(data stored in ACNUC7421 zone)

HOGENOM: FRASU_1_PE1005

ID   FRASU_1_PE1005                       STANDARD;      PRT;   578 AA.
AC   FRASU_1_PE1005; E3IYV5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=2-isopropylmalate synthase; EC=2.3.3 13;AltName:
DE   Full=Alpha-IPM synthase;AltName: Full=Alpha-isopropylmalate synthase;
DE   (FRASU_1.PE1005).
GN   Name=leuA; OrderedLocusNames=FraEuI1c_1020;
OS   FRANKIA SP. EUI1C.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=298654;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRASU_1.PE1005.
CC       Frankia sp. EuI1c chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E3IYV5_FRASU
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.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily.
CC   -!- GENE_FAMILY: HOG000110941 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E3IYV5; -.
DR   EMBL; CP002299; ADP79093.1; -; Genomic_DNA.
DR   RefSeq; YP_004014963.1; NC_014666.1.
DR   ProteinModelPortal; E3IYV5; -.
DR   GeneID; 9971443; -.
DR   GenomeReviews; CP002299_GR; FraEuI1c_1020.
DR   KEGG; fri:FraEuI1c_1020; -.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:HAMAP.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
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   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
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; 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.
DR   HOGENOMDNA; FRASU_1.PE1005; -.
KW   2-isopropylmalate synthase;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Leucine biosynthesis; Transferase.
SQ   SEQUENCE   578 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MITNPQVPSG MPIDKYRPFT PVALPDRTWP NAQITKAPLW CSVDLRDGNQ ALVDPMTPER
     KLKMFELLVG MGYKEIEVGF PAASQTDFDF IRQLIEEERI PDDVTIQVLT QAREELIERT
     VQSLVGSRRA LLHLYNSTST LQRRVVFNSD RAGITEIAVQ GARWTVQYAE KLLDDRTDLR
     WQYSPESFTG TELEYAVEVC EAVMDVWEPT ADRPVVLNLP ATVEMSTPNV YADQIEWVGR
     NLTRRDAVVL SLHPHNDRGC AVAAAELGVM AGADRVEGCL FGNGERTGNV CLVTLGMNLF
     SQGIDPQIDF SDIDEIRRTT EYCNQLPVHP RHPYGGDLVY TAFSGSHQDA IKKGLEAMDR
     TGQRVWEVPY LPIDPKDVGR TYEAVIRVNS QSGKGGVAYL LKSEHGLDLP RRLQIEFSGV
     VQRHTDGEGG EVTAGQLWEM FRREYFLDET AGPAPLEVLQ FAATAGSGAQ DEVTVSVRRD
     GAEEVLTGKG NGPIDAFVDA LSTRGVSVKV HDYNEHAIGA GADARAAAYL EVAVEDAQGA
     RVYWGVGIDP NIVTASLRAV VSAVNRAARA RTTPVVAS
//

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