UniProtKB - V5YM14 (DAPB2_PSEMX)
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>sp|V5YM14|DAPB2_PSEMX Dipeptidyl aminopeptidase BII OS=Pseudoxanthomonas mexicana OX=128785 GN=dapb2 PE=1 SV=1 MRPNLLAAAIAVPLSLLAAQIAQAGEGMWVPQQLPEIAGPLKKAGLKLSPQQISDLTGDP MGAVVALGGCTASFVSPNGLVVTNHHCAYGAIQLNSTAENNLIKNGFNAPTTADEVSAGP NARVFVLDEITDVTKDAKAAIAAAGDDALARTKALEAFEKKLIADCEAEAGFRCRLYSFS GGNTYRLFKNLEIKDVRLAYAPPGSVGKFGGDIDNWMWPRHTGDFAFYRAYVGKDGKPAA FSKDNVPYQPKHWLKFADQPLGAGDFVMVAGYPGSTNRYALAAEFDNTAQWTYPTIARHY KNQIAMVEAAGKQNADIQVKYAATMAGWNNTSKNYDGQLEGFKRIDAAGQKLREEAAVLG WLKGQGAKGQPALDAHAKLLDLLEQSKATRDRDLTLALFNNTAMLGSATQLYRLSIEREK PNAERESGYQERDLPAIEGGLKQLERRYVAAMDRQLQEYWLNEYIKLPADQRVAAVDAWL GGNDAAAVKRALDRLAGTKLGSTEERLKWFAADRKAFEASNDPAIQYAVAVMPTLLKLEQ ERKTRAGENLAARPVYLQALADYKKSQGEFVYPDANLSLRITFGNVMGYAPKDGMEYTPF TTLEGVVAKETGQDPFDSPKALLDAVAAKRYGGLEDKRIGSVPVNYLSDLDITGGNSGSP VLDAHGKLVGLAFDGNWESVSSNWVFDPKMTRMIAVDGRYLRWIMQEVYPAPQLLKEMNV GKCommunity curation ()Add a publicationFeedback
Dipeptidyl aminopeptidase BII
dapb2
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:8892831, PubMed:24827749).
Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749).
Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831).
May play a physiological role in feeding (PubMed:24598890).
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=1.7 mM for Gly-Phe-pNA (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- KM=0.87 mM for Ala-Ala-pNA (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- KM=7.2 mM for Gly-Phe-beta-naphthylamine (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- Vmax=3.4 µmol/min/mg enzyme with Gly-Phe-pNA as substrate2 Publications
Manual assertion based on experiment ini
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.3"Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Acta Crystallogr. F 70:221-224(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=10 µmol/min/mg enzyme with Ala-Ala-pNA as substrate2 Publications
Manual assertion based on experiment ini
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.3"Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Acta Crystallogr. F 70:221-224(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=9.4 µmol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- Vmax=20 µmol/min/mg enzyme with Ala-Ala-pNA as substrate (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- Vmax=10 µmol/min/mg enzyme with Gly-Phe-beta-naphthylamine as substrate (at pH 8 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
pH dependencei
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
Temperature dependencei
Manual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 86 | Charge relay system2 Publications <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
Active sitei | 224 | Charge relay system2 Publications Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 330 | Substrate1 Publication Manual assertion based on experiment ini
| 1 | |
Active sitei | 657 | Charge relay system2 Publications Manual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- dipeptidyl-peptidase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.3"Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Acta Crystallogr. F 70:221-224(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- identical protein binding Source: UniProtKBInferred from direct assayi
- Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- protein homodimerization activity Source: UniProtKBInferred from direct assayi
- Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- serine-type aminopeptidase activity Source: UniProtKBInferred from direct assayi
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.3"Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Acta Crystallogr. F 70:221-224(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
GO - Biological processi
- proteolysis involved in cellular protein catabolic process Source: UniProtKBInferred from direct assayi
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.3"Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Acta Crystallogr. F 70:221-224(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Aminopeptidase, Hydrolase, Protease |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.11.6, 14090 |
Protein family/group databases
MEROPS protease database More...MEROPSi | S46.003 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Dipeptidyl aminopeptidase BIIImported<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi (EC:3.4.14.-
Manual assertion based on experiment ini
Short name: DAP BII2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:dapb2Imported Manual assertion inferred from database entriesi |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Pseudoxanthomonas mexicana |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 128785 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Pseudoxanthomonas |
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei
Manual assertion based on opinion ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 86 | H → A: Loss of enzymatic activity. Loss of enzymatic activity; when associated with A-224 and A-657. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 195 | D → A: Decreased enzymatic activity to 23 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 214 | D → A: Decreased enzymatic activity to 1.5 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 214 | D → N: Decreased enzymatic activity to 3.0 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 215 | N → A: Loss of enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 216 | W → A: Loss of enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 224 | D → A: Decreased enzymatic activity to 0.026 percent relative to wild-type. Loss of enzymatic activity; when associated with A-86 and A-657. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 224 | D → N: Decreased enzymatic activity to 0.15 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 330 | N → A: Loss of enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 522 | D → A: Decreased enzymatic activity to 32 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 522 | D → N: Decreased enzymatic activity to 16 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 574 | D → A: Decreased enzymatic activity to 83 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 574 | D → N: Decreased enzymatic activity to 21 percent relative to wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 657 | S → A: Loss of enzymatic activity. Loss of enzymatic activity; when associated with A-86 and A-224. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 674 | D → A: Loss of enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 675 | G → R: Acquires the enzymatic activity for synthetic substrates with Asp/Glu at P1 position. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 24 | 1 Publication Manual assertion based on experiment ini
