ID A0A0M8T197_9ACTN Unreviewed; 1288 AA.
AC A0A0M8T197;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:KOU49631.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:KOU49631.1};
GN Name=kgd {ECO:0000313|EMBL:KOU49631.1};
GN ORFNames=ADK56_17435 {ECO:0000313|EMBL:KOU49631.1};
OS Streptomyces sp. MMG1522.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU49631.1, ECO:0000313|Proteomes:UP000037713};
RN [1] {ECO:0000313|EMBL:KOU49631.1, ECO:0000313|Proteomes:UP000037713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1522 {ECO:0000313|EMBL:KOU49631.1,
RC ECO:0000313|Proteomes:UP000037713};
RA Noorani M.;
RL Submitted (JUL-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:KOU49631.1}.
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DR EMBL; LGDF01000121; KOU49631.1; -; Genomic_DNA.
DR PATRIC; fig|1415545.3.peg.3735; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000037713; 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 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:KOU49631.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 940..1133
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 16..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 851..878
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 140806 MW; F221F751528A328D CRC64;
MISAVHHLVK RKRAVAAVSS QSPSNSSIST DQAGPGINPA AAFGANEWLV DEIYQQYLQD
PSSVDRAWWD FFADYKPGGS GTADKPAPGA GASGAPVTEA ASAPAAAPAK AAPAAAPAAP
AQPAPAKAAP APAKAAPAPA KPAAEKKPAA APAKPKAKAD ESTEAAGGPE YVTLRGPSAA
VAKNMNASLE LPTATSVRAV PVKLLFDNRI VINNHLKRAR GGKISFTHLI GYAMVQALKA
MPSMNYSFAE KDGKPTLVKP EHVNLGLAID LVKPNGDRQL VVAAIKKAET LNFFEFWQAY
EDIVRRARIG KLGMDDFTGV TASLTNPGGI GTVHSVPRLM PGQGLIMGVG AMDYPAEFQG
TSQDTLNKLG ISKVMTLTST YDHRVIQGAA SGEFLRVLSQ LLLGENEFYD EIFKALRIPY
EPVRWLKDID ASHDDDVTKA ARVFELIHSY RVRGHVMADT DPLEYHQRKH PDLDITEHGL
TLWDLEREFA VGGFAGKTMM KLRDILGVLR ESYCRTTGIE FMHIQDPKQR KWLQDRVERP
RPKPEREEQL RILRRLNAAE AFETFLQTKY VGQKRFSLEG GESVIPLLDA VLDSAAEARL
DEVVIGMAHR GRLNVLANIV GKSYAQIFRE FEGNLDPRSM HGSGDVKYHL GAEGTFTGLD
GEQIKVSLAA NPSHLEAVDP VLEGIARAKQ DIINKGGTDF TVLPVALHGD AAFAGQGVVA
ETLNMSQLRG YRTGGTVHVV INNQVGFTAA PESSRSSMYA TDVARMIEAP IIHVNGDDPE
AVVRVARLAF EFRQAFNKDV VIDLICYRRR GHNEGDNPEF TNPQMYTLID KKRSVRKLYT
ESLIGRGDIT LEEAEQALQD FQGQLEKVFA EVREATSQPA APHVPEPQAA FPVPVETAVS
AEVVKRIAES QVNIPESITV HPRLMPQMQR RAASVENGTI DWGMGETLAI GSLLMEGTPV
RLAGQDSRRG TFGQRHAVLV DQVTGEDYTP LLYLADDQAR YNVYDSLLSE YAAMGFEYGY
SLARPESLVI WEAQFGDFVN GAQTVVDEFI SSAEQKWGQT SGVTLLLPHG YEGQGPDHSS
ARPERFLQMC AQDNMTVAMP TLPSNYFHLL RWQVHNPHHK PLIVFTPKSM LRLKAAASSM
EEFTSGGFRP VIGDSTVKAE NVRKVVFVSG KLFYDLDAER EKRGDTETAI IRLERLYPLP
GAEIQAEIAK YPNAEKYLWA QEEPANQGAW PFIALNLIDH LDLAVGADVP HGERLRRISR
PRGSSPAVGS AKRHQAEQTQ LVNEVFEA
//
