LEU1_CAUVC
ID LEU1_CAUVC Reviewed; 524 AA.
AC Q9A823;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=CC_1541;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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}.
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 -!- 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}.
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DR EMBL; AE005673; AAK23520.1; -; Genomic_DNA.
DR PIR; D87440; D87440.
DR RefSeq; NP_420352.1; NC_002696.2.
DR RefSeq; WP_010919415.1; NC_002696.2.
DR AlphaFoldDB; Q9A823; -.
DR SMR; Q9A823; -.
DR STRING; 190650.CC_1541; -.
DR EnsemblBacteria; AAK23520; AAK23520; CC_1541.
DR KEGG; ccr:CC_1541; -.
DR PATRIC; fig|190650.5.peg.1569; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_5; -.
DR OMA; NTMRMLV; -.
DR BioCyc; CAULO:CC1541-MON; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001816; 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; 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..524
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140348"
FT DOMAIN 15..275
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 524 AA; 55990 MW; F8DBEA6B2AAD8B57 CRC64;
MTSVPAGAIS KRDNVVVFDT TMRDGEQSPG ASMSLEEKLE LAKILEEMGV DVIEAGFPIA
SNGDFEAVRQ IAELITESTV CGLARAAAGD IDRCAEAVRR AKRGRIHTFI STSPVHMKYK
LQMEPDAVLE AITRSVSHAR NLVGDVEWSA EDATRTERDF LKRCVEAAIK AGATTINLPD
TVGYSYPSEY GELFRDVITS VPGADKAIFS AHCHNDLGLA VANSIAAIEG GARQVEVAIN
GIGERAGNAA LEEIVMALRV RGDHLPYGTS VDPVHITRAS RYVSAITGFP VQFNKAIVGK
NAFAHESGIH QDGMLKNAET YEIMKPEDVG QGATNLVMGK HSGRHAFREK LKALGYELGQ
NALNDAFGRF KELADKKKHV FDDDIVALVD DALARGSEKI RVSRLRVVAG TDGQSAELTL
DIDGVASTAE ATGDGPVDAV FNAIHKIVPH SAALRLFQVH AVTEGTDAQA QVSVRLEEDG
RIATGAAADT DTLTASAKAY VNALNNLFAR KEKSRPEAAI ASGF
