ID G0J7W7_CYCMS Unreviewed; 372 AA.
AC G0J7W7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:AEL27815.1};
GN OrderedLocusNames=Cycma_4111 {ECO:0000313|EMBL:AEL27815.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL27815.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; CP002955; AEL27815.1; -; Genomic_DNA.
DR RefSeq; WP_014022099.1; NC_015914.1.
DR AlphaFoldDB; G0J7W7; -.
DR STRING; 880070.Cycma_4111; -.
DR KEGG; cmr:Cycma_4111; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_10; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000001635; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 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:UP000001635};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..369
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 372 AA; 39584 MW; CF8C1D7FD6BE37A2 CRC64;
MSIASKSAVA KGDGTFIITQ VNLTDPQEDE VLIKMKAAGL CHTDYDSINW GKPLVMGHEG
AGIVEKIGSA IKELKIGDQV ILNWATPCMH CFQCQEGNQH ICENNSPVVA GENGHTPGHA
KLESSQWNGE SIERSFNLGT LSEYALVKEA AVVKVEEPGL NFSAASIVSC GVMTGFGSVV
NAAKVEAGSS AVVLGCGGVG LNVINACKIS GAAKIIAVDV NPTKLELARK FGATDTILAD
KSDIGLLAAA KDVKELLGGR GSDYAFECTA IPALGAAPLA MVRNAGTAVQ VSGIEEEISI
DMRLFEWDKV YINPLYGKCR PQIDFPKIMK LYKKGELMLD QMITREYALE DLQQAFDDML
AGKNAKGVIV FK
//
