ID D3L7I2_OENOE Unreviewed; 221 AA.
AC D3L7I2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Lipoyl-binding domain-containing protein {ECO:0000259|PROSITE:PS50968};
GN ORFNames=AWRIB429_0312 {ECO:0000313|EMBL:EFD89082.1};
OS Oenococcus oeni AWRIB429.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=655225 {ECO:0000313|EMBL:EFD89082.1, ECO:0000313|Proteomes:UP000003075};
RN [1] {ECO:0000313|EMBL:EFD89082.1, ECO:0000313|Proteomes:UP000003075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRIB429 {ECO:0000313|EMBL:EFD89082.1,
RC ECO:0000313|Proteomes:UP000003075};
RX PubMed=20111862; DOI=10.1007/s00253-009-2425-6;
RA Borneman A.R., Bartowsky E.J., McCarthy J., Chambers P.J.;
RT "Genotypic diversity in Oenococcus oeni by high-density microarray
RT comparative genome hybridization and whole genome sequencing.";
RL Appl. Microbiol. Biotechnol. 86:681-691(2010).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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:EFD89082.1}.
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DR EMBL; ACSE01000004; EFD89082.1; -; Genomic_DNA.
DR AlphaFoldDB; D3L7I2; -.
DR Proteomes; UP000003075; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 71..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 24123 MW; 38D7A8399AB108B1 CRC64;
MTEIFKMPDI GEGMAEGEIS DWLVKVGDQV KTDDSVAEVQ NDKLLQEILS PYSGKVTKLF
VEPGTTVKVG EPLIEFDGDG SGSAADDGQR GKTEAKEIEE PAESEKKTAV SSQASPAAPT
SDSSNSSGAA TASNGNILAM PSVRHYAHEH GIDLSRLRPV GITAILRCPM LRTFLLLLLP
LRRNQKISQA RQKQRQNKRL RNLPRLKKPQ LPTHLKKAGF R
//
