ID F5YVW9_MYCSD Unreviewed; 1228 AA.
AC F5YVW9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme {ECO:0000256|ARBA:ARBA00020204};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE EC=2.2.1.5 {ECO:0000256|ARBA:ARBA00013148};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE EC=4.1.1.71 {ECO:0000256|ARBA:ARBA00012226};
DE AltName: Full=2-hydroxy-3-oxoadipate synthase {ECO:0000256|ARBA:ARBA00029773};
DE AltName: Full=2-oxoglutarate carboxy-lyase {ECO:0000256|ARBA:ARBA00030696};
DE AltName: Full=2-oxoglutarate decarboxylase {ECO:0000256|ARBA:ARBA00032880};
DE AltName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000256|ARBA:ARBA00032625};
DE AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase {ECO:0000256|ARBA:ARBA00033243};
GN Name=kgd {ECO:0000313|EMBL:AEF35216.1};
GN OrderedLocusNames=JDM601_1216 {ECO:0000313|EMBL:AEF35216.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35216.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF35216.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF35216.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(2011).
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=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde;
CC Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71;
CC Evidence={ECO:0000256|ARBA:ARBA00001408};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate +
CC CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000320};
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; succinate
CC from 2-oxoglutarate (transferase route): step 1/2.
CC {ECO:0000256|ARBA:ARBA00005053}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC subfamily. {ECO:0000256|ARBA:ARBA00007702}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002329; AEF35216.1; -; Genomic_DNA.
DR RefSeq; WP_013828157.1; NC_015576.1.
DR AlphaFoldDB; F5YVW9; -.
DR STRING; 875328.JDM601_1216; -.
DR KEGG; mjd:JDM601_1216; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000009224; Chromosome.
DR GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009224};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 877..1076
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 23..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 787..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 57..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 135289 MW; D3D660B6407E8505 CRC64;
MSGMSSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY KPGAQHDDGA ATSPPANATA
PPAPPAAPPA APAPTAKPAT TAPAAKPAQS KSPAPAADAE VQVLRGAAAA VVKNMATSLA
VPTATSVRAV PAKLMIDNRI VINNQLKRTR GGKISFTHLL GYALVQAVKQ FPNMNRHFAE
IDGKPNAVTP AHTNLGLAID LHGKDGKRSL VVAGIKEAES LRFAQFVAAY EDIVRRARDG
KLTAEDFAGV TISLTNPGTI GTVHSVPRLM AGQGAIIGVG AMEYPAEFQG ASEQRIAELG
VGKLITLTST YDHRIIQGAE SGDFLRTVHE LLLSDAFWDE IFFELSIPYE PVRWRTDNPD
SVVDKNARVV ELIAAYRNRG HLMADVDPLR LDNTRFRSHP DLDVQSHDLT LWDLDREFKV
EGLPGGDFRK LREILSVLRD AYCRHVGVEY THILEPEQQQ WLQERVEVKH IKPTVAQQKY
ILSKLNAAEA FESFLQTKYV GQKRFSLEGA EAVIPMMDAA IDQCAEYGLD EVVIGMPHRG
RLNVLANIVG KPYSQIFTEF EGNLNPAEAH GSGDVKYHLG STGVYLQMFG DNDIQVSLTA
NPSHLEAVDP VLEGLVRARQ DLLDRGASEN GERPAFSVVP MMLHGDAAFA GQGVVAETLN
MAMLPGYRVG GTIHIIVNNQ IGFTTAPDHS RSSEYCTDVA KMIGAPIFHV NGDDPEACDW
VARLAVDFRQ KFHKDVVIDM LCYRRRGHNE GDDPSMTNPY MYDVIGTKRG VRKSYTEDLI
GRGDISMKEA EDALRDYHGQ LERVFNEIRE LEKHAAQPSE SVESEQQVPR GLNTAVDKAM
LARIGEAFMS IPEGFTVHPR VLPVLERRKE MAYEGKVDWA FAELLALGSL VAEGKLVRLS
GQDTRRGTFS QRHSVIIDHT NGAEFSPLQL LATTPDGTPS GGKFLVYDSP LSEFAAVGFE
YGYTVGNPDA MVLWEAQFGD FVNGAQSIID EFISSGEAKW GQLSNVVLLL PHGHEGQGPD
HTSGRIERFL QLWAEGSMTI AMPSTPSNYF HLLRRHALDG IQRPLIVFTP KSMLRNKAVV
SDIKDFTDVK FRSVLEEPTY GDGEGDRNKV TRVLLTSGKL YYELAARKAK DGREDIALVR
IEQLAPLPKR RLAATLDRYP NAEQFFWVQE EPANQGAWPR FGLELPELLP EKLTGIKRIS
RRAMSAPSSG SSKVHAVEQQ EIIDLAFG
//
