ID U4KX50_PYROM Unreviewed; 454 AA.
AC U4KX50;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=PCON_05923 {ECO:0000313|EMBL:CCX06336.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX06336.1};
RN [1] {ECO:0000313|EMBL:CCX06336.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX06336.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX06336.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935285; CCX06336.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KX50; -.
DR STRING; 1076935.U4KX50; -.
DR eggNOG; KOG0559; Eukaryota.
DR OMA; MKVPSPG; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000018144; 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 Transferase {ECO:0000313|EMBL:CCX06336.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 70..145
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 146..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 48204 MW; D39F0B4EA570A51F CRC64;
MASRLAVRRL PTTRCLCSSA PTVARTSTRA FSNVSRAPSN TLLSAVARKP TSRFVKAASI
LNVQTRSYAD TVVKVPSMAE SISEGTLKQF SKQVGDFVEQ DEEIATIETD KIDVAVNAPI
AGTITELLVA EEDTVVVGQD LLKIAPGSAP EGGAAPKAEA AKEEPKAAAD VKTEAPKQEA
PAPKKEEAKA PAPAPKAAEK KPAAASPAPA AAPSAFGNRE ERRVKMNRMR LRIAERLKES
QNTAASLTTF NEIDMSALME MRKLYKDAVL EKTGVKLGFM SAFSKAAIEA MKDVPAVNAS
IEGPNGGDTI VYRDYVDISV AVATEKGLVT PIVRNAESLD MVGIESAIAG LGKKARDGKL
TIEDMAGGTF TISNGGVFGS LFGTPIINLP QTAVLGLHSI KEKPVAINGK VEIRPIMVVA
LTYDHRLLDG KEAVTFLVKI KNYIEDPRRL LLGV
//
