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 01-MAY-2013, entry version 35.
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; VHENDIV; -.
DR ProtClustDB; PRK00439; -.
DR BioCyc; CBOT508767:GHKO-2942-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:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA: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; Aconitase/3IPM_dehydase_swvl; 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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