ID   LEU1_METMA              Reviewed;         516 AA.
AC   P58968;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=MM_1284;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM30980.1; -; Genomic_DNA.
DR   RefSeq; WP_011033231.1; NC_003901.1.
DR   AlphaFoldDB; P58968; -.
DR   SMR; P58968; -.
DR   STRING; 192952.MM_1284; -.
DR   EnsemblBacteria; AAM30980; AAM30980; MM_1284.
DR   GeneID; 24879879; -.
DR   GeneID; 66137286; -.
DR   KEGG; mma:MM_1284; -.
DR   PATRIC; fig|192952.21.peg.1492; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000595; 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   Gene3D; 3.30.160.270; -; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011830; LEU1_arch.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 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..516
FT                   /note="Probable 2-isopropylmalate synthase"
FT                   /id="PRO_0000140415"
FT   DOMAIN          20..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   516 AA;  55799 MW;  C3C5C789FCA17725 CRC64;
     MYTLKEGIDF YIEPMQSKKV TVFDTTLRDG EQTPGVSLTS TQKLEIAHQL DKLGVDIIEA
     GFPISSEGDK ESVKSISNAG LDTTVCGLAR VLKKDIDACF ESDVGLVHTF VPTSDVQRIY
     TIKKSREEVI QLAVEAVQYI KDHGLKCMFS AMDATRTDPE YLIEVFKAVQ EAGCDIINVP
     DTVGVMVPSA MYRQIKGIAA EITIPIDVHC HNDFGLAVAN SLMAVEAGAS QVQVTINGIG
     ERAGNADLSQ TVMSLTSIYG AKTNIRTEYL VETSKMVENY TGIRLPPNTP VVGQNAFSHE
     SGIHSQGVLE KSDTFEPGIM TPEMVGHRRR IVLGKHTGKH AVKQSLESAG IKTNDNQLDE
     IVIRIKEIAN KGKQITDADL YAVASAVLGK ASSEEELIKL KEVSVMTGNI LTPTAVVKAD
     IEGKEIIAAR TGVGPVDAAL HAVRDILGES NHFRLQDFRI DAITGGADAL ADVYIGLENE
     KGRIVTARSA NPDIVMASVE ALVNAMNLLY KKENKS