LEU1_BUCML
ID LEU1_BUCML Reviewed; 502 AA.
AC Q9EVG4;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 68.
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};
DE Flags: Fragment;
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025};
OS Buchnera aphidicola subsp. Macrosiphoniella ludovicianae.
OG Plasmid pLeu (pBAp1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118105;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11133977; DOI=10.1128/jb.183.2.785-790.2001;
RA Wernegreen J.J., Moran N.A.;
RT "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT (Buchnera).";
RL J. Bacteriol. 183:785-790(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; AF197456; AAG31401.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EVG4; -.
DR SMR; Q9EVG4; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Plasmid; Transferase.
FT CHAIN <1..502
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140338"
FT DOMAIN <1..254
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT NON_TER 1
SQ SEQUENCE 502 AA; 55911 MW; 6A7E845D247560FE CRC64;
DGEQALQASL SVKEKLQIAL CLEKIGVDIM EIGFPISSPG DFKSVQIISK NIKNSRICSL
ARCVEKDIDA AGEAMSASNS FRIHIFLATS TLHMEYKLKK NFHEIIDMAI FAVKRALRYT
DDIEFSCEDA SRTTIDNLCR IVEKLIYHGV KTINIPDTVG YTVPNELSYI IKNLLERVPN
IHKSIISVHC HDDLGMAVGN SISAIQAGAR QIEGTINGIG ERAGNTALEE VIMAIKVRED
ILGVSTNINY KEIYHTSKII SRICNMPIPP NKAIVGSNAF SHSSGIHQDG VLKNRKNYEI
IDPSSIGFKK LKLNLTSRSG RAAVKYYMSE MGYKDTDYNI DELYADFLKL ADKKGQVFDY
DLESLAFISK HPEELEHFCL KFFSVQSISN GLSTASIKLL CGQKLYIESS TTSNGPVDAI
YQALNKITNF PIILQKFQLI AKGKGKDALG QVNILIEYKK RKFHGIGLAT DFIESSAKAM
VNVLNNIWQA EQVNKKLQEL KK
