LEU1_PSESM
ID LEU1_PSESM Reviewed; 556 AA.
AC Q886Y1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=PSPTO_1444;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO54965.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016853; AAO54965.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_791270.3; NC_004578.1.
DR RefSeq; WP_003380623.1; NC_004578.1.
DR AlphaFoldDB; Q886Y1; -.
DR SMR; Q886Y1; -.
DR STRING; 223283.PSPTO_1444; -.
DR PRIDE; Q886Y1; -.
DR EnsemblBacteria; AAO54965; AAO54965; PSPTO_1444.
DR GeneID; 61790065; -.
DR KEGG; pst:PSPTO_1444; -.
DR PATRIC; fig|223283.9.peg.1464; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_6; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000002515; 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; Reference proteome; Transferase.
FT CHAIN 1..556
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140439"
FT DOMAIN 33..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 556 AA; 61544 MW; F4C74D6A683BDC68 CRC64;
MTMLNDPSKK YRAFPTIDLP DRTWPSKTID AAPIWCSSDL RDGNQSLIEP MDSVKKLRFW
KTLVSVGVKE IEASFPAASQ TDFDFVRTLI EDGHIPDDTT IQVLTQARED LIARTFESLR
GAKKAIVHLY NATCPSFRRI VFNQDKAGVK EIAVNAAKLF VKYAAQQPET QWTFEYSPET
FSATELEFAK EVCDAVIEVW NPTPENKVIL NLPATVEVAT PNIYADQIEW FGRHITRRDS
VLISLHTHND RGTGVAATEL GLMAGADRVE GCLFGNGERT GNVDLVTVAL NLYTQGINPE
LDFSDIDGVR KVVEECNQIP VHPRHPYVGD LVHTAFSGSH QDAIRKGFTQ QKEGELWEVP
YLPIDPADIG RSYEAVIRVN SQSGKGGIAY LLEQEYGISL PRRMQIEFSQ VVQGETDRLG
LEMTAEQIHA LLRREYLQAN TPYALISHRL QEENGNSAVD AEVHVDGETQ HWRGKGKGAL
EALVAGLPVA VEIMDYNEHA IGSGTTAKAA AYIELRVNGD RAVHGVGIDE NITTASFRAL
FSALNRSLSQ AQAKAA
