ADH2_ORYSI
ID ADH2_ORYSI Reviewed; 379 AA.
AC Q4R1E8; P18332;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alcohol dehydrogenase 2;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
GN Name=ADH2;
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=2332167; DOI=10.1016/0378-1119(90)90300-g;
RA Xie Y., Wu R.;
RT "Molecular analysis of an alcohol dehydrogenase-encoding genomic clone
RT (adh2) from rice.";
RL Gene 87:185-191(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. IR36;
RX PubMed=16133310; DOI=10.1007/s00122-005-0054-8;
RA Yoshida K., Miyashita N.T.;
RT "Nucleotide polymorphism in the Adh2 region of the wild rice Oryza
RT rufipogon.";
RL Theor. Appl. Genet. 111:1215-1228(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; X16297; CAA34364.1; -; mRNA.
DR EMBL; M36469; AAA33889.1; -; Genomic_DNA.
DR EMBL; AB208537; BAE00045.1; -; Genomic_DNA.
DR PIR; JH0111; DERZA2.
DR AlphaFoldDB; Q4R1E8; -.
DR SMR; Q4R1E8; -.
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 2"
FT /id="PRO_0000291462"
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 4
FT /note="Missing (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..21
FT /note="KP -> EA (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="A -> R (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="P -> A (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="TG -> SR (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 254..255
FT /note="HE -> Q (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..299
FT /note="Missing (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="F -> LI (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="Missing (in Ref. 1; CAA34364 and 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..374
FT /note="ESLRCV -> RVSAAS (in Ref. 2; AAA33889)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..378
FT /note="RMD -> SMY (in Ref. 1; CAA34364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41207 MW; 2DF98CF6B6BEE8EA CRC64;
MATAGKVIKC KAAVAWEAGK PLSIEEVEVA PPQAMEVRVK ILYTALCHTD VYFWEAKGQT
PVFPRILGHE AGGIVESVGE GVTELAPGDH VLPVFTGECK ECDHCKSEES NMCDLLRINV
DRGVMIGDGK SRFTIKGKPI FHFVGTSTFS EYTVIHVGCL AKINPEAPLD KVCILSCGFS
TGFGATVNVA KPKKGQTVAI FGLGAVGLAA MEGARLSGAS RIIGVDLNPA KFEQAKKFGC
TDFVNPKDHS KPVHEVLIEM TNGGLDRAVE CTGNINAMIS CFECVHDGWG VAVLVGVPTK
DDVFKTHPMN FLNEKTLKGT FFGNYKPRTD LPNVVELYMK KELELEKFIT HSVPFSEINT
AFDLMLKGES LRCVMRMDE
