ID B1MLQ2_MYCA9 Unreviewed; 1238 AA.
AC B1MLQ2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=MAB_1393c {ECO:0000313|EMBL:CAM61479.1};
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS abscessus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM61479.1, ECO:0000313|Proteomes:UP000007137};
RN [1] {ECO:0000313|EMBL:CAM61479.1, ECO:0000313|Proteomes:UP000007137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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}.
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DR EMBL; CU458896; CAM61479.1; -; Genomic_DNA.
DR RefSeq; WP_012296425.1; NZ_MLCG01000002.1.
DR AlphaFoldDB; B1MLQ2; -.
DR KEGG; mab:MAB_1393c; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000007137; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 884..1083
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 47..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 794..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 135969 MW; B62A53614F445EDF CRC64;
MNGSNPQFGQ NEWLVEEMYR RFKEDPSSVD SSWHEFLSDF GAESVAEPAT ASANGHAAPA
PAPTPAAPAP APAPAAAPAP APAVKPASAP STAPAAPKPA APPIPTAEGD EAQVLRGAAA
AVVKNMSASL EIPTATSVRA IPAKLMIDNR IVINNHLKRT RGGKISFTHL LGYAIVQAIK
DFPNMNRHFA EVDGKPVAIT PAHVNLGLAI DLPGKDGNRT LVVAAIKGCE ALGFGQFIAA
YEDIVRRARD GKLTAEDFSG VTISLTNPGT IGTVHSVPRL MRGQGAIIGA GALEYPAEFQ
GASEERIADL GIGKHMTLTS TYDHRIIQGA ESGDFLRTVH QLLLSDDFFD DIFRELGIPY
EPVRWRIDNP DSIVDKNARV LELIAAYRNR GHLMADTDPL RLDKTRFRSH PDLDVLSHGL
TLWDLDREFK VSGFKGQEYM KLRDVLSVLR DAYCRHAGVE YTHILEPEQQ KWLQERIEAK
HDKPTVAEQK YILSKLNAAE AFETFLATKY VGQKRFSLEG AEGVIPMMDA VIDQSAEHGL
DEVVIGMPHR GRLNVLANIV GKPYSQIFTE FEGNLNPALA HGSGDVKYHL GASGTYIQMF
GDNDIEVSLT ANPSHLEAVD PVLEGLVRAK QDLLDVGTDG GRFTVVPLML HGDAAFAGQG
VVAETLNLAN LPGYRTGGTI HIVVNNQIGF TTAPEHSRST EYCTDIAKMI GAPIFHVNGD
DPEACVWVSR LAVDFRQKFN KDVVIDLVCY RRRGHNEGDD PSMTNPQMYE VIDTKRGVRK
TYTEALIGRG DISMKEAEDA LRDYQGQLER VFNEVRDLEK YQQRPSESVE EDQQLPQKLV
TAVDKALLQR IGDAFLSVPE DFSVHPRVKP VLDKRREMAY EGKVDWAFGE LLAFGTLVAE
GKVVRLSGQD SKRGTFTQRH AVIIDRHNGT EFSPLQLVGV DAEGNPTGGR LVVHDSALSE
YAALGFEYGY SVGNPDAMVL WEAQFGDFVN GAQSIIDEFI SSGEAKWGQL SEVVLLLPHG
HEGQGPDHTS GRIERFLQLC AEGSMTVAMP STPANYFHLL RRHALDGITR PMVVFTPKSM
LRNKAAVSDI KDFTDRKFRS VLEEPTYEDG VGDRSKVKRI LLTSGKLYYD LLARKNSDKR
DDVAIVRIEQ LYPIPRYRLE ETLSRYPDDA QYIWVQEEPA NQGAWPTFGL NLPEVVPRLT
GLTKISRRAM SAPSSGSSKV HAVEQQEIID EAFAPTSG
//
