ID B0RF83_CLAMS Unreviewed; 1268 AA.
AC B0RF83;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Dehydrogenase complex protein {ECO:0000313|EMBL:CAQ02168.1};
GN OrderedLocusNames=CMS2072 {ECO:0000313|EMBL:CAQ02168.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02168.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ02168.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ02168.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RF83; -.
DR STRING; 31964.CMS2072; -.
DR KEGG; cms:CMS2072; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000001318; 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 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 929..1122
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 53..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 139670 MW; C90133DFB8DEE9BC CRC64;
MTGTGTDDGS TGDFGANEWL VDEMYERFVV DKDSVDRSWW PILENYHTTV IEGREATPAT
GDQTAEAQIP DTESTSAPAT TNTGSPAPTP APASAGQPDA QAQQPATGSQ PAARTTSIAP
KQQPIPAQAP AKAPAKKGQE PTPPGEDEVS PLRGMAKSLA TNMDASLTIP TATSVRTIPA
KLMIDNRIVI NNHLKRARGG KVSFTHLIGW ALIQALKEFP SQNVHYDEVD GKPSVVSPAH
INLGIAIDMP KPDGTRALLV PSIKGAEAMT FGEFLSAYED LVKKARGNKL AAGDFAGTTI
SLTNPGGIGT VHSVPRLMKG QGAIIGAGAL EYPAEFQGSS PKTLVELGIG KTITLTSTYD
HRVIQGAGSG EFLKIVHERL IGQHGFYEDI FAALRIPYDP IQWATDINVD LSERVSKTSR
VQELINAYRV RGHLMADIDP LEYQQRTHPD LEITNHGLTF WDLDREFVTD GFGGRRQALL
RDVLGILRDS YCRTIGIEYM HIQQPDERRW IQGKVEQPYA KPTHDEQMRI LSKLNESEAF
ETFLQTKYVG QKRFSLEGGE STISLLDTLL QGAADHGLDE VAIGMAHRGR LNVLTNIAGK
SYGQIFREFE GTQDPRTVQG SGDVKYHLGT EGTFRGVHGE EMPVYLAANP SHLEAVNGVL
EGIVRAKQDR KPIGSFSVLP ILVHGDASMA GQGVVFETLQ LSQLRAYRTG GTVHIVINNQ
VGFTTPPSES RSSVYSTDVA KSIQAPIFHV NGDDPEAVAR VAHLAFEFRQ EFKKDVVIDL
VCYRRRGHNE GDDPSMTQPL MYNLIEAKRS VRKLYTEALV GRGDITQEEY DAAQKDFQDR
LERAFAETHA AQTSSIPIQT DDAGAVSDLE RPDSQQDDGH GEPETTGVSE AVIHSIGDAH
DNPPQGFSVH PKLQALMRKR LEMSRSGSID WAFGELLAIG SLLLENTPVR LAGQDSRRGT
FVQRHAVLHD RDNGQEWLPL ANLSDRQARF WIYDTLLSEY AAMGFEYGYS VERPDALVLW
EAQFGDFANG AQTIIDEFIS SAEQKWGQRS SVVLLLPHGY EGQGPDHSSA RIERFLQLCA
EQNMTVARPS TPASYFHLLR RQAYSRPRRP LVVFTPKAML RLRGATSDVE AFTSGRFEPV
IDDVRIEDRG AVRRVLLHSG KVHYDLLGEL EKRQDRSIAL VRLEQFYPFP EEQVRRVVES
YPDAEVVWVQ DEPENQGAWP FVHVEFGRVL PDRAVRVVSR PAAASPAAGS SKRHATEQTD
LIARATAE
//
