ID A0A0M5JV53_9ACTO Unreviewed; 1306 AA.
AC A0A0M5JV53;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN Name=kgd {ECO:0000313|EMBL:ALD00702.1};
GN ORFNames=AM609_09600 {ECO:0000313|EMBL:ALD00702.1};
OS Actinomyces sp. oral taxon 414.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALD00702.1, ECO:0000313|Proteomes:UP000061022};
RN [1] {ECO:0000313|Proteomes:UP000061022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
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DR EMBL; CP012590; ALD00702.1; -; Genomic_DNA.
DR STRING; 712122.AM609_09600; -.
DR KEGG; acq:AM609_09600; -.
DR PATRIC; fig|712122.3.peg.2176; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000061022; Chromosome.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ALD00702.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 955..1148
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 27..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1306 AA; 140972 MW; 4692E9EE309916FE CRC64;
MVEEMRDAWR SDPASVGPRW RSLFEAEAAA PAATAAAESS DAGSTATGPA TSQSATAGPT
ESPDPEGLAP APPSGTAHPP ADAQPPSDTA PRPRPAQDPA GPGAAPHRQI LSIQDVTRSD
LPPAPPSGTA PPTSPYAQRL ARQHRRNGGA GEDSSVRLRG AAARTAKNME ASLSIPTATS
ARAVPAKVLI ENRAIINGHL AHTRGGRVSF THLIGWAVVE SLSEMPSMNV SYAVDDAGRP
VRHEPAHIAF GLAVDAPGPD GERRLLVPSV KRADLMDLAG FVAACEDLVR RAREGGLGVD
DFRGTTVTLT NPGMFGTLHS VPRLMPGQGL IVGVGAMDYP AAFAGAGEKT LARHGIGKTL
TLTSTYDHRV IQGAASGEFL RLVERKLLGL DGFWERAFES LRIPHEPVVW ARDAVYDADL
ETGKPARVAE LIHAFRQRGH LAADTDPLTY RLRRHPDLDI TSYGLSLWDL DRAFPTGGLG
GTERATLREI LNRLRDAYCR TAGIEYMHIQ DPAQRAWWQE RLEGEWPTTT PAERRRILTK
LEQAEAFETF LQTKYVGQKR FSLEGGESLI VALDRLLDAA AHDGLDEVVI GMTHRGRLNV
LTNIAGKSYG QVFDEFDGAG VVEGAGTGDV KYHLGTDGVF TGTDGVSTRV SLAANPSHLE
TVDGVVEGIV RAKQDRIGLG ERGYTVMPVL VHGDAAFAGQ GVVYETLNMS QLPAYRTGGT
VHIIVNNQIG FTTGSASARS TTYATDLAKG LQVPIFHVNA DDPETVARAA RLAYDYRAAF
HKDVIIDLIC YRRRGHNEGD DPSMTQPVMY RLIDSLPSTR AVYTADLVGR GDITAEDARR
IERDSRDELE RIFAETRAHA RAARDRADRA DPPPSNDTID ATDPTKVGLQ TTGLEVPASQ
RAGQGMMIGW TSAVSRRVVE RIGDAQVAHP PGFTVHPKLE AMLDGRRRAT REGGIDWGLG
ELIAIGSLLM EGVPVRLAGE DARRATFAQR HAVLHDHVSG AEWTPLDFLT PDQAPLSVYD
SLLSEYAALA FEYGYAVERP EALTMWEAQF GDFANGAQCV IDEYVTSATQ KWGQRSGLVM
LLPHGQEGQG PDHSSARIER YLLMCAQDNL RVAQPSTPAN HFHLLREQAY SRPRRPLVVF
TPKQLLRLRA ATSAVEDFTS GVFRPVIGET DPAIASDGAG AGVSRVLVCS GRVYYDLLAE
RARRREAAEE GSTVAIVRLE QLYPLPLEEL AGALAPFAGA EVCWVQDEAA NQGVWPYLGL
HLPESMTASG PVRLISRPEA AAPAVGSVRM YRADQARLIA RAFARQ
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