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Database: UniProt/SWISS-PROT
Entry: LEUD_KLEP3
LinkDB: LEUD_KLEP3
Original site: LEUD_KLEP3 
ID   LEUD_KLEP3              Reviewed;         201 AA.
AC   B5Y1W5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   01-OCT-2014, entry version 43.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000255|HAMAP-Rule:MF_01031};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
DE            Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01031};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01031};
GN   Name=leuD {ECO:0000255|HAMAP-Rule:MF_01031};
GN   OrderedLocusNames=KPK_4665;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J.,
RA   Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C.,
RA   Triplett E.W., Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in
RT   mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01031}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01031}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01031}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC       Rule:MF_01031}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01031}.
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DR   EMBL; CP000964; ACI09462.1; -; Genomic_DNA.
DR   RefSeq; YP_002240456.1; NC_011283.1.
DR   STRING; 507522.KPK_4665; -.
DR   PRIDE; B5Y1W5; -.
DR   EnsemblBacteria; ACI09462; ACI09462; KPK_4665.
DR   GeneID; 6936822; -.
DR   KEGG; kpe:KPK_4665; -.
DR   PATRIC; 20442479; VBIKlePne121904_4581.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; YQDNSKR; -.
DR   OrthoDB; EOG661HCP; -.
DR   BioCyc; KPNE507522:GI0B-4666-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_1000135811.
SQ   SEQUENCE   201 AA;  22571 MW;  35D2C7EB1B840C95 CRC64;
     MAEKFTQHTG LVVPLDAANV DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL DDKGQQPNPD
     FVLNFPQYKG ASILLARENF GCGSSREHAP WALTDYGFKV VIAPSFADIF YGNSFNNQLL
     PVTLSDEQVD ELFKLVQANP GMTFEVDLEA QVVKAGDKTY SFKIDDFRRH CMLNGLDSIG
     LTLQHGEAIS DYERKLPAFM N
//
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