ID F5X5Z1_STRPX Unreviewed; 464 AA.
AC F5X5Z1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:BAK29831.1};
GN OrderedLocusNames=SGPB_0743 {ECO:0000313|EMBL:BAK29831.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK29831.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK29831.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
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 ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012054; BAK29831.1; -; Genomic_DNA.
DR RefSeq; WP_013851697.1; NC_015600.1.
DR AlphaFoldDB; F5X5Z1; -.
DR STRING; 981540.SGPB_0743; -.
DR GeneID; 76467712; -.
DR KEGG; stb:SGPB_0743; -.
DR HOGENOM; CLU_016733_0_0_9; -.
DR Proteomes; UP000007946; 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 CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:BAK29831.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAK29831.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 165..202
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 98..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 49791 MW; ACC87386D7A620C1 CRC64;
MANEIIMPKL GVDMQEGEIL EWKKAEGDEV NEGDILLEIM SDKTNMEIEA EDSGVLLKIV
HPAGDVVAVT EIIGYIGAEG ETLVDSVGEK HVEQSASAQE AKVQPLQAST APAISQKTSE
TGKVRATPAA RKLARERGID LEKITGSGEN GRIHKENVEQ FSKIRVTPLA RRIAKDKGVD
LETLVGTGVS GKITKEDVLA SLGDVAPQKE QADVKVTPQA GALADVTAAS DGVEVIKMSA
MRKAISKGMS HSYFTAPTFT LNYDIDMTNL IALRKQLIEP IMAKTGYKVT FTDLIGLAVI
KTLMKEEHRF LNASLINDAQ DIELHHFVNL AIAVGLSEGL VVPVVHGADQ MSLSDFVVAS
KDVIQKAQAG KLKAAEMSGS TFTITNLGMF GVKSFNPIIN QPNSAILGIS ATIETPVVHD
GEVVIRPIMG MSLTIDHRLV DGMNGAKFML DLKALLENPL ELLI
//
