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Database: UniProt
Entry: Q1MDH6
LinkDB: Q1MDH6
Original site: Q1MDH6 
ID   LEU1_RHIL3              Reviewed;         560 AA.
AC   Q1MDH6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   01-OCT-2014, entry version 58.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=RL3513;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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_00572}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC       (2S)-2-isopropylmalate + CoA. {ECO:0000255|HAMAP-Rule:MF_00572}.
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_00572}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR   EMBL; AM236080; CAK09001.1; -; Genomic_DNA.
DR   RefSeq; YP_769093.1; NC_008380.1.
DR   ProteinModelPortal; Q1MDH6; -.
DR   SMR; Q1MDH6; 4-552.
DR   STRING; 216596.RL3513; -.
DR   EnsemblBacteria; CAK09001; CAK09001; RL3513.
DR   GeneID; 4400996; -.
DR   KEGG; rle:RL3513; -.
DR   PATRIC; 23143775; VBIRhiLeg32091_4807.
DR   eggNOG; COG0119; -.
DR   HOGENOM; HOG000110941; -.
DR   KO; K01649; -.
DR   OMA; VERCNQI; -.
DR   OrthoDB; EOG62G5PZ; -.
DR   BioCyc; RETL1328306-WGS:GSTH-3108-MONOMER; -.
DR   BioCyc; RLEG216596:GKE5-3566-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_00572; LeuA_type2; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
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; TIGR00970; leuA_yeast; 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    560       2-isopropylmalate synthase.
FT                                /FTId=PRO_1000025040.
SQ   SEQUENCE   560 AA;  62262 MW;  CFBA7BFCDD890913 CRC64;
     MPDAAVKYRA YPQVNIPDRT WPTKTITKAP VWCSVDLRDG NQALVDPMGH DRKARMFHLL
     IEMGFKEIEI GFPSASQTDF DFARWCVEEG NVPDDVSLQV LVQCRPELIT RTFEALEGAN
     RPIVHFYNST SELQRRVVFA KDVQGIKQIA VDAAKMITDM ATKAGGGYRF EYSPESFTGT
     ELDVALEICN AVIEVVKPTP DNKLIINLPS TVEMATPNVY ADQIEWMCRN LDNRENLIVS
     LHPHNDRGTG IAAAELALLA GADRVEGTLF GNGERTGNVD MVTMALNMFT QGVDPEIDCS
     NIERIKEVFE YSNQMAIGER HPYVGELVYT AFSGSHQDAI NKGMKAAQVA NHPVWEVPYL
     PIDPRDVGRS YEAIIRINSQ SGKGGIAYIL QQDYGLNLPR NLQVEFREDI QRITDVEGKE
     LPSRRIYDRF IERYVTQPEG RLRFVDHHTY PDTEHKGQRI VAAEITDNGE IKRIEGRGNG
     PIDGFINALS HYLGIEMSVE DYSEHSLQHG SNAAAISYVE TSYPGGKLFG AGINTNIVAA
     SLEAIVSAAN RVLDVKAGKA
//
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