ID I0UUX4_9MICC Unreviewed; 1238 AA.
AC I0UUX4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EID51677.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:EID51677.1};
GN Name=sucA {ECO:0000313|EMBL:EID51677.1};
GN ORFNames=HMPREF1324_2266 {ECO:0000313|EMBL:EID51677.1};
OS Rothia aeria F0474.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=1125724 {ECO:0000313|EMBL:EID51677.1, ECO:0000313|Proteomes:UP000004863};
RN [1] {ECO:0000313|EMBL:EID51677.1, ECO:0000313|Proteomes:UP000004863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0474 {ECO:0000313|EMBL:EID51677.1,
RC ECO:0000313|Proteomes:UP000004863};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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}.
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:EID51677.1}.
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DR EMBL; AJJQ01000016; EID51677.1; -; Genomic_DNA.
DR RefSeq; WP_006887591.1; NZ_AJJQ01000016.1.
DR AlphaFoldDB; I0UUX4; -.
DR PATRIC; fig|1125724.3.peg.593; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000004863; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EID51677.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 899..1092
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 65..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 135719 MW; FECF3CC1E0793EAE CRC64;
MPNLPDHLVP EEFAGNEWFV EEQYERYQQN KNQVAPSWWP IFESIDKAIS GAPAGANTTE
AVASASTTAT VEKDTPNTAP AAAEAPKKSA AAPAKDAPLT APKADTPSPK AKNVEEIEDK
IVPLRGPAKA VATNMEDSLT VPTATTVRAV PAKLLIENRA AINKYLARTR GGKISFTHII
GYAVIRALAA MPSMNVTYGH DEKGKPIAIH NGHVNFGLAI DLPRPDGTRS LVVPNIKGAE
TLSFLEFWEA YDDIVKRGRA GQLGLEDFTG TTVSLTNPGG IGTVHSVPRL SKGQAAIIGV
GALEYPAEFR GVSDKIISQN AISKVITLTS TYDHRVIQGA GSGEFLKIVE SYLLGAEGFY
DEIFEAIRIP FKPLHWSRDN QVDPDIEVSK VARIQQLIHA YRVHGHLVAQ TNPLGYQVLS
HPDLELEKYG LSLWDLDRVW PTGGFGDKDA LPLRTILERL NEAYAGTLAV EYMYNESPEV
RQWFQDQLEH GYTKPCREEL LRVLNKLVEA EAFENFLQTK YLGQKRFSLE GGESLIPLLD
AIIDKAASKD MNGVAIGMAH RGRLNVLTNI AGKSYAQIFR EFSGTAEPAH GNSSGDVKYH
LGTEGTYTSD SGKQTQVYLA ANPSHLEAVN TVLEGIVRAK QDVLNEQGVE GRPVLPILIH
GDAAFAGQGI VMETLQMANL RGYTTGGTVH IVVNNQIGFT TAPEDGRTAT HATDIARMTK
APVFHVNADD PEAVVRAGRM AFEYRERFGQ DVVINLLCYR RRGHNEADDP SMTQPKMYQI
INEMPSTRTL YARALVGRGD VTQEEADEAL NAYHSKLDAI FAETQTAVPL VHSANVEGIE
LPSSQQGTEV VHGGVTAISR DTFELIANSF GNVPEGFTVH KKLQKLLQQR VEMGKSGKVN
WGMGELLALG SVLLEGTNVR MSGQDVQRGT FVQRHAVLHD HLTDQEWSPL QNLAAEQGTL
RIYNSLLSEY GVMGFEYGYS VERPDSLVVW EAQFGDFANG AQTIIDEFVS SSEQKWGQRS
SLVLLLPHGY EGQGPDHSSA RIERYLQLCA ENNMTVAVPS TPASYFHLLR RHSQHRPYKP
LVVISPKQLL RLKGATSSIE DFTEGSFQPV IGDRSGVNPA EVERLVLVSG RLYYDLEAER
AKRGDTKTAI VTVEQLYPLP EAEIKAQLAL YSNAQDVVWA QDEPANQGQW PFMALNLLPV
IDRPVRLAAR PASASPAAGT GKRHTAEHEV LLQQIFEG
//
