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Database: UniProt
Entry: F8N3D5_NEUT8
LinkDB: F8N3D5_NEUT8
Original site: F8N3D5_NEUT8 
ID   F8N3D5_NEUT8            Unreviewed;       625 AA.
AC   F8N3D5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   ORFNames=NEUTE1DRAFT_70741 {ECO:0000313|EMBL:EGO51742.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO51742.1};
RN   [1] {ECO:0000313|EMBL:EGO51742.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO51742.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) 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; GL891382; EGO51742.1; -; Genomic_DNA.
DR   RefSeq; XP_009855385.1; XM_009857083.1.
DR   AlphaFoldDB; F8N3D5; -.
DR   GeneID; 20829484; -.
DR   KEGG; nte:NEUTE1DRAFT70741; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_70741; -.
DR   HOGENOM; CLU_004588_3_0_1; -.
DR   OrthoDB; 275559at2759; -.
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:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..311
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          458..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  69031 MW;  CB00F7787D543F1C CRC64;
     MPMLKDPSTK YKPFPPLNLP DRQWPNKTIV KAPRWLATDL RDGNQSLVDP MNGDQKWRYF
     QMLTELGYKE IEVSFPSASQ TDYDFTRRLI ETPGAVPDDV WLQVLSPCRE DLIRRTVQSL
     KGAKKAIIHI YLATSECFRR IVFGFTEDES VELASKCAAL VKSLTKDDPE MAGTEWAFEF
     SPETFSDTSP EFAVRICEAV KAAWEPTVEN PIIFNLPATV EMATPNIYAD QVEYFCRNIT
     EREKVCISLH PHNDRGCAVA AAELAQMAGA DRVEGCLFGN GERTGNVDLV TLALNLYTQG
     VSPNIDFSDL GKVIKTVEEC NKIEVHPRAP YGGSLVVCAF SGSHQDAIKK GFSLREKEGK
     EYADYWQVPY LPLDPKDIGR DYQAVIRVNS QSGKGGTAWI IQQHLHLDMP RGLQVAFSKV
     VQRIADEKGR ELLPTEITDL FKKTYYLDEN PRFNIVDYSI NPDRSSSPAP PAPGKTQDTK
     NLGRVFEGVI SIEGHEYNLR GRGNGPISSL ANALKSVGVD LDVQDYKEHA VGRGRDVKAA
     TYIECTAAGQ TEKVWGVGIH ADVVQSSLIA LLSAASNFVG SRVGSPIIPK PVADKEVSGD
     VNLSVPNGVN GKSIIQALES QADEM
//
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