LEU1_BUCBP
ID LEU1_BUCBP Reviewed; 390 AA.
AC Q89A49;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative 2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=bbp_493;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. It lacks about 130 C-
CC terminal residues. {ECO:0000305}.
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DR EMBL; AE016826; AAO27198.1; -; Genomic_DNA.
DR RefSeq; WP_011091599.1; NC_004545.1.
DR AlphaFoldDB; Q89A49; -.
DR SMR; Q89A49; -.
DR STRING; 224915.bbp_493; -.
DR EnsemblBacteria; AAO27198; AAO27198; bbp_493.
DR GeneID; 56471028; -.
DR KEGG; bab:bbp_493; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_3_1_6; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000601; Chromosome.
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 InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 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 5: Uncertain;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="Putative 2-isopropylmalate synthase"
FT /id="PRO_0000140336"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 390 AA; 43227 MW; 780EA1D8D08D2B07 CRC64;
MTQKIIIFDT TLRDGEQSLK MSLSVKKKLK IAFALEKLGV DVIEAGFPIS SPGDFESVKK
ISERIKDAKI CSLARCIDGD IDIAAKAMKK ANSFRIHIFL GTSALHVQSK LKKTFDQIID
MMVSSVKRAQ KYTDDVEFSC EDAGRTSLDD LCRIIELAID LGVKTINIPD TVGYTIPYEF
SNIISSIYKK VPNIDKAIIS VHCHDDLGMA VANSISAIQV GARQIEGTIT GVGERAGNAA
LEEILMAIKI RKDILNFKTN IKYQEIYSTC RVISSICNIP VPVNKAIIGS NAFSHSSGIH
QDGILKDKKT YEIIVPESIG FVSQPLNLTS RSGRAAVKYR MKKIGYKDSD YNIDILYSRF
LKLADKKGRV SDSDLKQLVC FNNKLKNLKD
