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 KGD_MYCVP               Reviewed;        1243 AA.
A1TDK2;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
28-MAR-2018, entry version 72.
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;
Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=350058;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 7251 / 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: 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=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.
ProteinModelPortal; A1TDK2; -.
SMR; A1TDK2; -.
STRING; 350058.Mvan_4477; -.
EnsemblBacteria; ABM15252; ABM15252; Mvan_4477.
KEGG; mva:Mvan_4477; -.
eggNOG; ENOG4105C7P; Bacteria.
eggNOG; COG0508; LUCA.
eggNOG; COG0567; LUCA.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OrthoDB; POG091H03SK; -.
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.
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 1243 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310725.
REGION 1 40 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 41 103 Linker.
REGION 104 353 Succinyltransferase E2.
REGION 354 1243 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 557 558 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 622 624 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 661 663 Thiamine pyrophosphate binding.
{ECO:0000250}.
REGION 1105 1108 Allosteric activator. {ECO:0000250}.
REGION 1165 1166 Allosteric activator. {ECO:0000250}.
COILED 799 831 {ECO:0000255}.
ACT_SITE 332 332 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 661 661 Magnesium. {ECO:0000250}.
METAL 694 694 Magnesium. {ECO:0000250}.
METAL 696 696 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 597 597 2-oxoglutarate. {ECO:0000250}.
BINDING 622 622 2-oxoglutarate. {ECO:0000250}.
BINDING 968 968 Thiamine pyrophosphate. {ECO:0000250}.
BINDING 1036 1036 2-oxoglutarate. {ECO:0000250}.
BINDING 1054 1054 Allosteric activator. {ECO:0000250}.
BINDING 1070 1070 Allosteric activator. {ECO:0000250}.
BINDING 1158 1158 Allosteric activator. {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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