ID A0A0F0GSD7_9ACTN Unreviewed; 1289 AA.
AC A0A0F0GSD7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:KJK45486.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:KJK45486.1};
GN Name=kgd {ECO:0000313|EMBL:KJK45486.1};
GN ORFNames=UK14_26005 {ECO:0000313|EMBL:KJK45486.1};
OS Streptomyces sp. NRRL F-4428.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK45486.1, ECO:0000313|Proteomes:UP000033569};
RN [1] {ECO:0000313|EMBL:KJK45486.1, ECO:0000313|Proteomes:UP000033569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK45486.1,
RC ECO:0000313|Proteomes:UP000033569};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK45486.1}.
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DR EMBL; JYJI01000251; KJK45486.1; -; Genomic_DNA.
DR RefSeq; WP_045323676.1; NZ_JYJI01000251.1.
DR PATRIC; fig|1609137.3.peg.6312; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000033569; 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 Lyase {ECO:0000313|EMBL:KJK45486.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033569};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 941..1134
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 140126 MW; B2D05DC3883C6210 CRC64;
MSPQSPSNSS TTTDAAEGGK NPASGFGANE WLVDEIYQQY LQDPQSVDRA WWDFFADYKP
GGAAAPVTSA GPEKSTPTDG ASAQAATAAA GTPQAADAAT GAADAAPAPS ATPTPPPVSA
PAPAPAIPSG APAVTVTSQA PAAAPAAPAP ASVAPQKAAP TAEAPAGPEL VTLRGPAAAV
AKNMNASLDV PTATSVRAVP VKLLFDNRIV INNHLKRARG GKISFTHLIG YAMVQAIKAM
PSMNHSFAEK DGKPTLVKPD HVNFGLAIDL VKPNGDRQLV VAGIKKAETL NFFEFWQAYE
DIVRRARVGK LTMDDFTGVT CSLTNPGGLG TVHSVPRLMP GQSVIMGVGS MDYPAEFQGT
SQDTLNKLGI SKVMTLTSTY DHRVIQGAAS GEFLRIVANL LLGEEGFYDA VFESLRIPYE
PVRWNRDIDA SHDDDVTKAA RVFELIHSYR VRGHVMADTD PLEYKQRKHP DLDITEHGLT
LWDLEREFAV GGFSGKSMMK LRDILGVLRD SYCRTTGVEF MHIQDPKQRR WIQDRIERPH
TKPEREEQLR ILRRLNAAEA FETFLQTKYV GQKRFSLEGG ESVIPLLDAV IDSAAEARLE
EVVIGMAHRG RLNVLANIVG KSYAQIFREF EGNLDPKSMH GSGDVKYHLG AEGTFTGLDG
EQIKVSLVAN PSHLEAVDPV LEGVARAKQD IINKGGTDFT VLPVALHGDA AFAGQGVVAE
TLNMSQLRGY RTGGTVHVVI NNQVGFTAAP ESSRSSMYAT DVARMIEAPI FHVNGDDPEA
VVRVARLAFE FRQAFNKDVV IDLICYRRRG HNESDNPAFT QPLMYDLIDK KRSVRKLYTE
SLIGRGDITL EEAEQALQDF QGQLEKVFAE VREAATQPAA ASPAAPGTSA VFPVAVNTAI
SQDVVKRIAE SQVSIPEGVT VHPRLLPQLQ RRAAMIDEGT IDWGMGETLA FGSLLMEGTP
VRLSGQDSRR GTFGQRHAVL IDRETGEDYT PLLYLSDDQA RYNVYDSLLS EYAAMGFEYG
YSLARPDALV LWEAQFGDFV NGAQTVVDEF ISSAEQKWGQ TSGVTLLLPH GYEGQGPDHS
SARPERFLQM CAQDNMTVAM PTLPSNYFHL LRWQVHNPHH KPLIVFTPKS MLRLKAAASK
AEEFTSGSFR PVIGDSTVDP NAVRKVVFCA GKVYYDLEAE REKRGITDTA IIRIERLYPL
PGAELQAEIA KFPNAAKYIW AQEEPANQGA WPFIALNLID HLDLAVGAEV PAGERLRRIS
RPHGSSPAVG SAKRHQAEQQ QLINEVFEA
//
