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Database: UniProt
Entry: F8PKW2_SERL3
LinkDB: F8PKW2_SERL3
Original site: F8PKW2_SERL3 
ID   F8PKW2_SERL3            Unreviewed;       445 AA.
AC   F8PKW2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=SERLA73DRAFT_47073 {ECO:0000313|EMBL:EGO03921.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
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., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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; GL945475; EGO03921.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8PKW2; -.
DR   STRING; 936435.F8PKW2; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   HOGENOM; CLU_016733_0_1_1; -.
DR   InParanoid; F8PKW2; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 672at2759; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000008063; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          48..123
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          124..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48655 MW;  34AB6294CCA67356 CRC64;
     MLSKQVIAVA RNRAFFTGKH VQRAGALVMT AESHMRCAQF HSTHLLQAET IKVPQMAESI
     SEGTLRSWSK QVGDSVEVDE EVATIETDKI DVTVNASKAG KIVELLAKED DTVVVGQDLF
     RIEVGEGGQS NPSPKEQETS EEPKELAEES KVKDPEEPKD QQVDKKPSEH PPPSGKDKLS
     GGIPPEGPKE VKKDPKPSSA AAPKAPGSRN ETRVKMNRMR LRIAERLKES QNAAASLTTF
     NEIDMSSLME MRKKYKDEVL KEHDVKLGFM SAFARACTLA LKEIPAANAS IEGDEIIYRD
     YVDLSVAVAT PKGLVTPVVR NAEGMGFLEI EKEIASLGKK ASKYARDGKL TLEDMAGGSF
     TISNGGVFGS LYGTPIINLP QAAVLGMHSI KEKPVVVNGQ IVIRPIMVVA LTYDHRLLDG
     REAVTFLVKV RDYIEDPRKM LLALN
//
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