ID T0M0J5_COLGC Unreviewed; 347 AA.
AC T0M0J5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Methylisocitrate lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_05849 {ECO:0000313|EMBL:EQB54335.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB54335.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB54335.1}.
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DR EMBL; AMYD01001167; EQB54335.1; -; Genomic_DNA.
DR AlphaFoldDB; T0M0J5; -.
DR STRING; 1237896.T0M0J5; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_027389_3_1_1; -.
DR OMA; IAHACSY; -.
DR OrthoDB; 554215at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF13; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE (AFU_ORTHOLOGUE AFUA_2G00120); 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
SQ SEQUENCE 347 AA; 37970 MW; 4761F7967FB1F454 CRC64;
MSKSIINSIP YPFKFSPPVV EKKGKLGQTE NLTTTLVNVR GKIPSIQASR LRTMMLEAHN
NSDKILAHAC TYDGLSSRLV EEAGFPMVFL AGYAVASAYG LPDTGYIAMS EMCDKIGEAV
RQVSVPVMAD GDTGYGSPLN VRRTVESFAE AGAAGVMIED QTWPKRCGHT KGKSVVSRGE
AYARIQAACD ARDQGKDIFV LARTDALVVG WDEAMTRAKE FKRIGVDAVF VEALPDRDAM
RKCVETLQLP TFANIIEGGK TENLSAKDLA ELGFCAVAYP WTLVAAKLKS VRETLESLKR
SMTVGAPPMI LSFDEVCEGV GFKKYWELED RYKYDDDGPI NVHVSSR
//
