Reviewed,
UniProtKB/Swiss-Prot Q0JC10 (DCAM_ORYSJ)
Last modified
June 16, 2009.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: S-adenosylmethionine decarboxylase proenzyme Short name=AdoMetDC Short name=SAMDC EC=4.1.1.50 Cleaved into the following 2 chains: 1- Recommended name: S-adenosylmethionine decarboxylase alpha chain 2- Recommended name: S-adenosylmethionine decarboxylase beta chain | ||||||
| Gene names |
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| Organism | Oryza sativa subsp. japonica (Rice) | ||||||
| Taxonomic identifier | 39947 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza |
Protein attributes
| Sequence length | 398 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. |
| Cofactor | Pyruvoyl group. |
| Pathway | |
| Post-translational modification | Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain By similarity. |
| Sequence similarities | Belongs to the eukaryotic AdoMetDC family. |
| Sequence caution | The sequence CAD41510.3 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAZ14251.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis Spermidine biosynthesis |
| Ligand | Pyruvate S-adenosyl-L-methionine Schiff base |
| Molecular function | Decarboxylase Lyase |
| PTM | Autocatalytic cleavage Zymogen |
| Gene Ontology (GO) | |
| Biological process | spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW spermine biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular function | adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 77 | 77 | S-adenosylmethionine decarboxylase beta chain By similarity | PRO_0000030017 | |||||
| Chain | 78 – 398 | 321 | S-adenosylmethionine decarboxylase alpha chain By similarity | PRO_0000030018 | |||||
Sites | |||||||||
| Active site | 18 | 1 | By similarity | ||||||
| Active site | 21 | 1 | By similarity | ||||||
| Active site | 78 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity | ||||||
| Active site | 92 | 1 | Proton donor; for catalytic activity By similarity | ||||||
| Active site | 243 | 1 | Proton acceptor; for processing activity By similarity | ||||||
| Active site | 256 | 1 | Proton acceptor; for processing activity By similarity | ||||||
| Site | 77 – 78 | 2 | Cleavage (non-hydrolytic); by autolysis By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 78 | 1 | Pyruvic acid (Ser); by autocatalysis By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of monocot and dicot plant S-adenosyl-L-methionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames." Franceschetti M., Hanfrey C., Scaramagli S., Torrigiani P., Bagni N., Michael A.J. Biochem. J. 353:403-409(2001) [PubMed: 11139406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Nipponbare. |
| [2] | "Sequence and analysis of rice chromosome 4." Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. Han B.Nature 420:316-320(2002) [PubMed: 12447439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare. |
| [3] | "The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare. |
| [4] | "Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana." The rice annotation project (RAP) Genome Res. 17:175-183(2007) [PubMed: 17210932] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare. |
| [5] | "The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. Yang H.PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare. |
Cross-references
Sequence databases | |
|---|---|
| Y07766 mRNA. Translation: CAA69074.2. AL606594 Genomic DNA. Translation: CAD41510.3. Sequence problems. AL606627 Genomic DNA. Translation: CAD41242.2. AP008210 Genomic DNA. Translation: BAF15127.1. CM000138 Genomic DNA. Translation: EAZ14251.1. Sequence problems. | |
| PIR | T04099. |
| RefSeq | NP_001053213.1. |
| UniGene | Os.38386 Os.4786 Os.52749 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I72 based on UniProtKB P17707. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4336294. |
| KEGG | osa:4336294. |
Organism-specific databases | |
| Gramene | O24215. |
Family and domain databases | |
| InterPro | IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_sg. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view] |
| Gene3D | G3DSA:3.60.90.10. SAM_decarbox. 1 hit. |
| PANTHER | PTHR11570. SAM_decarbox. 1 hit. |
| Pfam | PF01536. SAM_decarbox. 1 hit. [Graphical view] |
| PIRSF | PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit. |
| ProDom | PD002379. SAM_decarbox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00535. SAM_DCase. 1 hit. |
| PROSITE | PS01336. ADOMETDC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DCAM_ORYSJ | ||||||||
| Accession | Primary (citable) accession number: Q0JC10 Secondary accession number(s): A2ZZV4 Q9SC65 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Oryza sativa (rice) Index of Oryza sativa entries and their corresponding gene designations |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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