ID Q4R1F4_ORYRU Unreviewed; 379 AA.
AC Q4R1F4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:BAE00039.1};
GN Name=Adh2 {ECO:0000313|EMBL:BAE00039.1};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EMBL:BAE00039.1};
RN [1] {ECO:0000313|EMBL:BAE00039.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PT1A {ECO:0000313|EMBL:BAE00039.1};
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; AB208531; BAE00039.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4R1F4; -.
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:SF62; 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..337
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 379 AA; 41245 MW; 85C00910FD5DB414 CRC64;
MATAGKVIKC KAAVAWEAGK PLSIEEVEVA PPQAMEVRVK ILYTALCHTD VYFWEAKGQT
PVFPRILGHE AGGIVESVGE GVTEHAPGDH VLPLFTGECK 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
//
