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Database: UniProt/SWISS-PROT
Entry: LEUD_CLOBA
LinkDB: LEUD_CLOBA
Original site: LEUD_CLOBA 
ID   LEUD_CLOBA              Reviewed;         161 AA.
AC   B2UYT4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   19-FEB-2014, entry version 39.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuD; OrderedLocusNames=CLH_0304;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska
RT   E43.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD (By similarity).
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
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DR   EMBL; CP001078; ACD53891.1; -; Genomic_DNA.
DR   RefSeq; YP_001919739.1; NC_010723.1.
DR   STRING; 508767.CLH_0304; -.
DR   EnsemblBacteria; ACD53891; ACD53891; CLH_0304.
DR   GeneID; 6320156; -.
DR   KEGG; cbt:CLH_0304; -.
DR   PATRIC; 19416878; VBICloBot115804_0270.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222940; -.
DR   KO; K01704; -.
DR   OMA; MKGRAWK; -.
DR   OrthoDB; EOG6PZXB8; -.
DR   ProtClustDB; PRK00439; -.
DR   BioCyc; CBOT508767:GHKO-302-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01032; LeuD_type2; 1.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR011827; IsopropMal_deHydtase_ssu.
DR   InterPro; IPR011824; IsopropMal_deHydtase_ssu_bac.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   TIGRFAMs; TIGR02084; leud; 1.
DR   TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Leucine biosynthesis; Lyase.
FT   CHAIN         1    161       3-isopropylmalate dehydratase small
FT                                subunit.
FT                                /FTId=PRO_1000135846.
SQ   SEQUENCE   161 AA;  17909 MW;  ADEECBA12CEDF43A CRC64;
     MSIKGRVFKY GDNVDTDVII PARYLNTSNH KELASHCMED IDKDFVNNVK DGDIIVANKN
     FGCGSSREHA PIAIKASGIS CVIASTFARI FYRNSINIGL PILECDEAVK NINDGDELEV
     DFSTGIIKNL SKNEKYKGEA FPEFMQKIID NDGLIGYIRN K
//
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