Basic Information
| Name | Isocitrate lyase (ICL) (EC 4.1.3.1) (Methylisocitrate lyase) (MICA) (EC 4.1.3.30) (Threo-D(S)-isocitrate glyoxylate-lyase) |
| Uniprot ID | P28240 |
| Systematic gene name | YER065C |
| Standard gene name | ICL1 |
| Gene names | ICL1 YER065C |
| Description from SGD | YER065C ICL1 SGDID:S000000867, Chr V from 286914-285241, Genome Release 64-3-1, reverse complement, Verified ORF, "Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose" |
| Protein length | 557 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MPIPVGNTKN DFAALQAKLD ADAAEIEKWW SDSRWSKTKR NYSARDIAVR
RGTFPPIEYP SSVMARKLFK VLEKHHNEGT VSKTFGALDP VQISQMAKYL
DTIYISGWQC SSTASTSNEP GPDLADYPMD TVPNKVEHLF KAQLFHDRKQ
LEARSKAKSQ EELDEMGAPI DYLTPIVADA DAGHGGLTAV FKLTKMFIER
GAAGIHMEDQ TSTNKKCGHM AGRCVIPVQE HVNRLVTIRM CADIMHSDLI
VVARTDSEAA TLISSTIDTR DHYFIVGATN PNIEPFAEVL NDAIMSGASG
QELADIEQKW CRDAGLKLFH EAVIDEIERS ALSNKQELIK KFTSKVGPLT
ETSHREAKKL AKEILGHEIF FDWELPRVRE GLYRYRGGTQ CSIMRARAFA
PYADLVWMES NYPDFQQAKE FAEGVKEKFP DQWLAYNLSP SFNWPKAMSV
DEQHTFIQRL GDLGYIWQFI TLAGLHTNAL AVHNFSRDFA KDGMKAYAQN
VQQREMDDGV DVLKHQKWSG AEYIDGLLKL AQGGVSATAA MGTGVTEDQF
KENGVKK
RGTFPPIEYP SSVMARKLFK VLEKHHNEGT VSKTFGALDP VQISQMAKYL
DTIYISGWQC SSTASTSNEP GPDLADYPMD TVPNKVEHLF KAQLFHDRKQ
LEARSKAKSQ EELDEMGAPI DYLTPIVADA DAGHGGLTAV FKLTKMFIER
GAAGIHMEDQ TSTNKKCGHM AGRCVIPVQE HVNRLVTIRM CADIMHSDLI
VVARTDSEAA TLISSTIDTR DHYFIVGATN PNIEPFAEVL NDAIMSGASG
QELADIEQKW CRDAGLKLFH EAVIDEIERS ALSNKQELIK KFTSKVGPLT
ETSHREAKKL AKEILGHEIF FDWELPRVRE GLYRYRGGTQ CSIMRARAFA
PYADLVWMES NYPDFQQAKE FAEGVKEKFP DQWLAYNLSP SFNWPKAMSV
DEQHTFIQRL GDLGYIWQFI TLAGLHTNAL AVHNFSRDFA KDGMKAYAQN
VQQREMDDGV DVLKHQKWSG AEYIDGLLKL AQGGVSATAA MGTGVTEDQF
KENGVKK
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
| [59, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
| [59, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
| [59, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |