LEU1_BURCM
ID LEU1_BURCM Reviewed; 514 AA.
AC Q0BDB9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=Bamb_2298;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-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; CP000440; ABI87854.1; -; Genomic_DNA.
DR RefSeq; WP_011657491.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BDB9; -.
DR SMR; Q0BDB9; -.
DR STRING; 339670.Bamb_2298; -.
DR EnsemblBacteria; ABI87854; ABI87854; Bamb_2298.
DR GeneID; 44692967; -.
DR KEGG; bam:Bamb_2298; -.
DR PATRIC; fig|339670.21.peg.2629; -.
DR eggNOG; COG0119; Bacteria.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000662; Chromosome 1.
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..514
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149149"
FT DOMAIN 5..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 514 AA; 55541 MW; 54A1DAAC934D22EC CRC64;
MTDKLIIFDT TLRDGEQSPG ASMTKEEKIR IAKHLERMKV DVIEAGFAAS SNGDFDAIHT
IAGLVKDSTI CSLARANDKD IQRAADALKP ANSARIHTFI ATSPLHMEKK LRMTPDQVFE
QARLAVRFAR KFTDNVEFSP EDGSRSDLDF LCRVLEAVIA EGATTINIAD TVGYGVPELY
GNLVKTLRER IPNSDKAIFS VHCHNDLGMA VANSLAGVKI GGARQVECTI NGLGERAGNT
SLEEIVMAVK TRKDYFGLDV GLDTTQIVPT SKLVSQITGF VVQPNKAVVG ANAFAHASGI
HQDGVLKARD TYEIMRAEDV GWTANKIVLG KLSGRNAFKQ RLQELGVSLD SETELNAAFM
RFKDLADRKS DIFDEDIIAI VSEESAFAQE QEHYKFVSLS QRSETGEQPQ AKVVLALDGK
EVTGEARGNG PVDATFNAIE GEVGSGSELL LYSVNAITTG TQAQGEVTVR LSKSGRIVNG
VGTDPDIVAA SAKAYIAALN KLHSKDDKLN PQRS
