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Database: UniProt
Entry: F8NJE6_SERL9
LinkDB: F8NJE6_SERL9
Original site: F8NJE6_SERL9 
ID   F8NJE6_SERL9            Unreviewed;       464 AA.
AC   F8NJE6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032406};
GN   ORFNames=SERLADRAFT_458150 {ECO:0000313|EMBL:EGO29844.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO29844.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO29844.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) 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; GL945429; EGO29844.1; -; Genomic_DNA.
DR   RefSeq; XP_007314086.1; XM_007314024.1.
DR   AlphaFoldDB; F8NJE6; -.
DR   GeneID; 18817658; -.
DR   KEGG; sla:SERLADRAFT_458150; -.
DR   HOGENOM; CLU_016733_0_0_1; -.
DR   OrthoDB; 672at2759; -.
DR   UniPathway; UPA00868; UER00840.
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; 1.
DR   Gene3D; 2.40.50.100; -; 1.
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; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          53..128
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          129..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  50573 MW;  BF9144424B4D0118 CRC64;
     MLSKQVIAVA RNRAFFTGKH VQRAGALVMS KGWRTAESHM RCAQFHSTHL LQAETIKVPQ
     MAESISEGTL RSWSKQVGDS VEVDEEVATI ETDKIDVTVN ASKAGKIVEL LAKEDDTVVV
     GQDLFRIEVG EGGQTSSPSP KEQETSEEPK ELAEESKVKD PEEPKDQQVD KKPSEHPPPS
     GKDKLSGGIP PEGPKEVKKD VAKGKDIPPS KGTAAEKPKP SSAAAPKAPG SRNETRVKMN
     RMRLRIAERL KESQNAAASL TTFNEIDMSS LMEMRKKYKD EVLKEHDVKL GFMSAFARAC
     TLALKEIPAA NASIEGDEII YRDYVDLSVA VATPKGLVTP VVRNAEGMGF LEIEKEIASL
     GKKARDGKLT LEDMAGGSFT ISNGGVFGSL YGTPIINLPQ AAVLGMHSIK EKPVVVNGQI
     VIRPIMVVAL TYDHRLLDGR EAVTFLVKVR DYIEDPRKML LALN
//
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