ID A0A1E3HAW8_9TREE Unreviewed; 456 AA.
AC A0A1E3HAW8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=L202_07995 {ECO:0000313|EMBL:ODN73489.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN73489.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN73489.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN73489.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN73489.1}.
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DR EMBL; AWGJ01000013; ODN73489.1; -; Genomic_DNA.
DR RefSeq; XP_018989401.1; XM_019142830.1.
DR AlphaFoldDB; A0A1E3HAW8; -.
DR STRING; 1295533.A0A1E3HAW8; -.
DR GeneID; 30159304; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000094065; 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:UP000094065};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 59..134
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 133..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 49622 MW; 396703FA9FA4554A CRC64;
MLRTQSRLAA AAPAITRSAL RATALPRHAA PQVSRVVLKS ASSHLLLRSS FHSSATRLAE
TVKVPQMAES ITEGTLKQWS KAVGDFVKQD EEIATIETDK IDVSVNAPIS GTITELLAQE
EDTVEVGADL LRIEPGEGGS ESSESKPQAK SEPKEAQEGK RDDPAPESHR EKNAGEENLK
KHDEKAPKLE QSKEEKPAPK QEAPKPKKEE KKEVQPEKAL GSRNETRVKM SRMRQTIAQR
LKASQNSAAS LTTFNEIDMS SLMEFRKLYK DGVLKADGVK LGFMSAFAKA SCLALKEIPG
ANASIEGDSI VYRDYVDLSV AVATPKGLVT PVVRNAESMG LVEIEQAIAE LGKKARDNKL
SIEDMSGGSF TISNGGVFGS LFGTPIINLP QAAVLGMHSI KEKPVVVNGQ IVIRPIMVVA
LTYDHRLLDG REAVTFLVRI KEYIEDTRRM LLPSPL
//
