ID   LEU1_SULTO              Reviewed;         386 AA.
AC   Q974X3;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=2-isopropylmalate synthase;
DE            Short=IPMS;
DE            EC=2.3.3.13 {ECO:0000250|UniProtKB:Q4JA78};
DE   AltName: Full=Alpha-isopropylmalate synthase;
DE            Short=Alpha-IPM synthase;
GN   Name=leuA; OrderedLocusNames=STK_05380;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate). Carries out the first
CC       step of the leucine biosynthesis pathway.
CC       {ECO:0000250|UniProtKB:Q4JA78}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC         Evidence={ECO:0000250|UniProtKB:Q4JA78};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21525;
CC         Evidence={ECO:0000250|UniProtKB:Q4JA78};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000250|UniProtKB:Q4JA78}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {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; BA000023; BAB65534.1; -; Genomic_DNA.
DR   RefSeq; WP_010978517.1; NC_003106.2.
DR   AlphaFoldDB; Q974X3; -.
DR   SMR; Q974X3; -.
DR   STRING; 273063.STK_05380; -.
DR   EnsemblBacteria; BAB65534; BAB65534; STK_05380.
DR   GeneID; 1458484; -.
DR   KEGG; sto:STK_05380; -.
DR   PATRIC; fig|273063.9.peg.618; -.
DR   eggNOG; arCOG02092; Archaea.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 26145at2157; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011830; LEU1_arch.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02090; LEU1_arch; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..386
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140425"
FT   DOMAIN          12..265
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   386 AA;  42433 MW;  A0E209F297D3DFA2 CRC64;
     MGCQFSVNSK KVRIFDTTLR DGEQAPGIDL TVEQKVKIAR KLAELGVDVI EAGFPAASEG
     EFIATKKILE EVGDQVEVIG LSRANKQDID KTIDTGISSI HVFIATSDIH LKYKLKMTRE
     QVLDKIYESV RYAKDHGLIV EYSPEDATRT DKDFLLKAVS TAIEAGADRI NIPDTVGVMH
     PFKFHDLIKD VVSVTKDKIV SVHCHNDFGL ATANSIAGVM AGARQVHVTV NGIGERAGNA
     SLEEVVMALK KLLGYEVNIK TYKLYETSRL VSELTGVPVP YFKAIVGENA FGHEAGIHVH
     GVIENPLTYE PISPEEVGNF RRLALGKHSG IHGLKKLLEE QGIYLNDQEL REVLNEIKKL
     AENGEKVNVD VAKEIAIKVS SKKIKV