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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_MYCSK               Reviewed;        1269 AA.
A1UK81;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 1.
23-MAY-2018, 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=Mkms_4047;
Mycobacterium sp. (strain KMS).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=189918;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KMS;
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
Mikhailova N., Miller C.D., Richardson P.;
"Complete sequence of chromosome of Mycobacterium sp. KMS.";
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: 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; CP000518; ABL93239.1; -; Genomic_DNA.
RefSeq; WP_011561352.1; NC_008705.1.
ProteinModelPortal; A1UK81; -.
SMR; A1UK81; -.
PRIDE; A1UK81; -.
EnsemblBacteria; ABL93239; ABL93239; Mkms_4047.
GeneID; 32420704; -.
KEGG; mkm:Mkms_4047; -.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OMA; IDMVCYR; -.
OrthoDB; POG091H03SK; -.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
Proteomes; UP000000638; 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 1269 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310720.
REGION 1 41 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 42 107 Linker.
REGION 108 378 Succinyltransferase E2.
REGION 379 1269 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 582 583 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 647 649 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 686 688 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 1130 1133 Allosteric activator. {ECO:0000250}.
REGION 1190 1191 Allosteric activator. {ECO:0000250}.
COILED 824 855 {ECO:0000255}.
ACT_SITE 357 357 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 686 686 Magnesium. {ECO:0000250}.
METAL 719 719 Magnesium. {ECO:0000250}.
METAL 721 721 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 622 622 2-oxoglutarate. {ECO:0000250}.
BINDING 647 647 2-oxoglutarate. {ECO:0000250}.
BINDING 993 993 Thiamine pyrophosphate. {ECO:0000250}.
BINDING 1061 1061 2-oxoglutarate. {ECO:0000250}.
BINDING 1079 1079 Allosteric activator. {ECO:0000250}.
BINDING 1095 1095 Allosteric activator. {ECO:0000250}.
BINDING 1183 1183 Allosteric activator. {ECO:0000250}.
SEQUENCE 1269 AA; 140119 MW; F6F4221B80E76B83 CRC64;
MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA SENGQQTRTA
APKAPPEPAP APAPKTPDSK TPDSKSQAPK QDSKPQESKP QAKAKPAESK SSTKPADAKS
EKSGKSGTNG AAKPAAQPAD DSDQNQVLRG AAAAVAKNMS ASLDVPTATS VRAIPAKLMI
DNRVVINNHL KRTRGGKISF THLIGYAIVA AVKKFPNMNR HFAEVDGKPN AVTPAHTNLG
LAIDLQGKDG NRQLVVAAIK KADTMRFGQF IAAYEDIVRR ARDGKLTAED FSGVTISLTN
PGTIGTVHSV PRLMRGQGAI IGVGAMEYPA EFQGASEERI ADLGIGKLIT LTSTYDHRII
QGAESGDFLR TVHQLLLSDD FFDEIFRELG IPYEPVRWRT DNPDSIEDKN ARVIELIAAY
RNRGHLMADI DPLRLDSNRF RSHPDLDVLT HGLTLWDLDR EFKVNGFAGA ERKKLRDVLA
VLRDAYCRHI GVEYTHILEP EQQQWLQERI EGKHEKPTVA QQKYILSRLN AAEAFETFLQ
TKYVGQKRFS LEGAETVIPA MDAVIDQCAE HALDEVVIGM PHRGRLNVLA NIVGKPYSQI
FSEFEGNLNP SQAHGSGDVK YHLGSSGTYL QMFGDNDITV SLTANPSHLE AVDPVMEGLV
RAKQDLLDKG DTEDGYTVVP LMLHGDAAFA GQGVVAETLN LALLRGYRTG GTIHLIVNNQ
IGFTTSPAAA KSSEYCTDVA KMIGAPIFHV NGDDPEAAVW VSRLAVDFRQ KFKKDVVIDL
LCYRRRGHNE GDDPSMTQPS MYDVIDTKRG VRKSYTEALI GRGDISMKEA EDALRDYQGQ
LEQVFNEVRE LEKHEIEPSE SVEADQQIPA KLATAVDKSL LARIGDAHLA VPEGFTVHPR
VKPVLEKRRE MAYEGKVDWA FAELLALGTM ISEGKLVRLS GQDTRRGTFT QRHSVVIDRK
TGKEFTPLQL LATDSDGNPT GGKFLVYDSP LSEFAAVGFE YGYSVGNPDA MVLWEAQFGD
FINGAQSIID EFISSGEAKW GQLSDVVLLL PHGHEGQGPD HTSGRIERFL QLWAEGSMTI
ALPSTPANYF HLLRRHSLDG IQRPLIVFTP KSMLRNKAAV SDIRDFTEQK FRSVLEEPTY
TDGDGDRNKV TRILLTSGKI YYELVARKNK ESRDDVAIVR IEQLAPLPKR RLAETLDKYP
NVEEKFWVQE EPANQGAWPT FGLTLPEMLP DHFTGIKRIS RRAMSAPSSG SSKVHAVEQQ
EILDEAFAP


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