ID A0A0X3XJA5_9ACTN Unreviewed; 1259 AA.
AC A0A0X3XJA5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:KUL69985.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:KUL69985.1};
GN Name=kgd {ECO:0000313|EMBL:KUL69985.1};
GN ORFNames=ADL34_30190 {ECO:0000313|EMBL:KUL69985.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69985.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL69985.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69985.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL69985.1}.
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DR EMBL; LLZN01000091; KUL69985.1; -; Genomic_DNA.
DR RefSeq; WP_062668283.1; NZ_LLZN01000091.1.
DR AlphaFoldDB; A0A0X3XJA5; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000052945; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:KUL69985.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 911..1104
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 822..849
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 137797 MW; 4A7E963C348FC0A7 CRC64;
MSPQSPSNAS SISTDADQAG KNPAAAFGAN EWLVDEIYQQ YLQDPNSVDR AWWDFFADYK
PGAAAAPAAA GTAAAGAAET TAPAAAPVPA PAPAAKPAPA KAAAPAAPAA PAAPATKPAP
AAKPAQPKKA EPAAASADGP EFVTLRGPSA AVAKNMNASL ELPTATSVRA VPVKLLFDNR
IVINNHLKRA RGGKISFTHL IGYAMVQAIK AMPSMNHSFA EKDGKPTLVK PDHVNLGLAI
DLVKPNGDRQ LVVAAIKKAE TLNFFEFWQA YEDIVRRARD GKLTMDDFSG VTVSLTNPGG
LGTVHSVPRL MPGQSVIMGV GSMDYPAEFQ GTSQDTLNKL GISKVMTLTS TYDHRVIQGA
ASGEFLRQVA NLLLGENGFY DDIFEALRIP YEPVRWLKDI DASHDDDVTK AARVFELIHS
YRVRGHVMAD TDPLEYRQRK HPDLDITEHG LTLWDLEREF AVGGFSGKSL MKLRDILGVL
RDSYCRTTGV EFMHIQDPKQ RKWIQDRIER PHTKPEREEQ LRILRRLNAA EAFETFLQTK
YVGQKRFSLE GGESVIPLLD AVIDSAAESR LDEVVIGMAH RGRLNVLANI VGKSYAQIFR
EFEGNLDPKS MHGSGDVKYH LGAEGTFTGL DGEQIKVSLT ANPSHLEAVD PVLEGVARAK
QDIINKGGTD FTVLPIALHG DAAFAGQGVV AETLNMSQLR GYRTGGTVHV VINNQVGFTA
APESSRSSMY ATDVARMIEA PIFHVNGDDP EAVVRVARLA FEFRQAFNKD VVIDLICYRR
RGHNESDNPA FTQPLMYDLI DKKRSVRKLY TESLIGRGDI TLEEAEQALQ DYQGQLEKVF
TEVREATSQP STAAPSDPQA EFPVAVNTAV TSEVVKRIAE SQVNIPDHIT VHPRLLPQLQ
RRASMVEDGT IDWGMGETLA VGSLLLEGVP VRLAGQDSQR GTFGQRHAVI IDRETGEEYT
PLQYLSEDQA RLNVYNSLLS EYAAMGFEYG YSLARPEALV MWEAQFGDFV NGAQTVVDEF
ISSAEQKWAQ TSGVVLLLPH GYEGQGPDHS SARPERFLQM CAQNNMTVAM PTSPSNYFHL
LRWQVHNPHH KPLVVFTPKS MLRLKAAAAK AEEFTTGQFQ PVIGDASVDP AAVKKVVFCA
GKVYYDLEAE RKKRGVTDTA IIRIERLYPL PGAELQAEIK KYPNAEKYLW AQEEPANQGA
WPFIALNLID HLDLAVGADV PHGERLRRIS RPHSSSPAVG SAKRHQAEQE QLVHEVFDA
//
