LEU1_BUCAP
ID LEU1_BUCAP Reviewed; 518 AA.
AC O85063; Q9R862;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=BUsg_PL4;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OG Plasmid pLeu-Sg (pBSg1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=9873079; DOI=10.1007/pl00006447;
RA Baumann L., Baumann P., Moran N.A., Sandstroem J.P., Thao M.L.;
RT "Genetic characterization of plasmids containing genes encoding enzymes of
RT leucine biosynthesis in endosymbionts (Buchnera) of aphids.";
RL J. Mol. Evol. 48:77-85(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=9812361; DOI=10.1111/j.1574-6968.1998.tb13253.x;
RA Silva F.J., van Ham R.C.H.J., Sabater B., Latorre A.;
RT "Structure and evolution of the leucine plasmids carried by the
RT endosymbiont (Buchnera aphidicola) from aphids of the family Aphididae.";
RL FEMS Microbiol. Lett. 168:43-49(1998).
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).
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; AF041836; AAD12593.1; -; Genomic_DNA.
DR EMBL; AJ006876; CAA07296.1; -; Genomic_DNA.
DR RefSeq; NP_047180.1; NC_001910.1.
DR AlphaFoldDB; O85063; -.
DR SMR; O85063; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000416; Plasmid pLeu-Sg.
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; 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; Plasmid; Transferase.
FT CHAIN 1..518
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140335"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 518 AA; 57221 MW; DD615E98D9538297 CRC64;
MNSQVIIFDT TLRDGEQALQ ASLSVKQKLQ IALSLENAGI DIIEVGFPIS SPGDFKSVQT
ISKNIKNSRI CSLARCLNKD IDTAAEAMSS SNTFRIHIFL ATSTLHMESK LKKNFDQIID
MAISSVKRAL RYTDDVEFSC EDASRTTMDN LCRIVEQLIK AGVKTINIPD TVGYTVPNEL
STIIHNLFKR VPNIDQSIIS VHCHNDLGMA VGNSISAIQA GARQIEGTIN GIGERAGNTA
LEEVIMAIKV REDILGVSTN IKHKEIYRTS QIISQICNLP IPPNKAIVGS NAFAHSSGIH
QDGVLKNRKN YEIMEPSSIG LKEVKLNLTS RSGRAAVKYY MTQMGYKECD YNIDELYTSF
LKLADKKGQV FDYDLEALAF INMQQEESEY FSLSFFSVQS ISNGLSTASV KLLCGKKVSI
ESATTSNGPI DAIYQALNRI TNFPITLQKY QLVAKGKGRD ALGQVDILVE YKKRKFHGVG
LATDIIESSA QAMVNVLNNI WKANQVNEKL KTLKKVNN
