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 KGD_MYCUA               Reviewed;        1238 AA.
A0PVU7;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 1.
28-MAR-2018, entry version 76.
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=MUL_4500;
Mycobacterium ulcerans (strain Agy99).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=362242;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Agy99;
PubMed=17210928; DOI=10.1101/gr.5942807;
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
"Reductive evolution and niche adaptation inferred from the genome of
Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
Genome Res. 17:192-200(2007).
-!- 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: 2-oxoglutarate + glyoxylate = 2-hydroxy-3-
oxoadipate + CO(2).
-!- CATALYTIC ACTIVITY: 2-oxoglutarate = succinate semialdehyde +
CO(2).
-!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
-!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
succinyldihydrolipoyl)lysine.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000250};
-!- ENZYME 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}.
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EMBL; CP000325; ABL06466.1; -; Genomic_DNA.
RefSeq; WP_011742065.1; NC_008611.1.
ProteinModelPortal; A0PVU7; -.
SMR; A0PVU7; -.
EnsemblBacteria; ABL06466; ABL06466; MUL_4500.
KEGG; mul:MUL_4500; -.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OMA; IDMVCYR; -.
OrthoDB; POG091H03SK; -.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
Proteomes; UP000000765; 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.
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; 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; Complete proteome;
Decarboxylase; Lyase; Magnesium; Metal-binding;
Multifunctional enzyme; Oxidoreductase; Thiamine pyrophosphate;
Transferase; Tricarboxylic acid cycle.
CHAIN 1 1238 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310724.
REGION 1 41 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 42 94 Linker.
REGION 95 343 Succinyltransferase E2.
REGION 344 1238 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 548 549 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 613 615 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 656 658 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 1100 1103 Allosteric activator. {ECO:0000250}.
REGION 1160 1161 Allosteric activator. {ECO:0000250}.
COILED 794 824 {ECO:0000255}.
COMPBIAS 48 119 Ala-rich.
ACT_SITE 322 322 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 656 656 Magnesium. {ECO:0000250}.
METAL 689 689 Magnesium. {ECO:0000250}.
METAL 691 691 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 588 588 2-oxoglutarate. {ECO:0000250}.
BINDING 613 613 2-oxoglutarate. {ECO:0000250}.
BINDING 963 963 Thiamine pyrophosphate. {ECO:0000250}.
BINDING 1031 1031 2-oxoglutarate. {ECO:0000250}.
BINDING 1049 1049 Allosteric activator. {ECO:0000250}.
BINDING 1065 1065 Allosteric activator. {ECO:0000250}.
BINDING 1153 1153 Allosteric activator. {ECO:0000250}.
SEQUENCE 1238 AA; 136742 MW; B9A7DB3108194D2A CRC64;
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTQEATE PAVVKPAAAP
AKPAPAPAPA KPAAGPPAAG NGSPAAAPSA KPAAAPAKAP APPPAEGDEM QVLRGAAAAV
VKNMSASLDV PTATSVRAVP AKLLIDNRIV INNQLKRNRG GKISFTHLLG YALVQAVKKF
PNMNRHYLDV DGKPNAVTPA HTNLGLAIDL QGKDGKRALV VAGIKRCETM RFAQFVTAYE
DIVRRARDGK LTAEDFSGVT ISLTNPGTIG TVHSVPRLMA GQGAIIGVGA MEYPAEFQGA
SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHQM LLADEFWDEI FRELSIPYLP
VRWRPDNPDS IVDKNARIIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD LDVCTHGLTL
WDLDRSFKVG GCFAGPQNMK LRDVLSILRD TYCRHVGVEY THILEPEQQQ WLQQRVEAKH
VKPTVAQQKY VLSKLNAAEA FETFLQTKYV GQKRFSLEGA ESVIPMMDAA IDQCAEYGLD
EVVIGMPHRG RLNVLANIVG KPYSQIFSEF EGNLNPSQAH GSGDVKYHLG ATGVYLQMFG
DNDIQVSLTA NPSHLEAVDP VLEGLVRAKQ DLLEHGETDT ENQRAFSVVP MMLHGDAAFA
GQGVVAETLN LANLPGYRVG GTIHIIVNNQ IGFTTAPEYS RSTEYCTDVA KTIGAPIFHV
NGDDPEACVW VARLAVDFRQ RFNKDVIIDM LCYRRRGHNE GDDPSMTNPR MYDVVDTKRG
VRKSYTEALI GRGDISIKEA EDALRDYQGQ LEQVFNEVRE LEKHGAQPSE SVESDQMIPA
GLATAVDKSL LARIGDAFLA VPDGFTTHPR VQPVLEKRRE MAYEGKIDWA FAELLALGSL
VAEGKLVRFS GQDTRRGTFS QRHSVIIDRH TREEFTPLQL LTTNKDGSPT GGKFLVYDSP
LSEYAAVGFE YGYTVGNPDA VVLWEAQFGD FVNGAQSIID EFISSGEAKW GQLSNVVLLL
PHGHEGQGPD HTSGRIERFL QLWAEGSMTI AMPSTPSNYF HLLRRHALDG IQRPLIVFTP
KSMLRNKAAV SDIKDFTEIK FRSVLEEPTY EDGVGDRNLV NRILLTSGKI YYEMVARKAK
DKREDVAIVR VEQLAPLPRR RLRETLDRYP NAKEFFWVQE EPANQGAWPR FGLELPELLP
EKLSGVKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG


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