ID KGD_MYCS2 Reviewed; 1227 AA.
AC A0R2B1; I7GDF5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme;
DE AltName: Full=2-hydroxy-3-oxoadipate synthase;
DE Short=HOA synthase;
DE Short=HOAS;
DE EC=2.2.1.5;
DE AltName: Full=2-oxoglutarate carboxy-lyase;
DE AltName: Full=2-oxoglutarate decarboxylase;
DE AltName: Full=Alpha-ketoglutarate decarboxylase;
DE Short=KG decarboxylase;
DE Short=KGD;
DE EC=4.1.1.71;
DE AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase;
DE Includes:
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE Short=ODH E1 component;
DE EC=1.2.4.2;
DE AltName: Full=Alpha-ketoglutarate dehydrogenase E1 component;
DE Short=KDH E1 component;
DE Includes:
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE EC=2.3.1.61;
DE AltName: Full=2-oxoglutarate dehydrogenase complex E2 component;
DE Short=ODH E2 component;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase;
GN Name=kgd; Synonyms=sucA; OrderedLocusNames=MSMEG_5049, MSMEI_4922;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN 2-OXOGLUTARATE DECARBOXYLATION, ACTIVITY REGULATION, KINETIC
RP PARAMETERS, AND INTERACTION WITH GARA.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL Mol. Microbiol. 70:1408-1423(2008).
RN [5] {ECO:0007744|PDB:2XT6, ECO:0007744|PDB:2XTA, ECO:0007744|PDB:2Y0P, ECO:0007744|PDB:2YIC, ECO:0007744|PDB:2YID}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 116-1227 IN COMPLEXES WITH
RP THIAMINE PYROPHOSPHATE; ACETYL-COA; ENAMINE-THDP REACTION INTERMEDIATE AND
RP MAGNESIUM, FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, SUBUNIT, PATHWAY, MUTAGENESIS OF HIS-539;
RP HIS-579; HIS-747; ARG-781; HIS-1020; GLU-1034 AND ARG-1062, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21867916; DOI=10.1016/j.chembiol.2011.06.004;
RA Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M.;
RT "Functional plasticity and allosteric regulation of alpha-ketoglutarate
RT decarboxylase in central mycobacterial metabolism.";
RL Chem. Biol. 18:1011-1020(2011).
CC -!- FUNCTION: Shows three enzymatic activities that share a first common
CC step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate,
CC KG), leading to the formation of an enamine-thiamine-PP intermediate
CC upon decarboxylation. Thus, displays KGD activity, catalyzing the
CC decarboxylation from five-carbon 2-oxoglutarate to four-carbon
CC succinate semialdehyde (SSA). Also catalyzes C-C bond formation between
CC the activated aldehyde formed after decarboxylation of alpha-
CC ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-
CC 3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-
CC hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate
CC dehydrogenase (ODH) complex, that catalyzes the overall conversion of
CC 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG
CC dehydrogenase reactions provide two alternative, tightly regulated,
CC pathways connecting the oxidative and reductive branches of the TCA
CC cycle. {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate +
CC CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde;
CC Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:21867916};
CC -!- ACTIVITY REGULATION: Alpha-ketoglutarate dehydrogenase and
CC decarboxylase activities are inhibited by unphosphorylated GarA, and
CC allosterically activated by acetyl-CoA, the main substrate of the TCA
CC cycle. Both the phosphoadenosine and acetyl moieties of acetyl-CoA are
CC important for activation because neither CoA nor the synthetic compound
CC S-(2-acetamidoethyl)-ethanethioate (which mimics the terminal acetyl-
CC phosphopantetheine group of acetyl-CoA) has an activation effect.
CC {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for alpha-ketoglutarate {ECO:0000269|PubMed:19019160};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from 2-oxoglutarate (transferase route): step 1/2.
CC {ECO:0000269|PubMed:21867916}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000269|PubMed:21867916}.
CC -!- SUBUNIT: Homodimer. Interacts with the FHA domain of unphosphorylated
CC GarA. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple
CC copies of three enzymatic components: 2-oxoglutarate dehydrogenase
CC (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide
CC dehydrogenase (E3). {ECO:0000269|PubMed:19019160,
CC ECO:0000269|PubMed:21867916}.
