ID   G2P237_STRV4            Unreviewed;      1281 AA.
AC   G2P237;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=2-oxoglutarate dehydrogenase, E1 subunit {ECO:0000313|EMBL:AEM81350.1};
GN   ORFNames=Strvi_1610 {ECO:0000313|EMBL:AEM81350.1};
OS   Streptomyces violaceusniger (strain Tu 4113).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=653045 {ECO:0000313|EMBL:AEM81350.1, ECO:0000313|Proteomes:UP000008703};
RN   [1] {ECO:0000313|EMBL:AEM81350.1, ECO:0000313|Proteomes:UP000008703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 4133 {ECO:0000313|Proteomes:UP000008703};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A., Katz L.,
RA   Fiedler H.-P., Keasling J., Fortman J., Woyke T.;
RT   "Complete sequence of chromosome of Streptomyces violaceusniger Tu 4113.";
RL   Submitted (AUG-2011) 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   ---------------------------------------------------------------------------
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; CP002994; AEM81350.1; -; Genomic_DNA.
DR   RefSeq; WP_014054861.1; NC_015957.1.
DR   KEGG; svl:Strvi_1610; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000008703; 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   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          933..1126
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1281 AA;  140390 MW;  5E1BED8FDD72E782 CRC64;
     MSPQSPNTSS VSTDEQDGQG SNPAAAFGPN EWLVDEIYQQ YLQDPNSVDR AWWDFFADYK
     PGQDTGSAVA KPPQGVAASA APAAPAQPAE AKPAVPAAKP AEAKPAAAAP AAPKPAPAQP
     AAPAAKAAPT APAAPAKPAP VKPTPAEPTV SKKEPAGPSV GPELVTLRGP SAAVAKNMNA
     SLELPTATSV RAVPVKLLFD NRIVINNHLK RARGGKVSFT HLIGYAMVQA LKAMPSMNNS
     FTEKDGKPTL VKPEHINLGL AIDLVKPNGD RQLVVAAIKK AETLNFFEFW QAYEDIVRRA
     RSGKLTMDDF TGVTASLTNP GGIGTVHSVP RLMPGQGLIV GVGAMEYPAE FQGTSQDTLN
     KLGISKVMTL TSTYDHRVIQ GAASGEFLRI MNQLLLGEND FFDEIFKALR IPYEPVRWLK
     DIDVSHDDDV TKAARVFDLI HSYRVRGHVM ADTDPLEYRQ RKHPDLDIIE HGLTLWDLER
     EFAVGGFAGK TMMKLRDILG VLRDSYCRTT GIEFMHIQDP KQRKWIQDRV ERNHDKPERE
     EQLRILRRLN AAEAFETFLQ TKYVGQKRFS LEGGESVIPL LDAVLDAAAE SRLDEVVVGM
     AHRGRLNVLA NIVGKSYAQI FREFEGNLDP KSMHGSGDVK YHLGAEGTFT GLDGEQIKVS
     LAANPSHLEA VDPVLEGVVR AKQDIIGKAG TDFTVLPVAL HGDAAFAGQG VVAETLNMSQ
     LRGYRTGGTV HIVINNQVGF TAAPAASRSS MYATDVARMI EAPIFHVNGD DPEAVVRVAR
     LAFEFRQAFN KDVVIDLICY RRRGHNETDN PGFTQPLMYD LIDKKRSVRK LYTESLIGRG
     DITLEEAEQA LQDFQGQLEK VFTEVRDAVS APAPAEVPEP QAEFPVTVQT AVSQEVVKRI
     AESQVNTPDR ITVHPRLFPQ LQRRAAMIED DSIDWGMGET LAIGSLLMEG TPVRLAGQDS
     RRGTFGQRHA VLVDRETGDD YTPLLYLTED QARYNIYDSL LSEYAAMGFE YGYSLARPNA
     LVMWEAQFGD FVNGAQTIVD EFISSAEQKW GQTSGVTLLL PHGYEGQGPD HSSARIERFL
     QLCAQNNMTV AAPTLPSNYF HLLRWQVHNP HHKPLVVFTP KSMLRLKAAA SRTDEFLNGS
     FRPVIGDETV DPAAVRKVVF CSGKVYYDVA AERDKRGAND TAIIRLERLY PLPGTELQAE
     IAKYSGVEKF VWAQEEPANQ GAWPFVALNL IDHLELSVGA DVPAAERLVR VSRPHSSSPA
     VGSNKRHQSE QQALVNEIFE I
//