ID E7NDF6_9ACTO Unreviewed; 1274 AA.
AC E7NDF6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:QCT33690.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:QCT33690.1};
DE SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EFW25781.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:EFW25781.1};
GN Name=sucA {ECO:0000313|EMBL:EFW25781.1};
GN ORFNames=FBF36_09670 {ECO:0000313|EMBL:QCT33690.1}, HMPREF9057_02840
GN {ECO:0000313|EMBL:EFW25781.1};
OS Actinomyces sp. oral taxon 171 str. F0337.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW25781.1, ECO:0000313|Proteomes:UP000005722};
RN [1] {ECO:0000313|EMBL:EFW25781.1, ECO:0000313|Proteomes:UP000005722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:EFW25781.1,
RC ECO:0000313|Proteomes:UP000005722};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCT33690.1, ECO:0000313|Proteomes:UP000310751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:QCT33690.1,
RC ECO:0000313|Proteomes:UP000310751};
RA Collins A.J., Murugkar P., Chen T., Dewhirst F.E.;
RT "Saccharibacteria TM7 and host bacteria genomes.";
RL Submitted (APR-2019) 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; AECW01000522; EFW25781.1; -; Genomic_DNA.
DR EMBL; CP040005; QCT33690.1; -; Genomic_DNA.
DR RefSeq; WP_009398211.1; NZ_GL637938.1.
DR AlphaFoldDB; E7NDF6; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000005722; Unassembled WGS sequence.
DR Proteomes; UP000310751; Chromosome.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase 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-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 Lyase {ECO:0000313|EMBL:QCT33690.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EFW25781.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:QCT33690.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 928..1121
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 22..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 139258 MW; E068E49997249AE7 CRC64;
MPTQDQTSPG FGANEWMVEE MRAAWSADPS SVSPQWRELF ETDPSAGLHR SSNPSNGFAS
AAAGGPRRAT ITPQVASPLR HSSAVQDVTR SDLPPAPPSD TAPPTSPYAQ RLAAHPAHDL
EGDGCEERSV RLKGAAARTA KNMDDSLSMP TATSARAVPA KVLIENRAVI NSHLARTRGG
KVSFTHLIGW AVVESLAEMP SMNVAYGVDE AGKPVLHEPA HVAFGLAIDV PGADGQRRLL
VPSIKQADLM DLSQFVEAYE AIVAKARDNK LDLDDFRGTT VTLTNPGMIG TLHSVPRLMP
GQGLIVGVGS MDYPAAFAGA SPDTLARQAI GKVVTLTSTY DHRVIQGAAS GDFLRLVERK
LLGLDGFWNR AFESLRIPLE PVAWMRDTTY DPELETGKPA RVAELIHAYR QRGHLAADND
PLTYRLRRHP DLDITSYGLS LWDLDRSFPT RGLGGRDRAT LREILKMLRD AYCRTVGVEY
MHIQDPAQRA WWQERLERDW ENIGDEERRR ILTKLEQAEA FETFLQTKYV GQKRFSLEGG
ESLIVALDRL LDAAAHDGLD EVVIGMAHRG RLNVLTNIAG KSYAQVFDEF EGNGVIEGAG
TGDVKYHLGT VGVFSGTDGV STRVSLAANP SHLETVDGVV EGIVRAKQDR IGLGEKGYTV
MPVLVHGDAA FAGQGVVYET LNMSQLPAYR TGGTVHIVVN NQIGFTTGSA SARSTIYATD
LAKGLQVPIF HVNADDPETV ARTARHAYEY RRTFHKDVII DLICYRRRGH NEGDDPSMTQ
PLMYRLIDSL DSTRGVYTSA LVGRGDVTPQ EAQEIAKSYQ DELERIFTEA RLQVTGGKVS
DTDAETTNTS AQDLSDPTKV GVPLSSLEIP YSQQAGIGMM LGWTSAVPRD VVERIGDAQV
SWPESFTVHP KLQAMLSKRR EATREGGIDW GLGELIALGS LLMEGVPIRL VGEDARRATF
AQRHAVLHDH TSGQEWTPLN FLTPDQAPLE IYDSLLSEYA ALAFEYGYSV ERPEGLTMWE
AQFGDFANGA QSVIDEYVTS AAQKWGQRSG LVMLLPHGQE GQGPDHSSAR IERYLQMCAQ
DNMLVAQPST PASYFHLLRE HTYRRPRRPL IVFTPKQLLR LKAACSPVED FTSGTFQPVI
GETDDAVLAA AQKQNVDRVL LCSGRVYYDL LAHRTKIGDT GTAIVRLEQL YPLDASAIAE
ALAPFSGAEL VWVQDEPANQ GMWPYLALNL PTDLTGGVLP TLVSRPEAAA PAVGTAGLHR
AQQEEIIHQA FTRD
//
