ID   LEUD_AQUAE              Reviewed;         168 AA.
AC   O67399;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 108.
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=aq_1398;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC07359.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000657; AAC07359.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70421; E70421.
DR   RefSeq; NP_213964.2; NC_000918.1.
DR   AlphaFoldDB; O67399; -.
DR   SMR; O67399; -.
DR   STRING; 224324.aq_1398; -.
DR   EnsemblBacteria; AAC07359; AAC07359; aq_1398.
DR   KEGG; aae:aq_1398; -.
DR   PATRIC; fig|224324.8.peg.1093; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_1_1_0; -.
DR   InParanoid; O67399; -.
DR   OMA; GLPIIEC; -.
DR   OrthoDB; 1384217at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000798; Chromosome.
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_01032; LeuD_type2; 1.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   InterPro; IPR011824; LeuD/DmdB_bac.
DR   InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR02084; leud; 1.
DR   TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..168
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141920"
SQ   SEQUENCE   168 AA;  18786 MW;  25A34FE7FFCA09F3 CRC64;
     MQMKFRGRVW KFGDNVDTDQ IIPARYLNTS DPYELAKHVM EDSEHPEFAK EHKEGDIIVA
     GKNFGSGSSR EHAPIAIKYS GVPVVIAKSF ARIFFRNAIN IGLPIVEAPE AVDEIEHGDE
     IEVDLEKGVI KNLRTGKEYQ ATKFPKELQD ILKAGGLMAY AKEKLASK