Reviewed,
UniProtKB/Swiss-Prot O84250 (PHSG_CHLTR)
Last modified
November 3, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycogen phosphorylase EC=2.4.1.1 | ||||
| Gene names |
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| Organism | Chlamydia trachomatis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 813 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 814 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties By similarity. |
| Catalytic activity | (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Sequence similarities | Belongs to the glycogen phosphorylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glycogen metabolism |
| Ligand | Pyridoxal phosphate |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Allosteric enzyme Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
Cross-references
Sequence databases | |
|---|---|
| AE001273 Genomic DNA. Translation: AAC67841.1. | |
| PIR | A71540. |
| RefSeq | NP_219753.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2GPN based on UniProtKB P00489. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GT35. Glycosyltransferase Family 35. |
Genome annotation databases | |
| GeneID | 884873. |
| GenomeReviews | Gene locus CT_248 in contig AE001273_GR. |
| KEGG | ctr:CT248. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O84250. |
| OMA | RFNAGDH. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:CT248-MON. |
| BRENDA | 2.4.1.1. 108. |
Family and domain databases | |
| InterPro | IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view] |
| PANTHER | PTHR11468. Glyco_trans_35. 1 hit. |
| Pfam | PF00343. Phosphorylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000460. Pprylas_GlgP. 1 hit. |
| TIGRFAMs | TIGR02093. P_ylase. 1 hit. |
| PROSITE | PS00102. PHOSPHORYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PHSG_CHLTR | ||||||||
| Accession | Primary (citable) accession number: O84250 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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