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Database: UniProt
Entry: B0D495_LACBS
LinkDB: B0D495_LACBS
Original site: B0D495_LACBS 
ID   B0D495_LACBS            Unreviewed;       433 AA.
AC   B0D495;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
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=LACBIDRAFT_384857 {ECO:0000313|EMBL:EDR10293.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR10293.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547097; EDR10293.1; -; Genomic_DNA.
DR   RefSeq; XP_001878743.1; XM_001878708.1.
DR   AlphaFoldDB; B0D495; -.
DR   STRING; 486041.B0D495; -.
DR   GeneID; 6074438; -.
DR   KEGG; lbc:LACBIDRAFT_384857; -.
DR   HOGENOM; CLU_016733_0_1_1; -.
DR   InParanoid; B0D495; -.
DR   OrthoDB; 672at2759; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001194; 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:UP000001194};
KW   Transferase {ECO:0000313|EMBL:EDR10293.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          47..122
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          125..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  46785 MW;  7D71175057DDF0B5 CRC64;
     MLSSRVIAIA RGRGLTQASS ASLLRALTIA NVNAKRAQFH SSNLLKAETI KVPQMAESIS
     EGTLKSWSKQ VGDTVTADEE VATIETDKID VSVNAPQSGT IVKLLANEED TVTVGQDLFV
     LEPGEVAASS PPPAKEEAVP AAEAPKESAE PAVPQPPSPS ESAKTPETKE PVKAKEEKPV
     KKEEKKKEDK SKPAAAPRVA GSRNETRVKM NRMRLRIAER LKESQNAAAS LTTFNEIDMS
     SLVEMRKKFK EQVMKDHEVK LGFMSAFAKA CTFALQEIPA ANASIEGEQI VYRDYVDLSV
     AVATPKGLVT PVVRNAEGMS FVEIEKEIAA LGKKAKDGKL TLEDMAGGTF TISNGGVFGS
     LYGTPIINLP QSAVLGMHAI KDKAVVVDGQ IVIRPIMIVA LTYDHRLLDG REAVTFLVRV
     KEYLEDPRKM LLV
//
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