ID A0A179H5M3_PURLI Unreviewed; 1166 AA.
AC A0A179H5M3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=VFPBJ_03821 {ECO:0000313|EMBL:OAQ85048.1}, VFPFJ_06008
GN {ECO:0000313|EMBL:OAQ89594.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ85048.1, ECO:0000313|Proteomes:UP000078240};
RN [1] {ECO:0000313|EMBL:OAQ85048.1, ECO:0000313|Proteomes:UP000078240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ85048.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ89594.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (JAN-2016) 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}.
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:OAQ85048.1}.
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DR EMBL; LSBH01000002; OAQ85048.1; -; Genomic_DNA.
DR EMBL; LSBI01000005; OAQ89594.1; -; Genomic_DNA.
DR RefSeq; XP_018178313.1; XM_018323083.1.
DR AlphaFoldDB; A0A179H5M3; -.
DR STRING; 33203.A0A179H5M3; -.
DR GeneID; 28888132; -.
DR KEGG; plj:VFPFJ_06008; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; 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:UP000078340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 575..853
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 133202 MW; 19965232F1240033 CRC64;
MAQRGARMTE FEERDYYPPP RRSAPEFDDM EYRMSRVATR SPPPRSRSRV AVRDEEIDVR
VRERDTNRTP AFLREDARRT EAGPMVLRQR DVETVDRHRR SPSPVRYREE RLVRRPKSVS
PPPMREEHEH LRFVERERVR SPSVVRRRSP SPIPVRFVER PRRSPSPPAR EHIHTRIVER
ERERMPSPSP SPPPPPPVIR GPTVEREVIT HYTDIDHGVL RAKRPSPPPP PPPAPRSRPR
ERETDIDISL SKNRTEVDIH RSSSRARSRS RERRSHYHDD DLDVVVRRDD HLRVDERSKR
HRRAHSAAPL GSPVDEESDY ITGKMDARGR MGEARGGATK DWTIVDVPPG TERVRMDGIG
GASTDTTWSR YSGVRRTQFI PERDGAVVPR APSPSPGPTR GRTSVAVDFN KTTEIDVDID
RRITKRPGPP PPPPPKEMWT EITKDLVVRE AIEQMGYEYE ETKWFFYIMD YLRYDDVLQL
TELSERIRCA RKTHEIRWER DYYDEWDHPY RRHHHENHHH HRHRGWDDER VREREVIYDS
RRPARLKEPW KKYKRFQPLH LPDRQWPNKT VDKAPRWLAT DLRDGNQSLV DPMNGEEKWR
YFKMLVDLGY KEIEVSFPSA SDTDFDFTRR LIETPGTVPD DVWLQVLSPC REDLIKRTVQ
SLKGAKKALV HIYLATSECF RRVVFSKNKE DTLATAVRCT KLVRALTKDD PSQSGTEWAF
EFSPETFSDT EPEFVIEVCE AVKAAWEPSV ENPIIFNLPA TVEMSTPNVY ADQIEYFCRN
VTEREKICVS LHPHNDRGCA VAAAELAQMA GADRVEGCLF GNGERTGNVD LVTLGLNLYT
QGIHPNIDFS DLGSIIETVE MCNKIPVHER APYGGSLVVC AFSGSHQDAI KKGFQLREKD
NLGYEDRWQI PYLPLDPQDI GRTYEAVIRV NSQSGKGGAA WIILRQLQLD LPRGLQVAFS
KVVQRKADAL GRELRPQEIT ELFEQTYFLN SNPRFGIVDY SIMPDRTTSP APPAPGKTQD
TKDLKRVFDG VIVCDGKEYK LRGRGNGPIS SLANALRSVG VNLDVQDYKE HAIGKGRDVK
AATYIECTAA GSNTKVWGVG IHEDVVQSSL IALLSAASNF ASSRPGSPFV ARPVSQGAEV
TELELNGNAD GPSSVVSALE AKANAM
//
