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
//