CC -!- DOMAIN: Is a fusion protein with two major domains exhibiting
CC structural features of an E1 and E2 protein, and a short sequence
CC stretch of E1 localized at the N-terminus, which is connected by a
CC linker region to the rest of the protein. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show any ODH
CC activity, in contrast to wild-type, demonstrating that this protein is
CC part of a functional ODH complex in mycobacteria.
CC {ECO:0000269|PubMed:21867916}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK74238.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41366.1; -; Genomic_DNA.
DR RefSeq; WP_011730279.1; NZ_SIJM01000019.1.
DR RefSeq; YP_889299.1; NC_008596.1.
DR PDB; 2XT6; X-ray; 2.74 A; A/B=116-1227.
DR PDB; 2XTA; X-ray; 2.20 A; A/B/C/D=361-1227.
DR PDB; 2Y0P; X-ray; 2.40 A; A/B/C/D=361-1227.
DR PDB; 2YIC; X-ray; 1.96 A; A/B/C/D=361-1227.
DR PDB; 2YID; X-ray; 2.25 A; A/B/C/D=361-1227.
DR PDB; 3ZHQ; X-ray; 2.50 A; A/B/C/D=361-1227.
DR PDB; 3ZHR; X-ray; 2.10 A; A/B/C/D=361-1227.
DR PDB; 3ZHS; X-ray; 2.10 A; A/B/C/D=361-1227.
DR PDB; 3ZHT; X-ray; 2.15 A; A/B/C/D=361-1227.
DR PDB; 3ZHU; X-ray; 2.30 A; A/B/C/D=361-1227.
DR PDB; 3ZHV; X-ray; 2.30 A; A/B/C/D=361-1227.
DR PDB; 6I2Q; X-ray; 2.15 A; A=361-1227.
DR PDB; 6I2R; X-ray; 2.20 A; A/C=361-1227.
DR PDB; 6I2S; X-ray; 2.40 A; A=361-1227.
DR PDB; 6R29; X-ray; 1.67 A; A/B=361-1227.
DR PDB; 6R2A; X-ray; 1.70 A; A/B=361-1227.
DR PDB; 6R2B; X-ray; 1.96 A; A/B/C/D=361-1227.
DR PDB; 6R2C; X-ray; 2.09 A; A/B/C/D=361-1227.
DR PDB; 6R2D; X-ray; 2.30 A; A/B/C/D=361-1227.
DR PDB; 8P5R; X-ray; 4.56 A; A/B/C/D/E/F/N/O/P/Q=2-1227.
DR PDBsum; 2XT6; -.
DR PDBsum; 2XTA; -.
DR PDBsum; 2Y0P; -.
DR PDBsum; 2YIC; -.
DR PDBsum; 2YID; -.
DR PDBsum; 3ZHQ; -.
DR PDBsum; 3ZHR; -.
DR PDBsum; 3ZHS; -.
DR PDBsum; 3ZHT; -.
DR PDBsum; 3ZHU; -.
DR PDBsum; 3ZHV; -.
DR PDBsum; 6I2Q; -.
DR PDBsum; 6I2R; -.
DR PDBsum; 6I2S; -.
DR PDBsum; 6R29; -.
DR PDBsum; 6R2A; -.
DR PDBsum; 6R2B; -.
DR PDBsum; 6R2C; -.
DR PDBsum; 6R2D; -.
DR PDBsum; 8P5R; -.
DR AlphaFoldDB; A0R2B1; -.
DR SMR; A0R2B1; -.
DR IntAct; A0R2B1; 1.
DR STRING; 246196.MSMEG_5049; -.
DR PaxDb; 246196-MSMEI_4922; -.
DR GeneID; 66736369; -.
DR KEGG; msg:MSMEI_4922; -.
DR KEGG; msm:MSMEG_5049; -.
DR PATRIC; fig|246196.19.peg.4927; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR BRENDA; 4.1.1.71; 3512.
DR SABIO-RK; A0R2B1; -.
DR UniPathway; UPA00223; UER00997.
DR UniPathway; UPA00223; UER01001.
