ID   LEUD_BUCPS              Reviewed;         202 AA.
AC   P59019;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 1.
DT   25-MAY-2022, entry version 68.
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   Buchnera aphidicola subsp. Pemphigus spyrothecae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=98799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11976137; DOI=10.1128/aem.68.5.2572-2575.2002;
RA   Sabater-Munoz B., Gomez-Valero L., van Ham R.C.H.J., Silva F.J.,
RA   Latorre A.;
RT   "Molecular characterization of the leucine cluster in Buchnera sp. strain
RT   PSY, a primary endosymbiont of the aphid Pemphigus spyrothecae.";
RL   Appl. Environ. Microbiol. 68:2572-2575(2002).
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; AJ426489; CAD20140.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59019; -.
DR   SMR; P59019; -.
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..202
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141800"
SQ   SEQUENCE   202 AA;  23775 MW;  20359A40D7144938 CRC64;
     MTLLNQYTGI VIPINISNID TDVIIPKQFL KKINKKGFGK YLFYNWRFND NEGKNINKNF
     ILNDLRYKKS SILLTRDNFG CGSSREHAVW ALMDYGFKVI IASSFGDIFY NNCLNNHLIP
     IILSENKINT LFDITSNYID VSFTIDLKNN TILAKNYAYY FKIDALHKFC IMHQLDQIDL
     TMKNEKKITK YEKKIFDFFI KK