ID A0A0D2A4G0_9EURO Unreviewed; 680 AA.
AC A0A0D2A4G0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PV07_01916 {ECO:0000313|EMBL:KIW35206.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW35206.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW35206.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW35206.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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; KN847040; KIW35206.1; -; Genomic_DNA.
DR RefSeq; XP_016255422.1; XM_016388494.1.
DR AlphaFoldDB; A0A0D2A4G0; -.
DR STRING; 569365.A0A0D2A4G0; -.
DR GeneID; 27341110; -.
DR VEuPathDB; FungiDB:PV07_01916; -.
DR HOGENOM; CLU_004588_3_0_1; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000054466; 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:UP000054466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..311
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 469..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 75571 MW; A20EBE978C2106D7 CRC64;
MPMLREPWKK YRKFKPLDLP NRQWPSRTND KPPRWLATDL RDGNQSLVDP MDGEQKLRFF
KMLVELGYKE IEVSFPSASQ TDFDFTRYLV DTPGVVPDDV WLQVLSPCRE DFIRRTVESL
RGAKKAILHL YLATSECFRR IVFGMTEDET LALAVKCTKF ARSITKDDPS HAGTEWLYEF
SPETFSDTSP EFAVRVCEAV KEAWGPTEDS KLIFNLPATV EMATPNIFAD QVEYFCTHMT
EREKFCVSVH PHNDRGCAVA AAELAQMAGA DRVEGTLFGN GERTGNVDLV TLALNLYTQG
IWPNIDFSDI NKVIRVCEES TKIPVNERWP YGGQLVVCAF SGSHQDAIKK GFQLRKKDGR
GPEDPWELPY LPLDPQDIGR TYEAVIRVNS QSGKGGVAWI IQRSLELDLP RGLQIAFSRI
VQKEADAKGR ELLPREIQAL FEESYHLKKN PRFTLIDYNI TAVRTPSPAP QMKISAGQPP
QTAAPAQNTS TAKRQFAGII AIDGVQHPIV GVGNGAISSL ANALHSLGID LDVADYKEHA
IGEGREVKAA TYIECTASNS NEKVWGVGIH EDVVQASLIA LLSAASSFLT SRVSTPVPFK
PKHLRQFSEA ELEALERLNL NNTPDSPNSP LRSSVTATEG SVTPSKLNME MNPSSVAAKK
INIDLLEQKA ESVNGHVEKS
//
