ID A0A0Q5B0Z3_9MICO Unreviewed; 1231 AA.
AC A0A0Q5B0Z3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:KQQ11411.1};
GN ORFNames=ASF46_05815 {ECO:0000313|EMBL:KQQ11411.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ11411.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ11411.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ11411.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ11411.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ11411.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQQ11411.1}.
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DR EMBL; LMNR01000001; KQQ11411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5B0Z3; -.
DR STRING; 1736327.ASF46_05815; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000050868; 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 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:KQQ11411.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 896..1089
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 30..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1231
FT /evidence="ECO:0000313|EMBL:KQQ11411.1"
SQ SEQUENCE 1231 AA; 135281 MW; 5A1C706BDC1A9D3D CRC64;
MEELYEQYSA DKASVDESWW PILERYGQQL AAKAPAAPTA AQPPAEKPAA EKPAAAGPST
SAGATVTHPV TAPQTGAAPA SRTTSKEPKK APIPADAPVG KPVDVDAEAQ EEDVVTPLRG
MAKSLATNMD ASLTIPTATS VRTIPAKLMI DNRIVINNHL RRTRGGKVSF THLIGWALIR
ALKDFPSQNV YYDEPGGKPS VVAPAHVNLG IAIDMPKPDG TRALLVPSIK RADTLSFTAY
LSAYEDLVKR ARGNKLVAGD FAGTTLSLTN PGGIGTVHSV PRLMKGQGCI IGAGALEYPA
EFQGSSEKTL IELGIGKTIT LTSTYDHRVI QGAGSGEFLK IVHELLLGGR GFYEDIFAAL
RIPYDPIHWS TDIAVDLAER VSKTSRVQEL INSFRVRGHL MADVDPLEYV QRSHPDLAIE
SHGLTFWDLD REFVTDGFGG KRQLKLRDIL GILRDSYCRT VGVEYMHIQD PEQRAWMQQK
LERGYEKPGH DEQLRILGRL NEAEAFETFL QTKYVGQKRF SLEGGESLIA LLDAVLQGAA
DEKLDEVAIG MAHRGRLNVL TNIAGKTYGQ IFREFEGTQD PKTVQGSGDV KYHLGTEGVF
RGAGGEEIPV YLAANPSHLE AVNGVLEGIV RAKQDRKPIG TFTTLPILVH GDAAMAGQGV
VVETLQMSQL RAYRTGGTIH ININNQVGFT TPPHEARTSV YSTDGAKTIQ APIFHVNGDD
PEAVVHVGQL AFEYRQRFHR DVVIDLICYR RRGHNEGDDP SMTQPLMYSL IEAKRSVRKL
YTEALVGRGD ISQEEYDRSH QDFQDRLERA FAETHAAQTG AIPVISPDGD SVADLELPDA
QQGGDYPGEP ESTGVKEEVV RLIGDAFNNP PEGFTVHPKL QQLLAKRQEM SRSGSIDWAF
GELLALGSLL IEDTPVRLVG QDTRRGTFVQ RHAVLHDRGN GQEWLPLMNL SEQQARLWIY
DSLLSEYAAM AFEYGYSVER PDSLVLWEAQ FGDFANGAQI VIDEFISSAE QKWGQRSSLV
LLLPHGYEGQ GPDHSSARIE RYLQMCAEQN MTVARPSTPA SYFHLLRRQA YSRPRRPLIV
FTPKAMLRLR GASSPVEDFT AGRFEPVLDD ARIQDASAVK RVLLHAGKVH YDLKAELEKK
PDDGIALVRL EQYYPAPIEG LRAIAERYPD AEFVWVQDEP ENQGAWPFIA LEVAPQLGRP
IRVVSRPSAA SPAAGSAKRH ASEQADLLAR A
//