DR EvolutionaryTrace; A0R2B1; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Allosteric enzyme; Coiled coil;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..1227
FT /note="Multifunctional 2-oxoglutarate metabolism enzyme"
FT /id="PRO_0000310718"
FT REGION 1..41
FT /note="2-oxoglutarate dehydrogenase E1, N-terminal part"
FT REGION 23..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..88
FT /note="Linker"
FT REGION 89..335
FT /note="Succinyltransferase E2"
FT REGION 336..1227
FT /note="2-oxoglutarate dehydrogenase E1, C-terminal part"
FT COILED 783..814
FT /evidence="ECO:0000255"
FT COMPBIAS 43..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Proton acceptor; for succinyltransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 579
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000305|PubMed:21867916,
FT ECO:0007744|PDB:2Y0P"
FT BINDING 604
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000305|PubMed:21867916,
FT ECO:0007744|PDB:2Y0P"
FT BINDING 604
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 606
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 645
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 645
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 646
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 647
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 678
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 678
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1020
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000305|PubMed:21867916,
FT ECO:0007744|PDB:2Y0P"
FT BINDING 1038
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1054
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1089
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1092
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1142
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1149
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT BINDING 1150
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:21867916,
FT ECO:0007744|PDB:2XTA"
FT MUTAGEN 539
FT /note="H->A: Loss of KG decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 579
FT /note="H->A: Loss of KG decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 747
FT /note="H->A: 40-fold decrease in KG decarboxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 781
FT /note="R->A: Increase in KG decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 1020
FT /note="H->A: Loss of KG decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 1034
FT /note="E->A: Loss of activation by acetyl-CoA."
FT /evidence="ECO:0000269|PubMed:21867916"
FT MUTAGEN 1062
FT /note="R->A: Loss of activation by acetyl-CoA."
FT /evidence="ECO:0000269|PubMed:21867916"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:2XT6"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:2XT6"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:2XT6"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 366..380
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:2YIC"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:2XT6"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:2XTA"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 432..443
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 476..499
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6R2C"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:2YIC"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 542..548
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 554..562
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 567..570
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:2YID"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 609..624
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 637..644
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 652..658
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 686..689
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 697..702
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 706..710
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 714..731
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 758..764
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 770..780
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 786..808
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 837..846
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 861..873
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 878..891
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 895..900
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 901..905
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 913..916
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 918..920
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 926..931
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 942..947
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 953..965
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 969..974
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 978..984
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 985..990
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 991..994
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 995..999
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1006..1010
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1014..1016
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1025..1031
FT /evidence="ECO:0007829|PDB:6R29"
FT TURN 1034..1036
FT /evidence="ECO:0007829|PDB:6R2C"
FT STRAND 1038..1040
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1045..1057
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1064..1068
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1071..1074
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1076..1078
FT /evidence="ECO:0007829|PDB:2Y0P"
FT HELIX 1082..1086
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1092..1094
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1097..1100
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1106..1108
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1111..1115
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1119..1130
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1135..1145
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1148..1155
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1163..1171
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1174..1176
FT /evidence="ECO:0007829|PDB:6R2B"
FT HELIX 1177..1187
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1189..1192
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1196..1200
FT /evidence="ECO:0007829|PDB:6R29"
FT STRAND 1204..1207
FT /evidence="ECO:0007829|PDB:6R29"
FT HELIX 1211..1225
FT /evidence="ECO:0007829|PDB:6R29"
SQ SEQUENCE 1227 AA; 135944 MW; 76C5BFFD1638A391 CRC64;
MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS NGRTTTAAPV
TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD ESQILRGAAA AVVKNMNASL
EVPTATSVRA IPAKLMIDNR VVINNHLKRT RGGKISFTHL LGYAIVQAVK KFPNMNRHFA
VVDGKPTAIT PAHTNLGLAI DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD
GKLTAEDFSG VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL
GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY EPVRWRTDNP
DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH PDLDVNSHGL TLWDLDREFK
VDGFAGVQRK KLRDILSVLR DAYCRHVGVE YTHILEPEQQ RWIQERVETK HDKPTVAEQK
YILSKLNAAE AFETFLQTKY VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR
GRLNVLANIV GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT
ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG QGVVAETLNL
ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK MIGAPIFHVN GDDPEACAWV
ARLAVDFRQA FKKDVVIDML CYRRRGHNEG DDPSMTQPYM YDVIDTKRGS RKAYTEALIG
RGDISMKEAE DALRDYQGQL ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML
QRIGDAHLAL PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG
QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL SEFAAVGFEY
GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG QLSDVVLLLP HGHEGQGPDH
TSGRIERFLQ LWAEGSMTIA MPSTPANYFH LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS
DIRDFTESKF RSVLEEPMYT DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI
EQLAPLPRRR LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR
RAMSAPSSGS SKVHAVEQQE ILDTAFG
//
