ID A8AXB0_STRGC Unreviewed; 347 AA.
AC A8AXB0;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Dihydrolipoamide S-acetyltransferase {ECO:0000313|EMBL:ABV10614.1};
DE EC=2.3.1.12 {ECO:0000313|EMBL:ABV10614.1};
GN Name=sucB {ECO:0000313|EMBL:ABV10614.1};
GN OrderedLocusNames=SGO_1131 {ECO:0000313|EMBL:ABV10614.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV10614.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV10614.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10614.1; -; Genomic_DNA.
DR RefSeq; WP_012000541.1; NC_009785.1.
DR AlphaFoldDB; A8AXB0; -.
DR STRING; 467705.SGO_1131; -.
DR KEGG; sgo:SGO_1131; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_2_1_9; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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 Acyltransferase {ECO:0000313|EMBL:ABV10614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW Transferase {ECO:0000313|EMBL:ABV10614.1}.
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; 37996 MW; F7E1E04BAF019D5A CRC64;
MADDKLRATP AARKLADDLG INLYDVSGSG ANGRVHKEDV ETYKDTNVVR ISPLAKRIAL
EHNIAWQEIQ GTGHRGKIMK KDVLALLPEN IENDTIKSPA QIEKVEEVPD TITPYGEIER
IPMTPMRKVI AQRMVESYLT APTFTLNYDV DMSEMLALRK KVLDPIMEAT GKKVTVTDLL
SLAVVKTLMK HPYINASLTE DGKTIITHNY VNLAMAVGMD NGLMTPVVYN AEKLSLSELV
VSFKDVIGRT LDGKLAPSEL QNSTFTISNL GMFGVQSFGP IINQPNSAIL GVSSTVEKPV
VVNGEIVIRP IMSLGLTIDH RVVDGMAGAK FMKDLKALIE DPISMLV
//
