ID I1GSA5_BRADI Unreviewed; 408 AA.
AC I1GSA5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=100822825 {ECO:0000313|EnsemblPlants:KQK15213};
GN ORFNames=BRADI_1g21300v3 {ECO:0000313|EMBL:KQK15213.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK15213.1};
RN [1] {ECO:0000313|EMBL:KQK15213.1, ECO:0000313|EnsemblPlants:KQK15213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK15213.1,
RC ECO:0000313|EnsemblPlants:KQK15213};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK15213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK15213.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK15213}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK15213};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; CM000880; KQK15213.1; -; Genomic_DNA.
DR EMBL; CM000880; KQK15215.1; -; Genomic_DNA.
DR RefSeq; XP_003562679.1; XM_003562631.3.
DR AlphaFoldDB; I1GSA5; -.
DR STRING; 15368.I1GSA5; -.
DR EnsemblPlants; KQK15213; KQK15213; BRADI_1g21300v3.
DR EnsemblPlants; KQK15215; KQK15215; BRADI_1g21300v3.
DR GeneID; 100822825; -.
DR Gramene; KQK15213; KQK15213; BRADI_1g21300v3.
DR Gramene; KQK15215; KQK15215; BRADI_1g21300v3.
DR KEGG; bdi:100822825; -.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; I1GSA5; -.
DR OMA; LSFDSCG; -.
DR OrthoDB; 451143at2759; -.
DR Proteomes; UP000008810; Chromosome 1.
DR ExpressionAtlas; I1GSA5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
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:SF10; ALCOHOL DEHYDROGENASE-LIKE 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 Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 37..132
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 210..335
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 408 AA; 43018 MW; BBEAC6569FE65093 CRC64;
MEQSTAKKPI RCKAAVSKVA GQPLEMVEVD VAPPRAHEVR IRILCTSLCH TDVTFWRMKD
FPAMYPSILG HEAAGVVESV GEEVVEVSPG DTVVPVFSGQ CGDCPDCLSD RSNICSGLPF
RFLPGMPRDG TTRFAFAGTG EPIHNFINVS SFVEYTVVDV AHLVRLGPGL MIPPDKACLL
SCGVSTGVGA AWKVAAVEPG STVAVFGLGA VGLAVAQGSK MRGAKRIIGV DLNPDKCEIG
KRMGITEFIN PNDTGGKAVS EVIKEMTGGG ADYCFECIGS TAVTAEAFSS SRMGWGKTIV
LGVASGAAAP ISIPSYEILR GRSVVGSLFG GLKPKTDVPL LAQKYLDEEL ELDEFVTHEM
GFDDINGAFD LLTQGKCLRC IIWMDGASAK ENGNGGVNVK PKQNGTLV
//
