ID F2C645_STRSA Unreviewed; 347 AA.
AC F2C645;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Dihydrolipoamide acetyltransferase {ECO:0000313|EMBL:EGF15502.1};
DE EC=2.3.1.12 {ECO:0000313|EMBL:EGF15502.1};
GN Name=acoC {ECO:0000313|EMBL:EGF15502.1};
GN ORFNames=HMPREF9386_0649 {ECO:0000313|EMBL:EGF15502.1};
OS Streptococcus sanguinis SK330.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888813 {ECO:0000313|EMBL:EGF15502.1, ECO:0000313|Proteomes:UP000005955};
RN [1] {ECO:0000313|EMBL:EGF15502.1, ECO:0000313|Proteomes:UP000005955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK330 {ECO:0000313|EMBL:EGF15502.1,
RC ECO:0000313|Proteomes:UP000005955};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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 -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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:EGF15502.1}.
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DR EMBL; AFBD01000002; EGF15502.1; -; Genomic_DNA.
DR RefSeq; WP_002915199.1; NZ_GL878548.1.
DR AlphaFoldDB; F2C645; -.
DR PATRIC; fig|888813.3.peg.635; -.
DR HOGENOM; CLU_016733_2_1_9; -.
DR Proteomes; UP000005955; Unassembled WGS sequence.
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:EGF15502.1};
KW Transferase {ECO:0000313|EMBL:EGF15502.1}.
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; 38107 MW; 0203A38D909428C7 CRC64;
MADDKLRATP AARKLADDLG INLYDVSGSG ANGRVHKEDV ETYKDTNVVR ISPLAKRIAQ
EHNIAWQEIQ GTGHRGKIMK KDVLAFLPEN VESDTIKSPA QIEKVEEVPD NVTPYGEIER
IPMTPMRKVI AQRMVESYLT APTFTLNYDV DMTEMLALRK KVLEPIMEAT GKKVTVTDLL
SLAVVRTLMK HPYLNSTLTE DGKTIITHNY VNLSMAVGMD NGLMTPVVYN AEKMSLSELV
VAFKDVIGRT LEGKLAPSEL QNSTFTVSNL GMFGVQSFGP IINQPNSAIL GVSSTVEKPV
VVNGEIVIRP IMSLGLTIDH RVVDGMAGAK FMKDLKALIE DPISMLV
//
