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Entry: LEUD_SALSV
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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   09-JUL-2014, entry version 41.
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;
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; 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   PATRIC; 32368931; VBISalEnt87589_0243.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   OMA; YQDNSKR; -.
DR   OrthoDB; EOG661HCP; -.
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: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    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
//
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