ID   LEU1_SACS2              Reviewed;         347 AA.
AC   Q97W36;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=SSO2407;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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}.
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DR   EMBL; AE006641; AAK42554.1; -; Genomic_DNA.
DR   PIR; C90412; C90412.
DR   AlphaFoldDB; Q97W36; -.
DR   SMR; Q97W36; -.
DR   STRING; 273057.SSO2407; -.
DR   EnsemblBacteria; AAK42554; AAK42554; SSO2407.
DR   KEGG; sso:SSO2407; -.
DR   PATRIC; fig|273057.12.peg.2489; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_4_2_2; -.
DR   InParanoid; Q97W36; -.
DR   OMA; VEICGFA; -.
DR   PhylomeDB; Q97W36; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
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; 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..347
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140424"
FT   DOMAIN          1..230
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   347 AA;  38401 MW;  7BDD692556BA46B6 CRC64;
     MIARKLADLG VDVIEAGFPA SSEGEFIATR KIFEEIGDQV EVIGLSRSNK NDIDKTISTG
     ISSIHLFIAT SELHMKYKLK MTKEEVLNKI YESVKYAKDH GMIVEFSPED ATRTEEDFLF
     TAIRTAIEAG ADRINIPDTV GTMHPFKYYD MIKKIVNFVG ERIIVSVHCH NDFGLATANS
     LAGVYAGARQ AHVTVNGIGE RAGNASLEEV VMGIKKLLNY ETNVKTWKLY EVSRFVAEMT
     GVPVPYFKAI VGDNAFGHES GIHVHGVIEN PFTYEPISPE EVGNFRRLAL GKHSGIHGLR
     KLLEEQGIYL SDDKLKIVLA EIKKLAESGN KVTVEDAKNI ALKLMNS