Q9PKU9 (MALQ_CHLMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
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: 4-alpha-glucanotransferase EC=2.4.1.25 Alternative name(s): Amylomaltase Disproportionating enzyme Short name=D-enzyme | ||||
| Gene names |
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| Organism | Chlamydia muridarum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83560 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia |
Protein attributes
| Sequence length | 527 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the disproportionating enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4-alpha-glucanotransferase activity Inferred from electronic annotation. Source: EC cation bindingInferred 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 – 527 | 527 | 4-alpha-glucanotransferase | PRO_0000170120 | |||
Sequences
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References
| [1] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002160 Genomic DNA. Translation: AAF39223.1. |
| PIR | A81712. |
| RefSeq | NP_296740.1. NC_002620.2. |
3D structure databases | |
| ProteinModelPortal | Q9PKU9. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH77. Glycoside Hydrolase Family 77. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1245715. |
| GenomeReviews | Gene locus TC_0362 in contig AE002160_GR. |
| KEGG | cmu:TC0362. |
| PATRIC | 20372126. VBIChlMur19118_0387. |
| TIGR | TC_0362. |
Phylogenomic databases | |
| HOGENOM | HBG413941. |
| OMA | VATTGTH. |
| PhylomeDB | Q9PKU9. |
| ProtClustDB | PRK14508. |
Enzyme and pathway databases | |
| BioCyc | CMUR243161:TC_0362-MONOMER. |
Family and domain databases | |
| InterPro | IPR003385. Glyco_hydro_77. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| KO | K00705. |
| Pfam | PF02446. Glyco_hydro_77. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MALQ_CHLMU | ||||||||
| Accession | Primary (citable) accession number: Q9PKU9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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