ID D5T1I2_LEUKI Unreviewed; 427 AA.
AC D5T1I2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=LKI_02940 {ECO:0000313|EMBL:ADG40131.1};
OS Leuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=762051 {ECO:0000313|EMBL:ADG40131.1, ECO:0000313|Proteomes:UP000002362};
RN [1] {ECO:0000313|EMBL:ADG40131.1, ECO:0000313|Proteomes:UP000002362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMSNU 11154 / KCTC 2386 / IH25
RC {ECO:0000313|Proteomes:UP000002362};
RX PubMed=20494991; DOI=10.1128/JB.00508-10;
RA Oh H.M., Cho Y.J., Kim B.K., Roe J.H., Kang S.O., Nahm B.H., Jeong G.,
RA Han H.U., Chun J.;
RT "Complete genome sequence analysis of Leuconostoc kimchii IMSNU 11154.";
RL J. Bacteriol. 192:3844-3845(2010).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP001758; ADG40131.1; -; Genomic_DNA.
DR RefSeq; WP_013102728.1; NC_014136.1.
DR AlphaFoldDB; D5T1I2; -.
DR STRING; 762051.LKI_02940; -.
DR KEGG; lki:LKI_02940; -.
DR PATRIC; fig|762051.18.peg.593; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000002362; Chromosome.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
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; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ADG40131.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 427 AA; 45829 MW; 4F82A4A39ADE96DE CRC64;
MTEIFTMPDI GEGMAEGDIT SWLVKVGDVV AMDDPVAEVQ NDKLLQEILS PYAGKVTHLY
VDAGTTVEVG DPLIEFDGSG TPDTGSDEKT VVETTAPSSE DEVPLVTSDD TTQMVKVANG
HVLAMPSVRH LAFEKGIDLT TVTPTGRHGH VTLSDVESFN KENVSESQAV APVEVATQQG
TKPNDITPKA PEVLHEGRQP MTPTRRAIAK AMGAQNATIP SVTNFDSVEV SKLVAHRSSF
KAQAQADGVR LTYLAYAVKA LAATAKKFPE INASVDMDTN EIIYHEDVNM GIAVNAPSGL
YVPVIMHADQ KSILTIAKEI VELSEAVREG SITSQQMRGS TITISNLGSA RGTWFTPIIN
GKEVAILGLG TIVKEPMIDE NDDIVVGQNM KLSLSYDHRL IDGMLGQAAL NYLKQLLADP
AYMLMEV
//