ID Q4R1E7_ORYSJ Unreviewed; 379 AA.
AC Q4R1E7;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=Adh2 {ECO:0000313|EMBL:BAE00046.1};
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 {ECO:0000313|EMBL:BAE00046.1};
RN [1] {ECO:0000313|EMBL:BAE00046.1}
RP NUCLEOTIDE SEQUENCE.
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:0000256|ARBA:ARBA00001146};
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:0000256|ARBA:ARBA00000781};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AB208538; BAE00046.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4R1E7; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08301; alcohol_DH_plants; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF59; ALCOHOL DEHYDROGENASE 2; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 36..121
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 205..334
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 379 AA; 41177 MW; 2DF98CE0512087EA 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 LPNVVVLYMK KELELEKFIT HSVPFSEINT
AFDLMLKGES LRCVMRMDE
//