| 24 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000433463 | 25 – 722 | Dipeptidyl aminopeptidase BIISequence analysisAdd BLAST | 698 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 70 ↔ 87 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
Disulfide bondi | 166 ↔ 174 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
|
Keywords - PTMi
Disulfide bondProteomic databases
PRoteomics IDEntifications database More...PRIDEi | V5YM14 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
2 PublicationsManual assertion based on experiment ini
- Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
GO - Molecular functioni
- identical protein binding Source: UniProtKBInferred from direct assayi
- Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
- protein homodimerization activity Source: UniProtKBInferred from direct assayi
- Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674. - Ref.2"Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24."
Ogasawara W., Kobayashi G., Okada H., Morikawa Y.
J. Bacteriol. 178:6288-6295(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 31 – 33 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 34 – 44 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 50 – 54 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 61 – 63 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 64 – 66 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 68 – 74 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 80 – 83 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 85 – 94 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 98 – 100 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 102 – 105 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 112 – 114 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 124 – 132 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 134 – 142 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 143 – 146 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 148 – 166 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
Beta strandi | 172 – 179 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 180 – 183 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 184 – 193 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 195 – 201 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 204 – 207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 208 – 210 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 211 – 214 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 226 – 232 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 266 – 271 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 282 – 290 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 292 – 313 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 22 | |
Helixi | 315 – 320 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 322 – 345 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 24 | |
Helixi | 347 – 363 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
Helixi | 364 – 369 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 370 – 387 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
Helixi | 390 – 399 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 403 – 417 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
Helixi | 422 – 424 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 431 – 433 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 434 – 443 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 444 – 446 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 450 – 465 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
Helixi | 469 – 471 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 474 – 480 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 482 – 484 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 485 – 496 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 503 – 511 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 514 – 518 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 523 – 566 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 44 | |
Beta strandi | 580 – 586 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 595 – 597 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 599 – 602 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 603 – 608 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 620 – 627 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 637 – 639 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 643 – 648 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 660 – 662 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 668 – 675 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 677 – 683 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 688 – 690 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 693 – 697 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 698 – 707 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 712 – 717 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | V5YM14 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 215 – 216 | Substrate-binding1 Publication Manual assertion based on experiment ini
| 2 | |
Regioni | 655 – 657 | Substrate-binding1 Publication Manual assertion based on experiment ini
| 3 | |
Regioni | 673 – 674 | Substrate-binding1 Publication Manual assertion based on experiment ini
| 2 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Manual assertion based on experiment ini
- Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Manual assertion inferred by curator fromi
- Ref.1"Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases."
Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.
Sci. Rep. 4:4292-4292(2014) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333; 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522; ASP-574 AND SER-657. - Ref.4"S46 peptidases are the first exopeptidases to be members of clan PA."
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M., Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.
