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Database: UniProt
Entry: D7TTE5_VITVI
LinkDB: D7TTE5_VITVI
Original site: D7TTE5_VITVI 
ID   D7TTE5_VITVI            Unreviewed;       352 AA.
AC   D7TTE5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   OrderedLocusNames=VIT_07s0129g01030 {ECO:0000313|EMBL:CBI33767.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI33767.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; FN596246; CBI33767.3; -; Genomic_DNA.
DR   RefSeq; XP_002283356.1; XM_002283320.3.
DR   AlphaFoldDB; D7TTE5; -.
DR   STRING; 29760.D7TTE5; -.
DR   PaxDb; 29760-VIT_07s0129g01030-t01; -.
DR   EnsemblPlants; Vitvi07g01673_t001; Vitvi07g01673_P001; Vitvi07g01673.
DR   GeneID; 100247381; -.
DR   Gramene; Vitvi07g01673_t001; Vitvi07g01673_P001; Vitvi07g01673.
DR   KEGG; vvi:100247381; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   InParanoid; D7TTE5; -.
DR   OMA; QMRNEIH; -.
DR   OrthoDB; 1550at2759; -.
DR   Proteomes; UP000009183; Chromosome 7.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IBA:GO_Central.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF36; CINNAMYL ALCOHOL DEHYDROGENASE 1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          16..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   352 AA;  38553 MW;  309E603D18A073D2 CRC64;
     MEGRRVVGWA ARDASGLLSP YSFTLRKTGP EDVVIKVLYC GMDHTDLHQM RNEVHSTNYP
     LVPGHEVVGE VVELGSEVKK YRVGDMVGVG CMVGSCGRCL SCNSNIEQYC NNRIFTYNGI
     YKDGRPTQGG FCSAMIVHQK FVVRIPEKLS PEQAAPLLCA GVTAYSPLRQ FMGSGKVLNA
     GILGLGGVGH LGVKIAKAMG HHVTVISSSD KKREEALQHL GADAFLVSSN AAEMEEAANN
     LDYILDTVPA LHPLQSYLSL LKVDGKLFLV GVSPKPLQFD ATDLILGKKN ITGSFIGSME
     ETQEILDFWA EKNLTSMIEI VKMDYVNKAF ERMERSDVRY RFVVDVAGSN LE
//
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