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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_MYCLE               Reviewed;        1238 AA.
Q9CC97;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
23-MAY-2018, entry version 95.
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=ML1095;
Mycobacterium leprae (strain TN).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=272631;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TN;
PubMed=11234002; DOI=10.1038/35059006;
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
Barrell B.G.;
"Massive gene decay in the leprosy bacillus.";
Nature 409:1007-1011(2001).
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAC31476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL583920; CAC31476.1; ALT_INIT; Genomic_DNA.
PIR; A87046; A87046.
RefSeq; NP_301802.2; NC_002677.1.
RefSeq; WP_010908126.1; NC_002677.1.
ProteinModelPortal; Q9CC97; -.
SMR; Q9CC97; -.
STRING; 272631.ML1095; -.
PRIDE; Q9CC97; -.
EnsemblBacteria; CAC31476; CAC31476; CAC31476.
GeneID; 910185; -.
KEGG; mle:ML1095; -.
PATRIC; fig|272631.5.peg.1959; -.
Leproma; ML1095; -.
eggNOG; ENOG4105C7P; Bacteria.
eggNOG; COG0508; LUCA.
eggNOG; COG0567; LUCA.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OrthoDB; POG091H03SK; -.
BioCyc; MLEP272631:G1GT5-1193-MONOMER; -.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
Proteomes; UP000000806; 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; Reference proteome;
Thiamine pyrophosphate; Transferase; Tricarboxylic acid cycle.
CHAIN 1 1238 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310716.
REGION 1 41 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 42 97 Linker.
REGION 98 346 Succinyltransferase E2.
REGION 347 1238 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 550 551 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 615 617 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 657 659 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 1101 1104 Allosteric activator. {ECO:0000250}.
REGION 1161 1162 Allosteric activator. {ECO:0000250}.
COILED 795 825 {ECO:0000255}.
ACT_SITE 325 325 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 657 657 Magnesium. {ECO:0000250}.
METAL 690 690 Magnesium. {ECO:0000250}.
METAL 692 692 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 590 590 2-oxoglutarate. {ECO:0000250}.
BINDING 615 615 2-oxoglutarate. {ECO:0000250}.
BINDING 964 964 Thiamine pyrophosphate. {ECO:0000250}.
BINDING 1032 1032 2-oxoglutarate. {ECO:0000250}.
BINDING 1050 1050 Allosteric activator. {ECO:0000250}.
BINDING 1066 1066 Allosteric activator. {ECO:0000250}.
BINDING 1154 1154 Allosteric activator. {ECO:0000250}.
SEQUENCE 1238 AA; 137020 MW; 62B154E8A1D9A0E8 CRC64;
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTAEPVL TDPTSTDKQP
SATPQAKPAA AADPVASRAK PATTPTVANG TAAGSAAAPA KTTTTPPIEG DELQVLRGAA
AVVVKNMSAS LDVPTATSVR AVPAKLMIDN RTVINNQLKR NRGGKISFTH LLGYALVQAV
KKFPNINRHY AEIDGKPIAV TPAHTNLGLA IDLQGKDGKR SLVVAGIKRC EELRFAQFVT
AYEDIVRRAR DGKLTAEDFA GVTISLTNPG TIGTVHSVPR LMTGQGAIIG VGAMEYPAEF
QGASAERIAE LGIGKLITLT STYDHRIIQG AESGDFLRTI HEMVLSDSFW DEIFRELSIP
YLPVRWRTDN PDSIVDKNAR VMELIAAYRN RGHLMADIDP LRLDNTRFRS HPDLDLLTHG
LTLWDLDRVF KVNGFGGWKY KKLRDVLGLL RDAYCRHIGV EYTHILDPEQ QEWLQQRVET
KNVKPTVAEQ KYILSKLNAA EAFETFLHTK YVGQKRFSLE GAESVIPMMD AAIDQCAKHG
LDEVVIGMPH RGRLNVLANI VGKPYSQIFT EFEGNLNPTL AHSSGDVKYH LGATGLYLQM
FGDNDIQVSL TANPSHLEAV DPVLEGLVRA KQDLLNKDTN GNQDEAFSVV PMMLHGDAAF
AGQGVVAETL NLANLPGYRV GGTIHIIVNN QIGFTTAPEY SRSSEYCTDV AKMIGAPIFH
VNGDDPEACV WVAKLAVDFR QRFKKDVVID MLCYRRRGHN EGDDPSMTNP YMYDVVDTKR
GARKSYTEAL IGRGDISLKE AEDALRDYQG QLERVFNEVR DLEKHGVQPS ESVESDQMIP
AGLSTAVDKA LLARIGDAFL AVPEGFTVHP RVQPVLEKRR EMAYEGKIDW AFAELLALGS
LVAEGKLVRL SGQDTKRGTF SQRHSVIIDR HTGEEFTPLQ LLANNPDGSP TGGKFLVYNS
PLSEYAAVGF EYGYTVGNPD AVVLWEAQFG DFVNGAQSII DEFINSGEAK WGQLSTVVLL
LPHGHEGQGP DHTSGRIERF LQLWAEGSMT FAVPSTPSNY FHLLRRHALD GIKRPLIVFT
PKSMLRNKAA VSDIKDFTEI KFRSVLEEPT YEDSIDDRSK VTRVLLTCGK LYYELAARKI
KDNRDDVAIV RIEQLAPLPR RRLGETLDRY ENAKEFFWVQ EEPANQGAWP RFGLELPELL
PRLTGIKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG


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