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Entry: LEUD_SHIFL
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Original site: LEUD_SHIFL 
ID   LEUD_SHIFL              Reviewed;         201 AA.
AC   P59714;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-OCT-2014, entry version 80.
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=SF0066, S0068;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN41731.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15612.1; -; Genomic_DNA.
DR   RefSeq; NP_706024.1; NC_004337.2.
DR   RefSeq; NP_835807.1; NC_004741.1.
DR   STRING; 198214.SF0066; -.
DR   PaxDb; P59714; -.
DR   EnsemblBacteria; AAN41731; AAN41731; SF0066.
DR   EnsemblBacteria; AAP15612; AAP15612; S0068.
DR   GeneID; 1024536; -.
DR   GeneID; 1076498; -.
DR   KEGG; sfl:SF0066; -.
DR   KEGG; sfx:S0068; -.
DR   PATRIC; 18701070; VBIShiFle31049_0077.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; YQDNSKR; -.
DR   OrthoDB; EOG661HCP; -.
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   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    201       3-isopropylmalate dehydratase small
FT                                subunit.
FT                                /FTId=PRO_0000141880.
SQ   SEQUENCE   201 AA;  22503 MW;  E5A99D82468E7787 CRC64;
     MAEKFIKHTG LVVPLDAANV DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL DEKGQQPNPD
     FVLNFPQYQG ASILLARENF GCGSSREHAP WALTDYGFKV VIAPSFADIF YGNSFNNQLL
     PVKLSDAEVD ELFALVKANP GIHFDVDLEA QEVKAGEKTY RFTIDAFRRH CMMNGLDSIG
     LTLQHDDAIA SYEAKQPAFM N
//
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