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}.
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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
//