ID   LEUD_BUCAI              Reviewed;         207 AA.
AC   P56935; Q9KGP7; Q9R6R2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=BUpL07;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10688696; DOI=10.1007/s002849910052;
RA   Soler T., Latorre A., Sabater B., Silva F.J.;
RT   "Molecular characterization of the Leucine plasmid from Buchnera
RT   aphidicola, primary endosymbiont of the aphid Acyrthosiphon pisum.";
RL   Curr. Microbiol. 40:264-268(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ006878; CAB56193.1; -; Genomic_DNA.
DR   EMBL; AP001071; BAA95426.1; -; Genomic_DNA.
DR   RefSeq; NP_057971.1; NC_002253.1.
DR   AlphaFoldDB; P56935; -.
DR   SMR; P56935; -.
DR   EnsemblBacteria; BAA95426; BAA95426; BAA95426.
DR   KEGG; buc:BUpL07; -.
DR   PATRIC; fig|107806.10.peg.13; -.
DR   HOGENOM; CLU_081378_0_3_6; -.
DR   OMA; AFTTHTG; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001806; Plasmid pLeu.
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; Plasmid; Reference proteome.
FT   CHAIN           1..207
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141797"
SQ   SEQUENCE   207 AA;  24049 MW;  E760E1C6264B712F CRC64;
     MFKFTGHAGI VVPLDISNID TDIIIPKQFL KRVNKIGFGK YLFHDWRFID ANQLVKNEDF
     ILNKKIYKNA SILLTRENFG CGSSREHAVW SLVDYGFKVI IAPSFADIFY NNSFNNKLLL
     ITLSSSEITF LFDIVKNNIG ITFDVSLVEK TVTVNKEVFS FELDDFHYFC LLNDLDNIDL
     TMKHLSEIKS YESRISDFLL ERRDFQS