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Database: UniProt
Entry: E8KBE5_9STRE
LinkDB: E8KBE5_9STRE
Original site: E8KBE5_9STRE 
ID   E8KBE5_9STRE            Unreviewed;       347 AA.
AC   E8KBE5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=2-oxo acid dehydrogenase acyltransferase (Catalytic domain) {ECO:0000313|EMBL:EFX40569.1};
DE            EC=2.3.1.12 {ECO:0000313|EMBL:EFX40569.1};
GN   Name=sucB {ECO:0000313|EMBL:EFX40569.1};
GN   ORFNames=HMPREF9180_0800 {ECO:0000313|EMBL:EFX40569.1};
OS   Streptococcus peroris ATCC 700780.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888746 {ECO:0000313|EMBL:EFX40569.1, ECO:0000313|Proteomes:UP000010304};
RN   [1] {ECO:0000313|EMBL:EFX40569.1, ECO:0000313|Proteomes:UP000010304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700780 {ECO:0000313|EMBL:EFX40569.1,
RC   ECO:0000313|Proteomes:UP000010304};
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 (DEC-2010) 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:EFX40569.1}.
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DR   EMBL; AEVF01000009; EFX40569.1; -; Genomic_DNA.
DR   RefSeq; WP_006145563.1; NZ_GL732463.1.
DR   AlphaFoldDB; E8KBE5; -.
DR   STRING; 888746.HMPREF9180_0800; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_2_1_9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000010304; 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:EFX40569.1};
KW   Transferase {ECO:0000313|EMBL:EFX40569.1}.
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;  38088 MW;  F042266D2B9360E3 CRC64;
     MADDKLRATP AARKLADDLG INLYDISGSG ANGRVHKEDV ETYKDTNVVR ISPLAKRIAL
     EHNIAWQEIQ GTGHRGKIMK KDVLAYLPEN IENDTIKSPA QIEKVEEVPD NVTPYGEIER
     IPMTPMRKVI AQRMVESYLT APTFTLNYDV DMSEMLALRK KVLDPIMEAT GKKITVTDLL
     SLAVVKTLMK HPYINASLTE DGKTIITHNY VNLAMAVGMD NGLMTPVVYN AEKMTLSELV
     VAFKDVIGRT LDGKLAPSEL QNSTFTISNL GMFGVQSFGP IINQPNSAIL GVSSTVEKPV
     VVNGEIVIRP IMSLGLTIDH RVVDGMAGAK FMKDLKALIE NPISMLV
//
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