ID   LEUD_RHIL3              Reviewed;         202 AA.
AC   Q1MA52;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=RL4705;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=3841 {ECO:0000303|PubMed:19597156};
RX   PubMed=19597156; DOI=10.1073/pnas.0903653106;
RA   Prell J., White J.P., Bourdes A., Bunnewell S., Bongaerts R.J., Poole P.S.;
RT   "Legumes regulate Rhizobium bacteroid development and persistence by the
RT   supply of branched-chain amino acids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:12477-12482(2009).
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   -!- DISRUPTION PHENOTYPE: Nodulates the roots of pea plants as long as
CC       branched-chain amino acids Leu, Ile and Val (LIV) are added to the
CC       plant growth medium, but forms fewer nodules compared to wild-type.
CC       Nodules infected by the mutant are more spherical and contain more
CC       starch than those infected with wild-type, however the bacteroids
CC       appear visually normal. {ECO:0000269|PubMed:19597156}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01031}.
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DR   EMBL; AM236080; CAK10188.1; -; Genomic_DNA.
DR   RefSeq; WP_003543984.1; NC_008380.1.
DR   AlphaFoldDB; Q1MA52; -.
DR   SMR; Q1MA52; -.
DR   STRING; 216596.RL4705; -.
DR   EnsemblBacteria; CAK10188; CAK10188; RL4705.
DR   GeneID; 61426171; -.
DR   GeneID; 67485104; -.
DR   KEGG; rle:RL4705; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_0_3_5; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000006575; 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.
FT   CHAIN           1..202
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000063813"
SQ   SEQUENCE   202 AA;  22127 MW;  B697E882EDE24135 CRC64;
     MDKFVKLTGV AAPLPVVNVD TDMIIPKDYL KTIKRTGLGT GLFAEARYNE DGSENPDFVL
     NKPAYRDAKI LVAGDNFGCG SSREHAPWAL LDFGIRCVIS TSFADIFYNN CFKNGILPIK
     VSQEDLDKLM DDASRGSNAI LTVDLENLEI TGPDGGLIKF DLDEFKRHCL LNGLDDIGLT
     LEKGKAIDSF EKKNAASHPW AA