ID A0A1S2PY08_9ACTN Unreviewed; 1292 AA.
AC A0A1S2PY08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:OIJ98340.1};
GN Name=kgd {ECO:0000313|EMBL:OIJ98340.1};
GN ORFNames=BIV23_30705 {ECO:0000313|EMBL:OIJ98340.1};
OS Streptomyces monashensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIJ98340.1, ECO:0000313|Proteomes:UP000179642};
RN [1] {ECO:0000313|EMBL:OIJ98340.1, ECO:0000313|Proteomes:UP000179642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 1 {ECO:0000313|EMBL:OIJ98340.1,
RC ECO:0000313|Proteomes:UP000179642};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 1.";
RL Submitted (OCT-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}.
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:OIJ98340.1}.
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DR EMBL; MLYO01000055; OIJ98340.1; -; Genomic_DNA.
DR RefSeq; WP_071384260.1; NZ_MLYO01000055.1.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000179642; 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 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:UP000179642};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 939..1132
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 56..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 140680 MW; 681BDDC1A6B90551 CRC64;
MSPQSPSNPS VSTDDQAGKN PAAAFGPNEW LVDEIYQQYL QDPNSVDRAW WDFFADYKPG
APATPAAAGT AAAGAAGTTS TAPQAQPAAP APQAAAAPAP AAPKPAAAPA PAPAAQAAPA
PAKPAQPAQA PAQPKPAAAA AKPGASTGST GAAGAAPTSA AAAPEGPELV TLRGPAAAVA
KNMNASLELP TATSVRAVPV KLLFDNRIVI NNHLKRARGG KISFTHLIGY AMVQAIKAMP
AMNHAFGEKD GKPTLIKPAH VNLGLAIDLV KPNGDRQLVV AAIKKAETLN FFEFWQAYED
IVRRARDGKL TMDDFTGVTV SLTNPGGLGT VHSVPRLMPG QSVIMGVGSM DYPAEFQGTS
QDTLNKLGIS KVMTLTSTYD HRVIQGAASG EFLRAVANLL LGENGFYDDI FEALRIPYEP
VRWLKDIDAS HDDDVTKAAR VFELIHSYRV RGHVMADTDP LEYKQRKHPD LDITEHGLTL
WDLEREFAVG GFSGKSLMKL RDILGVLRDS YCRTIGIEFM HIQDPKQRKW IQDRVERPHS
KMEREEQLRI LRRLNAAEAF ETFLQTKYVG QKRFSLEGGE SVIPLLDAVI DSAAESRLDE
VVIGMAHRGR LNVLANIVGK SYAQIFREFE GNLDPKSMHG SGDVKYHLGA QGTFTGLDGE
QIKVSLAANP SHLETVDPVI EGIARAKQDI INKGGTDFTV LPVALHGDAA FAGQGVVAET
LNMSQLRGYR TGGTVHIVIN NQVGFTAAPE SSRSSMYATD VARMIEAPIF HVNGDDPEAV
VRVARLAFEF RQAFNKDVVI DLICYRRRGH NESDNPAFTQ PLMYDLIDKK RSVRKLYTES
LIGRGDITLE EAEQALQDYQ GQLEKVFTEV REAVTSQQGT EPAPDPQADF PVAVNTAISS
EVVKRIAESQ VNIPDSFHVH PRLLPQLQRR ATMVEDGTID WGMGETLAVG SLLLEGTPVR
LSGQDSQRGT FGQRHAVLID RESGEEFTPL MYLAEEQARY NVYNSLLSEY AVMGFEYGYS
LARPDALVMW EAQFGDFVNG AQTVVDEYIS AAEQKWGQTS GVTLLLPHGY EGQGPDHSSA
RVERFLQLCA QNNMTVAMPT LPSNYFHLLR WQVHNPHHKP LVVFTPKSML RLKAAASKTE
EFTSGQFRPV IGDASVDPAA VRKVVFVAGK LYYDLEAERQ KRGVTDAAAA ETAIIRLERL
YPLPGSELQA EVNKYPNAEK YLWAQEEPAN QGAWPFIALN LIDHLDLAVG ADVPHGERLR
RISRPHGSSP AVGSAKRHQA EQEQLVREVF EA
//
