ID A0A1Q3L4H0_9MICO Unreviewed; 1202 AA.
AC A0A1Q3L4H0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN Name=kgd {ECO:0000313|EMBL:OJU40174.1};
GN ORFNames=BGN97_14990 {ECO:0000313|EMBL:OJU40174.1};
OS Microbacterium sp. 69-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1895783 {ECO:0000313|EMBL:OJU40174.1, ECO:0000313|Proteomes:UP000185697};
RN [1] {ECO:0000313|EMBL:OJU40174.1, ECO:0000313|Proteomes:UP000185697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69-10 {ECO:0000313|EMBL:OJU40174.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJU40174.1}.
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; MKRT01000024; OJU40174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3L4H0; -.
DR STRING; 1895783.BGN97_14990; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000185697; Unassembled WGS sequence.
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; 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 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 862..1055
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 56..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 132599 MW; 87A163C502C6C4CC CRC64;
MDELYEQFKQ DRNSVDKEWW PILENYTPDA AAAQTARTPE APSVAPVTAP IPVIGAQPVA
RTTTKPAKQA PIPAQAPKPQ AKEETESAEE DKVTPLRGMP KTLAANMDQS LSVPTATSVR
TIPAKLMIDN RIVINNHMSR TRGGKVSFTH LIGWALIKTL KEFPSQNVFY AEIDGKPSVV
APAHVNLGIA VDVPKPDGTR ALLVPSIKRA DTMTFGEYLL AYEDLIARAR NNKLTAGDFA
GTTVSLTNPG GIGTVHSVPR LMKGQGCIIG AGALNYPAEF QGSSEKVLTE LGIGKVITLT
STYDHRVIQG AGSGEFLKKV HELLIGERGF YDDIFAALRI PYQPIRWNAD IAVDLAERVD
KQARVQELIN SYRVRGHLMA DIDPLEYVQR SHPDLEIESH GLTFWDLDRE FVTGGFGGKR
VMKLREILGV LRDSYCRTLG IEYMHIQDPE QRRWFQEKVE VKYVKPGHDE QLRVLSKLNE
AEAFETFLQT KFVGQKRFSL EGGESLIPLL DEILQGAANA GLDGAAIGMA HRGRLNVLTN
IAGKTYGQVF REFEGSLTPG NQRGSGDVKY HLGTEGTFVA EDGAELPVYL AANPSHLETV
DGVLEGIARA KQDRKPIGTF TWLPILVHGD AAFAGQGVVV ETLQMSQLRG YRTGGTVHIV
VNNQVGFTTL PTDSRTSVYA TDVAKTIQAP IFHVNGDDPE SVIHVAQLAF EYRERFHRDV
VIDLVCYRRR GHNEGDDPSM TQPLMTDLIQ AKRSVRKLYT EALVGRGDIT EEEYDKAKAD
FQNRLEIAFA ETHAAETGAT PIAPELTQVD PQVGEPEITG VPLEVIHLIG DAHANKPDGF
TVHPKLQQQL DKRVEMSRTG GIDWGFGELL AFGSLLVEGT PVRLAGQDSR RGTFVQRHAV
LHDRKNGQEW LPLTNLSASQ GRFFVYDSLL SEYAALGFEY GYSVENTEAL VLWEAQFGDF
VNGAQSVIDE YISAAEQKWG QQSGVVLLLP HGYEGQGPDH SSARMERFLQ LCAQENMTVA
RPSTPASYFH LLRRQAYTRP RKPLIVFTPK AMLRLRGATS QVEDFTQGRF EPVIDDDRAL
DRAAVKRVVV HAGKIHWDLA SELEKNPNPE IALVRLEQFY PTPIDALKAI TDSYPNAELV
WAQDEPENQG AWPFLALAFA EVPGPRQFRV VSRPAAASPS TGSSKVHAAE QAALLKQALT
LD
//
