Q53641 (Q53641_9CREN) Unreviewed, UniProtKB/TrEMBL
Last modified
November 16, 2011.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Malto-oligosyltrehalose trehalohydrolase PIRNR PIRNR006337 Short name=MTHase PIRNR PIRNR006337 EC=3.2.1.141 PIRNR PIRNR006337 Alternative name(s): 4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase PIRNR PIRNR006337 Maltooligosyl trehalose trehalohydrolase PIRNR PIRNR006337 | ||
| Gene names |
| ||
| Organism | Sulfolobus acidocaldarius EMBL BAA11011.1 | ||
| Taxonomic identifier | 2285 [NCBI] | ||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus |
Protein attributes
| Sequence length | 556 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan. PIRNR PIRNR006337 |
| Pathway | Glycan biosynthesis; trehalose biosynthesis. PIRNR PIRNR006337 |
| Subcellular location | Cytoplasm By similarity PIRSR PIRSR006337-1. |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. PIRNR PIRNR006337 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosidase PIRNR PIRNR006337 Hydrolase |
| Gene Ontology (GO) | |
| Biological process | trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 253 | 1 | Nucleophile By similarity PIRSR PIRSR006337-1 | ||||||
| Active site | 284 | 1 | Proton donor By similarity PIRSR PIRSR006337-1 | ||||||
| Site | 376 | 1 | Transition state stabilizer By similarity PIRSR PIRSR006337-3 | ||||||
Sequences
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References
| [1] | "Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius." Maruta K., Mitsuzumi H., Nakada T., Kubota M., Chaen H., Fukuda S., Sugimoto T., Kurimoto M. Biochim. Biophys. Acta 1291:177-181(1996) [PubMed: 8980629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC33909 EMBL BAA11863.1. |
| [2] | "Gene analysis of trehalose-producing enzymes from hyperthermophilic archaea in Sulfolobales." Kobayashi K., Kato M., Miura Y., Kettoku M., Komeda T., Iwamatsu A. Biosci. Biotechnol. Biochem. 60:1720-1723(1996) [PubMed: 8987674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [3] | "Cloning and sequencing of a cluster of trehalose biosynthesis genes from thermophilic archaebacterium Sulfolobus acidocaldarius." Maruta K., Mitsuzumi H., Nakada T., Kubota M., Chaen H., Fukuda S., Sugimoto T., Kurimoto M. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC33909 EMBL BAA11863.1. |
| [4] | "The gene analysis of the new amylases from the hyper thermophilic archae Sulfolobus." Kato M., Kettoku M., Miura Y., Komeda T., Konishi Y., Shindo K., Kobayashi K., Iwamatsu A. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC33909 EMBL BAA11011.1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D64131 Genomic DNA. Translation: BAA11011.1. D83245 Genomic DNA. Translation: BAA11863.1. |
| PIR | JC5132. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EH9 based on UniProtKB Q55088. |
| ProteinModelPortal | Q53641. |
| SMR | Q53641. Positions 3-554. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| NMPDR | fig|330779.3.peg.1987. |
Phylogenomic databases | |
| HOGENOM | HBG367595. |
| OMA | EGFVYQG. |
| ProtClustDB | CLSK285578. |
Enzyme and pathway databases | |
| BioCyc | SACI330779:SACI_1440-MONOMER. |
Family and domain databases | |
| InterPro | IPR015902. Alpha_amylase. IPR006047. Glyco_hydro_13_cat_dom. IPR004193. Glyco_hydro_13_N. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR015156. Maltooligo_trehalose_arc_C. IPR012768. Trehalose_TreZ. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. |
| PANTHER | PTHR10357. Alpha_amylase. 1 hit. PTHR10357:SF21. PTHR10357:SF21. 1 hit. |
| Pfam | PF09071. Alpha-amyl_C. 1 hit. PF00128. Alpha-amylase. 2 hits. PF02922. CBM_48. 1 hit. [Graphical view] |
| PIRSF | PIRSF006337. Trehalose_TreZ. 1 hit. |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit. |
| TIGRFAMs | TIGR02402. Trehalose_TreZ. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | Q53641_9CREN | ||||||||
| Accession | Primary (citable) accession number: Q53641 Secondary accession number(s): O08064, O08279, Q4J8W4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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