FCY1
Protein
Cytosine deaminase
Gene
FCY1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli
Functioni
Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.2 Publications
Miscellaneous
Present with 5180 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- cytosine + H+ + H2O = NH4+ + uracil1 Publication
EC:3.5.4.11 Publication
Source: Rhea. « Hidecytosine
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+H+
+H2O
=NH4+
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+uracil
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Cofactori
Zn2+3 Publications
Kineticsi
kcat is 91 sec(-1) with cytosine as substrate and 17 sec(-1) with 5-fluorocytosine as substrate.1 Publication
- KM=1.1 mM for cytosine1 Publication
- KM=0.16 mM for 5-fluorocytosine1 Publication
Pathwayi: UMP biosynthesis via salvage pathway
This protein is involved in step 1 of the subpathway that synthesizes uracil from cytosine.1 Publication1 Publication
Proteins known to be involved in this subpathway in this organism are:
- Cytosine deaminase (FCY1)
This subpathway is part of the pathway UMP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes uracil from cytosine, the pathway UMP biosynthesis via salvage pathway and in Pyrimidine metabolism.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Binding sitei | 51 | SubstrateCombined sources2 Publications | 1 | |
| Metal bindingi | 62 | Zinc; catalyticCombined sources3 Publications | 1 | |
| Active sitei | 64 | Proton donorCombined sources1 Publication | 1 | |
| Metal bindingi | 91 | Zinc; catalyticCombined sources3 Publications | 1 | |
| Metal bindingi | 94 | Zinc; catalyticCombined sources3 Publications | 1 | |
| Binding sitei | 155 | SubstrateCombined sources2 Publications | 1 |
GO - Molecular functioni
- 5-fluorocytosine deaminase activity Source: UniProtKB-EC
- cytosine deaminase activity Source: SGD
- tRNA-specific adenosine-34 deaminase activity Source: GO_Central
- zinc ion binding Source: InterPro
GO - Biological processi
- cytidine metabolic process Source: SGD
- cytosine metabolic process Source: SGD
- pyrimidine-containing compound salvage Source: SGD
- tRNA wobble adenosine to inosine editing Source: GO_Central
- UMP salvage Source: UniProtKB-UniPathway
Keywordsi
| Molecular function | Hydrolase |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
| BioCyci | MetaCyc:YPR062W-MONOMER |
| BRENDAi | 3.5.4.1, 984 |
| UniPathwayi | UPA00574;UER00635 |
Names & Taxonomyi
| Protein namesi |
Recommended name:
Cytosine deaminase1 Publication (EC:3.5.4.11 Publication) Short name: yCD Alternative name(s): Cytosine aminohydrolase Fluorocytosine resistance protein 11 Publication |
| Gene namesi |
Name:FCY11 Publication Ordered Locus Names:YPR062W ORF Names:YP9499.17
|
| Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic identifieri | 559292 [NCBI] |
| Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
| Proteomesi |
|
Organism-specific databases
| SGDi | S000006266, FCY1 |
| VEuPathDBi | FungiDB:YPR062W |
Subcellular locationi
- UniProt annotation
- GO - Cellular component
Keywords - Cellular componenti
Pathology & Biotechi
Biotechnological usei
Also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. yCD/5FC is one of the most widely used enzyme/prodrug combinations for gene-directed enzyme prodrug therapy (GDEPT) for the treatment of cancers. 5FU is an anticancer drug used to treat breast, colon, rectal, stomach, and pancreatic cancers, and is the drug of choice for treating colorectal carcinoma. However, the drug has high gastrointestinal and hematological toxicities. In contrast, the prodrug 5FC is fairly non-toxic to human, because of the lack of CD activity in human cells. By producing 5FU in the tumor, the CD/5FC system minimizes the undesired toxic effects of 5FU.1 Publication
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000171702 | 1 – 158 | Cytosine deaminaseAdd BLAST | 158 |
Proteomic databases
| MaxQBi | Q12178 |
| PaxDbi | Q12178 |
| PRIDEi | Q12178 |
PTM databases
| iPTMneti | Q12178 |
Interactioni
Subunit structurei
Homodimer.
1 Publication
Protein-protein interaction databases
| BioGRIDi | 36235, 61 interactors |
| DIPi | DIP-1662N |
| IntActi | Q12178, 2 interactors |
| MINTi | Q12178 |
| STRINGi | 4932.YPR062W |
Miscellaneous databases
| RNActi | Q12178, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
3D structure databases
| SMRi | Q12178 |
| ModBasei | Search... |
| PDBe-KBi | Search... |
Miscellaneous databases
| EvolutionaryTracei | Q12178 |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 9 – 129 | CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST | 121 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Compositional biasi | 129 – 132 | Poly-Val | 4 |
Sequence similaritiesi
Belongs to the cytidine and deoxycytidylate deaminase family.Curated
Phylogenomic databases
| HOGENOMi | CLU_025810_7_2_1 |
| InParanoidi | Q12178 |
| OMAi | AILHAEM |
Family and domain databases
| InterProi | View protein in InterPro IPR016192, APOBEC/CMP_deaminase_Zn-bd IPR002125, CMP_dCMP_dom IPR016193, Cytidine_deaminase-like |
| Pfami | View protein in Pfam PF00383, dCMP_cyt_deam_1, 1 hit |
| SUPFAMi | SSF53927, SSF53927, 1 hit |
| PROSITEi | View protein in PROSITE PS00903, CYT_DCMP_DEAMINASES_1, 1 hit PS51747, CYT_DCMP_DEAMINASES_2, 1 hit |
Sequencei
Sequence statusi: Complete.
