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Database: UniProt
Entry: F4QKE8_9CAUL
LinkDB: F4QKE8_9CAUL
Original site: F4QKE8_9CAUL 
ID   F4QKE8_9CAUL            Unreviewed;       196 AA.
AC   F4QKE8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032406};
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00030325};
GN   ORFNames=ABI_05330 {ECO:0000313|EMBL:EGF92100.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92100.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the second step in the conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2).
CC       {ECO:0000256|ARBA:ARBA00004052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC         succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC         COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00043693};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|ARBA:ARBA00005145}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; GL883077; EGF92100.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4QKE8; -.
DR   STRING; 715226.ABI_05330; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_2_3_5; -.
DR   Proteomes; UP000006512; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transferase {ECO:0000313|EMBL:EGF92100.1}.
FT   DOMAIN          1..193
FT                   /note="2-oxoacid dehydrogenase acyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00198"
SQ   SEQUENCE   196 AA;  21207 MW;  83F6DC5F3B6DD969 CRC64;
     MSTIMNVRNA YKDAFEKRHG VKLGFMSFFA KAVVAALKDI PALNAEIEGG DIIYKNHYDL
     GVAVGTEKGL VVPVLRDVDT LSLAGIEKGI GALGKQARDG TLSLDQLQGG TFTITNGGIY
     GSLMSTPILN MPQVGILGMH AIKDRAMVVN GQVVVRPMMY LALSYDHRIV DGKEAVTFLV
     RVKDGLEDPQ RFVLEV
//
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