ID M1A1V9_SOLTU Unreviewed; 384 AA.
AC M1A1V9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EnsemblPlants:PGSC0003DMT400012845};
GN Name=102584791 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012845};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012845, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400012845}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012845};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; M1A1V9; -.
DR STRING; 4113.M1A1V9; -.
DR PaxDb; 4113-PGSC0003DMT400012845; -.
DR EnsemblPlants; PGSC0003DMT400012845; PGSC0003DMT400012845; PGSC0003DMG400005001.
DR Gramene; PGSC0003DMT400012845; PGSC0003DMT400012845; PGSC0003DMG400005001.
DR eggNOG; KOG0023; Eukaryota.
DR InParanoid; M1A1V9; -.
DR OMA; TCQHEDI; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1A1V9; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR029752; D-isomer_DH_CS1.
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:SF17; CINNAMYL ALCOHOL DEHYDROGENASE 1-RELATED; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000011115};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 20..377
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 384 AA; 41876 MW; 725B436F263EA3CD CRC64;
MTSASANENC LGWAARDPSG VLSPYEFNRR AVSSDDVLLD IAFCGMCFAD VLWTRNILGT
SKYPLVPGHE ITGIVREVGT DVKHFKVGDL VGVGTYVNSC RECEYCCDEL EVHCSEGAIN
TFDGIDVDGT VTKGGYSSYI VVNERYCFRI PENYPLASAA PLLCAGITVY TPMIRHNMNQ
PGKSLGVVGL GGLGHLAVKF GKAFGLKVTV FSTSISKREE AINVLGADKF VISSDEQQMM
ALSKSFDFII NTASGDIPFD TYLSLLKTAG VLVLVGFPSE VKFIPGNLIL GIIFYICSQF
EARLCSICRT LAKNESFLAG MKSIVGSVTG GTKQTQEMLD FCASHKIYPE IEIVPIQYVN
EALERLMKKD VKYRFVIDVA NSIK
//
