ID A0A0G3AAF2_9ACTN Unreviewed; 1269 AA. AC A0A0G3AAF2; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 22-FEB-2023, entry version 22. DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:AKJ10851.1}; DE EC=4.1.1.71 {ECO:0000313|EMBL:AKJ10851.1}; GN Name=kgd {ECO:0000313|EMBL:AKJ10851.1}; GN ORFNames=ABB07_12750 {ECO:0000313|EMBL:AKJ10851.1}; OS Streptomyces incarnatus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ10851.1, ECO:0000313|Proteomes:UP000035366}; RN [1] {ECO:0000313|EMBL:AKJ10851.1, ECO:0000313|Proteomes:UP000035366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366}; RX PubMed=26159526; RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K., RA Tamura T.; RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces RT the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-e00715(2015). CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase CC complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)- CC succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex CC component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, CC Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; CC Evidence={ECO:0000256|ARBA:ARBA00001267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)- CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA- CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, CC ChEBI:CHEBI:83120; EC=1.2.4.2; CC Evidence={ECO:0000256|ARBA:ARBA00033664}; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011497; AKJ10851.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G3AAF2; -. DR STRING; 665007.ABB07_12750; -. DR EnsemblBacteria; AKJ10851; AKJ10851; ABB07_12750. DR PATRIC; fig|665007.5.peg.2756; -. DR UniPathway; UPA00223; UER00997. DR Proteomes; UP000035366; Chromosome. 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 PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1. DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:AKJ10851.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}; KW Transferase {ECO:0000256|ARBA:ARBA00023315}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 921..1114 FT /note="Transketolase-like pyrimidine-binding" FT /evidence="ECO:0000259|SMART:SM00861" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 64..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1239..1258 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 832..859 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..128 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1269 AA; 138866 MW; 0F21DA194FD7A703 CRC64; MSPQSPSNPS VSTDDQAGKN PAAAFGPNEW LVDEIYQQYL QDPNSVDRAW WDFFADYKPG APATPAAAGT AAAGAAETTS TAAPAQPAVP PAQPAAPAPQ AAAPAAPAAA PKPAAAPAPA PAKPATPAQA PAQPKQAAPV AKAAAAAEGP ELITLRGPAA AVAKNMNASL ELPTATSVRA VPVKLLFDNR IVINNHLKRA RGGKISFTHL IGYAMVQAIK AMPSMNWSFG EKDGKPTLVK PPHVNLGLAI DLVKPNGDRQ LVVAAIKKAE TLNFFEFWQA YEDIVRRARD GKLTMDDFTG VTVSLTNPGG LGTVHSVPRL MPGQSVIMGV GSMDYPAEFQ GTSQDTLNKL GISKVMTLTS TYDHRVIQGA ASGEFLRQVA NLLLGENGFY DDIFEALRIP YEPVRWLKDI DASHDDDVTK AARVFELIHS YRVRGHVMAD TDPLEYRQRK HPDLDIVEHG LTLWDLEREF AVGGFAGKSM MKLRDILGVL RDSYCRTTGI EFMHIQDPKQ RKWIQDRVER GHSKPEREEQ LRILRRLNAA EAFETFLQTK YVGQKRFSLE GGESVIPLLD AVIDSAAESR LDEVVIGMAH RGRLNVLANI VGKSYAQIFR EFEGNLDPKS MHGSGDVKYH LGAEGTFTGL DGEQIKVSLV ANPSHLEAVD PVLEGVARAK QDIINKGGTD FTVLPVAIHG DAAFAGQGVV AETLNMSQLR GYRTGGTVHI VINNQVGFTA APESSRSSMY ATDVARMIEA PIFHVNGDDP EAVVRVARLA FEFRQAFNKD VVIDLICYRR RGHNESDNPA FTQPLMYDLI DKKRSVRKLY TESLIGRGDI TLEEAEQALQ DYQGQLEKVF TEVREATSQP AAVDAQAPQD GFPVTVPTAV SAEVVKRIAE SQVNIPENIT VHPRLQPQLQ RRAAMVEDGT IDWGMGETLA IGSLLLEGTP VRLAGQDSQR GTFGQRHAVL IDRETGEEYT PLQYLSEDQA RLNVYNSLLS EYAAMGFEYG YSLARPESLV MWEAQFGDFT NGAQTVVDEF ISSAEQKWGQ TSGVVLLLPH GYEGQGPDHS SARPERFLQL CAQNNMTVAM PTLPSNYFHL LRWQVHNPHH KPLIVFTPKS MLRLKAAASK AEEFTTGEFR PVIGDSSVDP AAVRKVVFCA GKVYYDLEAE RQKRGATDTA IIRIERLYPL PGAELQAEIK KYPNAEKYLW AQEEPANQGA WPFIALNLID HLDLAVGADV PHGERLRRIS RPHSSSPAVG SAKRHQAEQE QLVREVFEA //