ID A0A0C9TUW4_PAXIN Unreviewed; 857 AA.
AC A0A0C9TUW4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PAXINDRAFT_163505 {ECO:0000313|EMBL:KIJ14038.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ14038.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ14038.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ14038.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN819346; KIJ14038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9TUW4; -.
DR HOGENOM; CLU_004588_2_1_1; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000053647; 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; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00572; LeuA_type2; 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; 2.
DR SMART; SM00917; LeuA_dimer; 2.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 2.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 2.
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:UP000053647};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..313
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 857 AA; 94734 MW; 488382E07759518E CRC64;
MGCMLIDPSQ KYKPYTPLKL DCRTWPTKTF TKAPIWLSTD LRDGNQSLAN PMTVDQKLAF
FRLLVKSGFK EIEIAYPAAS DTEFSFVRYL IEHNEIPDDV WIQVMTPARE ELITRTFEAV
AGAKRVIIHM FNATCPKFRN VVFKYSKEQV IDLAVRHTIL VRELIDQYAA SHGTTFRYQY
SPETFSQTEV QFLVAICDAV KTAWGRASTG SERITFNLPA TVEVGPPNHY ADQVEYFCTH
ISERERIIVS LHPHNDRGTG IAAAELAILA GADRIEGCLF GNGERTGNVD IVNLALNLYT
QGIPPHLDFS DLQSVIDIVT QCNDIPIHPR HPYAGELVFT AFAGSHQDAV KKGFEEQGQR
HARNLANGEP QMWDMPYLPL DPADLGCTYD ALIRVNSQSG KGGIAYLVKQ HLHLDLPRKM
QIAFYRVIQK IAEREAREIT VEDITTAFRS TYYFGGPKYE GRLALKSFSV TMEASPESLD
TDEAPDERRR FDGTVSVDGM LRVICGDGNG PISSLLDAIR THLDIDLTLR EYSENTIGVG
ENAKSASYIE LVATTDIVKE IRGAPQSWWG VGVDSDVAAS GLRAVLSAVN SSIGDRALPK
LKLNVGFDST TGQADIANAL ANSLELQLPR RFQSSFFKVV QRAAHDSSGQ ISYEGLTKLF
QDTYGYETET AKQCRFELQS FDITKSIVAG RRQITAELLV DGEVRSVSGE GNGPLSAALA
ALHTQICGTL SIKEYIEHSV GEGARVKAVS FVELVYEVEG RTKESAWGVG GDSDITASGL
HAVMKAASSL NLATMPCLSD KVEALYEVER NVRDVWDNDS GLELELLLPE AERDEDHQRN
EGFIGQLCTT SGLTTRA
//
