ID   LEU1_ARCFU              Reviewed;         503 AA.
AC   O30020;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=AF_0219;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB91014.1; -; Genomic_DNA.
DR   PIR; C69277; C69277.
DR   AlphaFoldDB; O30020; -.
DR   SMR; O30020; -.
DR   STRING; 224325.AF_0219; -.
DR   EnsemblBacteria; AAB91014; AAB91014; AF_0219.
DR   KEGG; afu:AF_0219; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   OMA; NTMRMLV; -.
DR   PhylomeDB; O30020; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002199; 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..503
FT                   /note="Probable 2-isopropylmalate synthase"
FT                   /id="PRO_0000140407"
FT   DOMAIN          8..259
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   503 AA;  55212 MW;  67F8FD363D0A20FD CRC64;
     MSAVMTTIRV FDTTLRDGEQ MPGVSLPLEY KIRIAKQLDK LGVDVIEAGF PSATKGEFES
     VKEISSLSLN AEICGLARIV KEDIDAAINA NVDMVHIFVP TSRIQIEHTV KMSKEEIIEK
     SVECVEYIKS HGVKCMFSAM DATRTEVEYL KQIFKAVENA KVDIVNVPDT VGVATPFKFY
     ELIKQLREHL KVPIDVHCHN DFGLAVANTY AAVMAGANEV QVTVNGIGER AGNADLAQVV
     MILHAIEGIK TNIKTEHLFE TSKLVERLTG VKMPPNHPIV GENAFSHESG IHAHGVLKEY
     STFEPGVVTP EMVGHKRRIV IGKHAGRYQI KKILEEAGYH LDDEKLNQIF EKVKEMGDKG
     KRVTDLDLFA IAEVVIGELK REEKAILVDE VTVLTGNKIT PTAVLNAEVF GHRKVTSAIG
     VGPVDASLKA VTSLVGESIR ITEFRMDAIT GGSDALAEVY VTVEDDEGHS FTSRGAAQDI
     VMASIDAVIN AVNYLLRMKR RKS