ID   LEUD_NEILA              Reviewed;         137 AA.
AC   P50181;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
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;
DE   Flags: Fragment;
GN   Name=leuD;
OS   Neisseria lactamica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC   A7515;
RX   PubMed=8190068; DOI=10.1007/bf00283872;
RA   Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RT   "The NlaIV restriction and modification genes of Neisseria lactamica are
RT   flanked by leucine biosynthesis genes.";
RL   Mol. Gen. Genet. 243:24-31(1994).
RN   [2]
RP   ERRATUM OF PUBMED:8190068.
RA   Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RL   Mol. Gen. Genet. 244:167-167(1994).
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}.
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DR   EMBL; U06074; AAA53236.1; -; Genomic_DNA.
DR   PIR; S43885; S43885.
DR   AlphaFoldDB; P50181; -.
DR   SMR; P50181; -.
DR   STRING; 486.B2G52_08320; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 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..137
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141843"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  15758 MW;  78477FA52BA945C2 CRC64;
     RQILLTRKNF GCGSSREHAP WALDDYGFRA IIAPSFADIF FNNCYKNGLL PIVLTEEQVD
     RLFKEVEANE GYRLSIDLAE QTLTTPSGET FTFDITEHRK HCLLNGLDEI GLTLQHADEI
     HAFEEKRRQS QPWLFNG