ID   LEUD_STRGN              Reviewed;         196 AA.
AC   Q9AIM2;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
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};
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GP1223;
RX   PubMed=11545273;
RA   Franke C.A., Bolken T.C., Hruby D.E.;
RT   "Studies on the genomic organization of recombinant Streptococcus gordonii
RT   and the development of a novel intergenic integration site for foreign gene
RT   expression.";
RL   J. Mol. Microbiol. Biotechnol. 3:545-555(2001).
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; AF251027; AAK28430.1; -; Genomic_DNA.
DR   RefSeq; WP_008808885.1; NZ_LR594041.1.
DR   AlphaFoldDB; Q9AIM2; -.
DR   SMR; Q9AIM2; -.
DR   OMA; AFTTHTG; -.
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..196
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141892"
SQ   SEQUENCE   196 AA;  22574 MW;  BC1FC069E2409C01 CRC64;
     MEKFTIYTGT TVPLMNDNID TDQILPKQFL KLIDKKGFGK YLMYAWRYLD NQYTEDPDFV
     FNRPEYRKAT ILITGDNFGA GSSREHAAWA LADYGFKVVI AGSFGDIHYN NELNNGMLPI
     VQPLEVRQAL ANLKPTDQVT VDLEQQKIFS PVGEFSFDID GEWKHKLLNG LDDIGITLLY
     EDLIAEYEKN RPSYWQ