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
//