ID I0ZAQ3_COCSC Unreviewed; 428 AA.
AC I0ZAQ3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=GroES-like protein {ECO:0000313|EMBL:EIE27722.1};
GN ORFNames=COCSUDRAFT_26878 {ECO:0000313|EMBL:EIE27722.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE27722.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE27722.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE27722.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIE27722.1}.
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DR EMBL; AGSI01000001; EIE27722.1; -; Genomic_DNA.
DR RefSeq; XP_005652266.1; XM_005652209.1.
DR AlphaFoldDB; I0ZAQ3; -.
DR STRING; 574566.I0ZAQ3; -.
DR GeneID; 17045737; -.
DR KEGG; csl:COCSUDRAFT_26878; -.
DR eggNOG; KOG0023; Eukaryota.
DR OrthoDB; 1550at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 83..413
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 428 AA; 45510 MW; 92A2325EE93C2E85 CRC64;
MVRVTQPTTD EIAKFPREFA LFTQIPGAKA GEVDTEALAE FVKTYGTGSA PSGGELAFAD
VAAALKKKGT PIEGTGNTIA WAAQDDSGHL APYKFTRRDV GPDDVAIQIA YAGICHSDLH
QIKNDWGNSS FPMVPGHEIV GVITEVGKNA EGHFALGDAA GVGCMVRACR ECEECHSGDD
QYCTRIVFTY NGKDWGEGGV DTQGGYSNRI VLDHRYALKV PASLPLVAAA PLLCAGITTY
SPLKHYGLDK PGQKLGVVGL GGLGHMAVKF GKGFGQEVTV ISTSPNKEKE ARETLKADHF
IVSKDEAQMS AAVNSLDGII DTVSAGHEIS ALLPLLKTNG KLILLGVPTE PHTFGAGAVL
FKRLTIGGSL IGGIKETQEM LDFCGEKGIV CDVEKVDIDY VNTAMDRLAK NDVHYRFSID
IQGSLIDE
//
