ID A0A0B5D2E7_9CORY Unreviewed; 1245 AA.
AC A0A0B5D2E7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:AJE32866.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:AJE32866.1};
GN Name=kgd {ECO:0000313|EMBL:AJE32866.1};
GN ORFNames=B842_05075 {ECO:0000313|EMBL:AJE32866.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE32866.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE32866.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) 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}.
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DR EMBL; CP005286; AJE32866.1; -; Genomic_DNA.
DR RefSeq; WP_040085535.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5D2E7; -.
DR STRING; 1223515.B842_05075; -.
DR KEGG; chm:B842_05075; -.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000031524; 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:AJE32866.1};
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 893..1089
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 22..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 137810 MW; 52C2980C3433EB43 CRC64;
MSSASTFGPN EWLVDEMFQQ FQKDPQSVDK EWRELFEKNG APQSAATTAA PRSASQPASV
PSAGPIGSDK NEERKTVVTE QAKAAQATTQ KAAAAPARPA RRKPVSPIDR AANTPKPEAG
STPLRGMFRA IAKNMDESLE VPTATSVRDM PVKLMFENRA MVNDHLARTR GGKISFTHII
GYAMVKAIMA HPDMNVSYEI KDGKPSVVVP ENINLGLAID LPQKDGSRAL VVAAIKETEN
MAFDEFVEAY EDIVERSRVG KLKLDDYQGV TVSLTNPGGI GTRHSVPRLT KGQGTIIGVG
SMDYPAEFAG ASEDRLAELG VGKLVTITST YDHRVIQGAE SGEFLRTMSQ LLVDDKFWDH
IFDRMNIPYA PMRWAQDLPN RGIDKNTRVM QLIEAYRSRG HLIADTNPLQ WIQPGMPVPD
HRDLDIETHG LTIWDLDRTF HVGGFGGKES MTLREVLSRL RAAYTLKVGS EYTHILDRDE
REWLQDRLEA GMPKPTNAEQ KYILQKLNAA EAFENFLQTK YVGQKRFSLE GAEALIPLMD
AAIDTAAGQG LDEVVIGMPH RGRLNVLFNI VGKSLATIFN EFEGNITQGQ IGGSGDVKYH
LGSEGTHIQM FGDGEIKVSL TANPSHLEAV NPVMVGMARA KQDLLDKGDD GFTVMPLMLH
GDASFAGLGI VQETINLYGL RGYTVGGTVH IVVNNQIGFT TTPDSSRSTH YATDVAKGFD
CPVFHVNGDD PEAVVWVGQL ATEYRRRFGK DVFIDLICYR RRGHNEADDP SMTQPLMYDL
IADRKSVRAR YTDDLVGRGD LSAEDAAIAA QDFHDQMESV FNEVKEAEKE GPQEQTGITG
SQELTRGLDT SITREDLVEI GMAYSNAPED FEFHPRVAPV AKRRAESVRE GGIDWGWGEL
IAFSSLANEG RLVRLAGEDS RRGTFTQRHA IPIDPRNGNE FNPLNELAVE KGNGGKFLVY
NSALTEYAGM GFEYGYTMGN SDAVVAWEAQ FGDFANGAQT IIDEYVSSGE AKWGQTSGVI
LLLPHGYEGQ GPDHSSARIE RFLQLCAEGS MTVAQPTTPA NHFHLLRRHA LGTMRRPLVV
FTPKSMLRMK DAASPVEHFT DVKSFQSVYN DPRLVDLEGN IIGDAEKVTT IMLCSGKVYY
ELEKRRKKDK REDIAIVRVE MLHPIPFNRL REAFECYPNA TEVRFVQDEP ANQGPWPFYN
EHLRNLIPGM PEMRRISRRA QSSTATGVTK VHQLEQAQLI DEAFA
//
