LEU1_PSEMY
ID LEU1_PSEMY Reviewed; 556 AA.
AC A4XY24;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Pmen_3492;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP86240.1; -; Genomic_DNA.
DR RefSeq; WP_012019496.1; NC_009439.1.
DR AlphaFoldDB; A4XY24; -.
DR SMR; A4XY24; -.
DR STRING; 399739.Pmen_3492; -.
DR EnsemblBacteria; ABP86240; ABP86240; Pmen_3492.
DR KEGG; pmy:Pmen_3492; -.
DR PATRIC; fig|399739.8.peg.3538; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_1_6; -.
DR OMA; WPDKVID; -.
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..556
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000025035"
FT DOMAIN 33..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 556 AA; 61093 MW; 885949427238C001 CRC64;
MTMLKDPSQK YRPFTPIALP DRTWPDKVID RAPIWLSTDL RDGNQSLIEP MDAEKKMRFF
KCLVAVGLKE IEVGFPSASQ TDFDFVRELI EGGHIPDDVT IQVLTQARDD LIERTFESLK
GAKRAIVHYY NACAPSFRKI VFNQDKAGVK AIAVAAGKTI KRLAAAQPDT QWGFEYSPEV
FSSTETDFAV EVCNAVIEVF QPTPANKLIL NLPATVECAT PNNYADQIEW FGRHVDRRDS
VLISVHTHND RGTGVAASEL AVMAGADRVE GCLFGNGERT GNVCLVTLAL NLYTQGVDPQ
LDFSDIDAVR KVVEDCNQIP VHPRHPYAGD LVHTAFSGSH QDAIRKGFAQ QKDDAVWEVP
YLPIDPADIG RDYEAVIRVN SQSGKGGITF LLEQEYGISL PRRMQIEFSQ VVQRETDRLG
LEMTAAQIYQ LLESEYLQAS APYALKGHRL QEENGTSAVD VEVISAGESH HWRGIGKGPL
EALVAGLPVA VEIMDYSEHA IGAGTNAKAA AYIELRVNGG RALHGIGIDE NLTTASFRAL
FSALNRALSQ AESRAA