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Database: UniProt
Entry: B2JDN6
LinkDB: B2JDN6
Original site: B2JDN6 
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-OCT-2014, entry version 45.
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};
GN   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).
CC       {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC       (2S)-2-isopropylmalate + CoA. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000255|HAMAP-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; 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; ICSLARC; -.
DR   OrthoDB; EOG6CGCF3; -.
DR   BioCyc; BPHY391038:GI4Z-2067-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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   Complete proteome; Leucine biosynthesis; Reference proteome;
KW   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
//
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