LEU1_THEFY
ID LEU1_THEFY Reviewed; 568 AA.
AC Q47RM9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=Tfu_0850;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|HAMAP-
CC Rule:MF_00572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00572};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_00572}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR EMBL; CP000088; AAZ54888.1; -; Genomic_DNA.
DR RefSeq; WP_016188375.1; NC_007333.1.
DR AlphaFoldDB; Q47RM9; -.
DR SMR; Q47RM9; -.
DR STRING; 269800.Tfu_0850; -.
DR PRIDE; Q47RM9; -.
DR EnsemblBacteria; AAZ54888; AAZ54888; Tfu_0850.
DR KEGG; tfu:Tfu_0850; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_11; -.
DR OMA; FGQGERT; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00970; leuA_yeast; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Transferase.
FT CHAIN 1..568
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000129513"
FT DOMAIN 37..313
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 568 AA; 63389 MW; 4920B68910817B52 CRC64;
MIPQQQPSGM PFHRYQPFKP VDLPDRTWPS KTITKAPRWL STDLRDGNQA LIEPMDTERK
REIFDLLVRM GYKEIEVGFP AASQTDYDFV RYLIEEDRIP DDVQISVLTQ AREELIERTV
QSLVGAKRAT VHLYNATSPE FRRIVFGVNR EECKGIAVEG TRTVLKFAEQ YLKDTEYFGY
EYSPEIFIDT ELEFALEVCE AVMDVYQPGP DREIILNLPA TVERATPNVY ADQIEWMSRN
LSRREYVCLS VHPHNDRGTA VAAAELAVMA GADRVEGCLF GHGERTGNVC LVTLGLNLFS
QGIDPMIDFS NIDEIRRTVE HCTQLPVNPR HPYGGDLVYT AFSGSHQDAI KKGFHALEAD
AAAAGVPVDE YRWNMPYLPI DPKDVGRTYE AVIRVNSQSG KGGVSYVLQR DYSIDLPRRL
QIEFSRVVQQ FADAEGGEFS GERIWEIFTD TYLSEGVVGV MAYRSETSED GEYCISADVR
LRGEIREITG TGNGPISAFV DALAGVGFKL RVLDYSEHAL SEGGDARAAA YVEAEVDGNV
LWGVGISSNI TTASLKAVCS AVNRAQQS