LEU1_RHIME
ID LEU1_RHIME Reviewed; 558 AA.
AC Q9X7L2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 3.
DT 25-MAY-2022, entry version 115.
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=R02379;
GN ORFNames=SMc02717;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GR4;
RX PubMed=12070767; DOI=10.1007/s00203-002-0421-7;
RA Sanjuan-Pinilla J.M., Munoz S., Nogales J., Olivares J., Sanjuan J.;
RT "Involvement of the Sinorhizobium meliloti leuA gene in activation of
RT nodulation genes by NodD1 and luteolin.";
RL Arch. Microbiol. 178:36-44(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(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_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=CAB39977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC46958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ132004; CAB39977.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591688; CAC46958.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_386485.3; NC_003047.1.
DR AlphaFoldDB; Q9X7L2; -.
DR SMR; Q9X7L2; -.
DR STRING; 266834.SMc02717; -.
DR EnsemblBacteria; CAC46958; CAC46958; SMc02717.
DR KEGG; sme:SMc02717; -.
DR PATRIC; fig|266834.11.peg.3862; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_5; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001976; 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..558
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140442"
FT DOMAIN 30..303
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 255
FT /note="E -> D (in Ref. 1; CAB39977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61751 MW; 2F863AB5B0F2310B CRC64;
MPEAAVKYQP YPQIVLPDRT WPSKAITEAP IWCSVDLRDG NQALVDPMGH DRKARMFHLL
LDMGFKEIEI GFPSASQTDY DFARWCVEEG NVSEDVSLQV LVQCRPELIA RTFEALEGAH
RPIVHFYNST SELQRRVVFG KDVAGIKQIA TDAAKMITDM AAKAGGGYRF EYSPESFTGT
ELEVALEICN AVIEIVRPTA DNKLIINLPS TVEMATPNIY ADQIEWMCRN LDNRENLIVS
LHPHNDRGTG IAATELGLMA GADRVEGTLF GNGERTGNVD VVTLALNMFT QGVDPKLDCS
DIERIKEVYE YSNQMVIPER HPYVGELVYT AFSGSHQDAI NKGMKAIKQA NKPTWEVPYL
PIDPRDVGRS YEAIIRINSQ SGKGGIAYIL QEDYGINLPR NLQIEFREEV QRITDEEGKE
LPSKRIHQRF IESYVEQPGA RIKFVDHHTY PAGEHKGLRV VAAEITDGGE TRQIEGKGTG
PIDGFINALS IYLGIELSVA DYSEHSLQHG SNAAAIAYVE VEYPGGKLFG VGINTNIVAA
SLEAIVSAAN RVLDVVGK
