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Database: UniProt/TrEMBL
Entry: A3DHI3_CLOTH
LinkDB: A3DHI3_CLOTH
Original site: A3DHI3_CLOTH 
ID   A3DHI3_CLOTH            Unreviewed;       189 AA.
AC   A3DHI3;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   14-MAY-2014, entry version 48.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuD; OrderedLocusNames=Cthe_2210;
OS   Clostridium thermocellum (strain ATCC 27405 / DSM 1237).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) 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; CP000568; ABN53412.1; -; Genomic_DNA.
DR   RefSeq; YP_001038605.1; NC_009012.1.
DR   ProteinModelPortal; A3DHI3; -.
DR   SMR; A3DHI3; 23-183.
DR   STRING; 203119.Cthe_2210; -.
DR   EnsemblBacteria; ABN53412; ABN53412; Cthe_2210.
DR   GeneID; 4811075; -.
DR   KEGG; cth:Cthe_2210; -.
DR   PATRIC; 19518366; VBICloThe47081_2351.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222940; -.
DR   KO; K01704; -.
DR   OMA; DIARHCL; -.
DR   OrthoDB; EOG6PZXB8; -.
DR   BioCyc; CTHE203119:GIW8-2277-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.
SQ   SEQUENCE   189 AA;  20875 MW;  DB8087E96AC8A861 CRC64;
     MNFNLKSYMQ RVEYVEVKER GKMKAQGKAI KYGDNVDTDV IIPARYLNTS DPNELAKHCM
     EDIDTEFVSK VQKGDIIVAG KNFGCGSSRE HAPIAIKASG ISCVIAETFA RIFYRNAINI
     GLPIIECPEA AKDISDGDIV SIDFDTGKIV NVTKNKEYTG VPFPEFMQEI IASDGLIGYI
     KKQIGNKEA
//
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