ID E0WBF4_9POAL Unreviewed; 230 AA.
AC E0WBF4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
DE Flags: Fragment;
GN Name=adh3 {ECO:0000313|EMBL:ACV87884.1};
OS Elymus caninus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Elymus.
OX NCBI_TaxID=129741 {ECO:0000313|EMBL:ACV87884.1};
RN [1] {ECO:0000313|EMBL:ACV87884.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PI564910 {ECO:0000313|EMBL:ACV87884.1};
RA Liu Q., Lu B.-R., Yang J.;
RT "Polyploid speciation of the StY genome Elymus (Poaceae: Triticeae) species
RT insights from low-copy nuclear genes.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ597880; ACV87884.1; -; Genomic_DNA.
DR AlphaFoldDB; E0WBF4; -.
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:SF37; ALCOHOL DEHYDROGENASE ADH3D; 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 1..81
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 158..227
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV87884.1"
FT NON_TER 230
FT /evidence="ECO:0000313|EMBL:ACV87884.1"
SQ SEQUENCE 230 AA; 24399 MW; 42E45BBBBAC1D53E CRC64;
HTDVYFWEAK GQTPVFPRIL GHEAGGIVES VGEGVTELVP GDHVLPVFTG ECKECAHCRS
EESNLCDLLR INVDRGVMIG DGQSRFTIDG KPIFHFVGMS TFSEYTVIHV GCLAKIDPEA
PLDKVCLLSC GISTGLGATL NVAKPKKGMT VAIFGLGAVG LAAMEGARMS GASRIIGVDL
NPAKHEQAKK FGCTDFVNPK DHTKAVQEVI VEMTDGGVDR AVECTGNINA
//