LEU1_METPB
ID LEU1_METPB Reviewed; 520 AA.
AC B1ZDN3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=Mpop_2796;
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-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; CP001029; ACB80951.1; -; Genomic_DNA.
DR RefSeq; WP_012454673.1; NC_010725.1.
DR AlphaFoldDB; B1ZDN3; -.
DR SMR; B1ZDN3; -.
DR STRING; 441620.Mpop_2796; -.
DR EnsemblBacteria; ACB80951; ACB80951; Mpop_2796.
DR KEGG; mpo:Mpop_2796; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_5; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000007136; 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; Reference proteome; Transferase.
FT CHAIN 1..520
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149222"
FT DOMAIN 12..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 520 AA; 56122 MW; 13914164CD77EBC5 CRC64;
MANTTESAKD RVVIFDTTLR DGEQCPGATM TLDEKLAVAE LLDAMGVDII EAGFPIASNG
DFEAVSEIAR RTKRATIAGL ARAIPADIAR AGEAVRHAKA GRIHTFVSTS AIHLAHQMRK
TQDEVIEIIL KTVTQARDLV EDVEWSAMDA TRTDIDYLCR CVEAAIRSGA TTINLPDTVG
YATPQEYGAM FRQVRERVPN SDKAIFSVHC HNDLGLAVAN SLAGLEGGAR QIECTVNGIG
ERAGNAALEE IVMAIRTRAD VMPYDTGIDT TMLTRASKLV SHAANFPVQY NKAIVGRNAF
AHESGIHQDG MLKHSETYEI MTPASVGLSK TSLVMGKHSG RAAFKSKLAE LGISLSDNQF
QDVFERFKDL ADRKKHVYDE DIEALVDEKL ATAHDRIKLL SLSVIAGTRG PQRATMKIEM
DGRTFTEEAD GNGPVDAVFN AIHEIVPHDA VLELYQVHAV TEGTDAQAEV SVRLKAGERS
VTARGADPDT LVASAKAYLS ALNKLSAASV RLHAQHAAVV