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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //