ID A0A0D0I5Y3_9MICO Unreviewed; 1227 AA.
AC A0A0D0I5Y3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Kgd protein {ECO:0000313|EMBL:KIP88347.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:KIP88347.1};
GN Name=kgd {ECO:0000313|EMBL:KIP88347.1};
GN ORFNames=RU09_16330 {ECO:0000313|EMBL:KIP88347.1};
OS Microbacterium sp. MEJ108Y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1587523 {ECO:0000313|EMBL:KIP88347.1, ECO:0000313|Proteomes:UP000032119};
RN [1] {ECO:0000313|EMBL:KIP88347.1, ECO:0000313|Proteomes:UP000032119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEJ108Y {ECO:0000313|EMBL:KIP88347.1,
RC ECO:0000313|Proteomes:UP000032119};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-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:KIP88347.1}.
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DR EMBL; JXQX01000038; KIP88347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0I5Y3; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000032119; 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; IPR032106; 2-oxogl_dehyd_N.
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; PF16078; 2-oxogl_dehyd_N; 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:KIP88347.1};
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 887..1080
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 83..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 134971 MW; 23C8EE9881F505CF CRC64;
MSNQVTGVGG DGGFGANSWL VEELYEQYKV NRDSVDKEWW PILEKYQSDA ATGTAAPAPA
AEQPAHPVTA PIPVIGAQPV ARTTTKPAAA APIPAQAPKP AAKAEAPESA DPVEEDKVTP
LRGLPKTLAA NMDESLTVPT ATSVRTVPAK LMIDNRIVIN NHMARTRGGK ISFTHLIGWA
LIRTLDEFRS QNVFYAEIDG KPSVVAPAHV NLGIAIDLPK PDGTRALMVP SIKRADTLTF
SEYLVAYEDL VTRARNNKLT AADFQGTTVS LTNPGGIGTV HSVPRLMKGQ GCIIGAGALE
YPAEFQGASE KTLNELAIGK TITLTSTYDH RVIQGAGSGE FLKKVHELLI GQRGFYDDIF
AALRIPYSPI RWNPDIAVDL AERVDKQSRV QELINSFRVR GHLMADIDPL EYVQRSHPDL
EIESHGLTFW DLDREFVTGG FGGRRVAKLR DILGVLRDSY CRTLGIEYMH IQDPEQRRWF
QEKVEVKYQK PGHDEQLRVL RKLNEAEAFE TFLQTKFVGQ KRFSLEGGES LVPLLDEILQ
GAATSGLEGA AIGMAHRGRL NVLTNIAGKT YGHVFQEFEG TQTPGNQRGS GDVKYHLGTE
GTFVADDGSE LPVYLAANPS HLETVDGVLE GIVRAKQDRK PIGTFAWLPI LVHGDAAFAG
QGVVVETLQM SQLRGYRTGG TIHVVVNNQV GFTTLPNDSR SSVYSTDVAK TIQAPVFHVN
GDDPEAVIHV AQLAFEYRER FHRDVVIDLV CYRRRGHNEG DDPSMTQPLM TDLIQAKRSV
RKLYTESLVG RGDITEEEYD EAKADFQNRL EIAFAETHAA ETGANPVAQD LPPADEQVGA
PEITGVSNEV IQLIGDAFVN KPEGFTVHPK LQQQLEKRLD MSRNGNIDWG FGELLAFGSL
LVEGTPVRLA GQDSRRGTFV QRHATLHDRA NGQEWLPLSN LSDSQGRFFV YDSLLSEYAA
LGFEYGYSVE APEALVLWEA QFGDFVNGAQ SVIDEYISAA EQKWGQQSSV TLLLPHGYEG
QGPDHSSSRI ERFLQMCAQD NMIVSRPSTP ASYFHLLRRQ AYARPRKPLI VFTPKAMLRL
RGATSPVEAF TQGRFEPVLD DNRGLDRNAV KRVLVHSGKV HWDLKAELDK NPNPEIALVR
LEQLYPTPID GLKAITDSYP NAELVWVQEE PENQGAWPFL ALAFADVPGD RSFRPVSRPA
SASPATGSSK VHAAEQAKLL RDALTIS
//
