ID Q9M6Y8_9ORYZ Unreviewed; 198 AA.
AC Q9M6Y8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=Alcohol dehydrogenase 1 {ECO:0000256|ARBA:ARBA00041139};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
DE Flags: Fragment;
GN Name=Adh1 {ECO:0000313|EMBL:AAF37409.1};
OS Oryza ridleyi.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=83308 {ECO:0000313|EMBL:AAF37409.1};
RN [1] {ECO:0000313|EMBL:AAF37409.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10588717; DOI=10.1073/pnas.96.25.14400;
RA Ge S., Sang T., Lu B.R., Hong D.Y.;
RT "Phylogeny of rice genomes with emphasis on origins of allotetraploid
RT species.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14400-14405(1999).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AF148590; AAF37409.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9M6Y8; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF40; ALCOHOL DEHYDROGENASE 1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
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 6..77
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 148..194
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF37409.1"
FT NON_TER 198
FT /evidence="ECO:0000313|EMBL:AAF37409.1"
SQ SEQUENCE 198 AA; 20768 MW; C0F47A971E74BFE0 CRC64;
GQTPVFPRIF GHEAGGIVES VGDGVTDLAP GDHVLPVFTG ECKECPHCKS AESNMCDLLR
INTDRGVMIG DGKSRFSING KPIYHFVGTS TFSEYTVMHV GCVAKINPEA PLDKVCVLSC
GISTGLGATI NVAKPPKGST VAIFGLGAVG LAAAEGARIA GASRIIGVDL NPNRFEEARK
FGCTEFVNPK DHDKPVQQ
//