ID W9XZ50_9EURO Unreviewed; 1246 AA.
AC W9XZ50;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=A1O1_05862 {ECO:0000313|EMBL:EXJ85498.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ85498.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ85498.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ85498.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ85498.1}.
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DR EMBL; AMWN01000005; EXJ85498.1; -; Genomic_DNA.
DR RefSeq; XP_007724936.1; XM_007726746.1.
DR AlphaFoldDB; W9XZ50; -.
DR STRING; 1182541.W9XZ50; -.
DR GeneID; 19160735; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_007089_0_0_1; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000019484; 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:UP000019484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 601..879
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 223..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 137597 MW; 94E9DB58C1B5BB6C CRC64;
MRYQNWDVLM FPGSSRVPIQ EFDTKCYGLE QNPGFSTVLP AIDTDRNSFE SMTVVPVLTS
FVASLERGAA FRVSIHCWDK PKPSNLLLNY KTPDESVLFR ARVYIDGVLA AHRTFEGGTW
PEVIANVLEH GDQRLRFPAF HKEILQQPHW EPGESLGRVK VIISEGVLRD ITPPAPADTM
FDRLRDVVVF SFQHAPQNIL EFSNIAWPNT KIFARLSKRV PRPGPIGSRL PPVSGHEAHS
HSPLRPAAAI RGGKPLSSGL DGFQRLLNAQ TFSDLQSDPV SKASTFPLSD KESPERRELV
GGTVTCEDPF ICPQPISSQQ WRLQLRSTSH DLPMPDYTSN KTETSGGCTE MSGVSFPRAN
FLRHMNEANP QEIVQALSPA RQEELLQVLS ASHSPVRGTH APTNTPRSLS DQSRPQSPLI
KDGAGTRQMI RLDGPPGRRD PSDSYWPLRL QKREQRRRTY SDSSIRSTSG PVKESIKHDI
SPVLPREWAG KDGSGPLVPI GMKSLSMNAQ RQRSTSNASK RKRGPASPSV GIGKTQDPIH
VVIDSSTSGA GLEAGLKHNT PTRIVVALND ELREPWKKYR KFKPLDLPNR QWPSKTNEKP
PRWLATDLRD GNQSLPDPMD GEQKLRFFKM LVELGYKEIE VSFPSASQTD YDFTRSLVET
PGVVPDDVWL QVLSPCREDL IRRTVESLRG AKKAILHLYL ATSDCFRRIV FGMTEDESIA
LAVKCTKLAR SLTKDDPSQA GTEWLYEFSP ETFSDTSPEF AVRICEAVKE AWGPTEDAKL
IFNLPATVEM STPNVFADQV EYFSTHMTER EKFCISVHPH NDRGCAVAAA ELAQMAGAER
VEGTLFGNGE RTGNVDLVTL ALNLYTQGIW PNVDFSDIGK VIRVCEESTK IPVNERWPYG
GQLVVCAFSG SHQDAIKKGF QVRKNKGLGQ QDPWEVPYLP LDPQDLGRTY EAVIRVNSQS
GKGGVAWIIQ RSLELDLPRG LQVAFSKIVQ KEADAKGREL LPREIQALFE ESYHLKKNPR
FTLVDYNITA VRTTSPAPTM KSSVGQPPQT AAPAQNTSTA KRQFAGIIAI DGIQHPVVGV
GNGAISSLAN ALHSLGIDLD VADYKEHAIG EGREVKAATY IECTASGSHE KVWGVGIHED
VVQASLIALL SAASSFLTSR VSTPVPFRPK HTPHFSDAEL QALERLNLNA SDTPSSPLRS
SMTADSVPAP SKLNMEPNAG SVSANRIDID LLERKAEDIN GQSQKS
//
