ID   A0A1X7RW26_ZYMTR        Unreviewed;       573 AA.
AC   A0A1X7RW26;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-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=ZT3D7_G6603 {ECO:0000313|EMBL:SMQ51450.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51450.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ51450.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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   -!- 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; LT853697; SMQ51450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RW26; -.
DR   STRING; 1276538.A0A1X7RW26; -.
DR   Proteomes; UP000215127; Chromosome 6.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.160.270; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR46911; -; 1.
DR   PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 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   Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          39..320
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   573 AA;  62898 MW;  B8A4F17CC2A709D5 CRC64;
     MTTYQCCCGL SAEEKYGGRD VGFSYPERKW PNRTIDEAPV LLSCDLRDGN QSLGSPMTFD
     QKMEMFLLLV ALGFKEIEVG FPCANTTEFD FVRYLVDTPG LIPDDVWIQV LSPCREDAIR
     TTIDSVRGAR QVLIFTYLPS SDLARQTVLG LTEAQWIDQA VRGARWIRSL TEDDVEGKSK
     SKTRWRFGFG FEDFASARAE AVIACADAIS AAWQPSREEW IYLGVASSVE VSQPNVFADQ
     VEHFSNSIAR RDCIRLAVHA HNDRGTAVAS AELACLAGAQ RVEGCLFGNG ERAGNLDLVT
     FALNLLARGI DPTLDLRRLD DVRGHCERLT GIPVHLRAPY AGDYSFRAFS GGHQDAISKG
     VHRRAAGASS VNGGSSPVWP QWRIPYLPID PAEVGRSIYS VMGITSQSGK AGVVMAVRTG
     LELDVPVELA RAFSRSVKQR SLDVAAELSV EETCAYFLST FRVREAVKLA AEQFNEHTDN
     ATTVAVTAAY DARTHGTFVS SHPVYNTSGV WTRWSNHLST STSKTAEPLV ASYIRLQVEL
     HLDVWGVGIG QDEEHARMCA AYSAVLARNG PLQ
//