Q12178-1 [UniParc]FASTAAdd to basket
« Hide
10 20 30 40 50MVTGGMASKW DQKGMDIAYE EAALGYKEGG VPIGGCLINN KDGSVLGRGH 60 70 80 90 100NMRFQKGSAT LHGEISTLEN CGRLEGKVYK DTTLYTTLSP CDMCTGAIIM 110 120 130 140 150YGIPRCVVGE NVNFKSKGEK YLQTRGHEVV VVDDERCKKI MKQFIDERPQ DWFEDIGE
Length:158
Mass (Da):17,507
Last modified:November 1, 1996 - v1
Checksum:i19DB41E9AF26ADDC
GO
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi |
U55193 Genomic DNA Translation: AAC13409.1 AF005261 Genomic DNA Translation: AAB67713.1 Z71255 Genomic DNA Translation: CAA95006.1 Z49219 Genomic DNA Translation: CAA89179.1 BK006949 Genomic DNA Translation: DAA11483.1 |
| PIRi | S54083 |
| RefSeqi | NP_015387.1, NM_001184159.1 |
Genome annotation databases
| EnsemblFungii | YPR062W_mRNA; YPR062W; YPR062W |
| GeneIDi | 856175 |
| KEGGi | sce:YPR062W |
Similar proteinsi
- 100% Identity
- 90% Identity
- 50% Identity
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q12178 | BJ4_G0056360.mRNA.1.CDS.1 | 158 | UniRef100_Q12178 | |||
| FCY1p Cytosine deaminase | 158 | |||||
| K7_Fcy1p | 158 | |||||
| Fcy1p | 158 | |||||
| Fcy1p | 158 | |||||
| +5 | ||||||
Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi |
U55193 Genomic DNA Translation: AAC13409.1 AF005261 Genomic DNA Translation: AAB67713.1 Z71255 Genomic DNA Translation: CAA95006.1 Z49219 Genomic DNA Translation: CAA89179.1 BK006949 Genomic DNA Translation: DAA11483.1 |
| PIRi | S54083 |
| RefSeqi | NP_015387.1, NM_001184159.1 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji |
PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1OX7 | X-ray | 1.43 | A/B | 1-158 | [»] | |
| 1P6O | X-ray | 1.14 | A/B | 1-158 | [»] | |
| 1RB7 | X-ray | 2.10 | A/B | 1-158 | [»] | |
| 1UAQ | X-ray | 1.60 | A/B | 1-158 | [»] | |
| 1YSB | X-ray | 1.70 | A/B | 1-158 | [»] | |
| 1YSD | X-ray | 1.90 | A/B | 1-158 | [»] | |
| 2O3K | X-ray | 2.30 | A/B | 1-158 | [»] | |
| SMRi | Q12178 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 36235, 61 interactors |
| DIPi | DIP-1662N |
| IntActi | Q12178, 2 interactors |
| MINTi | Q12178 |
| STRINGi | 4932.YPR062W |
PTM databases
| iPTMneti | Q12178 |
Proteomic databases
| MaxQBi | Q12178 |
| PaxDbi | Q12178 |
| PRIDEi | Q12178 |
Genome annotation databases
| EnsemblFungii | YPR062W_mRNA; YPR062W; YPR062W |
| GeneIDi | 856175 |
| KEGGi | sce:YPR062W |
Organism-specific databases
| SGDi | S000006266, FCY1 |
| VEuPathDBi | FungiDB:YPR062W |
Phylogenomic databases
| HOGENOMi | CLU_025810_7_2_1 |
| InParanoidi | Q12178 |
| OMAi | AILHAEM |
Enzyme and pathway databases
| UniPathwayi | UPA00574;UER00635 |
| BioCyci | MetaCyc:YPR062W-MONOMER |
| BRENDAi | 3.5.4.1, 984 |
Miscellaneous databases
| EvolutionaryTracei | Q12178 |
| PROi | PR:Q12178 |
| RNActi | Q12178, protein |
Family and domain databases
| InterProi | View protein in InterPro IPR016192, APOBEC/CMP_deaminase_Zn-bd IPR002125, CMP_dCMP_dom IPR016193, Cytidine_deaminase-like |
| Pfami | View protein in Pfam PF00383, dCMP_cyt_deam_1, 1 hit |
| SUPFAMi | SSF53927, SSF53927, 1 hit |
| PROSITEi | View protein in PROSITE PS00903, CYT_DCMP_DEAMINASES_1, 1 hit PS51747, CYT_DCMP_DEAMINASES_2, 1 hit |
| ProtoNeti | Search... |
| MobiDBi | Search... |
Entry informationi
| Entry namei | FCY1_YEAST | |
| Accessioni | Primary (citable) accession number: Q12178 Secondary accession number(s): D6W467 |
|
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1996 | |
| Last modified: | February 10, 2021 | |
| This is version 177 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Fungal Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteome
Documents
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XVI
Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
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