ID   LEU1_BRUME              Reviewed;         555 AA.
AC   Q8YIJ3;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   25-MAY-2022, entry version 107.
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=BMEI0451;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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=AAL51632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL51632.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE3308; AE3308.
DR   AlphaFoldDB; Q8YIJ3; -.
DR   SMR; Q8YIJ3; -.
DR   STRING; 224914.BMEI0451; -.
DR   EnsemblBacteria; AAL51632; AAL51632; BMEI0451.
DR   KEGG; bme:BMEI0451; -.
DR   KEGG; bmel:DK63_972; -.
DR   PATRIC; fig|224914.52.peg.1026; -.
DR   eggNOG; COG0119; Bacteria.
DR   OMA; WPDKVID; -.
DR   UniPathway; UPA00048; UER00070.
DR   PRO; PR:Q8YIJ3; -.
DR   Proteomes; UP000000419; Chromosome I.
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; Transferase.
FT   CHAIN           1..555
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140428"
FT   DOMAIN          30..303
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   555 AA;  61614 MW;  81553964182F649A CRC64;
     MPIAGTKYAP FPAPQLDDRT WPSKRIEKAP IWCSVDLRDG NQALIDPMGH DRKERMFRLL
     IDMGFPEIEI GFPSASQTDF DFCRWAIEQG DVPDDVDLQV LVQCRPELIT RTFEALEGAK
     TPIIHFYNST SELQRRVVFA KDVGGIKQIA TDAAKMIMDM AAKAGGGYRF QYSPESFTGT
     ELDVALEICN AVIEIVKPTP DNKLIVNLPS TVEMNTPNVY ADQIEWMCRN LDNRESLIIS
     LHPHNDRGTG IAATELGLMA GADRGEGTLF GNGERTGNVD VVTLALNMYT QGIDPGLDCT
     DINRMKEVYE YSNQLKIAER HPYVGELVYT AFSGSHQDAI NKGMKARRSA NSPVWEVPYL
     PIDPQDVGRS YEAIIRINSQ SGKGGIAYIL QADYGLNLPR NLQVEFREII QHITDEEGKE
     LPSKRIYEEF QKLYVTQPDA RIKFVDHHTY PHPEQKGRRI LTAEITDNGV TKTIEGKGTG
     PIDGFVDALS KYLGVKMSVV DYSEHSLQQG SDASAISYVE MVYPGGKLFG VGINDNIVSA
     SLEAVVSAAN RVIAK