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Database: UniProt
Entry: G1XM40_ARTOA
LinkDB: G1XM40_ARTOA
Original site: G1XM40_ARTOA 
ID   G1XM40_ARTOA            Unreviewed;       625 AA.
AC   G1XM40;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   ORFNames=AOL_s00140g9 {ECO:0000313|EMBL:EGX45693.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX45693.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX45693.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:0000256|ARBA:ARBA00000064};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004689}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGX45693.1}.
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DR   EMBL; ADOT01000227; EGX45693.1; -; Genomic_DNA.
DR   RefSeq; XP_011125552.1; XM_011127250.1.
DR   AlphaFoldDB; G1XM40; -.
DR   STRING; 756982.G1XM40; -.
DR   GeneID; 22896628; -.
DR   eggNOG; KOG2367; Eukaryota.
DR   HOGENOM; CLU_004588_3_0_1; -.
DR   InParanoid; G1XM40; -.
DR   OMA; DQIEYMH; -.
DR   OrthoDB; 275559at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   CDD; cd07942; DRE_TIM_LeuA; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR00970; leuA_yeast; 1.
DR   PANTHER; PTHR46911; -; 1.
DR   PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 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 {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          33..313
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   625 AA;  69343 MW;  6A01645E21C228DF CRC64;
     MPMLNDPSRK YKPFKPLRLP GRQWPDQTIT KAPRWLNTDL RDGNQSLANP LDGEQKLRFF
     NLLVEIGYKE IEISFPAASQ IDFDFTRHLI ETPNLVPEDV VLQVISPCRK DLIKRTAEAL
     YGAKKVIFHL YLATSECFRR IVFNNMTEDE TLNLAVECTK LVRSLTKDSP DPAVRATEWQ
     YQFTPETFSD TSLEYSIKLC NAVREAWEPT THPIIFNLPA TVELSTPNVY ADQIEYFCKN
     ISEREKVCVS LHPHNDRGCA VAASELAQMA GADRVEGCLF GNGERTGNVD LVTLALNLYT
     QGISPGVDFS DISKVISTVE DLTKIPVHPR QPYGGQFAVC AFSGSHQDAI KKGFQSRKDL
     TDDDPWVMPY LPFDSQDIGR NYEAVIRVNS QSGKGGVAWI ILQNLHLDIP KPLQQAFSKI
     VQKHTETVNR ELQPAEIVKL FEEAYLPKAN SPIRLVDYCI RTDRATSNDN FPITNEAAEQ
     QSGLHFEGTI ALNGVEKPIK GEGNGTISSL VNCLNGLGVD LTVNYFKEQA VGSEGVNNTK
     AAAYIECSLS AKNGGKRELV WGVGLHEDMV QAGLMALLSA ASSAHENRLE DATQLKSATH
     PHLKTSAIKV PSTMVTVTEL CSDVD
//
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