(data stored in SCRATCH zone)

SWISSPROT: C0ZN67_RHOE4

ID   C0ZN67_RHOE4            Unreviewed;       602 AA.
AC   C0ZN67;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS01061848};
DE            EC=2.3.3.13 {ECO:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS01061848};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_00572,
GN   ECO:0000313|EMBL:BAH31119.1};
GN   OrderedLocusNames=RER_04110 {ECO:0000313|EMBL:BAH31119.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31119.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31119.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(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:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS01061844}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524,
CC         ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC         EC=2.3.3.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00572,
CC         ECO:0000256|SAAS:SAAS01114948};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|HAMAP-Rule:MF_00572, ECO:0000256|SAAS:SAAS01061841}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00572,
CC       ECO:0000256|SAAS:SAAS01061839}.
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DR   EMBL; AP008957; BAH31119.1; -; Genomic_DNA.
DR   RefSeq; WP_019746565.1; NC_012490.1.
DR   STRING; 234621.RER_04110; -.
DR   EnsemblBacteria; BAH31119; BAH31119; RER_04110.
DR   GeneID; 31540269; -.
DR   KEGG; rer:RER_04110; -.
DR   PATRIC; fig|234621.6.peg.852; -.
DR   eggNOG; ENOG4107QXN; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000110941; -.
DR   KO; K01649; -.
DR   OMA; CVSLHPH; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002204; 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   CDD; cd07942; DRE_TIM_LeuA; 1.
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; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
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;
DR   PRODOM; C0ZN67.
DR   SWISS-2DPAGE; C0ZN67.
KW   Acyltransferase {ECO:0000313|EMBL:BAH31119.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00161459};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00572, ECO:0000256|SAAS:SAAS00160591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS01061847};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00131367, ECO:0000313|EMBL:BAH31119.1}.
FT   DOMAIN       67    341       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   602 AA;  66104 MW;  889B404EA7655CA2 CRC64;
     MSPADAFTTG TRTITPPTKP APSDQPAWNT QKNSSMPTFR YRPFAEEVET VTLPDRTWPD
     KIIDRAPQWC AVDLRDGNQA LIDPMSPARK RRMFDLLVRM GYKEIEVGFP SASQTDFDFV
     REIIEDGAIP SDVTIQVLTQ SRPELIKRTF EACEGAENAI VHFYNSTSIL QRRVVFRADK
     DTIKKIATDA AELVLAESKK YPDTNWRWEY SPESYTGTEL EYAKEVCDAV TETLGATPAN
     PVILNLPATV EMATPNVYAD SIEWMHRNLA RRDSVILSLH PHNDRGTGVA AAELGYQAGA
     DRIEGCLFGN GERTGNVCLV TLALNMFTRG VDPQIDFSNI DEIRRTVEYC NQLPVHERHP
     YGGDLVYTAF SGSHQDAINK GLDAMKVDAD NQDSDVDDIL WQVPYLPIDP KDVGRSYEAV
     IRVNSQSGKG GVAYIMKADH GLVLPRRLQV EFSQSVQKIT DGEGGEVSPK EMWDVFHEEY
     LAPVTPLERM KQKVTASEED GGTDAITAIV KVNGKEQEIS GTGNGPLAAF VDALGSINFD
     VRVLDYSEHA MSAGDDAQAA AYVECAVTGP DGQSTVVWGV GIATSITTAS LRAVVSAVNR
     AS
//

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