ID A0A1L7CWX1_9CORY Unreviewed; 1237 AA.
AC A0A1L7CWX1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:APT90366.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:APT90366.1};
GN Name=kgd {ECO:0000313|EMBL:APT90366.1};
GN ORFNames=CSPHI_04070 {ECO:0000313|EMBL:APT90366.1};
OS Corynebacterium sphenisci DSM 44792.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1437874 {ECO:0000313|EMBL:APT90366.1, ECO:0000313|Proteomes:UP000185469};
RN [1] {ECO:0000313|EMBL:APT90366.1, ECO:0000313|Proteomes:UP000185469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44792 {ECO:0000313|EMBL:APT90366.1,
RC ECO:0000313|Proteomes:UP000185469};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium sphenisci CECT 5990(T) (=DSM
RT 44792(T)), isolated from healthy wild penguins.";
RL Submitted (AUG-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; CP009248; APT90366.1; -; Genomic_DNA.
DR RefSeq; WP_075691604.1; NZ_CP009248.1.
DR AlphaFoldDB; A0A1L7CWX1; -.
DR STRING; 1437874.CSPHI_04070; -.
DR KEGG; csph:CSPHI_04070; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000185469; Chromosome.
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 Lyase {ECO:0000313|EMBL:APT90366.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000185469};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 891..1087
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 44..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 135586 MW; 61CC184AF2D17F61 CRC64;
MSSDMSFGQN EWLVDEIFQR FKKDPQSVDE EWRDYFTRNT SAADVAARSA TGAKAPTSAA
DPAPLAKRAA ATAAEAERTG RRPAKGPEPK TSPQAPAKPK AKASPMAKAA KAEAPEAGQA
QLKGVAKAIA KNMDISLEIP TATSVRDMPA RLMFENRALV NDQLARARGG KISFTHIIGY
AMVKAVMLHP DMNNSYAVVD GKPTIVTPEH INLGLAIDMP GKDGSRALVV AAIRECETLS
FREFVDAYED IVTRARQGKL TGKDFSGVTI SLTNPGGIGT RHSVPRLTKG QGAIIGVGSM
DYPAEFAGAS ADRLAELGVG KLVTITSTYD HRIIQGAESG EFLRTMSTLL VDDKFWDHIF
TSMNVPYTPV RWAQDYPNTG IDKNTRVMRL IEAYRMRGHL LADIDPLRFH APGSQIPDHR
DLDIATHGLS LWDYDRTFNV GGFGGKESMT LREVLSRLRN AYCLKVGTEY MHILDADERE
WLQDRLEGGQ PKPTNAEQKY ILQKLNAAEA FENFLQTKYV GQKRFSLEGA EGLIPMMDAA
IDTAAGAGLD EVVIGMPHRG RLNVLANIVG KPLSQIFTEF EGNMDPAQPG GSGDVKYHLG
TTGRHIQMFG EGEIDVTLTA NPSHLEAVNP VVEGLARAKQ DLLDKGEEGY SVMPVLLHGD
AAFAGLGIVQ ETLNLMDLRG YKVGGTINIV VNNQIGFTTA PDSGRSSYYC TDLAKAYGCP
VFHVNGDDPE ALVWVAQLAV EYRNRFGKDV FIDLVCYRRR GHNEADDPSI TQPLMYDVID
GKEGVRAQYT EDLIGRGDLS EEEAEAARRD FHDQMESVFN EVRAAEGAHP GDQTGIASSQ
PLPHGLETNV DRATLVEMGE YYGNPPEGFT IHKRIRKVAA QRAEMVKSGN VDWATAELLA
LGSIAADGRI VRLAGEDVRR GTFTQRHAVL VDPETAEEYN PLDAYARDAG RGGRFMTYNS
ALTEYAGMGF EYGYTLGNPE AMVLWEAQFG DFANGAQTII DQYVSSGEAK WGQTSKLVLL
LPHGYEGQGP DHSSARIERF LQLCAEGSFT VAQPSEPANY FHLLRRHALS DLHRPLVVFT
PKSMLRNKAA VSAVADFTET AKFESVIDDP AFAEGADRSK VTTVLLCSGK IYWELAKKKE
ADGREDVAIV RLEQLHPVPH NRLRTVLEQY PDAELRWVQD EPANQGPWPF LALQLPELLP
DLPPLTRVSR RAQSSTATGV AKVHAMEEKA LLEQAFE
//
