ID   C9ZA89_STRSW            Unreviewed;      1253 AA.
AC   C9ZA89;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Putative 2-oxoglutarate dehydrogenase {ECO:0000313|EMBL:CBG70083.1};
GN   OrderedLocusNames=SCAB_29781 {ECO:0000313|EMBL:CBG70083.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG70083.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG70083.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG70083.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG70083.1; -; Genomic_DNA.
DR   RefSeq; WP_013000761.1; NC_013929.1.
DR   AlphaFoldDB; C9ZA89; -.
DR   STRING; 680198.SCAB_29781; -.
DR   GeneID; 24314394; -.
DR   KEGG; scb:SCAB_29781; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000001444; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          905..1098
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1253 AA;  137302 MW;  8FC0016B13DB55B5 CRC64;
     MSPQSPSNSS ISTDADQAGK NPAAAFGPNE WLVDEIYQQY LQDPNSVDRA WWDFFADYKP
     GAPAASAPVS TAAAAPAAPA QAAPAAPAAP APAAPKPAAV PAPAVAKPAA AAPAPAKPAA
     AAPAKQAAPA EGPELITLRG PAAAVAKNMN ASLELPTATS VRAVSVKLLF DNRIVINNHL
     KRARGGKISF THLIGYAMVQ AIKTMPSMNW HYAEKDGKPT LVKPPHVNFG LAIDLVKPNG
     DRQLVVAGIK KAETLNFFEF WQAYEDIVRR ARDGKLTMDD FTGVTVSLTN PGGLGTVHSV
     PRLMPGQSVI MGVGSMDYPA EFQGTSQDTL NKLGISKVMT LTSTYDHRVI QGAASGEFLR
     IVANYLLGEG GFYDDIFEAL RIPYEPVRWL KDIDASHDDD VTKAARVFEL IHSYRVRGHV
     MADTDPLEYR QRKHPDLDIT EHGLTLWDLE REFAVGGFSG KSLMKLRDIL GVLRDSYCRT
     TGVEFMHIQD PKQRRWIQDR IERPHSKPER EEQLRILRRL NAAEAFETFL QTKYVGQKRF
     SLEGGESVIP LLDAVIDSAA ESRLDEVVIG MAHRGRLNVL ANIVGKSYAQ IFREFEGNLD
     PKSMHGSGDV KYHLGAEGTF TGLDGEQIKV SLVANPSHLE AVDPVLEGVA RAKQDIINKG
     GTDFTVLPVA LHGDAAFAGQ GVVAETLNMS QLRGYRTGGT VHIVINNQVG FTAAPESSRS
     SMYATDVARM IEAPIFHVNG DDPEAVVRVA RLAFEFRQAF NKDVVIDLIC YRRRGHNESD
     NPAFTQPLMY DLIDKKRSVR KLYTESLIGR GDITLEEAEQ ALQDFQGQLE KVFTEVREAI
     AQPAASAAAD APQDGFPVSV NTAITAETVK RIAESQVNVP DHITAHPRLL PQLQRRAGMV
     EDGTIDWGMG ETLAIGSLLL EGTPVRLAGQ DSQRGTFGQR HAVIIDRETG EEFTPLMYLS
     EDQARLNVYN SLLSEYAAMG FEYGYSLARP ESLVLWEAQF GDFVNGAQTV VDEFISSAEQ
     KWSQTSGVTL LLPHGYEGQG PDHSSARPER FLQMCAQNNM TVAMPTSPSN YFHLLRWQVH
     NPHHKPLVVF TPKSMLRLKA AASKAEEFTS GEFRPVIGDS SVDPNAVKKV VFCAGKVYYD
     LEAERQKRGI TDTAIIRIER LYPLPGAEVQ AEVNKYPNAE KYLWTQEEPA NQGAWPFIAL
     NLIDHLDLAV GADVPHGERL RRISRPHGSS PAVGSAKRHQ AEQEQLVREV FDA
//