ID A0A3R8VY44_9CORY Unreviewed; 1265 AA.
AC A0A3R8VY44;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:RRQ05236.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:RRQ05236.1};
GN Name=kgd {ECO:0000313|EMBL:RRQ05236.1};
GN ORFNames=CXF42_02560 {ECO:0000313|EMBL:RRQ05236.1};
OS Corynebacterium bovis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=36808 {ECO:0000313|EMBL:RRQ05236.1, ECO:0000313|Proteomes:UP000278422};
RN [1] {ECO:0000313|EMBL:RRQ05236.1, ECO:0000313|Proteomes:UP000278422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-2004 {ECO:0000313|EMBL:RRQ05236.1,
RC ECO:0000313|Proteomes:UP000278422};
RA Gulvik C.A.;
RT "Twenty Corynebacterium bovis Genomes.";
RL Submitted (JAN-2018) 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:RRQ05236.1}.
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DR EMBL; PQNQ01000004; RRQ05236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8VY44; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000278422; 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 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:RRQ05236.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000278422};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:RRQ05236.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 918..1114
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 21..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 139024 MW; D7DC5B7EF0213D78 CRC64;
MSSANFGQNE WLVDQMYQQY KEDPSSVDPE WRTLFEKDEP QTATSAAGGT SGAGTDDATG
STTTAATGGT TPRRGSEGHG IETRGMNAAA AADSTRPGKP AVTPGPGGRA AAQEPSNHGR
SAQPIPQRVA PPEPKHPVER PEPGEKTIKG AARAVVKNMD QSLSIPTATS VRDMPAKLMF
ENRSMINEQL TSRGGGKISF THIIGWALVK AVLAHPDMNN SYAVVDGKPT LVTPEHVNLG
LAIDMTAKNG SRSLVVAAIR ECESLTFDEF VDHYEDIVHR AREGKLTMED FSGVTISLTN
PGGIGTRHSV PRLTEGQGTI VGVGSIDYPA EFAGASEDRL GEMGIGKLVT ITSTYDHRII
QGAESGEFLR TMSRLLINDA FWDEIFIAMK IPYAPVRWSQ DLPNIGVEKS TRVMQLIEAY
RSRGHLVADT DPLQWTQPGL PIPDHSDLNI ESHGLTLWDF DRHFHVGGFA GRETMTLREV
LATLRRAYTL KVGSEYTHIL DKEERLWLQD RIEAGQPRLS GPEQKYLLQK LNSAEAFENF
LQTKYVGQKR FSLEGAESLI PMMDAAIDEA ATLGHDEVVI GMPHRGRLNV LANIVGKPYA
QIFTEFEGNM EPAAAGGSGD VKYHLGAKGH YMQMFGDNEI DVTLTANPSH LEAVNPVMEG
LARAHEDLLA PAEGDHPVMP LLLHGDAAFA GLGIVQETIN LFKLRGYGVG GTVHIVVNNQ
IGFTTTPDAG RSTFYATDLA KGFDCPVFHV NGDDPEAVVW VAKLAVDYRR RFGKDVFIDL
VCYRRRGHNE ADDPSMTQPQ MYDIIHDRPT VRALYTDTLI GRGDLSEEDA ERVARDFHDQ
LETVFNEVRQ AEKGATPAKQ TGIAGSQELS HGLDTSVTKE EIARIGDYFS NLPEGFNAHQ
RVKPVIKRRL EMSRSGNIDW GFGELLAFGS LVDGGTLVRL SGEDSLRGTF TQRHAVLYDS
EMSNHYNPLQ ALAEDSGRGG SFRAYNSALT EYAGMGFEYG YSVGNPDALV AWEAQFGDFA
NGAQTIIDEY VSSGEAKWGQ ISSVVLLLPH GYEGQGPDHS SARIERFLQL CAEGSMTVAQ
PSTPANYFHL LRRHVLGSLK RPLVVFTPKS MLRNKAATSS IEEFTDVKKF RSVLDDPRFD
SAGDSPRKDI STVLLCSGKI YWDLEKKRQA DGRDDVAIVR IEMLYPIPHN RIKDITERYP
EAEFRWVQDE PANQGPWPFL ALNLPELIPG FTMKRISRRA QTSTATGVAK VHQLEEKQLI
EDAFA
//
