ID   LEUD1_PYRFU             Reviewed;         164 AA.
AC   Q8U2A0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit 1;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase 1;
DE            Short=IPMI 1;
DE   AltName: Full=Isopropylmalate isomerase 1;
GN   Name=leuD1; OrderedLocusNames=PF0939;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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}.
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DR   EMBL; AE009950; AAL81063.1; -; Genomic_DNA.
DR   RefSeq; WP_011012075.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2A0; -.
DR   SMR; Q8U2A0; -.
DR   STRING; 186497.PF0939; -.
DR   EnsemblBacteria; AAL81063; AAL81063; PF0939.
DR   GeneID; 41712749; -.
DR   KEGG; pfu:PF0939; -.
DR   PATRIC; fig|186497.12.peg.995; -.
DR   eggNOG; arCOG02230; Archaea.
DR   HOGENOM; CLU_081378_1_1_2; -.
DR   OMA; DDVNTDY; -.
DR   OrthoDB; 86621at2157; -.
DR   PhylomeDB; Q8U2A0; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001013; 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..164
FT                   /note="3-isopropylmalate dehydratase small subunit 1"
FT                   /id="PRO_0000141947"
SQ   SEQUENCE   164 AA;  18257 MW;  F959DB935A677034 CRC64;
     MKARGRAWKY GDNIDTDVII PARYLNTSDP KELAQHVLED LDPEFRYKMK PGDIIVAGEN
     FGCGSSREHA PLAIKAAGVS AVIAKSFARI FYRNAINIGL PILEAPEAVE RIETGDEIEI
     DFSTGEIRNL TKGEVYHANP FPEFIMEIIK AGGLVEWAKR RLAK