ID LEUD_SALSV Reviewed; 201 AA.
AC B4TWV8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-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=SeSA_A0126;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M.,
RA Leclerc J., Cebula T., Sebastian Y.;
RT "Complete genome of Salmonella schwarzengrund strain CVM19633.";
RL Submitted (JUL-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 1 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001127; ACF92071.1; -; Genomic_DNA.
DR RefSeq; YP_002113129.1; NC_011094.1.
DR STRING; 439843.SeSA_A0126; -.
DR PRIDE; B4TWV8; -.
DR EnsemblBacteria; ACF92071; ACF92071; SeSA_A0126.
DR GeneID; 6516516; -.
DR KEGG; sew:SeSA_A0126; -.
DR PATRIC; 32368931; VBISalEnt87589_0243.
DR eggNOG; COG0066; -.
DR HOGENOM; HOG000222939; -.
DR KO; K01704; -.
DR OMA; YQDNSKR; -.
DR ProtClustDB; PRK01641; -.
DR BioCyc; SENT439843:GHHR-3560-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_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 PANTHER; PTHR11670:SF2; PTHR11670:SF2; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 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 1 201 3-isopropylmalate dehydratase small
FT subunit.
FT /FTId=PRO_1000135832.
SQ SEQUENCE 201 AA; 22520 MW; 203FAA4F06B0BE2C CRC64;
MAEKFTQHTG LVVPLDAANI DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL DEKGQQPNPE
FVLNFPEYQG ASILLARENF GCGSSREHAP WALTDYGFKV VIAPSFADIF YGNSFNNQLL
PVTLSDAQVD ELFALVKANP GIKFEVDLEA QVVKAGDKTY SFKIDDFRRH CMLNGLDSIG
LTLQHEDAIA AYENKQPAFM R
//