ID LEU1_BURP8 Reviewed; 516 AA.
AC B2JDN6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=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=Bphy_2017;
OS Burkholderia phymatum (strain DSM 17167 / STM815).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / STM815;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D.,
RA Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Bacher J., Blanchard J., Cohan F.,
RA James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P.,
RA Riley M., Souza V., Wertz J., Young P.;
RT "Complete sequence of chromosome 1 of Burkholderia phymatum STM815.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC (2S)-2-isopropylmalate + CoA.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily.
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DR EMBL; CP001043; ACC71196.1; -; Genomic_DNA.
DR RefSeq; YP_001858242.1; NC_010622.1.
DR ProteinModelPortal; B2JDN6; -.
DR STRING; 391038.Bphy_2017; -.
DR EnsemblBacteria; ACC71196; ACC71196; Bphy_2017.
DR GeneID; 6243506; -.
DR KEGG; bph:Bphy_2017; -.
DR PATRIC; 19190477; VBIBurPhy25146_2150.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; PRK00915; -.
DR BioCyc; BPHY391038:GI4Z-6730-MONOMER; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 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; 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; 2-isopropylmalate_synth_dimer; 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 Complete proteome; Leucine biosynthesis; Transferase.
FT CHAIN 1 516 2-isopropylmalate synthase.
FT /FTId=PRO_1000149154.
SQ SEQUENCE 516 AA; 55873 MW; 222F4FEF2C0D7C81 CRC64;
MADKLIIFDT TLRDGEQSPG ASMTKEEKIR IAKQLERMKV DVIEAGFAAS SNGDFDAIHT
IAGMIKDSTI CSLARANDKD IQRAADALKP ADHFRIHTFI ATSPLHMEKK LRMSPEQVLE
QAKLAVRFAR KFTNDVEFSP EDGSRSDMDF LCRVLEAVIA EGATTINIAD TVGYGVPELY
GNLVKTLRER IPNSDKAVFS VHCHNDLGMA VANSLAGVKI GGARQVECTI NGLGERAGNT
SLEEIVMAVR TRKDYFGLDL GIDTTQIVPA SKLVSQITGF VVQPNKAVVG ANAFAHASGI
HQDGVLKARD TYEIMRAEDV GWTANKIVLG KLSGRNAFKQ RLQELGISLD SESELNLAFQ
RFKELADRKA EIFDEDIIAI VTEESAEAQE KEHYKFVSLS QHSETGERPH ARIVFSVEGK
EVVGEANGNG PVDATLNAIE TEVGSGSELL LYSVNAITTG TQAQGEVTVR LSKAGRIVNG
VGTDPDIVAA SAKAYISALN RLYAGADKLN PQRADI
//
