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Database: UniProt
Entry: A0A151WJX1_9HYME
LinkDB: A0A151WJX1_9HYME
Original site: A0A151WJX1_9HYME 
ID   A0A151WJX1_9HYME        Unreviewed;       490 AA.
AC   A0A151WJX1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000256|ARBA:ARBA00020294};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=E2K {ECO:0000256|ARBA:ARBA00031331};
GN   ORFNames=ALC60_12807 {ECO:0000313|EMBL:KYQ48158.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ48158.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ48158.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ48158.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ48158.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ983028; KYQ48158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151WJX1; -.
DR   STRING; 64791.A0A151WJX1; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   NCBIfam; TIGR01347; sucB; 1.
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   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW   Transferase {ECO:0000313|EMBL:KYQ48158.1}.
FT   DOMAIN          126..158
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   DOMAIN          260..486
FT                   /note="2-oxoacid dehydrogenase acyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00198"
FT   REGION          164..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  52680 MW;  348B444C0E3764FC CRC64;
     MAAMLSNCSR FAPRVITRSS VLRAEVSTMN EPFPPLSSAA ADDRHFTRPE LIQRMLAAAN
     RGSVCSSRDR CVVKGALLSL FALSTPNMCL MPKLCWEIRE VVVPAFAESV SEGDVRWEKK
     VGDQTSVPVP SPGPGVIKEL FFKDGDTVKP GQKLCTIDIG ATGGAAAAPG EKAPQPPAAA
     PVEKAPKPVP PPPTPSAPSV APPLPRSAAP IPPPAAEPPS PQAPTASMPV AAIKHAQSLE
     GAKVQLPPAD YTREIIGTRT EQRVKMNRMR LRIAERLKDA QNTNAMLTTF NEIDMSRIIE
     FRKAHQESFT KKYGIKLGFM SPFVAASAYA LKDQPVVNAV IDGTDIVYRD YVDISVAVAT
     PKGLVVPVLR SVENKNFAEI EIALAALGEK ARKGKITVED MDGGTFTISN GGVFGSMLGT
     PIINPPQSAI LGMHGVFDRP IAVKGEVKIR PMMYIALTYD HRLIDGREAV MFLRKIKDSV
     EDPRIILAGL
//
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