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Database: UniProt
Entry: H0TI30_9BRAD
LinkDB: H0TI30_9BRAD
Original site: H0TI30_9BRAD 
ID   H0TI30_9BRAD            Unreviewed;       374 AA.
AC   H0TI30;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (E2) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) {ECO:0000313|EMBL:CCE06118.1};
DE            EC=2.3.1.12 {ECO:0000313|EMBL:CCE06118.1};
GN   Name=pdhC {ECO:0000313|EMBL:CCE06118.1};
GN   ORFNames=BRAS3843_160003 {ECO:0000313|EMBL:CCE06118.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE06118.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(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   -!- 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:CCE06118.1}.
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DR   EMBL; CAFK01000068; CCE06118.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0TI30; -.
DR   Proteomes; UP000002686; 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; 1.
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; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:CCE06118.1};
KW   Pyruvate {ECO:0000313|EMBL:CCE06118.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW   Transferase {ECO:0000313|EMBL:CCE06118.1}.
FT   DOMAIN          70..107
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..55
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  38770 MW;  B96C3BE2C91F57AD CRC64;
     MLAGDGEDVK AAGSAAPTKS APPAEAPAPK PAAAAPAASP APAAAPKPAA APAPQAAAPA
     PQMNGHDRVF SSPLARRLAK DAGIDLARIS GTGPHGRVIA RDVEEAKSGK GLKAPAAAPA
     AGLALAPSMS DKQILALFEP GSYDIVPHDG MRRTIAQRLT ASVQNVPHFY LTIDCDIGKL
     LAAREEINAA APKDKEKKPL YKLSVNDFVI KAMAVALQKI PDCNVSWTEG GMVKHKHSDV
     GVAVAMPGGL ITPIIRKAET KTLSVISGEM KDFAARARSR KLKPEEYQGG TTAVSNLGMY
     GINHFTAVIN PPHATILAVG TSEERPVVRG GKIEIASIMS VTLSCDHRAI DGALGAELIG
     AFKQLIENPV MMMV
//
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