I (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="G -> A (in Ref. 1; CAA34363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 40984 MW; 1281E87F3DB30545 CRC64;
MATAGKVIKC KAAVAWEAAK PLVIEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQT
PVFPRIFGHE AGGIVESVGE GVTDLAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT
DRGVMIGDGK SRFSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPAAPLD KVCVLSCGIS
TGLGATINVA KPPKGSTVAI FGLGAVGLAA AEGARIAGAS RIIGIDLNAN RFEEARKFGC
TEFVNPKDHD KPVQQVLAEM TNGGVDRSVE CTGNINAMIQ AFECVHDGWG VAVLVGVPHK
DAEFKTHPMN FLNERTLKGT FFGNYKPRTD LPNVVELYMK KELEVEKFIT HSVPFSEINT
AFDLMHKGEG IRCIIRMEN
