ID W6T927_9LACO Unreviewed; 348 AA.
AC W6T927;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Molecular chaperone GroES {ECO:0000313|EMBL:ETY74951.1};
GN ORFNames=LFAB_04365 {ECO:0000313|EMBL:ETY74951.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY74951.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY74951.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY74951.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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|ARBA:ARBA00008072, 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:ETY74951.1}.
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DR EMBL; AWWK01000022; ETY74951.1; -; Genomic_DNA.
DR RefSeq; WP_024624745.1; NZ_KK036475.1.
DR AlphaFoldDB; W6T927; -.
DR STRING; 1400520.LFAB_04365; -.
DR PATRIC; fig|1400520.3.peg.857; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_9; -.
DR OrthoDB; 9769198at2; -.
DR Proteomes; UP000019247; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08287; FDH_like_ADH3; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 348 AA; 37163 MW; 97FE7089C8167395 CRC64;
MKTAVFVEPG KVAARELPKA QVQKPTDAVI KIVRACVCGS DLWWFRGISK RQQPSAVGHE
AIGIVESVGD EVTNVQPGDF VIVPFTHGCG HCAACLAGFD GDCLNRDEND TEIVGYQGEY
LRFKNANWAL VKVPGQPSDY TDDQLNDLLT LSDVMATGYH AAAMAEVKAG DTVVVMGDGA
VGLCGVISAK LLGAKRIIAM SRHADRQALA QEFGATDIIA ERGDEAVKKV FEVTDGAGAD
AVLECVGTEQ SVDTAVKVGR PGAVVGRVGV PQKAEMNTNN LFWRNIGLRG GIASVTTDDR
NTLLQAVLAG DIHPGKVFTQ RFDLDHVQQA YEAMDQRKAI KSLLIVSE
//