Sci. Rep. 4:4977-4977(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY, PHYLOGENETIC STUDY, ACTIVE SITES, MUTAGENESIS OF HIS-86; ASN-215; TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
Keywords - Domaini
SignalFamily and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR019500, Pep_S46 IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin |
The PANTHER Classification System More...PANTHERi | PTHR38469, PTHR38469, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF10459, Peptidase_S46, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50494, SSF50494, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MRPNLLAAAI AVPLSLLAAQ IAQAGEGMWV PQQLPEIAGP LKKAGLKLSP
60 70 80 90 100
QQISDLTGDP MGAVVALGGC TASFVSPNGL VVTNHHCAYG AIQLNSTAEN
110 120 130 140 150
NLIKNGFNAP TTADEVSAGP NARVFVLDEI TDVTKDAKAA IAAAGDDALA
160 170 180 190 200
RTKALEAFEK KLIADCEAEA GFRCRLYSFS GGNTYRLFKN LEIKDVRLAY
210 220 230 240 250
APPGSVGKFG GDIDNWMWPR HTGDFAFYRA YVGKDGKPAA FSKDNVPYQP
260 270 280 290 300
KHWLKFADQP LGAGDFVMVA GYPGSTNRYA LAAEFDNTAQ WTYPTIARHY
310 320 330 340 350
KNQIAMVEAA GKQNADIQVK YAATMAGWNN TSKNYDGQLE GFKRIDAAGQ
360 370 380 390 400
KLREEAAVLG WLKGQGAKGQ PALDAHAKLL DLLEQSKATR DRDLTLALFN
410 420 430 440 450
NTAMLGSATQ LYRLSIEREK PNAERESGYQ ERDLPAIEGG LKQLERRYVA
460 470 480 490 500
AMDRQLQEYW LNEYIKLPAD QRVAAVDAWL GGNDAAAVKR ALDRLAGTKL
510 520 530 540 550
GSTEERLKWF AADRKAFEAS NDPAIQYAVA VMPTLLKLEQ ERKTRAGENL
560 570 580 590 600
AARPVYLQAL ADYKKSQGEF VYPDANLSLR ITFGNVMGYA PKDGMEYTPF
610 620 630 640 650
TTLEGVVAKE TGQDPFDSPK ALLDAVAAKR YGGLEDKRIG SVPVNYLSDL
660 670 680 690 700
DITGGNSGSP VLDAHGKLVG LAFDGNWESV SSNWVFDPKM TRMIAVDGRY
710 720
LRWIMQEVYP APQLLKEMNV GK
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AB889525 Genomic DNA Translation: BAO18427.1 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
V5YM14 | Dipeptidyl-peptidase | 722 | UniRef90_V5YM14 | |||
Dipeptidyl-peptidase | 722 | |||||
Peptidase S46 (Fragment) | 64 | |||||
Dipeptidyl-peptidase | 722 | |||||
Dipeptidyl-peptidase | 722 | |||||
+15 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
V5YM14 | Dipeptidyl-peptidase | 722 | UniRef50_V5YM14 | |||
Dipeptidyl-peptidase | 722 | |||||
Dipeptidyl-peptidase | 722 | |||||
Dipeptidyl-peptidase | 722 | |||||
Dipeptidyl-peptidase | 722 | |||||
+628 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB889525 Genomic DNA Translation: BAO18427.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3WOI | X-ray | 2.10 | A/B | 25-722 | [»] | |
3WOJ | X-ray | 2.20 | A/B | 25-722 | [»] | |
3WOK | X-ray | 1.95 | A/B | 25-722 | [»] | |
3WOL | X-ray | 1.74 | A/B | 25-722 | [»] | |
3WOM | X-ray | 1.86 | A/B | 25-722 | [»] | |
3WON | X-ray | 1.75 | A/B | 25-722 | [»] | |
3WOO | X-ray | 1.80 | A/B | 25-722 | [»] | |
3WOP | X-ray | 1.95 | A/B | 25-722 | [»] | |
3WOQ | X-ray | 1.82 | A/B | 25-722 | [»] | |
3WOR | X-ray | 2.10 | A/B | 25-722 | [»] | |
4Y06 | X-ray | 2.18 | A/B | 1-722 | [»] | |
SMRi | V5YM14 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | S46.003 |
Proteomic databases
PRIDEi | V5YM14 |
Enzyme and pathway databases
BRENDAi | 3.4.11.6, 14090 |
Family and domain databases
Gene3Di | 2.40.10.10, 1 hit |
InterProi | View protein in InterPro IPR019500, Pep_S46 IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin |
PANTHERi | PTHR38469, PTHR38469, 1 hit |
Pfami | View protein in Pfam PF10459, Peptidase_S46, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | DAPB2_PSEMX | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | V5YM14Primary (citable) accession number: V5YM14 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 24, 2015 |
Last sequence update: | February 19, 2014 | |
Last modified: | June 2, 2021 | |
This is version 27 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families