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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_MYCTA               Reviewed;        1231 AA.
A5U1U6;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
05-JUN-2019, entry version 74.
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=MRA_1256;
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=419947;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25177 / H37Ra;
PubMed=18584054; DOI=10.1371/journal.pone.0002375;
Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
Wang H., Wang S., Zhao G., Zhang Y.;
"Genetic basis of virulence attenuation revealed by comparative
genomic analysis of Mycobacterium tuberculosis strain H37Ra versus
H37Rv.";
PLoS ONE 3:E2375-E2375(2008).
-!- 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=ABQ72996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; CP000611; ABQ72996.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_003898790.1; NZ_CP016972.1.
SMR; A5U1U6; -.
STRING; 419947.MRA_1256; -.
PRIDE; A5U1U6; -.
EnsemblBacteria; ABQ72996; ABQ72996; MRA_1256.
KEGG; mra:MRA_1256; -.
eggNOG; COG0508; LUCA.
eggNOG; COG0567; LUCA.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OrthoDB; 29166at2; -.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
Proteomes; UP000001988; 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; Complete proteome;
Decarboxylase; Lyase; Magnesium; Metal-binding;
Multifunctional enzyme; Oxidoreductase; Thiamine pyrophosphate;
Transferase; Tricarboxylic acid cycle.
CHAIN 1 1231 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310723.
REGION 1 41 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 42 88 Linker.
REGION 89 337 Succinyltransferase E2.
REGION 338 1231 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 541 542 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 606 608 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 649 651 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 1093 1096 Allosteric activator. {ECO:0000250}.
REGION 1153 1154 Allosteric activator. {ECO:0000250}.
COILED 787 817 {ECO:0000255}.
COMPBIAS 61 113 Ala-rich.
ACT_SITE 316 316 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 649 649 Magnesium. {ECO:0000250}.
METAL 682 682 Magnesium. {ECO:0000250}.
METAL 684 684 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 581 581 2-oxoglutarate. {ECO:0000250}.
BINDING 606 606 2-oxoglutarate. {ECO:0000250}.
BINDING 956 956 Thiamine pyrophosphate. {ECO:0000250}.
BINDING 1024 1024 2-oxoglutarate. {ECO:0000250}.
BINDING 1042 1042 Allosteric activator. {ECO:0000250}.
BINDING 1058 1058 Allosteric activator. {ECO:0000250}.
BINDING 1146 1146 Allosteric activator. {ECO:0000250}.
SEQUENCE 1231 AA; 135902 MW; 96C255612BA12889 CRC64;
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA EPTRVTSPLV
AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE GDEVAVLRGA AAAVVKNMSA
SLEVPTATSV RAVPAKLLID NRIVINNQLK RTRGGKISFT HLLGYALVQA VKKFPNMNRH
YTEVDGKPTA VTPAHTNLGL AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA
RDGKLTTEDF AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA
ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI PYLPVRWSTD
NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR SHPDLEVLTH GLTLWDLDRV
FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ
QKYILSKLNA AEAFETFLQT KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP
HRGRLNVLAN IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS
LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA AFAGQGVVAE
TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT DVAKMIGAPI FHVNGDDPEA
CVWVARLAVD FRQRFKKDVV IDMLCYRRRG HNEGDDPSMT NPYVYDVVDT KRGARKSYTE
ALIGRGDISM KEAEDALRDY QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD
KSLLARIGDA FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV
RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY DSPLSEYAAV
GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE AKWGQLSNVV LLLPHGHEGQ
GPDHTSARIE RFLQLWAEGS MTIAMPSTPS NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK
AAVSEIKDFT EIKFRSVLEE PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA
IVRLEQLAPL PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK
RISRRAMSAP SSGSSKVHAV EQQEILDEAF G


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