(data stored in ACNUC1104 zone)

SWISSPROT: A4F6E9_SACEN

ID   A4F6E9_SACEN            Unreviewed;       596 AA.
AC   A4F6E9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 92.
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:CAL99623.1};
GN   OrderedLocusNames=SACE_0274 {ECO:0000313|EMBL:CAL99623.1};
GN   ORFNames=A8924_0669 {ECO:0000313|EMBL:PFG93428.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99623.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99623.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99623.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93428.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93428.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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: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; AM420293; CAL99623.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93428.1; -; Genomic_DNA.
DR   RefSeq; WP_011873000.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0274; -.
DR   EnsemblBacteria; CAL99623; CAL99623; SACE_0274.
DR   KEGG; sen:SACE_0274; -.
DR   eggNOG; ENOG4107QXN; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000110941; -.
DR   KO; K01649; -.
DR   OMA; CVSLHPH; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; SERY405948:SACE_RS01345-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F6E9.
DR   SWISS-2DPAGE; A4F6E9.
KW   Acyltransferase {ECO:0000313|EMBL:CAL99623.1};
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:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS01061847};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00572,
KW   ECO:0000256|SAAS:SAAS00131367, ECO:0000313|EMBL:CAL99623.1}.
FT   DOMAIN       68    342       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   596 AA;  65916 MW;  1D21F54493399666 CRC64;
     MSIPPEPQTP ISNRVRKPSR PAPADQQPWN PQLGSSMPFH RYRPFHELVE DVSLPDRTWP
     DNRITRAPLW CAVDLRDGNQ ALIDPMSPAR KRRMFDLLVR MGFKEIEVGF PAASQTDFDF
     VREIIEDGAV PDDVRIQVLT QCRPELIERT FASLEGAAKA VVHIYNSTSI LQRRVVFREE
     REGIKKIATM GAEMALEFAG KYPDTDFRFQ YSPESYTGTE LSYAAEVCDA VTEIWQPTPE
     RPVILNLPAT VEMATPNVYA DSIEWMHRNL SRRDSVLLSL HPHNDRGTGI AAAELGYQAG
     ADRIEGCLFG NGERTGNVDL VALGMNLFSQ GIDPQIDFSD LDYIKRTVEH CNQLPVHERH
     PWGGELVYTA FSGSHQDAIN KGLNALREEA AKAGAEVDAH PWEVPYLPID PKDVGRSYEA
     VIRVNSQSGK GGVAYIMKTE HQLDLPRKMQ IEFSKLVQAR TDSEGGEVTP DQMWAVFSDE
     YLGARTPLEL VRQRLDGEAG DETITATVVV DGDEREITGS GNGPIAAFVD ALSTVGFDVR
     VMDYSEHALT AGDDALAAAY LECAVGDDVL WGVAIDSSTV KASLHAIVSA VNRAGR
//

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