LEU1_RHOPS
ID LEU1_RHOPS Reviewed; 524 AA.
AC Q138Z2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=RPD_2112;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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; CP000283; ABE39347.1; -; Genomic_DNA.
DR AlphaFoldDB; Q138Z2; -.
DR SMR; Q138Z2; -.
DR STRING; 316057.RPD_2112; -.
DR EnsemblBacteria; ABE39347; ABE39347; RPD_2112.
DR KEGG; rpd:RPD_2112; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_5; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR BioCyc; RPAL316057:RPD_RS10605-MON; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001818; 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_1000149260"
FT DOMAIN 12..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 524 AA; 57526 MW; 5831C67A3B2B6D76 CRC64;
MTTTPKSEQD RVIIFDTTLR DGEQCPGATM TFEEKLNVAA MLDEMGVDVI EAGYPFASDG
DFEAVHEIAK RSKNSVICGL SRAAHKDIDR CAEAIKPAER GRIHTFLSTS PVHMKYKLQM
EAAQVYEMVI SSVTRARNHT DDVEWSAEDA TRTEFDFLCR CIEAAIKAGA TTINLPDTVG
YAVPEEYREM FRKVRETVPN ADKARFSVHC HDDLGMAVAN SIAGVQGGAR QIECTINGIG
ERAGNAALEE VVMAMRVRQD KVPYWNRIES KMLTHASKTV SAATSFPVQY NKAIVGRNAF
AHESGIHQDG MIKNAQTYEI MTPETVGVKG TSLVMGKHSG RAGLIHKMEE LGYKLSRNQI
EDVFVRFKAL ADRKKDVYDE DIEALVDEQL LHGQDLIRLK SLTVIAGTHG PQRATMKIDV
DGQLRIEEAE GNGPVDAVFN CIKALVPHDA KLELYQVHAV TEGTDAQAEV SVRLSHEGRS
MTARAADPDT LVASAKAYLG ALNKIVAKRQ RDVRQDAPAV AVAG