LEU1_SALTI
ID LEU1_SALTI Reviewed; 523 AA.
AC Q8Z9I0;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=STY0132, t0117;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL513382; CAD01270.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67849.1; -; Genomic_DNA.
DR RefSeq; NP_454725.1; NC_003198.1.
DR RefSeq; WP_000082813.1; NZ_WSUR01000009.1.
DR AlphaFoldDB; Q8Z9I0; -.
DR SMR; Q8Z9I0; -.
DR STRING; 220341.16501398; -.
DR EnsemblBacteria; AAO67849; AAO67849; t0117.
DR KEGG; stt:t0117; -.
DR KEGG; sty:STY0132; -.
DR PATRIC; fig|220341.7.peg.133; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_6; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..523
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140374"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 523 AA; 57355 MW; 9713F98D31850D72 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 RKDIINVHTN INHHEIWRTS QTVSQICNMP IPANKAIVGS GAFAHSSGIH
QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MEEMGYKDTD YNMGHLYDAF
LKLADKKGQV FDYDLEALAF INKQQEEPEH FRLDYFSVQS GSSDIATASV KLACGEEIKA
EAANGNGPVD AIYQAINRIT GYDVELVKYD LNAKGQGKDA LGQVDIVVNH HGRRFHGVGL
ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQNKENNK ETV