ID K6I1P5_9LEPT Unreviewed; 468 AA.
AC K6I1P5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=LEP1GSC068_3592 {ECO:0000313|EMBL:EKO77480.1};
OS Leptospira sp. Fiocruz LV3954.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193012 {ECO:0000313|EMBL:EKO77480.1, ECO:0000313|Proteomes:UP000002809};
RN [1] {ECO:0000313|EMBL:EKO77480.1, ECO:0000313|Proteomes:UP000002809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz LV3954 {ECO:0000313|EMBL:EKO77480.1,
RC ECO:0000313|Proteomes:UP000002809};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Selengut J.D., Sanka R., DePew J.,
RA Ko A.I., Reis M.G., Ribeiro G.S., Wunder E.Jr., Vinetz J.M., Sutton G.G.,
RA Nelson W.C., Fouts D.E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00043782};
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}.
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:EKO77480.1}.
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DR EMBL; AKWV02000060; EKO77480.1; -; Genomic_DNA.
DR RefSeq; WP_008398662.1; NZ_AKWV02000060.1.
DR AlphaFoldDB; K6I1P5; -.
DR PATRIC; fig|1193012.3.peg.3068; -.
DR Proteomes; UP000002809; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE 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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EKO77480.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EKO77480.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 189..226
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 93..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 49688 MW; 4B2420CFFAD7E1FC CRC64;
MAKIAEMTQL SPTMSEGKIV RWLKQKGDSV SPGEIIAEVE TDKAVMEMEA FETGVLLEIL
APEGSLLPVG APVAIIGKSG EDVSTLVETA KKSIPAKKEG SVPNANVSTG TPTSTSPVTS
TAGPTVTSEN VSSSDRQTSS EISNVSDNKG ESPRANTTSA ANRQSTKTSY GSEESSKSSR
GVHGGSPIKA SPLAKNLAFQ KGIDLGEVVG SGPGGRIIKR DVLSHQSSGD DRSSFVKRQD
RKLELTGMRK TIASRLAHSA STIPHFYLTT ELNAGPIEDL RNSINMDLGL NGQGKISVND
FILKACSYVL LQVPEINSSW RDDHILEHGR VDIGVAVSIE GGLVTPYVRN ADRKTVLEIS
REIKGLASRA RDRKLKPGEY TDGTFTVSNL GMFGVSSFTA VINEPEAAIL AVGALVEKPV
IKEGNIVAGK TLNVTLSCDH RVVDGATGAR FLSLFRDLME HPLRLLIG
//
