ID G9MQP1_HYPVG Unreviewed; 616 AA.
AC G9MQP1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=TRIVIDRAFT_89506 {ECO:0000313|EMBL:EHK24108.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK24108.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK24108.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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:EHK24108.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABDF02000005; EHK24108.1; -; Genomic_DNA.
DR RefSeq; XP_013958306.1; XM_014102831.1.
DR AlphaFoldDB; G9MQP1; -.
DR STRING; 413071.G9MQP1; -.
DR EnsemblFungi; EHK24108; EHK24108; TRIVIDRAFT_89506.
DR GeneID; 25798867; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_89506; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_004588_3_0_1; -.
DR InParanoid; G9MQP1; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000007115; 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 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; 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:UP000007115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..313
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 616 AA; 68015 MW; 50EB7FB4840D435A CRC64;
MPMLKEPWKK YKAFKPPHLP NRQWPDKVIE KAPRWLSSCL RDGNQSLPDP MNGEEKWRYF
QMLCALGYKE IEVSFPSASQ IDFDFTRRLI ETPGAVPDDV FLQVLSPCRP DLIRRTVESV
RGAKNAIIHI YLATSECFRQ VVFGYTEEQT LELAVECTKL VRSLTKDNPE ASGTRWQFEF
SPECFSDTDS DYALRVCRAV KAAWGPNGEA GDQIIFNLPA TVELSTPNVY ADLVEYFSNN
IGDRESVCVS LHPHNDRGCS IAAAELGQMA GADRVEGCLF GNGERTGNVD LVTLALNLYT
QGVSPQIDFS DMNSVIEVVE SCTKIPVHQR APYGGSLVCA AFSGSHQDAI KKGFQNRQNL
GLSSEDPWLG MPYLPLDPQD IGRNYEAIIR VNSQSGKGGS AFILRAKLEL DLPRGLQVAF
SKIVQRRAEE LGRELLANEI TNLFETTYFL HENHRLSLID YSISPDRSQS PMPSASGKTQ
DTKSMIRIFD GVILLDGQEI KLRGRGNGPI SSMAAALKQV GIDLDVHDYK EHAIGEGRGV
KAASYIECKP TGSKQTVWGV GIHEDVVQSS LLAMLSAASN FLTSRPTSPL LKPVAITAPQ
ETPSVISILE EKANGI
//
