ID A0A0B2A717_9MICO Unreviewed; 1232 AA.
AC A0A0B2A717;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:KHK98880.1};
GN ORFNames=LK09_08455 {ECO:0000313|EMBL:KHK98880.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK98880.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK98880.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK98880.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) 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}.
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:KHK98880.1}.
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DR EMBL; JTDK01000006; KHK98880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2A717; -.
DR STRING; 1348253.LK09_08455; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000031030; Unassembled WGS sequence.
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 PIRSF; PIRSF000157; Oxoglu_dh_E1; 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:KHK98880.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 893..1086
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 54..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 135242 MW; A452379BF5158694 CRC64;
MSSQVTGVGA SSEGEFGANE WLVDELYEQF SKDRNLVDKA WWPILEAYHP STPATPGAAA
PAAPAAPATP TTEAAPPTTP IPVIGTQPVA RTTAKPAREQ PIPAQAPKVQ PSVGESSTEQ
DVVTPLRGLA KTLATNMDQS LTVPTATSVR TVPAKLMIDN RIVINNHMGR TRGGKVSFTH
LIGWAIIQAL KDFPSQNVAY AEVDGKPSVV APAHVNLGIA IDMPRPDGSR ALLVPSIKHA
ESLTFGEYLA SYEDLVKRAR ANKLTAADFQ GTTISLTNPG GIGTEHSVPR LMPGQGCIVG
AGALEYPAAF QGSSDKTLAG LGIGKTITLT STYDHRVIQG AGSGEFLKIV HQLLIGERRF
YDHIFAALRI PTAPIRWSQD INVDLAERVD KTARVQELIN SYRVRGHLMA DIDPLEYVQR
THPDLEIETH GLTFWDLDRQ FVTGGFGGQR QMKLRDILGV LRDSYCRTIG IEYMHIQDPA
QRQWFQDNME VRYEKPGHDE QLRILSKLNQ AEAFETFLQT KYVGQKRFSL EGSESLVPLL
DQILQGAAAD GLDGAVIGMA HRGRLNVLTN IAGKTYSQIF REFEGLAAVG NKSGSGDVKY
HLGTDGTFVA DGGQELPVHL AANPSHLETV DGVVEGIARA KQDRKPIGSF TYLPILVHGD
AAFAGQGVVV ETLQMSQLRG YRTGGTIHVV VNNQVGFTTT PADGHTSVYA TDVAKTIQAP
ILHVNGDDPE AVVHVAEVAY RYRQEFHRDI VIDVVSYRRR GHNEGDDPSM TQPLMTNLIE
AKRSVRKLYT EALVGRGDIT EEEYDKAKAD FQGRLEVAFA ETHEAETGTS PIITVDAAHL
DPYTGEPETT AVSRNVVETI ADAFVNKPEG FTVHPKLAQL MDRRVKMSRE GGVDWGFGEL
LAFGSLLMEG TAVRLAGQDA QRGTFVQRHS VLHDRVNGQE WIPLVNLSDS QARFWVYNSL
LSEYAAMAYE YGYSVERPDA LVLWEAQFGD FANGAQSVID EYISAADQKW GQQSSLVLLL
PHGYEGQGPD HSSARIERYL QMCAQNNMTV ARPSTPASYF HLLRRQAYAR PRRPLVVFTP
KAMLRLRDAT SPIEDFLQGR FEPVLDDSRP LDKQNVKRVL LHSGKIHWDL RAELTKNPND
QIALVRLEQF YPAPVDELNA VVDSYPNAEL VWVQEEPENQ GAWPFISLEV VKHLHGRTIK
RVSRPAAASP ATGSPKVHAA QSAELLRSAL SL
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