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Database: UniProt/SWISS-PROT
Entry: LEUD_BURCM
LinkDB: LEUD_BURCM
Original site: LEUD_BURCM 
ID   LEUD_BURCM              Reviewed;         216 AA.
AC   Q0BAC6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   14-MAY-2014, entry version 58.
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=Bamb_3342;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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 1 subfamily.
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DR   EMBL; CP000441; ABI88897.1; -; Genomic_DNA.
DR   RefSeq; YP_775231.1; NC_008391.1.
DR   ProteinModelPortal; Q0BAC6; -.
DR   STRING; 339670.Bamb_3342; -.
DR   EnsemblBacteria; ABI88897; ABI88897; Bamb_3342.
DR   GeneID; 4312344; -.
DR   KEGG; bam:Bamb_3342; -.
DR   PATRIC; 19022477; VBIBurAmb61564_3496.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; YQDNSKR; -.
DR   OrthoDB; EOG661HCP; -.
DR   BioCyc; BAMB339670:GH48-3412-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-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Leucine biosynthesis; Lyase.
FT   CHAIN         1    216       3-isopropylmalate dehydratase small
FT                                subunit.
FT                                /FTId=PRO_1000063740.
SQ   SEQUENCE   216 AA;  24644 MW;  01192951B5878B21 CRC64;
     MEKFTVHTGV VAPLDRENVD TDAIIPKQFL KSIKRTGFGP NAFDEWRYLD HGEPGQDNSK
     RPLNPDFVLN QPRYQGASVL LARKNFGCGS SREHAPWALQ QYGFRAIIAP SFADIFFNNC
     YKNGLLPIVL TEQQVDHLFN DTYAFNGYQL TVDLDAQVVR TGDGREYPFE IAAFRKYCLL
     NGFDDIGLTL RHADKIRQFE AERLAKQPWL NNKLVG
//
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