ID A0A1J9PET5_9EURO Unreviewed; 646 AA.
AC A0A1J9PET5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=AJ78_04687 {ECO:0000313|EMBL:OJD15032.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD15032.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD15032.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD15032.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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}.
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:OJD15032.1}.
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DR EMBL; LGRN01000181; OJD15032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PET5; -.
DR STRING; 1447872.A0A1J9PET5; -.
DR VEuPathDB; FungiDB:AJ78_04687; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000182235; 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:UP000182235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..311
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 646 AA; 71500 MW; C8245BB9086C127E CRC64;
MPMLKDPSKK YRRFKPLDLP SRQWPSKTLD KPPRWLATDL RDGNQSLVDP MDGDQKLRYF
RMLVGIGYKE IEISFPSASQ TDFDFTRHLI ETPGEVPDDV WLQVLCPCRE DFIRRTVDSL
KGAKKAILHL YLATSECFRR VVFSMSKQES VEMAVRCTKY ARSITKDDPS TAGTEWLFEF
SPETFSDTDP DFVLEICEAV KAAWEPTVEA PLIFNLPATV EMSTPNVYAD QIEYFSTRIS
ERDKVCVSLH PHNDRGCAVA AAELAQMAGA QRVEGTLFGN GERTGNVDLV TLALNLYTQG
ISPKVDFSDI NSIIKVVEES NKIPVNERWP YGGQLVVCAF SGSHQDAIKK GFQVRESSKA
SNEDRWQIPY LPIDPEDIGR NYEAIIRVNS QSGKGGVAWV ILRSLELDLP RGLQIAFSKV
IQKQADTLGR ELLPKEIVSL FEEAYHLKQN PRFSLVDYNI TTDRSQSPAP PEPGKALNTK
NLKRRFAGIV EIDGMQHAIV GVGNGAISSL ANALKSLGID LDVVDYKEHA IGSHSETKAA
TYIECTSADS PEKVWGVGIH QDVVQASLTA LLSAASSFLT SRTNTPAPFR PSHMKNLTEA
DLEALDQIQG NTGPARALVP DNANVGATSA NQKVNIAQLE SKANIL
//
