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Database: UniProt
Entry: A0A1M5E7T9_9ACTN
LinkDB: A0A1M5E7T9_9ACTN
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ID   A0A1M5E7T9_9ACTN        Unreviewed;      1274 AA.
AC   A0A1M5E7T9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:SHF75121.1};
GN   ORFNames=SAMN05443575_0810 {ECO:0000313|EMBL:SHF75121.1};
OS   Jatrophihabitans endophyticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC   Jatrophihabitantaceae; Jatrophihabitans.
OX   NCBI_TaxID=1206085 {ECO:0000313|EMBL:SHF75121.1, ECO:0000313|Proteomes:UP000186132};
RN   [1] {ECO:0000313|EMBL:SHF75121.1, ECO:0000313|Proteomes:UP000186132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45627 {ECO:0000313|EMBL:SHF75121.1,
RC   ECO:0000313|Proteomes:UP000186132};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQVU01000001; SHF75121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5E7T9; -.
DR   STRING; 1206085.SAMN05443575_0810; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000186132; 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:UP000186132};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          937..1130
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          48..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  138624 MW;  8865646F9CC58DAC CRC64;
     MATDQSTDNP STRGDFGANE WLVEDMYERY LDDPHSVDAA WHDFFADYRP GTASAPGSSS
     ANGTASANGA ARTGTADPSD TAESTETSDT EPGRSPSAGV PEQAAPARTS PAPTDSPAAA
     PAAPASDQNR PTPAASTDEG KAPEAPAAEN AKAAQPAPSA PAPKVEGPGR APLRGAAARV
     VTNMEQSLHV PTATSVRAVP AKLLFDNRVV INNHLRRARG GKVSFTHLIG YAVVKALGVH
     PEMNNAFAEV DGKPMLVTPE HVNLGIAIDL AGKNGARSLV VASIKGAETL DFAAFWNAYE
     DIIRRARNGK LTTDDFAGTT ISLTNPGTIG TNHSVPRLMQ GQGTIVGVGS MEYPAEFSGM
     NPAALLDRAI SKIMTLTSTY DHRIIQGAQS GEFLKVVHEL LLSDAFYDEI FAALKIPYEP
     VRWLVDRDFT HEGQIGKNAR VIELINAYRT NGHLMADTDP LEFTVRSHPD LDITRHGLTL
     WDLDREFPVD GFAGEKLMTL RDILGVLRDA YCRRVGVEYM HITDPAQRRW LQERIEIQQG
     QPSRDEQLHI LGRLNVAEAF ETFLQTKYVG QKRFSLEGGE TVIALLDRVL AEAADQDLDE
     VVIGMPHRGR LNVLANIVGK PYAKIFNEFE GNIDPGTAQG SGDVKYHLGA DGTFTSPSGH
     EIAVSLTANP SHLEAVNPVL EGIVRAKQDK LDKGDDGFTV LPVLMHGDAA FAGQGVVAET
     LNVSQLRGYR TGGTVHVVVN NQVGFTTSPS SSRSSLYCTD IARMISAPIF HVNGDDPEAC
     VRVAELAVQY RREFRKDVVI DMVCYRRRGH NEADNPSFTQ PMMYDIIDAK RSVRKLYTEA
     LVGRGDITLT DAEAALKDFQ AQLEKVFVET RDASDKAAPQ HEIERETPSQ QVTTAIRAEV
     IKRIAEAYAN PPEGFTLHPR LKPQIDRRVA MASSGKVDWA TAELFAFGSL VMDGRTVRLS
     GQDSRRGTFT QRHATLIDRN TGEEYTPLKQ LGEDQAPFFP YDSLLSEYAA VGFEYGYSVA
     REDALVCWEA QFGDFVDGAQ TVIDEFISAG EAKWGQRSAV TLLLPHGYEG QGPDHSSARP
     ERFLQLCAEN NMTVAMCSSP ANYFHLLRRQ GLSPVRRPLI AMTPKSLLRL KAAVSELDDF
     TTGTFAPVLP DLSADAGKVT RVLLCAGKIY YDLVAEREKS GRDDVAIVRV EQLYPLPAAE
     IRAQLATYRD AEVVWVQEEP ANQGGWPFMA LNLPEHLEGR GLRLASRRAS ASPAVGSLSV
     HEAQQREVVT TAFG
//
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