Basic Information
Name | Peroxisomal-coenzyme A synthetase (EC 6.-.-.-) |
Uniprot ID | P38137 |
Systematic gene name | YBR222C |
Standard gene name | PCS60 |
Gene names | PCS60 FAT2 YBR222C YBR1512 |
Description from SGD | YBR222C PCS60 SGDID:S000000426, Chr II from 668351-666720, Genome Release 64-3-1, reverse complement, Verified ORF, "Oxalyl-CoA synthetase; capable of catalyzing conversion of oxalate to oxalyl-CoA; catalyzes first step in pathway of oxalate degradation that functions to protect yeast from inhibitory effects of oxalate; peroxisomal protein that binds mRNA; localizes to both peroxisomal peripheral membrane and matrix, expression is highly inducible by oleic acid; similar to E. coli long chain acyl-CoA synthetase" |
Protein length | 543 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MTSAATVTAS FNDTFSVSDN VAVIVPETDT QVTYRDLSHM VGHFQTMFTN
PNSPLYGAVF RQDTVAISMR NGLEFIVAFL GATMDAKIGA PLNPNYKEKE
FNFYLNDLKS KAICVPKGTT KLQSSEILKS ASTFGCFIVE LAFDATRFRV
EYDIYSPEDN YKRVIYRSLN NAKFVNTNPV KFPGFARSSD VALILHTSGT
TSTPKTVPLL HLNIVRSTLN IANTYKLTPL DRSYVVMPLF HVHGLIGVLL
STFRTQGSVV VPDGFHPKLF WDQFVKYNCN WFSCVPTISM IMLNMPKPNP
FPHIRFIRSC SSALAPATFH KLEKEFNAPV LEAYAMTEAS HQMTSNNLPP
GKRKPGTVGQ PQGVTVVILD DNDNVLPPGK VGEVSIRGEN VTLGYANNPK
ANKENFTKRE NYFRTGDQGY FDPEGFLVLT GRIKELINRG GEKISPIELD
GIMLSHPKID EAVAFGVPDD MYGQVVQAAI VLKKGEKMTY EELVNFLKKH
LASFKIPTKV YFVDKLPKTA TGKIQRRVIA ETFAKSSRNK SKL
PNSPLYGAVF RQDTVAISMR NGLEFIVAFL GATMDAKIGA PLNPNYKEKE
FNFYLNDLKS KAICVPKGTT KLQSSEILKS ASTFGCFIVE LAFDATRFRV
EYDIYSPEDN YKRVIYRSLN NAKFVNTNPV KFPGFARSSD VALILHTSGT
TSTPKTVPLL HLNIVRSTLN IANTYKLTPL DRSYVVMPLF HVHGLIGVLL
STFRTQGSVV VPDGFHPKLF WDQFVKYNCN WFSCVPTISM IMLNMPKPNP
FPHIRFIRSC SSALAPATFH KLEKEFNAPV LEAYAMTEAS HQMTSNNLPP
GKRKPGTVGQ PQGVTVVILD DNDNVLPPGK VGEVSIRGEN VTLGYANNPK
ANKENFTKRE NYFRTGDQGY FDPEGFLVLT GRIKELINRG GEKISPIELD
GIMLSHPKID EAVAFGVPDD MYGQVVQAAI VLKKGEKMTY EELVNFLKKH
LASFKIPTKV YFVDKLPKTA TGKIQRRVIA ETFAKSSRNK SKL
Legend
- X K-Succinylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[173, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[181, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[434, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[523, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[535, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |