ID F8Q7P5_SERL3 Unreviewed; 816 AA.
AC F8Q7P5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=SERLA73DRAFT_76679 {ECO:0000313|EMBL:EGN95583.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(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 -!- 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; GL945485; EGN95583.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q7P5; -.
DR STRING; 936435.F8Q7P5; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_004588_2_0_1; -.
DR InParanoid; F8Q7P5; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000008063; 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 InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 2.
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.
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:UP000008063};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 456..615
FT /note="2-isopropylmalate synthase LeuA allosteric
FT (dimerisation)"
FT /evidence="ECO:0000259|SMART:SM00917"
FT DOMAIN 689..812
FT /note="2-isopropylmalate synthase LeuA allosteric
FT (dimerisation)"
FT /evidence="ECO:0000259|SMART:SM00917"
FT REGION 490..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 89762 MW; BE6DD4DA6D98B048 CRC64;
MPCMLLNPHI KYKPYTPLKL ENRAWPTKTF TKAPIWLSTD LRDGNQALAN PMTVEQKNIF
YDTLVKCGFK EIEVAYPAAS DTDFSFVRGL VEGGKVPDDV WIQVLTPARE DLIRRTFEAI
AGFKHVIIHM YNATSPTFRN VVFHNTKEQT IDLAVKHTKI IRQLSNEYAA KYGTRFKYEY
SPETFSQTEV EFSVEICNAV KATWGKAGTG DERIIFNLPA TVEVGPPNHY ADQIEYFCSH
ITEREKVVVS LHPHNDRGKS FALDPYSLLI HVHSSGTGIA ATELAFLGGA DRVEGCLFGN
GERTGNVDIV NLALNLYTQG IPPNLDFSDL QSIIDIVTSC NDLPVHPRHP YAGELVFTAF
SGSHQDAIKK GFEAQSVRHA QAAAKGEPLM WDVPYMPIDP ADLGCSYEAV IRVNSQSGKG
GIAYIVKQHL QLDMPRKMQI SFYQIIQGIS DREAREVTVE DITTAFRTKY YLGGPKYEGR
LVLKSFRITT EPSPDPISQT NDDEDAPDER RRFDGTISVD GVLRVIRGDG NGPLSALLDA
LRTYLEIDLT LREYSEHTIG EGQNAKAASY IELVASGPDV KETRKATQSW WGVGIDSDIA
GSGLRAILSA ANSAIGDRPL PELKLDVGFN VASGQADVAD AIVNSLNLQL PRRFQASFFE
VVQRATANSG GKILFEDLTA LFQTTYGYEI ADEWHFALRS FKLEPIGDGS HRLFSGELAV
DGQVQSVSGE GNGPLSSALA ALHTLITGTL SIREYAEHSV GEGTEVKAVS FVELLYEKEG
QKQKEAAWGV GSDTNITTSG LKAVLRAANR LSVVGK
//
