ID E3RIZ0_PYRTT Unreviewed; 629 AA.
AC E3RIZ0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PTT_08055 {ECO:0000313|EMBL:EFQ94308.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94308.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94308.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL533400; EFQ94308.1; -; Genomic_DNA.
DR RefSeq; XP_003297595.1; XM_003297547.1.
DR AlphaFoldDB; E3RIZ0; -.
DR STRING; 861557.E3RIZ0; -.
DR EnsemblFungi; EFQ94308; EFQ94308; PTT_08055.
DR KEGG; pte:PTT_08055; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_004588_3_0_1; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000001067; 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:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..311
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 580..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 69844 MW; C79F5CF84BF76C89 CRC64;
MPMLAEPWKK YQPFKPLHLP DRTWPSKTIE KPPRWLSTDL RDGNQSLVDP MDGAQKWDYF
NMLVKLGYKE IEVSFPSASQ TDFDFTQRLI QTPGIVPDDV WVQVLSPCRK ELIRRTVDSL
KGARKAILHL YLATSPCFQQ IVFDMNDEET IALAVECTRY ARAITKDDPA QAGTEWAYEF
SPETFSDSSP EFVIKVCEAV KAAWEPSVEN PLIFNLPATV EMSTPNVYAD QIEYFCKNIS
EREKICVSLH PHNDRGCAVA AAELAQMAGA DRVEGTLFGN GERTGNVDLV TLGLNLYTQG
IHPKIDFSDL KSIIDMVESC NKIPIHPRAP YGGQLVVCAF SGSHQDAIKK GFQMRKKNGA
TNESRWQIPY LPLDPQDIGR TYEAIIRVNS QSGKGGIAWI IQRQLELDLP RGLQIAFSKI
VQKETDMLGR ELLPTEITHL FEEAYHLKRN PRFSLVDYEI KADRSETPQP PQDGRTVSSR
NLRRIFNGVI EIDGQEHKIQ GSGNGALSSL ANALRSLGID LDVVDYNEHT IGTSKDAKAA
TYIGCTAAQS SQKVWGVGIH HDVVQASLIA MLSAASSFLS SRPTTPIPFR PKRSNTLEIP
SPNSSPTRTG KQANGSSIVD KLEAAVSGS
//
