(data stored in ACNUC7421 zone)

HOGENOM: RALPJ_1_PE1014

ID   RALPJ_1_PE1014                       STANDARD;      PRT;   570 AA.
AC   RALPJ_1_PE1014; B2UJY9;
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   (RALPJ_1.PE1014).
GN   Name=leuA; OrderedLocusNames=Rpic_4806;
OS   RALSTONIA PICKETTII 12J.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RALPJ_1.PE1014.
CC       Ralstonia pickettii 12J chromosome 2, complete sequence.
CC       96802056..97720880 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:LEU1_RALPJ
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. LeuA type 2 subfamily.
CC   -!- GENE_FAMILY: HOG000110941 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B2UJY9; -.
DR   EMBL; CP001069; ACD29890.1; -; Genomic_DNA.
DR   RefSeq; YP_001893317.1; NC_010678.1.
DR   ProteinModelPortal; B2UJY9; -.
DR   SMR; B2UJY9; 4-551.
DR   STRING; B2UJY9; -.
DR   GeneID; 6285501; -.
DR   GenomeReviews; CP001069_GR; Rpic_4806.
DR   KEGG; rpi:Rpic_4806; -.
DR   OMA; APRWCAV; -.
DR   ProtClustDB; PRK03739; -.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
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; RALPJ_1.PE1014; -.
KW   2-isopropylmalate synthase;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Leucine biosynthesis; Transferase.
SQ   SEQUENCE   570 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLKNPATKYR PFPAIALADR TWPNKTITRA PIWMSTDLRD GNQALFEPMN AERKMRMFKM
     LVQIGFKEIE AAFPAASQTD FDFVRELIEG GHIPDGVAIE VLTQAREDLI RRTMESLRGA
     KRAIIHVYNA TAPVFRRTVF NTDREGVKRI AVQSAKLIRE IAQTMPETQW TYQYSPEVFS
     GTELDFALEV CNAVTEVWEP TPEHKIIFNL PATVEMATPN IYADQIEWMH RNLARRDSII
     LSVHPHNDRG TAVAAAELAV MAGADRVEGC LFGNGERTGN VDIVTLALNL YSQGVDPELD
     FSHINDVART CEDCTQLPVH PRHPYVGDLV FTAFSGSHQD AIKKGFAVQK PDAPWEMPYL
     PIDPADVGRT YDSIIRVNSQ SGKGGIAYLL ESGYGVAMPR RLQVEFSSTV QKLTDASGRE
     ATGADIWALF QQTYLRSDGA IGYVSHRLTE RDDGSQHIRL VVNIDDHEHI CEGSGNGPLD
     ALVHALSHVL TAPVSIHHYE ERALGQGANA DAIAFAELAA TGVAGSVFGV GVDANLTTAS
     IRAVVGGVNR LIARTGQGML RRSSAQATVA
//

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