ID A0A059CGC5_EUCGR Unreviewed; 475 AA.
AC A0A059CGC5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=EUGRSUZ_D01602 {ECO:0000313|EMBL:KCW77241.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW77241.1};
RN [1] {ECO:0000313|EMBL:KCW77241.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW77241.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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; KK198756; KCW77240.1; -; Genomic_DNA.
DR EMBL; KK198756; KCW77241.1; -; Genomic_DNA.
DR RefSeq; XP_010053008.1; XM_010054706.2.
DR RefSeq; XP_010053009.1; XM_010054707.2.
DR RefSeq; XP_018727743.1; XM_018872198.1.
DR RefSeq; XP_018727744.1; XM_018872199.1.
DR STRING; 71139.A0A059CGC5; -.
DR EnsemblPlants; KCW77240; KCW77240; EUGRSUZ_D01602.
DR EnsemblPlants; KCW77241; KCW77241; EUGRSUZ_D01602.
DR GeneID; 104441560; -.
DR Gramene; KCW77240; KCW77240; EUGRSUZ_D01602.
DR Gramene; KCW77241; KCW77241; EUGRSUZ_D01602.
DR KEGG; egr:104441560; -.
DR eggNOG; KOG0559; Eukaryota.
DR OMA; TPIFMEA; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 99..174
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 175..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51079 MW; DB890E9045C7755F CRC64;
MMLGVVRRRV ASGGGSASVS SLGQALLISR SAGSARRIAS VADERVVLSR GCGPVRSFCH
LAVMRCSVGS RPTRVVAFNN QAVEILPQWR LFSTESGDLV DAVVPFMGES ITDGTLAKFL
KNPGDRVELD EPIAQIETDK VTIDVASPEA GVIQKFLAKE GETVEPGTKI AVISKSGEGA
THVAPSESAG EKAASPPPPA EKVEEKQKPK AEAAPAAEKP KAPSPPPPPP PKRSATEPQL
PPKDRERRIP MTRLRKRVAA RLKDSQNTFA LLTTFNEVDM TNLMKLRSDY KDAFVEKHGV
KLGLMSGFVK AAVSGLQNQP IINAVIDGDD IIYRDYVDIS IAVGTPKGLV VPVIRNAENM
NFADIEKEIN TLAKKANDGS ISIDEMAGGT FTISNGGVYG SLLSTPIINP PQSAILGMHS
IVSRPMVVGG NVVPRPMMYI ALTYDHRLID GREAVFFLRR IKDVVEDPRR LLLDI
//
