ID A0A2N5TH96_9BASI Unreviewed; 621 AA.
AC A0A2N5TH96;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PCANC_06924 {ECO:0000313|EMBL:PLW49245.1}, PCASD_05229
GN {ECO:0000313|EMBL:PLW24768.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW24768.1, ECO:0000313|Proteomes:UP000235392};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW49245.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW24768.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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:PLW24768.1}.
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DR EMBL; PGCI01000604; PLW24768.1; -; Genomic_DNA.
DR EMBL; PGCJ01000097; PLW49245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5TH96; -.
DR STRING; 200324.A0A2N5TH96; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; 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:UP000235388};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 53..336
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 68711 MW; 26E7F9D750401976 CRC64;
MIRAPFGHSR VARFNASHPA RGMLKRPSTK YHSPPTVNLP DRTWPGNTIS KVPRWCAVDL
RDGNQSLVNP MTVEQKTTFF NLLLQCGFKE IEVGFPAASD TDFDFVRKIA KSRQPNLDDV
AIQVLSPARE DLIRRTFDAV KDGRNVIIHM YNATSPLFRQ TVFQASKAKT IDLAVRHAEL
VRQLSDEAMS RGDRTDWQFQ YSPETFSQTE PEFAVEICEA VKKVWFKGKD MKKSHPIIFN
LPATVEVSTP NVYADQIEYF CRNITDREHC HISLHTHNDR GTGVAATELG LMAGADRVEG
CLFGNGERTG NVDLVTVALN MYSHGLAPNL DFSDIKKVID VVTECNDIPV HPRHPYSGDL
VFTAFSGSHQ DAIKKGFAIQ QANSPWEMPY LSIDPHDIGC DYEAVIRVNS QSGKGGVAYL
IQEHLGLDMP RKMQVAFYGI VQNLADRTGR EMTVEDLTKC FRTAYHLGLG HEGRFKLQDY
SIANMAQGDG THQIDPTTGE PLPPRKVLRA TILKDKKKVE LSGEGNGPVS AMMNAMRTHC
GLLLDVVSYS EKAIGSGSGT KAASYIELKD ERGRHVWGVG VDEDVTTSLL KAVISAANTA
STSAQQQSDE IFTTVVGSKP A
//
