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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]

 KGD_MYCVP               Reviewed;        1243 AA.
A1TDK2;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
22-APR-2020, entry version 83.
RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme;
AltName: Full=2-hydroxy-3-oxoadipate synthase;
Short=HOA synthase;
Short=HOAS;
EC=2.2.1.5;
AltName: Full=2-oxoglutarate carboxy-lyase;
AltName: Full=2-oxoglutarate decarboxylase;
AltName: Full=Alpha-ketoglutarate decarboxylase;
Short=KG decarboxylase;
Short=KGD;
EC=4.1.1.71;
AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase;
Includes:
RecName: Full=2-oxoglutarate dehydrogenase E1 component;
Short=ODH E1 component;
EC=1.2.4.2;
AltName: Full=Alpha-ketoglutarate dehydrogenase E1 component;
Short=KDH E1 component;
Includes:
RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
EC=2.3.1.61;
AltName: Full=2-oxoglutarate dehydrogenase complex E2 component;
Short=ODH E2 component;
Short=OGDC-E2;
AltName: Full=Dihydrolipoamide succinyltransferase;
Name=kgd; OrderedLocusNames=Mvan_4477;
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 /
PYR-1) (Mycobacterium vanbaalenii).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycolicibacterium.
NCBI_TaxID=350058;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 7251 / JCM 13017 / NRRL B-24157 / PYR-1;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
Anderson I.J., Miller C., Richardson P.;
"Complete sequence of Mycobacterium vanbaalenii PYR-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Shows three enzymatic activities that share a first common
step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate,
KG), leading to the formation of an enamine-thiamine-PP intermediate
upon decarboxylation. Thus, displays KGD activity, catalyzing the
decarboxylation from five-carbon 2-oxoglutarate to four-carbon
succinate semialdehyde (SSA). Also catalyzes C-C bond formation between
the activated aldehyde formed after decarboxylation of alpha-
ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-
3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-
hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate
dehydrogenase (ODH) complex, that catalyzes the overall conversion of
2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG
dehydrogenase reactions provide two alternative, tightly regulated,
pathways connecting the oxidative and reductive branches of the TCA
cycle (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate +
CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5;
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde;
Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71;
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + [dihydrolipoyllysine-residue
succinyltransferase]-(R)-N(6)-lipoyl-L-lysine + H(+) =
[dihydrolipoyllysine-residue succinyltransferase]-(R)-N(6)-(S(8)-
succinyldihydrolipoyl)-L-lysine + CO2; Xref=Rhea:RHEA:12188,
Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
ChEBI:CHEBI:83120; EC=1.2.4.2;
-!- CATALYTIC ACTIVITY:
Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Alpha-ketoglutarate dehydrogenase and
decarboxylase activities are inhibited by unphosphorylated GarA, and
allosterically activated by acetyl-CoA, the main substrate of the TCA
cycle. {ECO:0000250}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
from 2-oxoglutarate (transferase route): step 1/2.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
-!- SUBUNIT: Homodimer. The 2-oxoglutarate dehydrogenase (ODH) complex
contains multiple copies of three enzymatic components: 2-oxoglutarate
dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
-!- DOMAIN: Is a fusion protein with two major domains exhibiting
structural features of an E1 and E2 protein, and a short sequence
stretch of E1 localized at the N-terminus, which is connected by a
linker region to the rest of the protein. {ECO:0000250}.
-!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABM15252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; CP000511; ABM15252.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_041306940.1; NC_008726.1.
SMR; A1TDK2; -.
STRING; 350058.Mvan_4477; -.
PRIDE; A1TDK2; -.
EnsemblBacteria; ABM15252; ABM15252; Mvan_4477.
KEGG; mva:Mvan_4477; -.
eggNOG; ENOG4105C7P; Bacteria.
eggNOG; COG0508; LUCA.
eggNOG; COG0567; LUCA.
HOGENOM; CLU_004709_1_0_11; -.
KO; K01616; -.
OrthoDB; 29166at2; -.
BioCyc; MVAN350058:G1G7S-4547-MONOMER; -.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
Proteomes; UP000009159; Chromosome.
GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.559.10; -; 1.
Gene3D; 3.40.50.11610; -; 1.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR032106; 2-oxogl_dehyd_N.
InterPro; IPR011603; 2oxoglutarate_DH_E1.
InterPro; IPR023213; CAT-like_dom_sf.
InterPro; IPR001017; DH_E1.
InterPro; IPR031717; KGD_C.
InterPro; IPR042179; KGD_C_sf.
InterPro; IPR029061; THDP-binding.
InterPro; IPR005475; Transketolase-like_Pyr-bd.
PANTHER; PTHR23152; PTHR23152; 1.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF16078; 2-oxogl_dehyd_N; 1.
Pfam; PF00676; E1_dh; 1.
Pfam; PF16870; OxoGdeHyase_C; 1.
Pfam; PF02779; Transket_pyr; 1.
PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
SMART; SM00861; Transket_pyr; 1.
SUPFAM; SSF52518; SSF52518; 2.
TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
3: Inferred from homology;
Acyltransferase; Allosteric enzyme; Coiled coil; Decarboxylase; Lyase;
Magnesium; Metal-binding; Multifunctional enzyme; Oxidoreductase;
Reference proteome; Thiamine pyrophosphate; Transferase;
Tricarboxylic acid cycle.
CHAIN 1..1243
/note="Multifunctional 2-oxoglutarate metabolism enzyme"
/id="PRO_0000310725"
REGION 1..40
/note="2-oxoglutarate dehydrogenase E1, N-terminal part"
REGION 41..103
/note="Linker"
REGION 104..353
/note="Succinyltransferase E2"
REGION 354..1243
/note="2-oxoglutarate dehydrogenase E1, C-terminal part"
REGION 557..558
/note="Thiamine pyrophosphate binding"
/evidence="ECO:0000250"
REGION 622..624
/note="Thiamine pyrophosphate binding"
/evidence="ECO:0000250"
REGION 661..663
/note="Thiamine pyrophosphate binding"
/evidence="ECO:0000250"
REGION 1105..1108
/note="Allosteric activator"
/evidence="ECO:0000250"
REGION 1165..1166
/note="Allosteric activator"
/evidence="ECO:0000250"
COILED 799..831
/evidence="ECO:0000255"
ACT_SITE 332
/note="Proton acceptor; for succinyltransferase activity"
/evidence="ECO:0000250"
METAL 661
/note="Magnesium"
/evidence="ECO:0000250"
METAL 694
/note="Magnesium"
/evidence="ECO:0000250"
METAL 696
/note="Magnesium; via carbonyl oxygen"
/evidence="ECO:0000250"
BINDING 597
/note="2-oxoglutarate"
/evidence="ECO:0000250"
BINDING 622
/note="2-oxoglutarate"
/evidence="ECO:0000250"
BINDING 968
/note="Thiamine pyrophosphate"
/evidence="ECO:0000250"
BINDING 1036
/note="2-oxoglutarate"
/evidence="ECO:0000250"
BINDING 1054
/note="Allosteric activator"
/evidence="ECO:0000250"
BINDING 1070
/note="Allosteric activator"
/evidence="ECO:0000250"
BINDING 1158
/note="Allosteric activator"
/evidence="ECO:0000250"
SEQUENCE 1243 AA; 136980 MW; 88066C7C78C4835D CRC64;
MNSPSPFGQN EWLVEEMYRK FREDPSSVDP SWHEFLVDYS PEPTNDAPAG NGKPAAAPTA
PPEPASAPAP KPASTNGGAP PAKADTSTTR APEKKPEEKT SPAPKAKTAA PAGVSDDDET
QVLRGAAAAV VKNMSASLDV PTATSVRAIP AKAMIDNRIV INNHLKRTRG GKISFTHLLG
YAIVQAVKKF PNMNRHFAEI DGKPVAVTPA HTNLGLAIDL PGKDGKRSLV VAAIKNCETM
HFGQFIAAYE DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMK GQGAIVGAGA
MEYPAEFQGA SEERIAELGV GKLMTLTSTY DHRIIQGAES GDFLRTIHTL LLDDEFYDEI
FRELGIPHEP VRWRIDNPDS IEDKNARVIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD
LDVNTHGLTL WDLDREFKVN GFAGKTHKKL RDILGLLRDA YCRHIGVEYT HILEPEQQQW
LQERIEVKHE KPTVAEQKYI LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE TVIPMMDAAI
DQCAEHGLDE VVIGMPHRGR LNVLANIVGK PYSQIFTEFE GNLNPSQAHG SGDVKYHLGA
NGTYIQMFGD NDIDVSLVAN PSHLEAVDPV LEGLVRAKQD ILDKGNGPDG FTVVPMMLHG
DAAFAGQGVV AETLNLALLR GYRTGGTIHI IVNNQIGFTT SPYDSRSSEY CTDVAKMIGA
PIFHVNGDDP EACVWVAKLA VDFRQKFKKD VVIDMLCYRR RGHNEGDDPS MTQPTMYDVI
DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLERVF NEVRELEKHA IAPSSSVESD
QMVPAGMSTA VDKSLLARIG DAHLGYPDDF NVHPRVKPVL EKRREMAYEG KVDWAFAELL
ALGTFLAEGK TIRFTGQDTR RGTFTQRHSV IIDRQTGREF TPLDLLTVDS DGNPTGGKFM
AYDSALSEFA AVGFEYGYSV GNPNALVLWE AQFGDFVNGA QSIIDEFISS GEAKWGQLSD
VVLLLPHGHE GQGPDHTSGR IERFLLLWAE GSMTIAMPST PANYFHLLRR HGLDGIHRPL
IVFTPKSMLR NKAAVSDLKD FTEMKFRSVL EEPTYTEGTG DRSKAKRILL TSGKLYYELA
ARKSKEGRDD VAILRLEQLA PLPKRRLAAT LDEYPNAEQY FWVQEEPANQ GAWPTLGLTL
PEVLPEKLAG IKRISRRAMS APSSGSSKVH AVEQQEIIDE AFG


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