Q5R979 (PGM2L_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glucose 1,6-bisphosphate synthase EC=2.7.1.106 Alternative name(s): Phosphoglucomutase-2-like 1 | ||
| Gene names |
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| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 622 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities By similarity. |
| Catalytic activity | 3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate. |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism |
| Molecular function | Isomerase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glucose-1,6-bisphosphate synthase activity Inferred from electronic annotation. Source: EC intramolecular transferase activity, phosphotransferasesInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 622 | 622 | Glucose 1,6-bisphosphate synthase | PRO_0000147786 | |||||
Sites | |||||||||
| Active site | 175 | 1 | Phosphoserine intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 175 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 598 | 1 | L → P in CAH91272. Ref.1 | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR859079 mRNA. Translation: CAH91272.1. CR859513 mRNA. Translation: CAH91681.1. |
| RefSeq | NP_001125984.1. NM_001132512.1. |
| UniGene | Pab.1510. |
3D structure databases | |
| ProteinModelPortal | Q5R979. |
| SMR | Q5R979. Positions 562-606. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q5R979. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSPPYT00000004370; ENSPPYP00000004199; ENSPPYG00000003674. |
| GeneID | 100172923. |
| KEGG | pon:100172923. |
Organism-specific databases | |
| CTD | 283209. |
Phylogenomic databases | |
| HOVERGEN | HBG056917. |
| InParanoid | Q5R979. |
| OMA | IGEDVDM. |
Family and domain databases | |
| InterPro | IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. [Graphical view] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| KO | K11809. |
| Pfam | PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view] |
| SUPFAM | SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| PROSITE | PS00710. PGM_PMM. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PGM2L_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R979 Secondary accession number(s): Q5RAD8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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