ID   G2P237_STRV4            Unreviewed;      1281 AA.
AC   G2P237;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-JAN-2026, entry version 67.
DE   RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme {ECO:0000256|ARBA:ARBA00020204};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE            EC=2.2.1.5 {ECO:0000256|ARBA:ARBA00013148};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE            EC=4.1.1.71 {ECO:0000256|ARBA:ARBA00012226};
DE   AltName: Full=2-hydroxy-3-oxoadipate synthase {ECO:0000256|ARBA:ARBA00029773};
DE   AltName: Full=2-oxoglutarate carboxy-lyase {ECO:0000256|ARBA:ARBA00030696};
DE   AltName: Full=2-oxoglutarate decarboxylase {ECO:0000256|ARBA:ARBA00032880};
DE   AltName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000256|ARBA:ARBA00032625};
DE   AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase {ECO:0000256|ARBA:ARBA00033243};
GN   ORFNames=Strvi_1610 {ECO:0000313|EMBL:AEM81350.1};
OS   Streptomyces violaceusniger (strain Tu 4113).
OC   Bacteria; Bacillati; 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}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 4113 {ECO:0000313|EMBL:AEM81350.1};
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(+) = succinate semialdehyde + CO2;
CC         Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71;
CC         Evidence={ECO:0000256|ARBA:ARBA00049135};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00052761};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + 2-oxoglutarate + H(+) = 2-hydroxy-3-oxoadipate +
CC         CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00047721};
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; succinate
CC       from 2-oxoglutarate (transferase route): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005053}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC       CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004813}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC       subfamily. {ECO:0000256|ARBA:ARBA00007702}.
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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:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
DR   GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
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   FunFam; 3.30.559.10:FF:000011; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.11610:FF:000002; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.970:FF:000018; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 1.10.287.1150:FF:000003; 2-oxoglutarate dehydrogenase, E1 subunit; 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; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 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   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00022793};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008703};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..111
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..134
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..146
FT                   /note="Pro 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
//