Reviewed,
UniProtKB/Swiss-Prot P57749 (PGM_ASPOR)
Last modified
September 22, 2009.
Version 53.
History...
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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: Phosphoglucomutase Short name=PGM EC=5.4.2.2 Alternative name(s): Glucose phosphomutase | ||||
| Gene names |
| ||||
| Organism | Aspergillus oryzae [Complete proteome] | ||||
| Taxonomic identifier | 5062 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 555 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | This enzyme participates in both the breakdown and synthesis of glucose By similarity. |
| Catalytic activity | Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activityInferred 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 – 555 | 555 | Phosphoglucomutase | PRO_0000147793 | |||||
Sites | |||||||||
| Active site | 114 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 114 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 279 | 1 | Magnesium By similarity | ||||||
| Metal binding | 281 | 1 | Magnesium By similarity | ||||||
| Metal binding | 283 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and characterization of phosphoglucomutase from Aspergillus oryzae." Nakajima K., Kunihiro S., Sano M., Eto S., Machida M. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 42149 / RIB 40. |
| [2] | "Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H.Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40. |
Cross-references
Sequence databases | |
|---|---|
| AB032275 mRNA. Translation: BAB12235.1. AP007155 Genomic DNA. Translation: BAE57887.1. | |
| RefSeq | XP_001819889.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 3PMG based on UniProtKB P00949. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5991872. |
| GenomeReviews | Gene locus pgmA in contig AP007155_GR. |
| KEGG | aor:AO090003000746. |
Enzyme and pathway databases | |
| BRENDA | 5.4.2.2. 2240. |
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. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| 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] |
| PRINTS | PR00509. PGMPMM. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PGM_ASPOR | ||||||||
| Accession | Primary (citable) accession number: P57749 Secondary accession number(s): Q2UKM8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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