(data stored in ACNUC7421 zone)

SWISSPROT: LEU1_SALTY

ID   LEU1_SALTY              Reviewed;         523 AA.
AC   P15875; P74845;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000305};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000269|PubMed:4976555, ECO:0000269|PubMed:6195343};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000303|PubMed:6195343};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000303|PubMed:4976555};
GN   Name=leuA {ECO:0000303|PubMed:6195343}; OrderedLocusNames=STM0113;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2181403; DOI=10.1093/nar/18.5.1290;
RA   Ricca E., Calvo J.M.;
RT   "The nucleotide sequence of leuA from Salmonella typhimurium.";
RL   Nucleic Acids Res. 18:1290-1290(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC   STRAIN=LT2;
RX   PubMed=388423; DOI=10.1073/pnas.76.10.4941;
RA   Gemmill R.M., Wessler S.R., Keller E.B., Calvo J.M.;
RT   "Leu operon of Salmonella typhimurium is controlled by an attenuation
RT   mechanism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:4941-4945(1979).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-12, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=LT2;
RX   PubMed=6195343; DOI=10.1016/s0022-2836(83)80226-5;
RA   Gemmill R.M., Jones J.W., Haughn G.W., Calvo J.M.;
RT   "Transcription initiation sites of the leucine operons of Salmonella
RT   typhimurium and Escherichia coli.";
RL   J. Mol. Biol. 170:39-59(1983).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=CV-19;
RX   PubMed=4976555;
RA   Kohlhaw G., Leary T.R., Umbarger H.E.;
RT   "Alpha-isopropylmalate synthase from Salmonella typhimurium. Purification
RT   and properties.";
RL   J. Biol. Chem. 244:2218-2225(1969).
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_01025, ECO:0000269|PubMed:4976555, ECO:0000269|PubMed:6195343}.
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_01025,
CC         ECO:0000269|PubMed:4976555, ECO:0000269|PubMed:6195343};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA, mercuric salts and by leucine.
CC       Inhibition by leucine is non-competitive with respect to 3-methyl-2-
CC       oxobutanoate and competitive with respect to acetyl-CoA, and is more
CC       sensitive at pH 6.5 than pH 8.5. {ECO:0000269|PubMed:4976555}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.06 mM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:4976555};
CC         KM=1.1 mM for 2-oxobutanoate {ECO:0000269|PubMed:4976555};
CC         KM=10 mM for pyruvate {ECO:0000269|PubMed:4976555};
CC         KM=0.2 mM for acetyl-CoA {ECO:0000269|PubMed:4976555};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:4976555};
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_01025}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025,
CC       ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35931.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; X51583; CAA35931.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE006468; AAL19077.1; -; Genomic_DNA.
DR   EMBL; X00059; CAA24935.1; -; Genomic_DNA.
DR   RefSeq; NP_459118.1; NC_003197.2.
DR   RefSeq; WP_000082819.1; NC_003197.2.
DR   SMR; P15875; -.
DR   PaxDb; P15875; -.
DR   PRIDE; P15875; -.
DR   EnsemblBacteria; AAL19077; AAL19077; STM0113.
DR   GeneID; 1251631; -.
DR   KEGG; stm:STM0113; -.
DR   PATRIC; fig|99287.12.peg.119; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046859; -.
DR   KO; K01649; -.
DR   OMA; IHMQYKL; -.
DR   PhylomeDB; P15875; -.
DR   BioCyc; SENT99287:STM0113-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01025; LeuA_type1; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR005671; LeuA_bact_synth.
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; TIGR00973; leuA_bact; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P15875.
DR   SWISS-2DPAGE; P15875.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Direct protein sequencing; Leucine biosynthesis; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6195343"
FT   CHAIN           2..523
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140375"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   CONFLICT        113
FT                   /note="S -> R (in Ref. 1; CAA35931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  57431 MW;  0F5271BC488E7671 CRC64;
     MSQQVIIFDT TLRDGEQALQ ASLSAKEKLQ IALALERMGV DVMEVGFPVS SPGDFESVQT
     IARTIKNSRV CALARCVEKD IDVAAQALKV ADAFRIHTFI ATSPMHIATK LRSTLDEVIE
     RAVYMVKRAR NYTDDVEFSC EDAGRTPVDD LARVVEAAIN AGARTINIPD TVGYTMPFEF
     AGIISGLYER VPNIDKAIIS VHTHDDLGIA VGNSLAAVHA GARQVEGAMN GIGERAGNCA
     LEEVIMAIKV RKDIMNVHTN INHHEIWRTS QTVSQICNMP IPANKAIVGS GAFAHSSGIH
     QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MEEMGYKDTD YNMDHLYDAF
     LKLADKKGQV FDYDLEALAF INKQQEEPEH FRLDYFSVQS GSSDIATASV KLACGEEIKA
     EAANGNGPVD AIYQAINRIT GYDVELVKYD LNAKGQGKDA LGQVDIVVNH HGRRFHGVGL
     ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQNKENNK ETV
//

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