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ADH1_ORYSJ
ID   ADH1_ORYSJ              Reviewed;         379 AA.
AC   Q2R8Z5; P20306; Q2R8Z6; Q2R8Z7; Q9LLP9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN   Name=ADH1; Synonyms=DUPR11.3;
GN   OrderedLocusNames=Os11g0210300, LOC_Os11g10480; ORFNames=OsJ_032001;
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10715324; DOI=10.2307/3870943;
RA   Tarchini R., Biddle P., Wineland R., Tingey S., Rafalski A.;
RT   "The complete sequence of 340 kb of DNA around the rice Adh1-Adh2 region
RT   reveals interrupted colinearity with maize chromosome 4.";
RL   Plant Cell 12:381-391(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA   Yoon U.H., Kim Y.H.;
RT   "Molecular cloning of alcohol dehydrogenase 1 genes in rice seeds.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q2R8Z5-1, P20306-1;
CC         Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AF172282; AAF34414.1; -; Genomic_DNA.
DR   EMBL; EF122490; ABL74577.1; -; mRNA.
DR   EMBL; DP000010; ABA92029.2; -; Genomic_DNA.
DR   EMBL; DP000010; ABA92030.1; -; Genomic_DNA.
DR   EMBL; DP000010; ABA92031.2; -; Genomic_DNA.
DR   EMBL; AP008217; BAF27847.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT13173.1; -; Genomic_DNA.
DR   EMBL; CM000148; EAZ17792.1; -; Genomic_DNA.
DR   EMBL; AK069330; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015616853.1; XM_015761367.1. [Q2R8Z5-1]
DR   AlphaFoldDB; Q2R8Z5; -.
DR   SMR; Q2R8Z5; -.
DR   BioGRID; 819090; 1.
DR   STRING; 4530.OS11T0210300-01; -.
DR   PaxDb; Q2R8Z5; -.
DR   PRIDE; Q2R8Z5; -.
DR   EnsemblPlants; Os11t0210300-01; Os11t0210300-01; Os11g0210300. [Q2R8Z5-1]
DR   GeneID; 4350053; -.
DR   Gramene; Os11t0210300-01; Os11t0210300-01; Os11g0210300. [Q2R8Z5-1]
DR   KEGG; osa:4350053; -.
DR   eggNOG; KOG0022; Eukaryota.
DR   HOGENOM; CLU_026673_14_0_1; -.
DR   InParanoid; Q2R8Z5; -.
DR   OMA; VCEMSGH; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000007752; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   ExpressionAtlas; Q2R8Z5; baseline and differential.
DR   Genevisible; Q2R8Z5; OS.
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   Alternative splicing; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..379
FT                   /note="Alcohol dehydrogenase 1"
FT                   /id="PRO_0000160707"
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"
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
 
 
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