ID A0A2S8ZZ27_9MICO Unreviewed; 1224 AA.
AC A0A2S8ZZ27;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:PRB06470.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:PRB06470.1};
GN Name=kgd {ECO:0000313|EMBL:PRB06470.1};
GN ORFNames=CQ047_14775 {ECO:0000313|EMBL:PRB06470.1};
OS Microbacterium sp. MYb72.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB06470.1, ECO:0000313|Proteomes:UP000238041};
RN [1] {ECO:0000313|EMBL:PRB06470.1, ECO:0000313|Proteomes:UP000238041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb72 {ECO:0000313|EMBL:PRB06470.1,
RC ECO:0000313|Proteomes:UP000238041};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PRB06470.1}.
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DR EMBL; PCOT01000029; PRB06470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8ZZ27; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000238041; 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:PRB06470.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:PRB06470.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 885..1078
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 134407 MW; A5C8B16356AB7337 CRC64;
MSNQVTGVGG DGGFGANSWL VEELYEQFKV NRDSVDKEWW PILEKYQSDA ATGTAAAASP
APAQPAHPVT APIPVIGAQP VARTTAKPAA AAPIPAQAPK PEAKDAAVDA AEEDKVTPLR
GLPKTLAANM DESLTVPTAT SVRTVPAKLM IDNRIVINNH MARTRGGKIS FTHLIGWALI
RTLDEFRSQN VFYAEIDGKP SVVAPAHVNL GIAIDLPKPD GTRALMVPSI KRADTMTFSE
YLVAYEDLVT RARNNKLTAA DFQGTTVSLT NPGGIGTVHS VPRLMKGQGC IIGAGALEYP
AEFQGASDKT LNELAIGKTI TLTSTYDHRV IQGAGSGEFL KKVHELLIGQ RGFYDDIFAA
LRIPYAPIRW NADIAVDLAE RVDKQARVQE LINSFRVRGH LMADIDPLEY VQRSHPDLEI
ENHGLTFWDL DREFVTGGFG GRRIAKLRDI LGVLRDSYCR TLGIEYMHIQ DPEQRRWFQE
KVEVKYQKPG HDEQLRVLRK LNEAEAFETF LQTKFVGQKR FSLEGGESLV PLLDEILQGA
ANAGLEGAAI GMAHRGRLNV LTNIAGKTYG QVFQEFEGHQ TPGNQRGSGD VKYHLGTEGT
FIAEDGAQLP VYLAANPSHL ETVDGVLEGI VRAKQDRKPI GTFTWLPILV HGDAAFAGQG
VVVETLQMSQ LRGYRTGGTI HVVVNNQVGF TTTPNDGRTS VYSTDVAKTI QAPVFHVNGD
DPEAVIHVAQ LAFEYRERFH RDVVIDLVCY RRRGHNEGDD PSMTQPLMTD LIQAKRSVRK
LYTESLVGRG DITEEEYDQA KADFQNRLEI AFAETHAAET GATPIAPDLL PVDEQIGAPE
VTGVAKEVIQ LIGDAFVNKP EGFTVHPKIQ QLLDKRLDMS RNGGIDWGFG ELLAFGSLLV
EGTPVRLAGQ DSRRGTFVQR HATLHDRANG QEWLPLSNLS DAQGRFFVYD SLLSEYAALG
FEYGYSVEAP EALVLWEAQF GDFVNGAQSV IDEYISAAEQ KWGQQSSVTL LLPHGYEGQG
PDHSSARIER FLQLCAQENM IVARPSTPAS HFHLLRRQAY ARPRKPLIVF TPKAMLRLRG
ATSPVEAFTS GRFEPVIDDD RGLDRSAVKR VLVHSGKVHW DLRADLEKNP NPEVALVRLE
QLYPTPIDEL KAITDSYPNA ELVWVQEEPE NQGAWPFLAL AFADVPGDRT FRPVARAASA
SPATGSSKVH AAEQATLIRE ALTV
//
