ID   LEU1_PYRAE              Reviewed;         364 AA.
AC   Q8ZW35;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Probable 2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
GN   Name=leuA; OrderedLocusNames=PAE1993;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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). {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AE009441; AAL63867.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZW35; -.
DR   SMR; Q8ZW35; -.
DR   STRING; 178306.PAE1993; -.
DR   EnsemblBacteria; AAL63867; AAL63867; PAE1993.
DR   KEGG; pai:PAE1993; -.
DR   PATRIC; fig|178306.9.peg.1472; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_4_2_2; -.
DR   InParanoid; Q8ZW35; -.
DR   OMA; VEICGFA; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002439; 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; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 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..364
FT                   /note="Probable 2-isopropylmalate synthase"
FT                   /id="PRO_0000140420"
FT   DOMAIN          1..240
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   364 AA;  39819 MW;  9F7ABEA3CEE778DF CRC64;
     MPGVALSISE KLEIAMALDD AGVDMIEAGF AAVSDDEKEA IKLISKEVSR AKVVSLARMT
     KSDVDAAAEA DVDMIHLFIA TSDIHLKYKL GITREEALRR IEEVVSYAKS YGVEILFSAE
     DATRSDLEFL AKAYKTAIEA GADEINVPDT VGVMTPSRMA YLIKYLRERL PPIPMHVHCH
     DDFGMAVANT VTAIENGADV AQVVVNNFGE RAGNAALEEV VAAVHYLLGL RTNIKLEKLY
     SLSQLVSKLF GVPVPPNKAV VGENAFSHEA GIHVHGVLNN PFTYEPMRPE DVGNRRRIVL
     GKHSGRHSVI WALKNLGVEP SEDLVNYVLD AVKKLAVKKV KVDEAVLREI VNRYNKGLSM
     SYAV