ID G8S0B7_ACTS5 Unreviewed; 1246 AA.
AC G8S0B7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:AEV88425.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:AEV88425.1};
GN Name=sucA {ECO:0000313|EMBL:AEV88425.1};
GN OrderedLocusNames=ACPL_7545 {ECO:0000313|EMBL:AEV88425.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV88425.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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; CP003170; AEV88425.1; -; Genomic_DNA.
DR AlphaFoldDB; G8S0B7; -.
DR STRING; 134676.ACPL_7545; -.
DR KEGG; ase:ACPL_7545; -.
DR PATRIC; fig|134676.3.peg.7467; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000005440; 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 ECO:0000313|EMBL:AEV88425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 901..1094
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 136893 MW; 056330C4F5B1D69E CRC64;
MTNTVKEANA AVSTQQTSQD NPLADFGPNE WIVDEMYQRY LADPTSVDPA WHDFFADYKP
ATASGSIVTP DEATAANATK SAAKAGTDAP AAATVAPAKP VTPPAPAAKK AEPVKAAPKP
AAAAQPAPAG AKTTVLRGVA GKIVQNMEAS LQVPTATSVR AVPAKLMIDN RIVINNHLSR
GRGGKVSFTH LIGWALVRAV VAHPEMNNIY AEVDGKPTLV QPEHINLGIA IDLAKKDGSR
TLVVPSIKNC EQMDFRQFWQ AYEDVVRRAR RNELTMDDYA GTTISLTNPG GIGTVHSIPR
LMNGQSAIIG VGALEYPAPY AGMSDETLTD HGVSKVTTLT STYDHRVIQG AQSGEFLKVM
HELLLGGRDF YDEIFTSLRI PYEPVRWVRD VAHTSEGQID KAARVIELIH AYRVRGHLMA
DTDPLEFTIR KHPDLDVLQH GLTLWDLDRT FPVGGFAGKQ KMKLRDVLGV LRDSYCRRIG
IEYMHIQDPE ERRWVQERIE VKYAKPDTDE QKQILLRLNR AEAFETFLQT KYVGQKRFSL
EGGESLIPLL DAVLQSSAEA GLDEMVIGMA HRGRLNVLTN IVGKPYEKLF NEFEGWMDPK
SAHGSGDVKY HLGQTGKYTT PDGRHSTTVS VVANPSHLEA VDPVLEGIVR AKQDRLDLGL
HGYTVLPVLV HGDAAFAGQG VVAETLNLSQ LRGYRTGGTV HVVVNNQVGF TTAPEYSRSS
MYSTDVARMV EAPIFHVNGD DPEAVVRVAK LAFEYRQTFN KDVVIDMICY RRRGHNEGDD
PSMTNPRMYQ IIDTKRSVRK LYTEELIGRG DITVQDAEEQ LRDYQSRLEE VFKATRDAAG
SPPRPHIIAE EPEPQVATAV EADTVRAVGQ AHIELPEGFT PHKRVQQLLD RRAKMSTDGG
IDWGFGELIA FGSLLAQGVT VRLAGQDSRR GTFTSRHASI VDSRTGKDFL PIASLATGTA
RFFVHDSLLS EYAAMGFEYG YSVENPDALV LWEAQFGDFV NGAQSIVDEF LSSGEVKWGQ
QSSLVLLLPH GMEGQGPDHS SGRPERFLQL CAQDNMRVAN PTTPANYFHL LRRQALSSKR
KPLVVMSPKS LLRHKLAVSS VADFTQGTFQ PVLGDAGVNG QPLDAGSVKR VLFCSGKVYY
DLFQARADRG ITDTAIIRME QIYPLPVDEL KAVLAQYPNA EDFAWVQEEP ANQGAWSFVA
LNLLEHLEGV RLRRISRPAA AAPAVGSAKM HEAEQQALIE ASLPRP
//
