Reviewed,
UniProtKB/Swiss-Prot O42154 (G6PC_HAPXE)
Last modified
November 4, 2008.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glucose-6-phosphatase Short name=G-6-Pase Short name=G6Pase EC=3.1.3.9 | ||||
| Gene names |
| ||||
| Organism | Haplochromis xenognathus | ||||
| Taxonomic identifier | 51185 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Labroidei › Cichlidae › African cichlids › Pseudocrenilabrinae › Haplochromini › Ptyochromis |
Protein attributes
| Sequence length | 277 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | D-glucose 6-phosphate + H2O = D-glucose + phosphate. |
| Pathway | |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
| Sequence similarities | Belongs to the glucose-6-phosphatase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glucose-6-phosphatase 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 – 277 | ›277 | Glucose-6-phosphatase | PRO_0000087412 | |||||
Regions | |||||||||
| Transmembrane | 39 – 59 | 21 | Potential | ||||||
| Transmembrane | 67 – 87 | 21 | Potential | ||||||
| Transmembrane | 131 – 151 | 21 | Potential | ||||||
| Transmembrane | 215 – 235 | 21 | Potential | ||||||
| Transmembrane | 250 – 270 | 21 | Potential | ||||||
| Motif | 274 – 277 | 4 | Prevents secretion from ER Potential | ||||||
Sites | |||||||||
| Active site | 40 | 1 | Proton donor Potential | ||||||
| Active site | 97 | 1 | Nucleophile By similarity | ||||||
| Binding site | 4 | 1 | Substrate Potential | ||||||
| Binding site | 91 | 1 | Substrate Potential | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Isolation and sequencing of cDNA clones coding for the catalytic unit of glucose-6-phosphatase from two haplochromine cichlid fishes." Nagl S., Mayer W.E., Klein J. DNA Seq. 10:25-29(1999) [PubMed: 10565541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF008946 mRNA. Translation: AAB69286.1. | |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | O42154. |
Family and domain databases | |
| InterPro | IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view] |
| Pfam | PF01569. PAP2. 1 hit. [Graphical view] |
| SMART | SM00014. acidPPc. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | G6PC_HAPXE | ||||||||
| Accession | Primary (citable) accession number: O42154 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


