ID   LEUD2_SALTY             Reviewed;         208 AA.
AC   Q8ZRI9;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit 2;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase 2;
DE            Short=IPMI 2;
DE   AltName: Full=Isopropylmalate isomerase 2;
GN   Name=leuD2; OrderedLocusNames=STM0330;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000250}.
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       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; AE006468; AAL19284.1; -; Genomic_DNA.
DR   RefSeq; NP_459325.1; NC_003197.2.
DR   RefSeq; WP_000379343.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRI9; -.
DR   SMR; Q8ZRI9; -.
DR   STRING; 99287.STM0330; -.
DR   PaxDb; Q8ZRI9; -.
DR   EnsemblBacteria; AAL19284; AAL19284; STM0330.
DR   GeneID; 1251849; -.
DR   KEGG; stm:STM0330; -.
DR   PATRIC; fig|99287.12.peg.350; -.
DR   HOGENOM; CLU_081378_0_3_6; -.
DR   OMA; NCQRNGV; -.
DR   PhylomeDB; Q8ZRI9; -.
DR   BioCyc; SENT99287:STM0330-MON; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001014; Chromosome.
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; Reference proteome.
FT   CHAIN           1..208
FT                   /note="3-isopropylmalate dehydratase small subunit 2"
FT                   /id="PRO_0000141876"
SQ   SEQUENCE   208 AA;  22932 MW;  2F4CBB6F8BBCC72A CRC64;
     MDTFKQISGR IAPMLEPNID TDVIMPKQFL KGIDRQGLDK GVFFDRRFMA GGQPNPDFIL
     NMPGWQSATF LLVGPNFGCG SSREHAVWGL KQLGVRGLIG STFAGIFDDN CQRNGILTVS
     LDEPALARLA QLAASADTNS ITVSLDRCEI TTAEETISFV ISELKRAMLA AGEDAIAWTL
     QYLPEIENFE VAHYSRRPWL KRPASPRG