ID   LEUD_MYCBO              Reviewed;         198 AA.
AC   P65278; A0A1R3Y4Q4; O53236; X2BM97;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuD; OrderedLocusNames=BQ2027_MB3011C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=BCG / Pasteur;
RX   PubMed=16006064; DOI=10.1016/j.femsle.2005.06.004;
RA   Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.;
RT   "Thiol specific oxidative stress response in Mycobacteria.";
RL   FEMS Microbiol. Lett. 249:87-94(2005).
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   -!- INDUCTION: Induced in response to the thiol oxidant diamide.
CC       {ECO:0000269|PubMed:16006064}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU01635.1; -; Genomic_DNA.
DR   RefSeq; NP_856656.1; NC_002945.3.
DR   RefSeq; WP_003415110.1; NC_002945.4.
DR   AlphaFoldDB; P65278; -.
DR   SMR; P65278; -.
DR   EnsemblBacteria; SIU01635; SIU01635; BQ2027_MB3011C.
DR   GeneID; 45426976; -.
DR   PATRIC; fig|233413.5.peg.3310; -.
DR   OMA; AFTTHTG; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001419; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase.
FT   CHAIN           1..198
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141837"
SQ   SEQUENCE   198 AA;  21780 MW;  705B4A11FB41DB8B CRC64;
     MEAFHTHSGI GVPLRRSNVD TDQIIPAVFL KRVTRTGFED GLFAGWRSDP AFVLNLSPFD
     RGSVLVAGPD FGTGSSREHA VWALMDYGFR VVISSRFGDI FRGNAGKAGL LAAEVAQDDV
     ELLWKLIEQS PGLEITANLQ DRIITAATVV LPFKIDDHSA WRLLEGLDDI ALTLRKLDEI
     EAFEGACAYW KPRTLPAP