ID A4FND0_SACEN Unreviewed; 1206 AA.
AC A4FND0;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:CAM05555.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:CAM05555.1};
GN Name=sucA {ECO:0000313|EMBL:CAM05555.1};
GN OrderedLocusNames=SACE_6385 {ECO:0000313|EMBL:CAM05555.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05555.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM05555.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM05555.1; -; Genomic_DNA.
DR AlphaFoldDB; A4FND0; -.
DR STRING; 405948.SACE_6385; -.
DR KEGG; sen:SACE_6385; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000006728; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAM05555.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 865..1058
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 33..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..802
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 132529 MW; D6414CF26CEF84DB CRC64;
MYEQFLHDPT SVDSAWHEFF ADYKPGQATE TTAAATGSAA APKATATAAR VVETNGQTPP
PSATAPSKPK PAEPKPSPQE AAKAAPVKEA PAGEQAKPLR GAAAAIAKNM EQSLTVPTAT
SVRAVPAKLL FDNRIVINNH LKRNKGGKVS FTHLIGYALI RALRNHPDMN RHYGEDAKGK
PAVVTPEHVN LGLAIDMPAK DGSRSLVVAS IKGCEEMTFQ QFWQAYEDII RKARNSALTA
DDFSGTTISL TNPGPSGTNH SVPRLTKGQS AIIGVGAMDY PAEFQGASEQ ALVDMGISKI
VTLTSTYDHR VIQGAESGDF LRTVHQLLLG ENGFYDDIFT SLRIPYEPVR WTRDIPEGAV
DKTARVLELI DAYRTRGHLM ADIDPLNYRQ RRHEDLDVLS HSLTLWDLDR TFAVGGFAGK
ERMKLRDVLG VLRDSYCRTV GVEYMHILEP DEREWLQGRV EKPHTKPEPT EQKYILSKLN
AAEAFETFLQ TKYVGQKRFS LEGAETVVPL LDAVLDTAAA SELDEVVIGM PHRGRLNVLA
NIVGKPISQI FREFEGNLDP GQAHGSGDVK YHLGAEGKYF RMFGDGETKV SLTSNPSHLE
AVDPVLEGIV RAKQDILDKG QEGFTVLPVL LHGDAAFAGQ GVVAETLNLS LLRGYRTGGT
VHVIVNNQVG YTTAPEHSRS SKYSTDVAKM IGAPVFHVNG DDPEACVWVA KLAVEYRQAF
GKDVVIDMVC YRRRGHNEGD DPSMTQPAMY DAIDKMRSVR KTYTEALIGR GDITVEEAEK
ALKDYASQLE HVFNEVRELE KHPPEPSPSV ESEQVVPQGL ATAIPVDTLK RIADAQVNMP
EGFTPHSRVK PVLERRAKMA TEGGIDWAFG ELLAFGSLTM EGRPVRLTGQ DSRRGTFGQR
HSVLIDRKTG AEYTPLQNLS EDQAKFLVYD SALSEFAAMG FEYGYSVANP DALVLWEAQF
GDFFNGAQSI IDEFISSGEA KWGQRSDVVL LLPHGHEGQG PDHSSARIER WLQLCAEGSM
TVAMPSTPAN YFHLLRRHAL DGIHRPLVVF TPKSMLRLKA ATSPVEDFTE GKFTSVIDDP
TQPDPASVRR VVLCTGKLYY ELAAEKAKQG HDDTAVVRLE QLYPLPHRKL GRLLERYSNA
TDVRWVQEEP ANQGAWPFLG LALPELFPER LAGLRRVSRR PMAAPATGMA KVHEVEQAEV
VQGAFA
//
