ID   LEUD_MYCSK              Reviewed;         197 AA.
AC   A1UEA9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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}; OrderedLocusNames=Mkms_1968;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01031};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC       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; CP000518; ABL91167.1; -; Genomic_DNA.
DR   RefSeq; WP_011559322.1; NC_008705.1.
DR   AlphaFoldDB; A1UEA9; -.
DR   SMR; A1UEA9; -.
DR   STRING; 189918.Mkms_1968; -.
DR   EnsemblBacteria; ABL91167; ABL91167; Mkms_1968.
DR   KEGG; mkm:Mkms_1968; -.
DR   HOGENOM; CLU_081378_0_1_11; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; 1384217at2; -.
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-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase.
FT   CHAIN           1..197
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000063790"
SQ   SEQUENCE   197 AA;  22188 MW;  C625C0F4550FA7E9 CRC64;
     MEAFRTHTGI GVPLRRSNVD TDQIIPAVYL KRVTRTGFED GLFAAWRNDP SFVLNLPPFD
     RGSVLVAGPD FGTGSSREHA VWALMDYGFR VVISSRFADI FRGNAGKAGL LAAEVNQNDV
     ELLWKLIEQN PGLEITVNLQ DRNIIAGTVM VPFTIDDYTA WRLLEGLDDI GLTLRKQSEI
     EDYERRRPSW KPRTLPV