ID A0A291QFE9_9ACTN Unreviewed; 1261 AA.
AC A0A291QFE9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dihydrolipoamide succinyltransferase component (E2) of 2-oxoglutarate dehydrogenase complex {ECO:0000313|EMBL:ATL30431.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:ATL30431.1};
DE EC=2.3.1.61 {ECO:0000313|EMBL:ATL30431.1};
GN ORFNames=KY5_5413c {ECO:0000313|EMBL:ATL30431.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL30431.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL30431.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL30431.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022685; ATL30431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291QFE9; -.
DR KEGG; sfk:KY5_5413c; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000221011; 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 Acyltransferase {ECO:0000313|EMBL:ATL30431.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ATL30431.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:ATL30431.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 913..1106
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 824..851
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 138580 MW; 45526BF0BB4E6C32 CRC64;
MSSQSPSSSS ISTDQDGQGK DPAAAFGPNE WLVDEIYQQY LQDPNSVDRA WWDFFADYKP
GVGASVAAAP AKPAGDAAAG AAPTTPAAPA KPAAKAAPAA PAAPAAPAAK PAAAAPAPAA
KPAAAKPAAK AEPAKEAPAG PEYVTLRGPS AAVAKNMNAS IEVPTATSVR AVPVKLLFDN
RIVINNHLKR ARGGKISFTH LIGYAMVQAI KAMPSMNYSF VEKDGKPTLV KPEHINFGLA
IDLVKPNGDR QLVVAGIKKA ETLNFFEFWQ AYEDIVRRAR DGKLGMDDFT GVTVSLTNPG
GLGTVHSVPR LMPGQSVIMG VGSMDYPAEF QGTSQDTLNK LGISKVMTLT STYDHRVIQG
AASGEFLRIV ANLLLGEQDF YDEIFKALRI PYEPVRWLKD IDASHDDDVT KAARVFELIH
SYRVRGHVMA DTDPLEYKQR KHPDLDITEH GLTLWDLERE FAVGGFAGKS MMKLRDVLGV
LRDSYCRTTG VEFMHIQDPK QRRWLQDRIE RQHATKPERE EQLRILRRLN SAEAFETFLQ
TKYVGQKRFS LEGGESVIPL LDAVIDSAAE SRLDEVVIGM AHRGRLNVLA NIVGKSYAQI
FREFEGNMDP KSMHGSGDVK YHLGAEGTFT GLDGEQIKVS LAANPSHLET VDPIIEGIVR
AKQDIINKGG TDFTVLPVAL HGDAAFAGQG VVAETLNMSQ LRGYRTGGTV HIVINNQVGF
TAAPESSRSS MYATDVARMI EAPIFHVNGD DPEAVVRVAR LAFEFRQAFN KDVVIDLICY
RRRGHNESDN PAFTQPLMYD LIDKKRSVRK LYTESLIGRG DITLEEAEQA LQDFQGQLEK
VFTEVREATA QPGEAEVPAP EAEFPVKIDT AISQEIVKRI AESQVNIPDR VTVHPRLLPQ
LQRRATMVEE GTIDWGMGET LAIGSLLLEG TPVRLSGQDS RRGTFGQRHA VLIDRATGED
FTPLLYLSED QARYNVYDSL LSEYAVMGFE YGYSLARPEA LVMWEAQFGD FVNGAQTVVD
EYISAAEQKW NQHSGVTLLL PHGYEGQGPD HSSARIERFL QLCAQNNMTV AMPTLPSNYF
HLLRWQVHNP HHKPLVVFTP KSMLRLKAAA SKTEEFTSGG FRPVIGDATV DPAAVRKVVF
CAGKLYYDLE AERTKRGATD TALIRIERLY PLPGAELQAE IAKFPNAEKY LWAQEEPANQ
GAWPFIALNL IDHLDLAVGA DIPHGERLRR ISRPHGSSPA VGSKKRHEQE QEQLVREVFE
A
//
