ID A0A0X3S556_9ACTN Unreviewed; 885 AA.
AC A0A0X3S556;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=2-oxoglutarate dehydrogenase subunit E1 {ECO:0000313|EMBL:KUJ36921.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:KUJ36921.1};
GN Name=sucA {ECO:0000313|EMBL:KUJ36921.1};
GN ORFNames=ADL25_30835 {ECO:0000313|EMBL:KUJ36921.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ36921.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUJ36921.1}.
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DR EMBL; LMWH01000249; KUJ36921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3S556; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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-KW.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
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; 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; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KUJ36921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 549..741
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 885 AA; 97125 MW; 5E12C0B1B0D5294C CRC64;
MEEQYERYLH DPTSVDEAWR EFFRSPSAMT PTRHEANTMS DPADGSAVKA VRVAALIHAY
RMRGHLVADT DPLTTHQRDG QSELDITAFG LGTEDLDRVF VVDDFAGRDA MTLRDVLHVL
RESYCGSLGA QYMHIQSFEE RHWVQQRLET THLRPDRAEQ LQILYRLGAA EAFETFLHTK
YVGQKRYSLE GGESAIVLLD ALLRRSIRNG AREAVIGMAH RGRLNVLANI VGKSYAEIFH
EFEDEVDIRS VQGSGDVKYH LGAEGTYRAP DGGAMAVSVV ANPSHLEIVG PVAEGVVRAK
QEVADAGGIS SVLPVLVHGD AAFAGQGVVG ETLNMSQLPG YRTGGTVHII INNQLGFTTS
PAHGRSSTYA TDAAKTVEAP IFHVNGDDPE AVVRVAQLAF DYRQAFHKDV VIDLICYRRH
GHSEVDDPSI TQPAMYDRID ARPSVRRLYA GALVRRGDIT EQQVEGALRD YRERLERAFV
ETQAASASDS PELLAVVGDG ADGVSTAITE ATARRVIASQ TALPPGFTVH PRVLPQLQRR
ITMLDAGTID WATAETLAIG SLLLDGVPVR LAGQDSQRGT FGQRHAVLTD RRTGIEHTPL
NSLGASVDFA PCNSMLSELA ALAFEYGYSL ARPEALVLWE AQFGDFANGA QTVVDEYIAS
SEQKWGQRSG VTLLLPHGLE GQGPDHSSAR VERFLQLCAQ ENMTVAMPSL PGNYFHLLRQ
HALGERRRPL VIFTPKSMLR LKAATSALPE FTTGAFRAVL PDETADPARI ERVLVCSGKV
FYDLAAHRRN SNLSDTAIVR VERLYPFPEH ELSTELGRYP ADAEVLWVQE EPENQGAWPF
LGPRVQRLTK RPIGCISRAQ APAPAVGSAR RHAGEQKELV AAAFR
//
