LEU1_PSEPG
ID LEU1_PSEPG Reviewed; 557 AA.
AC B0KRD9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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};
GN OrderedLocusNames=PputGB1_1023;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABY96933.1; -; Genomic_DNA.
DR RefSeq; WP_012270717.1; NC_010322.1.
DR AlphaFoldDB; B0KRD9; -.
DR SMR; B0KRD9; -.
DR STRING; 76869.PputGB1_1023; -.
DR EnsemblBacteria; ABY96933; ABY96933; PputGB1_1023.
DR KEGG; ppg:PputGB1_1023; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_6; -.
DR OMA; WPDKVID; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000002157; Chromosome.
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..557
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000082330"
FT DOMAIN 33..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 557 AA; 61794 MW; C4875251D4B3BA23 CRC64;
MTMLKDPSKK YRAFPTIDLP DRTWPSKTIT EAPIWCSSDL RDGNQSLIEP MDSEKKLRFW
KTLVQVGVKE IEASFPSASQ TDFDFVRTLI QDGHIPDDTT IQVLTQARED LIARTFESLR
GAKKAIVHLY NATSPSFRRI VFNQDKQGVK DIAVNAAKLF VKYAAQQPET HWTFQYSPET
FSATEMEFAK EVCDAVIEVW NPTPEHKIIL NLPATVEVST PNIYADQIEW FCRNVSRRDS
VIISLHCHND RGTGIAATEL GLMAGADRAE GCLFGNGERT GNVDLVTLAL NLYTQGIDPQ
LDFSDIDGVR KVVEECNQLP VHPRHPYVGD LVHTAFSGSH QDAIRKGFAK QQEGERWEVP
YLPIDPADIG RSYEAVIRVN SQSGKGGITY LLEQEYGISL PRRMQIEFSQ VVQGETDRLG
LEMTAQQIYS LLHKEYLQAN APYALVSHRL QEENGHSAVE VEVAGEGETT LHWRGKGNGA
LEALVAGLPI AVEIMDYNEH AIGAGTNAKA AAYIELRVAG GRPVHGVGID ENITTASFKA
LFSALNRSLS QQEAKAA
