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Database: UniProt
Entry: T0QHV9_SAPDV
LinkDB: T0QHV9_SAPDV
Original site: T0QHV9_SAPDV 
ID   T0QHV9_SAPDV            Unreviewed;       533 AA.
AC   T0QHV9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN   ORFNames=SDRG_09281 {ECO:0000313|EMBL:EQC33300.1};
OS   Saprolegnia diclina (strain VS20).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC33300.1, ECO:0000313|Proteomes:UP000030762};
RN   [1] {ECO:0000313|EMBL:EQC33300.1, ECO:0000313|Proteomes:UP000030762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS20 {ECO:0000313|EMBL:EQC33300.1,
RC   ECO:0000313|Proteomes:UP000030762};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA   de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Saprolegnia declina VS20.";
RL   Submitted (APR-2012) 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}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; JH767160; EQC33300.1; -; Genomic_DNA.
DR   RefSeq; XP_008613423.1; XM_008615201.1.
DR   AlphaFoldDB; T0QHV9; -.
DR   STRING; 1156394.T0QHV9; -.
DR   EnsemblProtists; EQC33300; EQC33300; SDRG_09281.
DR   GeneID; 19950008; -.
DR   VEuPathDB; FungiDB:SDRG_09281; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   InParanoid; T0QHV9; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 672at2759; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000030762; Unassembled WGS sequence.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
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; 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; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW   Transferase {ECO:0000313|EMBL:EQC33300.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          60..135
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          171..246
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   533 AA;  55643 MW;  B1CE3BC675159144 CRC64;
     MLRQLHKLKA VRALPRFVAG RRVPALSAAS FNGASRAISM TSMGRVQVGA PNMARRMFST
     IDIPVPSMGD SISEGTVVEW VKAVGDRVEA DDVVVVLETD KVSVDVRSPQ AGVVAEHLAI
     VDATVLVGAP LFRLTEGAAG AASTPAPVAS TPAPATAAPA AAPAAAVSGE PITVNVPSMG
     DSISEGTVVS WTKGAGDHVD VDEVVLVLET DKVSVDVRAP QAGVIQKTLV NVDDVVEIGA
     PLFHMVPGAA PAAAPKPVAT PVAAAPAAEP KAAAPAAKAA TPKVAENIAS PVMLGGASRE
     VRREKMNRMR LRIAERLKES QNTSASLTTF QEVDMSKLMA MRKTYKDAFE AKHNVKLGFM
     SAFIKASANA LLEVPGVNAS IDEAHSEIVY RDFVDISVAV ATPKGLVTPV LRNTESMGFA
     DIEKSLAHLA EKARAGAITM EDMAGGTFTI SNGGVFGSLM GTPIINVPQS GILGMHATKM
     RPVVLANGEI VARPMMYLAL TYDHRLVDGR EAVTCLKSIA DKIADPERLL LDL
//
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