ID X5DSW6_9CORY Unreviewed; 1245 AA.
AC X5DSW6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:AHW63762.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:AHW63762.1};
GN Name=sucA {ECO:0000313|EMBL:AHW63762.1};
GN ORFNames=CGLY_06585 {ECO:0000313|EMBL:AHW63762.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63762.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW63762.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63762.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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; CP006842; AHW63762.1; -; Genomic_DNA.
DR RefSeq; WP_038547673.1; NZ_CP006842.1.
DR AlphaFoldDB; X5DSW6; -.
DR STRING; 1404245.CGLY_06585; -.
DR KEGG; cgy:CGLY_06585; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000023703; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AHW63762.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 898..1094
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 20..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 137157 MW; DA7E9688EDE61C14 CRC64;
MNSTNFGQNE WLVDQMYQQF KEDPQSVDPE WRELFNKRPD TVDHASGTPS PSSTTSGNGG
KTAETKSAPA TKTTKATGSV ENKTKSAPKS APATPKKSLS ASVNPIPERV APPAPKSPAE
APTAGEHPLK GAQKSIAKNM DISLEIPTAT TVRDMPAKLM FENRAMVNDH LQSRGKGKIS
FTHIIGWAMV KAVQAHPSMN NSYKVVDGKP VQVTPEHINL GLAIDMVSKN GARNLVVAAI
RECETLTFDG FVDAYEDIVK RARIGKLTMD DFSGVTIQLT NPGGIGTRHS VPRLTRGQGT
IVGVGAMDYP AEFAGASEDR LADMGVGKLV TMTSTYDHRI IQGAESGEFL RDISRLLIND
DFWDDLFSAM SVPYAPVRWS QDLPNIGVDK STRVMQLIEA YRSRGHLIAD IDPLQWTQPG
LPVPDHSDLE IETHGLTLWD YDRSFNVGGF AGREKMTLRE VLATLRRAYT LKVGSEYTHI
LDHDERQWLE EQIEGGQPKL SNPEQKYLLQ TLNSAEAFEN FLQTKYIGQK RFSLEGAESL
IPLLDAAVDS AAEQGLEEVV IGMPHRGRLN VLANIVGKPY SKVFTEFEGN IEPTVAGGSG
DVKYHLGQTG QYTQMFGDND IDITLTANPS HLEAVNPVME GIARAHQDIS TNGHDHPIMP
ILMHGDAAFT GLGIVQETIN LAKLDGYTVG GTVHVVVNNQ IGFTTTPDAG RSTHYVTDLA
KGFDAPIFHV NGDDPESVVW VARLAVEYRR RFGKDVFIDL VCYRRRGHNE SDDPSMTQPE
MYDRIQDRAT VRALYHDTLV GRGELSEEDA QRAADDFQGQ LETVFNQVRE AEKGTAPAEQ
TGIAGSQSLT RGLDTSISRE VLEAVGDAFT GVPEGFNVHQ RVKPVVKRRQ EMTRKGGIDW
AFGELLAFST LAQDGRLVRL AGEDSLRGTF TQRHAVLFDS ETTEPYSPLE KLADESGNGG
SFRAYNSPLT EFAGLGFEYG YSVGNLDAVV AWEAQFGDFV NGGQTIIDQY IASGEAKWGQ
LSSVILLLPH GYEGQGPDHS SARIERFLQM AAEGSMTIAQ PSTPANHFHL LRRHAMGTMR
RPLVVFTPKS MLRNKAATSA VEDFTDVTSF RSVLDDPRLS DSAATHDDIT TVLLCSGKIY
YDLEKKRQED ERDDVAIARV EMLHPLPHNR IKEVLDRYPN AEFRWVQDEP ANQGPWPFIA
LNLPERIEGL KLKRVSRRAQ SSTATGLAKV HKLEQEQLLN EAFAK
//
