ID A0A0M2K0H7_9MYCO Unreviewed; 1263 AA.
AC A0A0M2K0H7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:KKF02377.1};
GN ORFNames=WN67_08860 {ECO:0000313|EMBL:KKF02377.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF02377.1, ECO:0000313|Proteomes:UP000034150};
RN [1] {ECO:0000313|EMBL:KKF02377.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKF02377.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-2015) 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=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 -!- 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:KKF02377.1}.
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DR EMBL; LAUZ02000031; KKF02377.1; -; Genomic_DNA.
DR RefSeq; WP_046362655.1; NZ_LAUZ02000031.1.
DR AlphaFoldDB; A0A0M2K0H7; -.
DR STRING; 1807.MOBUDSM44075_00483; -.
DR PATRIC; fig|1807.13.peg.3020; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000034150; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KKF02377.1};
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 912..1111
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 22..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 822..849
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 139535 MW; E38A7841501E5144 CRC64;
MNSPSPFGQN EWLVEEMYRK FREDPSSVDP SWHEFLVDYS PEPTTDASSA PARANGSSTR
SSGPVSPPEP APAPPPKTAS SNGAAKATPA QKAPEKPAAK APEKTQAAKT DVKAPEKAPE
KKAPEKSAPN SDGGDETQVL RGAAAAVVKN MSASLDVPTA TSVRAIPAKA MIDNRIVINN
HLKRTRGGKI SFTHLLGYAI VQAVKKFPNM NRHFAEVDGK PNAITPAHTN LGLAIDLQGK
NGSRQLVVAS IKNCETMRFG QFIAAYEDIV RRARDGKLTA EDFAGVTISL TNPGTIGTVH
SVPRLMQGQG AIIGAGAMEY PAEFQGASEE RINEVGIGKL MTLTSTYDHR IIQGAESGDF
LRTIHQLLLD DEFYDEIFRE LGIPYEPVRW RIDNPDSIED KNARVIELIA AYRNRGHLMA
DIDPLRLDNT RFRSHPDLDV NTHGLTLWDL DREFKVNGFA GKTHKKLRDV LGLLRDAYCR
HVGVEYTHIL EPEQQQWLQE RIEVKHEKPT VAEQKYILSK LNAAEAFETF LQTKYVGQKR
FSLEGAETVI PMMDAAIDQA AEHGLHEVVI GMPHRGRLNV LANIVGKPYS QIFTEFEGNL
NPSQAHGSGD VKYHLGASGT YLQMFGDNDI AVSLVANPSH LEAVDPVLEG IVRAKQDMLD
TGEETNGSND FTVVPMMLHG DAAFAGQGVV AETLNLALLR GYRTGGTIHI IVNNQIGFTT
SPYDSRSSEY CTDVAKMIGA PIFHVNGDDP EAAVWVAKLA MDFRQKFKKD VVIDMLCYRR
RGHNEGDDPS MTQPNMYDVI DTKRGVRKTY TEALIGRGDI SMKEAEDALR DYQGQLERVF
NEVRELEKHA VEPSHSVESD QMVPAGMTTA VDKSLLARIG DAHLAFGEDF NVHPRVKPVL
EKRREMAYEG KVDWAFAELL ALGTFLAEGK TIRLTGQDTR RGTFTQRHSV IIDRKTGKEF
TPLDLLTVDS DGNPTGGRFM VYDSALSEYA AVGFEYGYSV GNPKALVLWE AQFGDFVNGA
QSIIDEFISS GEAKWGQLSD VVLLLPHGHE GQGPDHTSAR IERFLLLWAE GSMTIAMPST
PANYFHLLRR HGLDGIQRPL IVATPKSMLR NKAAVSDLKD FTEQKFRSVL EEPTYDEGDG
DRSKVTRILL TSGKLYYELA ARKTKDKRED VAIVRVEQLA PLPRRRLAET LDRYPNAKEK
FWVQEEPANQ GAWPTMGLTL PELLPDHLAG IKRISRRAMS APSSGSSKVH AVEQQEIIDE
AFA
//
