LEU1_RHOPT
ID LEU1_RHOPT Reviewed; 524 AA.
AC B3QCX5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Rpal_2259;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACF00780.1; -; Genomic_DNA.
DR RefSeq; WP_012495562.1; NC_011004.1.
DR AlphaFoldDB; B3QCX5; -.
DR SMR; B3QCX5; -.
DR EnsemblBacteria; ACF00780; ACF00780; Rpal_2259.
DR KEGG; rpt:Rpal_2259; -.
DR HOGENOM; CLU_022158_0_1_5; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR BioCyc; RPAL395960:RPAL_RS11215-MON; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001725; Chromosome.
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; Transferase.
FT CHAIN 1..524
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149261"
FT DOMAIN 12..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 524 AA; 57553 MW; 331439CC8D71A49E CRC64;
MTTTTQSEQD RVIIFDTTLR DGEQCPGATM TFEEKLNVAR MLDDMGVDVI EAGYPFASDG
DFEAVHEIAK RSKNSVICGL SRAAHKDIDR CAEAIKPAER GRIHTFLSTS PVHMKYKLQM
EAAQVYEMVI SSVTRARNHT DDVEWSAEDA TRTEFDFLCR CIEAAIKAGA TTINLPDTVG
YAVPEEYREL FRKVRETVPN SDKARFSVHC HNDLGMAVAN SMAGVAGGAR QIECTINGIG
ERAGNAALEE VVMAMRVRQD KLPYWNRIET TMLTHASKTV SAATSFPVQY NKAIVGRNAF
AHESGIHQDG MIKNAQTYEI MTPETVGVKG TSLVMGKHSG RAGLIHKMEE LGYKLSRNQI
EDVFVRFKAL ADRKKDVYDE DIEALVDEQL LHGQDQIKLM SLTVIAGTHG PQRATMKLDV
DGQIRIEEAE GNGPVDAVFN CIKALVPHDA KLELYQVHAV TEGTDAQAEV SVRLSHEGRS
MTARAADPDT LVASAKAYLG ALNKIVAKRQ RSVREDAPTV AVAG