ID W6K0I7_9MICO Unreviewed; 1166 AA.
AC W6K0I7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=BN11_1110001 {ECO:0000313|EMBL:CCH71824.1};
OS Tetrasphaera australiensis Ben110.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH71824.1, ECO:0000313|Proteomes:UP000035763};
RN [1] {ECO:0000313|EMBL:CCH71824.1, ECO:0000313|Proteomes:UP000035763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH71824.1,
RC ECO:0000313|Proteomes:UP000035763};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH71824.1}.
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DR EMBL; CAJA01000015; CCH71824.1; -; Genomic_DNA.
DR AlphaFoldDB; W6K0I7; -.
DR STRING; 1193182.BN11_1110001; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000035763; 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 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:CCH71824.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035763};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 821..1014
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 128172 MW; 0A2F074823A4373B CRC64;
MRAPERPAPT APNATPRDAA KPAAAKATEE PTVSPIRGAS ARVVTNMETS LEIPTATSVR
SVPAKLLMDN RIVINNHLGR TRGGKVSFTH IIGYALVKAL AQMPEMNNSF TEENGKPALS
VPAHVNLGIA IDLAKPDGTR QLLVPSIKAA ETMDFGRFWS SYEDIIKKAR GGKLVVEDFM
GTTISLTNPG TIGTVLSVPR LMKGQGAIIG VGALEYPAEW QGASTTVLHR HGVSKILTLT
STYDHRIIQG AQSGDLLRII HNLLLGQDGF YDEIFESVRI PYEPVRWVQD IDASHDDDIN
KVARVQELIH SYRVRGHLMA DTDPLEYRQR RHPDLDVTTH GLTLWDLDRH FATGGFGGVP
FLPLRKILGI LRDSYCRGIG IEYMHITDPE QREWIQKKVE VGYAKTSRDE QLRILRRLNA
AEAFETFLQT KFVGQKRFSL EGGESVIALL DRVLSRAAQD GLDEVCIGMP HRGRLNVLAN
IAGKSSGQIF REFEGRQDPR SVQGSGDVKY HLGTEGVFTA ESGDTTKVYL AANPSHLEAV
NPVLEGIARA KQDRINLGGE DFTVLPILLH GDAAFAGQGV VAETLNLSQL RGYRTGGTVH
VVINNQVGFT TAPSSSRSST YCTDVAKMVQ APIFHVNGDD PEACVRVAEL AYEFRKTFQK
DVVVDMVCYR RRGHNEGDDP SMTQPLMYKL IEAKRSVRKL YTESLIGRGD ISQDEAEAAL
RDYQQQLEKV FVETKEALKE ADKPAEPTLA GTDAEGHSGL EPPTAQTSDA TTHSATHTAI
SVEALQRIGD VHLEAPPGFT VHPKLAQLME RRSAMVREGG IDWGMAEIIA FGSLLMDGTP
VRMSGQDSRR GTFVQRHAVL IDKQNAGEWT PLRYLSDNQA KLWIYDSLLS EFAAMGFEYG
YSVERPDALV LWEAQFGDFV NGAQTIIDEF VSSSEQKWAQ RSSVCILLPH GYEGQGPDHS
SARVERFLTL CAEDNMTVTY PSSPANYFHL LRRQAYARPR RPLVVFTPKS MLRLKAASSM
PDEFTTGTFR PVMPDRPAAT PDKHAVTRVL LASGKVVYEL EAEREKRGDT STAILRLEQL
YPLAAAEIAA ALTEYPNAEL VLVQGEPKNQ GAWPFLGLNL PPALAERGYT KPLRVVARAA
SASPATGSSK KHAVEQQALL DAAFGR
//
