ID D1ACE9_THECD Unreviewed; 1229 AA.
AC D1ACE9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=2-oxoglutarate dehydrogenase, E1 subunit {ECO:0000313|EMBL:ACY99208.1};
GN OrderedLocusNames=Tcur_3675 {ECO:0000313|EMBL:ACY99208.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99208.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY99208.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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}.
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DR EMBL; CP001738; ACY99208.1; -; Genomic_DNA.
DR RefSeq; WP_012853992.1; NC_013510.1.
DR AlphaFoldDB; D1ACE9; -.
DR STRING; 471852.Tcur_3675; -.
DR KEGG; tcu:Tcur_3675; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000001918; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 889..1082
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 794..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 135184 MW; E941ECB469025767 CRC64;
MSTESSRTSA DPRTTDFGAN EWLVDELYQK YLEDPNSVDQ AWWNFFADYQ PDSRPSAQGA
TATAPGGAPS ANGAPAAAAP PVKAPGGDGR AAPPPAKAKP EKAAPAAVPA GAEEVRLKGV
AARTVANMEA SLQVPTATSV RAVPAKLLID NRIVINNHLR RGRGGKVSFT HLLGFAVVRA
LKTMPEMNYS YAEVDGKPVL VKPEHVNLGL AIDLKKEDGQ RQLVVPSIKA AETLDFRQFW
AAYEELVRKA RAGKLTLEDF QGTTISLTNP GTIGTVHSVP RLMPGQGTII GAGAMEYPAE
FAGASDETLA RMGISKVMTL TSTYDHRIIQ GAQSGEFLRR IHQLLLGEDG FYDEIFEALR
IPYEPVRWVQ DISASHEDDV DKVARVHELI HAYRVRGHLM ADTDPLEYKQ RRHPDLDILQ
HGLTLWDLER EFATGGFGGK PKMKLREILG VLRDSYCRTV GIEYMHIQDP EERAWIQQRV
EVPHPKPSRE EQLHILRRLN SAEAFETFLQ TKFVGQKRFS LEGGESLIPL LDSVISAAAR
ARLDEVVIGM AHRGRLNVLA NIVGKSYAQI FSEFEGNLDP RSAQGSGDVK YHLGAEGDFE
SHDGAKIRVS LVANPSHLEA VNPVLEGVVR AKQDILDVGE AGFTVLPVLI HGDAAFAGQG
VVAETLNLSQ LRGYRTGGTV HIVVNNQVGF TTAPQHSRSS VYATDVARMI QAPIFHVNGD
DPEACARVAR LAFEYRQAFK KDVVIDMVCY RRRGHNESDN PSFTQPLMYD LIDAKRSVRK
LYTEALIGRG DITVEEAEQA LRDYQEQLER AFTETREALA KSPEPGSVIK PAEPEHVPID
HGAAGTAIDL ETIKQIIETQ VDLPEGFTVH PRLQPILQRR AQAISDDSVD WATAELLAFG
SLLIDGHPVR LVGQDSRRGT FGQRHAVLVD RKTGEEHTPL KRFDKGVSKF YVHDSLLSEF
AAMGFEYGYS LTRPDALVCW EAQFGDFANG AQSIIDEFVV SGEQKWGQRS SVTLLLPHGY
EGQGPDHSSA RIERFLQLCA QDNVTVVYPT TAANYFHLLR WQVLSQRRKP LIVFTPKSLL
RHKGAASPVA QFTSGAFQPV IGEQGAIEPS GVKRVLITTG KIYYEVVERR AKKGVTDTAV
IRLERLYPLP VAELKAELAK YPADAQLVVV QDEPANQGAW PYLALTLGPL LEGRPLHRIS
RPASSSPAVG SAKMHAIEQE ALLQQVFPD
//
