ID A0A137QM48_9AGAR Unreviewed; 610 AA.
AC A0A137QM48;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=AN958_07490 {ECO:0000313|EMBL:KXN88345.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN88345.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN88345.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN88345.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ962165; KXN88345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QM48; -.
DR STRING; 1714833.A0A137QM48; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..261
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 610 AA; 67110 MW; C2CCCCE41C921295 CRC64;
MSNPTKLELF RALVKIGFKE IEVAYPSASE QEYQFCRSII ENGEVPDDVA LQIITPARPD
LIERSIKSLA GCKKAIIHLY NAVSPVFREV VFRNTKEQTI DLTLNAVRLV KKLAEEEFAR
SGTHYTLLYC LETFSQTEID FAAELGNRVY DEWGKATPED PIMFNLAATV ECGPSNHYAD
MVEYFDNNIK NRDSVVLSIH PHNDRGTAVA AAELALLAGG DRIEGCLLGN GERTGNVDLI
SLALNMYSQG ISPNLDFSNL PEIVELVCKC NEMAVPTRYP YAGQLVFSAF AGTHQDAIKK
GLDAQAKRWE DVDRSGQGKK YWAMPYIPLD PKDLGYGYEN LIRVSSQSGK AGTAYVIKQT
MLLDLPRRMQ VSFYKVVQDE SERSGKEMTP AMITTAFRTA YSVCSKPMNR IFLKSYRLLP
LSPSTLEPSS PMSDFSDDPF TLTPPDEDQS LIRFEADLII DGAERTISGD GRGIVLAALD
ALKSDLDLSF QIGESAAHTI NADNLSHSKC ATFLELSMTG TTPSKSGVGS TWGIGISSDV
ATSKCRAVIS AANCLVGDRS FPRSKMVFTP RSSGHIVQGD SWLQEVKLRA GRLLSYGSDS
RQSLKLQTTA
//
