ID C6ZWI0_LISMN Unreviewed; 257 AA.
AC C6ZWI0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Dihydrolipoamide acetyltransferase {ECO:0000313|EMBL:ACN19631.1};
DE Flags: Fragment;
GN Name=pdhC {ECO:0000313|EMBL:ACN19631.1};
GN ORFNames=lmo1054 {ECO:0000313|EMBL:ACN19631.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:ACN19631.1};
RN [1] {ECO:0000313|EMBL:ACN19631.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL_B-33034 {ECO:0000313|EMBL:ACN19631.1}, NRRL_B-33225
RC {ECO:0000313|EMBL:ACN19700.1}, NRRL_B-33311
RC {ECO:0000313|EMBL:ACN19823.1}, NRRL_B-33326
RC {ECO:0000313|EMBL:ACN19844.1}, NRRL_B-33353
RC {ECO:0000313|EMBL:ACN19880.1}, NRRL_B-33433
RC {ECO:0000313|EMBL:ACN19925.1}, and NRRL_B-33443
RC {ECO:0000313|EMBL:ACN19949.1};
RA Ward T.J., Ducey T.F., Usgaard T.R., Dunn K.A., Bielawski J.P.;
RT "Multilocus Genotyping Assays for SNP-Based Subtyping of Listeria
RT monocytogenes.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FJ029748; ACN19631.1; -; Genomic_DNA.
DR EMBL; FJ029771; ACN19700.1; -; Genomic_DNA.
DR EMBL; FJ029812; ACN19823.1; -; Genomic_DNA.
DR EMBL; FJ029819; ACN19844.1; -; Genomic_DNA.
DR EMBL; FJ029831; ACN19880.1; -; Genomic_DNA.
DR EMBL; FJ029846; ACN19925.1; -; Genomic_DNA.
DR EMBL; FJ029854; ACN19949.1; -; Genomic_DNA.
DR AlphaFoldDB; C6ZWI0; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Transferase {ECO:0000313|EMBL:ACN19631.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 112..187
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 237..257
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 257
FT /evidence="ECO:0000313|EMBL:ACN19631.1"
SQ SEQUENCE 257 AA; 27304 MW; B97928F8927BF109 CRC64;
MAYSFKLPDI GEGIHEGEIV KWFVQPGDKI EEDESLFEVQ NDKSVEEITS PVSGTIKEIK
VAEGTVATVG QVLVTFDGVE GHEDDAEEES AAPKAESTES TPAPAQASGK GIFEFKLPDI
GEGIHEGEIV KWFIQPGDKV EEDQSIFEVQ NDKSVEEITS PVDGTVKDIL VSEGTVATVG
QVLVTFEGDF EGEASHESTP ESPAEEAELT NNNATSAPAT GGNGTPSSKK DPNGLVIAMP
SVRKYAREKG VNIAEVA
//
