ID   LEUD_AFIC5              Reviewed;         201 AA.
AC   B6JAR2; F8BSU6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
GN   OrderedLocusNames=OCAR_4276, OCA5_c02440;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/jb.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91425.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI04973.1; -; Genomic_DNA.
DR   RefSeq; WP_012561456.1; NC_015684.1.
DR   AlphaFoldDB; B6JAR2; -.
DR   SMR; B6JAR2; -.
DR   STRING; 504832.OCAR_4276; -.
DR   EnsemblBacteria; AEI04973; AEI04973; OCA5_c02440.
DR   KEGG; oca:OCAR_4276; -.
DR   KEGG; ocg:OCA5_c02440; -.
DR   PATRIC; fig|504832.7.peg.258; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_0_3_5; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000007730; 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..201
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_1000135821"
SQ   SEQUENCE   201 AA;  22535 MW;  33BEC6FF203F3501 CRC64;
     MEKFTVVNSV AAPLKIINVD TDMIIPKQYL KTIKRTGLGK GLFSEQRYKE DGSENPDFVL
     NKPAYRNAQI LVAGDNFGCG SSREHAPWAL ADFGIRCVIS TSFGDIFYNN SFKNGLLPIR
     VTHEQLDKLF EDAERGANAT LTIDLEKQEI RGPDGGVINF EIDPFRKHCL LNGLDDIGLT
     MQKKPSIDSF EAREKVARPW L