LEU1_BRUSU
ID LEU1_BRUSU Reviewed; 555 AA.
AC Q8FZC4; G0KC46;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 103.
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};
GN OrderedLocusNames=BR1566, BS1330_I1560;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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=AAN30472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014291; AAN30472.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002997; AEM18888.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FZC4; -.
DR SMR; Q8FZC4; -.
DR EnsemblBacteria; AEM18888; AEM18888; BS1330_I1560.
DR KEGG; bms:BR1566; -.
DR KEGG; bsi:BS1330_I1560; -.
DR PATRIC; fig|204722.22.peg.527; -.
DR HOGENOM; CLU_004588_3_0_5; -.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:Q8FZC4; -.
DR Proteomes; UP000007104; 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_0000140429"
FT DOMAIN 30..303
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 555 AA; 61634 MW; F84880E937F4E7CE 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 GADRVEGTLF GNGERTGNVD VVTLALNMYT QGIDPGLDCT
DINRMKEVYE YSNQLKIAER HPYVGELVYT AFSGSHQDAI NKGMKARRSA NSPVWEVPYL
PIDPQDVGRS YEAIIRINSQ SGKGGIAYIL QADYGLNLPR NLQVEFREII QHITDEEGKE
LPSKRIYEEF QKLYVTQPDA RIKFVDHHTY PDPEQKGRRI LTAEITDNGV TKTIEGKGTG
PIDGFVDALS KYLGVKMSVV DYSEHSLQQG SDASAISYVE MVYPGGKLFG VGINDNIVSA
SLEAVVSAAN RVIAK
