ID Q9FBR4_STRCO Unreviewed; 1272 AA.
AC Q9FBR4;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=2-oxoglutarate dehydrogenase {ECO:0000313|EMBL:CAC04496.1};
GN OrderedLocusNames=SCO5281 {ECO:0000313|EMBL:CAC04496.1};
GN ORFNames=SCCB12.05c {ECO:0000313|EMBL:CAC04496.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC04496.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC04496.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939123; CAC04496.1; -; Genomic_DNA.
DR RefSeq; NP_629426.1; NC_003888.3.
DR RefSeq; WP_011030150.1; NZ_VNID01000008.1.
DR AlphaFoldDB; Q9FBR4; -.
DR STRING; 100226.gene:17762932; -.
DR PaxDb; 100226-SCO5281; -.
DR PATRIC; fig|100226.15.peg.5366; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR InParanoid; Q9FBR4; -.
DR OrthoDB; 9759785at2; -.
DR PhylomeDB; Q9FBR4; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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:UP000001973};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 924..1117
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1261
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"
FT COMPBIAS 99..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 139208 MW; FEC500479C586A64 CRC64;
MSPQSPSNSS ISTDTDQAGT AGKNPAAAFG ANEWLVDEIY QQYLQDPNSV DRAWWDFFAD
YKPGAAATPT AAGTVPTDAG STPPAAPAPR AQAPAQPQAA APAPAPAKPA AAAPAAPAAP
ATKPAAAPAK PAAKPQAKAA APAKDAGAAP EGPELVTLRG PAAAVAKNMN ASLELPTATS
VRAVPVKLLF DNRIVINNHL KRARGGKISF THLIGYAMVQ AIKAMPTMNH SFGEKDGKPT
LVKPAHINLG LAIDLVKPNG DRQLVVAAIK KAETLNFFEF WQAYEDIVRR ARDNKLTMDD
FTGVTVSLTN PGGLGTVHSV PRLMPGQSVI LGVGSMDYPA EFQGTSQDTL NKLGISKVMT
LTSTYDHRVI QGAASGEFLR QVANLLLGEN GFYDDIFKAL RIPYEPVRWL KDIDASHDDD
VTKAARVFEL IHSYRVRGHV MADTDPLEYQ QRKHPDLDIT EHGLTLWDLE REFAVGGFAG
KSLMKLRDIL GVLRDSYCRT TGVEFMHIQD PKQRKWIQDR IERSHTKPER EEQLRILRRL
NAAEAFETFL QTKYVGQKRF SLEGGESVIP LLDAVIDSAA ESRLDEVVIG MAHRGRLNVL
ANVVGKSYAQ IFREFEGNLD PKSMHGSGDV KYHLGAEGTF TGLDGEQIKV SLVANPSHLE
AVDPVLEGVS RAKQDIINKG GTDFTVLPVA IHGDAAFAGQ GVVAETLNMS QLRGYRTGGT
VHVVINNQVG FTAAPESSRS SMYATDVARM IEAPIFHVNG DDPEAVVRVA RLAFEFRQAF
NKDVVIDLIC YRRRGHNETD NPAFTQPLMY DLIDKKRSVR KLYTESLIGR GDITLEEAEQ
ALQDYQGQLE KVFTEVREAV SQPASAEPSE PQAEFPVAVN TAITAETVKR IAESQVNIPD
HITVHPRLLP QLQRRAAMVE DGTIDWGMGE TLAVGSLLLD GVPVRLTGQD SQRGTFGQRH
AVVIDRETGD EFTPLLYLSE DQARYNVYNS LLSEYAVMGF EYGYSLARPD ALVMWEAQFG
DFVNGAQTVV DEFISSAEQK WNQTSGVTLL LPHGYEGQGP DHSSARPERF LQLCAQNNMT
VAMPTLPSNY FHLLRWQVHN PHHKPLVVFT PKSMLRLKAA ASKAEEFTTG QFRPVIGDDS
VDPAAVKKVV FTAGKVYYDL DAERKKRGLT DTAIIRIERL YPLPGAELQA EIAKYPNAEK
YLWAQEEPAN QGAWPFIALN LIDHLDLAVG ADVPHGERLR RISRPHGSSP AVGSAKRHQA
EQEQLVREVF EA
//
