ID A0A076N777_AMYME Unreviewed; 1231 AA.
AC A0A076N777;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:AIJ25852.1};
GN Name=kgd {ECO:0000313|EMBL:AIJ25852.1};
GN ORFNames=AMETH_5760 {ECO:0000313|EMBL:AIJ25852.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ25852.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ25852.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ25852.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009110; AIJ25852.1; -; Genomic_DNA.
DR RefSeq; WP_017984687.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076N777; -.
DR STRING; 1068978.AMETH_5760; -.
DR KEGG; amq:AMETH_5760; -.
DR PATRIC; fig|1068978.7.peg.6185; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000062973; Chromosome.
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 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000062973};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 891..1084
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 42..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 801..828
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1231 AA; 135400 MW; 6CAEA670503D7155 CRC64;
MSSSSPASQF GPNEWLVEEM YDQFLADPSS VDAAWHEFFS DFKPTQTTES KPDAAPAPVR
EQPAKPGNGQ VNQAATAPAA PAQPKPAAKP AAQPAKPAAA KPAAAKPAAA ATKPAAEPES
KQLRGAAAAI AKNMDASLAV PTATSVRAVP AKLMADNRIV INNHLKRTRG GKISFTHLIG
YAMVRALQDF PNMNRHYALV DGKPHAVTPE HVNLGLAIDM KGKDGGRALV VASIKNCENM
TFRQFWQAYE DIVKKARNNK LTADDFAGTT ISLTNPGGIG TNHSVPRLQA GQGAIIGVGA
MQYPAHFEGT SEETLVKLGI SKIMTLTSTY DHRIIQGAES GEYLKRIHEL LLGEDGFYDD
IFTSLRLPYE PVRWVSDIPE GEIDKTARVL ELIDAYRMRG HLMADTDPLN YRQRRHEDLD
VLSHGLTLWD LDREFAVGGF AGQQKMKLRD VLGVLRDSYC RTVGVEYTHI LDPEERRWIQ
DRVEVPHAKP DPNVQKYILS KLNAAEAFET FLQTKYVGQK RFSLEGGETV IPMLDTVLDK
AAEHELDEVV IGMPHRGRLN VLANIVGKPI SQIFQEFEGN LDPGQAHGSG DVKYHLGAEG
KYFRMFGDGE TRVSLTANPS HLETVDPVLE GIVRAKQDIL DKGDSDTGGF SVLPVLLHGD
AAFAGQGVVA ETLNLALLRG YRTGGTVHII INNQVGFTTA PEHSRSSQYA TDVAKMIGAP
IFHVNGDDPE AAHWVAKLAV DYRQAFNKDV VIDMICYRRR GHNEGDDPSM TQPAMYDIID
TKRSVRKTYT ESLIGRGDIS VEEAEAALRD FSSQLEHVFN EVRELEKHPI APSPSVEEEQ
QVPAKVPTAV PAEVIERIGD AFVNVPEGFT PHPRVKPVME RRYKMSREGG VDWAFGELLA
FGSLAMEGRL VRLSGQDSRR GTFTQRHSVL IDRKTGREYA PLQNLAEDQG RVMIYDSALS
EYAAVGFEYG YSVANSDALV LWEAQFGDFV NGAQTVIDEY ISSGEAKWGQ RSDVVLLLPH
GHEGQGPDHT SGRIERFLSL CAEGSMTVAV PSTPANYFHL LRRHALDGIQ RPLIVFTPKS
MLRNKAATSG LEDFTGDSKF MSVIDDAEVE PGKVRKVLLT SGKLYWELVA ERAKRDADDV
AIVRIEQYYP LPKKKLLAAL ERYTGAEVVW VQEEPENQGA WPFFGLHLPR MFPDVLGKLD
VVSRRPMAAP SAGSSKVHEV EQKALIAKAF S
//
