ID A0A165KG10_9APHY Unreviewed; 229 AA.
AC A0A165KG10;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=DAEQUDRAFT_815842 {ECO:0000313|EMBL:KZT63085.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63085.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT63085.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT63085.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429275; KZT63085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KG10; -.
DR STRING; 1314783.A0A165KG10; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.287.1400; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 1..147
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 229 AA; 25242 MW; 3D80570D355E680E CRC64;
MSSGIIAHLP DILKRDSPGT NNKGVARHCP QWDVHSESRA VTAFEDWIIF DLPAMVEIGP
PNRYVDQMQS LCHHICEREK IYVSLHPHND QGQGITAAEL TMLGGADPVE SCLSGNGERT
GNIDLVNLAS NQYPQGINPG LYFSELCFTA FSGSHSHAVK KGFEHQRGRW VEAEHKGEPK
ILRIPYLPID LTDLGCNYEA VIRINAQSSK GGIAYRVQRA AEPHAQHAA
//
