ID C1CEC8_STRZJ Unreviewed; 347 AA.
AC C1CEC8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Dihydrolipoamide acetyltransferase {ECO:0000313|EMBL:ACO18212.1};
GN OrderedLocusNames=SPJ_1081 {ECO:0000313|EMBL:ACO18212.1};
OS Streptococcus pneumoniae (strain JJA).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488222 {ECO:0000313|EMBL:ACO18212.1, ECO:0000313|Proteomes:UP000002206};
RN [1] {ECO:0000313|Proteomes:UP000002206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJA {ECO:0000313|Proteomes:UP000002206};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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 -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; CP000919; ACO18212.1; -; Genomic_DNA.
DR RefSeq; WP_000752705.1; NC_012466.1.
DR AlphaFoldDB; C1CEC8; -.
DR SMR; C1CEC8; -.
DR KEGG; sjj:SPJ_1081; -.
DR HOGENOM; CLU_016733_2_1_9; -.
DR Proteomes; UP000002206; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 2.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
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; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:ACO18212.1}.
FT DOMAIN 7..44
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 50..87
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 347 AA; 38098 MW; C7E0498A940F4347 CRC64;
MADDKLRATP AARKLADDLG INLYDVSGSG ANGRVHKEDV ETYKDTNVVR ISPLAKRIAL
EHNIAWQEIQ GTGHRGKIMK KDVLALLPEN IENDSIKSPA QIEKVEEVPD NVTPYGKIER
IPMTPMRKVI AQRMVESYLT APTFTLNYEV DMTEMLALRK KVLEPIMEAT GKKTTVTDLL
SLAVVKTLMK HPYINASLTE DGKTIITHNY VNLAMAVGMD NGLMTPVVYN AEKMSLSELV
VAFKDVIGRT LDGKLAPSEL QNSTFTISNL GMFGVQSFGP IINQPNSAIL GVSSTIEKPV
VVNGEIVIRP IMSLGLTIDH RVVDGMAGAK FMKDLKELIE TPISMLI
//
