Reviewed,
UniProtKB/Swiss-Prot P38939 (APU_THEP3)
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June 16, 2009.
Version 77.
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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: Amylopullulanase Alternative name(s): Alpha-amylase/pullulanase Including the following 2 domains: 1- Recommended name: Alpha-amylase EC=3.2.1.1 Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase 2- Recommended name: Pullulanase EC=3.2.1.41 Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase Alpha-dextrin endo-1,6-alpha-glucosidase | ||||
| Gene names |
| ||||
| Organism | Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 340099 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter |
Protein attributes
| Sequence length | 1481 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides. Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. Contains 1 CBM20 (carbohydrate binding type-20) domain. Contains 2 fibronectin type-III domains. |
| Sequence caution | The sequence ABY95795.1 differs from that shown. Reason: Frameshift at position 1477. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Domain | Repeat Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW carbohydrate bindingInferred from electronic annotation. Source: InterPro pullulanase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 31 | 31 | Potential | ||||||
| Chain | 32 – 1481 | 1450 | Amylopullulanase | PRO_0000001322 | |||||
Regions | |||||||||
| Domain | 924 – 1013 | 90 | Fibronectin type-III 1 | ||||||
| Domain | 1156 – 1249 | 94 | Fibronectin type-III 2 | ||||||
| Domain | 1250 – 1357 | 108 | CBM20 | ||||||
Sites | |||||||||
| Active site | 628 | 1 | Nucleophile By similarity | ||||||
| Active site | 657 | 1 | Proton donor By similarity | ||||||
| Active site | 734 | 1 | By similarity | ||||||
| Metal binding | 398 | 1 | Calcium By similarity | ||||||
| Metal binding | 400 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 403 | 1 | Calcium By similarity | ||||||
| Metal binding | 404 | 1 | Calcium By similarity | ||||||
| Metal binding | 449 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 451 | 1 | Calcium By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 628 | 1 | D → N or E: Loss of function. Ref.2 | ||||||
| Mutagenesis | 657 | 1 | E → Q or D: Loss of function. Ref.2 | ||||||
| Mutagenesis | 734 | 1 | D → Q or E: Loss of function. Ref.2 | ||||||
| Sequence conflict | 185 | 1 | G → R Ref.1 | ||||||
| Sequence conflict | 185 | 1 | G → R in AAA23201. Ref.2 | ||||||
| Sequence conflict | 264 – 265 | 2 | SP → FA Ref.1 | ||||||
| Sequence conflict | 264 – 265 | 2 | SP → FA in AAA23201. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum." Mathupala S.P., Saha B.C., Zeikus J.G. Biochem. Biophys. Res. Commun. 166:126-132(1990) [PubMed: 2302196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis." Mathupala S.P., Lowe S.E., Podkovyrov S.M., Zeikus J.G. J. Biol. Chem. 268:16332-16344(1993) [PubMed: 8344920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 625-630, MUTAGENESIS OF ASP-628; GLU-657 AND ASP-734. |
| [3] | "Complete sequence of Thermoanaerobacter pseudethanolicus 39E." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.  Richardson P.Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| M97665 Genomic DNA. Translation: AAA23201.1. CP000924 Genomic DNA. Translation: ABY95795.1. Frameshift. | |
| PIR | S28669. |
| RefSeq | YP_001666131.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JI1 based on UniProtKB Q60053. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM20. Carbohydrate-Binding Module Family 20. CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13. |
Genome annotation databases | |
| GeneID | 5873743. |
| GenomeReviews | Gene locus Teth39_2173 in contig CP000924_GR. |
| KEGG | tpd:Teth39_2173. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | P38939. GAPTIYY. |
Family and domain databases | |
| InterPro | IPR006048. A-amylase_b_C. IPR008957. Fibronectin_typ-III-like_fold. IPR003961. FN_III. IPR006047. Glyco_hydro_13_cat. IPR004185. Glyco_hydro_13_lg-like. IPR006589. Glyco_hydro_13_sub_cat. IPR002044. Glyco_hydro_carb-bd. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [Graphical view] |
| Gene3D | G3DSA:2.60.40.30. FN_III-like. 2 hits. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. |
| Pfam | PF00128. Alpha-amylase. 1 hit. PF02903. Alpha-amylase_N. 1 hit. PF00686. CBM_20. 1 hit. PF00041. fn3. 2 hits. [Graphical view] |
| SMART | SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. SM00060. FN3. 2 hits. [Graphical view] |
| PROSITE | PS51166. CBM20. 1 hit. PS50853. FN3. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | APU_THEP3 | ||||||||
| Accession | Primary (citable) accession number: P38939 Secondary accession number(s): B0K7X5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
