ID A0A0M2HIG8_9MICO Unreviewed; 1244 AA.
AC A0A0M2HIG8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Multifunctional 2-oxoglutarate metabolism enzyme {ECO:0000313|EMBL:KJL44089.1};
DE EC=2.2.1.5 {ECO:0000313|EMBL:KJL44089.1};
GN Name=kgd {ECO:0000313|EMBL:KJL44089.1};
GN ORFNames=RS82_01050 {ECO:0000313|EMBL:KJL44089.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL44089.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL44089.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL44089.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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}.
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:KJL44089.1}.
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DR EMBL; JYJA01000028; KJL44089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2HIG8; -.
DR PATRIC; fig|69370.6.peg.1083; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000034098; Unassembled WGS sequence.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:KJL44089.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 905..1098
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 102..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 136344 MW; 4834F746781DBC26 CRC64;
MSSQVTGVGV SNEGEFGANE WLVEELYEQF KIDRNSVDKA WWPVLEAYHP ADGAAPTQAA
PAAAAAPAAA APAAAAPAAT QPAASEPRPV TAPIPVIGSQ PVARTTARPA APQPIPAQAP
KAQPSAADGE ADADVVTTLR GMPKTLAANM DESLTVPTAT SVRTVPAKLM IDNRIVINNH
MARTRGGKVS FTHLIGWAII QALKEFPSQN VFYAEIDGKP SLVAPAHINL GIAIDLPKPD
GTRALLVPSI KRAEQLTFNE YLTTYEDLVT RARNNKLTAA DFQGTTISLT NPGGIGTVHS
VPRLMKGQGC IVGAGALEYP AEFQGASEKT LNELAIGKTI TLTSTYDHRV IQGAGSGEFL
KKVHELLIGQ RSFYDDIFAA LRIPYAPIHW AADINVDLAE RVDKTARVQE LINSFRVRGH
LMADIDPLQY VQRTHPDLEI EQHGLTFWDL DREFVTGGFG GKRQMKLRDI LGVLRDSYCR
TIGIEYMHIQ DPTQRAWFQE NVEVKYQKPG HDEQLRILDK LNQAEAFETF LQTKYVGQKR
FSLEGGESLI PLLDEILQGA AQAGLDGAAI GMAHRGRLNV LTNIAGKTYG QVFREFEGSV
AIGSKSGSGD VKYHLGTEGT FVADNESELP VYLAANPSHL ETVDGVLEGI VRAKQDRKPI
GTFTWLPILV HGDAAFSGQG VVVETLQMSQ LRGYRTGGTV HVVVNNQVGF TTTPTDARTS
VYATDVAKTI QAPIFHVNGD DPEAVTRVAQ LAFAYRERFH RDVVVDIVCY RRRGHNEGDD
PSMTQPLMTN LIEAKRSVRR LYTEALVGRG DITEQEYEKA KQDFQNRLEI AFAETHAAET
GSSPILVPDA DIQPAAGEPA TTGVSREMVS LIGDTFVNKP NGFTVHAKLQ QLLDKRLDMS
RNGSIDWGFG ELLAFGSLLL EKTDVRLAGQ DSRRGTFVQR HAVLHDRANG QEWIPLTNLS
EDQGRFYVYD SLLSEYAAMA FEYGYSVERA DSLVLWEAQF GDFANGAQSV IDEYISAADQ
KWGQQSSVVL LLPHGYEGQG PDHSSARIER YLQMCAQDNM TVARPSTPAS YFHLLRRQAY
ARPRRPLIVF TPKAMLRLRG ATSPVEDFLT GRFEPVIDEN RGLDKSAVKR VLLHAGKIHW
DLRAELDKNP NPEIALVRLE QYYPAPIDEL NAVIDSYPNA ELVWVQDEPE NQGAWPFIAL
EVVKNLNGRT ISRVSRASAA STATGSPKVH AAEQAAIMQQ ALTL
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