ID A0A0C2B9M9_9ACTN Unreviewed; 1182 AA.
AC A0A0C2B9M9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE Flags: Fragment;
GN Name=kgd {ECO:0000313|EMBL:KIF76664.1};
GN ORFNames=QR77_27920 {ECO:0000313|EMBL:KIF76664.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF76664.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF76664.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF76664.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-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 -!- 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:KIF76664.1}.
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DR EMBL; JTHL01000001; KIF76664.1; -; Genomic_DNA.
DR RefSeq; WP_040024807.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2B9M9; -.
DR STRING; 1576605.QR77_27920; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000031584; 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; 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; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:KIF76664.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 829..1022
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 740..767
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIF76664.1"
SQ SEQUENCE 1182 AA; 130125 MW; 8E86A0A11EAA15F4 CRC64;
APAAPAKPVV TAPAPAQPAK PVTAPVPVTP KPAAEPAGKT GPAQNGNAPA AEAAAEGPEY
VTLRGPSAAV AKNMNLSLEL PTATSVRAVP VKLLFDNRIV INNHLKRARG GKISFTHLIG
YAMVQALKAM PSMNYSFTTK DGKPTLVKPE HVNLGLAIDL VKPNGDRQLV VAGIKKAETL
GFFEFWQAYE DIVRRARTNK LTMDDFSGVT ASLTNPGGIG TVHSVPRLMP GQGLILGVGA
MDYPAEFQGT SQDTLNKLGI SKVMTLTSTY DHRVIQGAAS GEFLRILSQL LLGENDFFDE
IFESLRIPYE PVRWLKDIDA SHDDDVTKAA RVFELIHSYR VRGHVMADTD PLEYRQRKHP
DLDVTEHGLT LWDLEREFAV GGFAGKTMMK LRDVLGVLRE SYCRTTGIEF MHIQDPKQRK
WLQDRVERPR AKPEREEQLR ILRRLNAAEA FETFLQTKYV GQKRFSLEGG ESTIPLLDAV
LDAAAEARLD EVVIGMAHRG RLNVLANIVG KSYAQIFREF EGNLDPKSMH GSGDVKYHLG
AEGTFTGLDG EQIKVSLAAN PSHLETVDPV IEGIARAKQD IINKAGTDFT VLPVALHGDA
AFAGQGVVAE TLNMSQLRGY RTGGTVHIVI NNQVGFTAAP ESARSSMYAT DVARMIEAPI
IHVNGDDPEA VVRVARLAFE FRQAFNKDVV IDLICYRRRG HNEGDNPKFT NPKMYNLIDK
KRSVRKLYTE SLIGRGDITL EEAEQALQDF QGQLEKVFAE VREATSQPAP TQVSDPQPEF
PVSVTTAVSQ EVVKRIAESQ VNIPDHITVH PRLMPQMQRR TASVDDGTID WGMGETLAIG
SLLMEGTPVR LSGQDTRRGT FGQRHAVLVD QETGEDYTPL LYLSEDQARY NVYDSLLSEY
AAMGFEYGYS LARPESLVMW EAQFGDFVNG AQTIVDEYIS AAEQKWGQTS GVTLLLPHGY
EGQGPDHSSA RPERFLQMCA QNNMTVAMPT LPSNYFHLLR WQVHNPHHKP LIVFTPKSML
RLKAAASKAE EFTTGGFRPV IGDPAVAAGT LDPSAVRKVV FTAGKVYYDL EAERENRGVT
DTAILRLERL YPLPGKELQA EIAKFPNADT YLWAQEEPAN QGAWPFIALN LIDHLDLAVG
ADIPGAERLR RISRPHSSSP AVGSAKRHQA EQQQLVNEVF DA
//
