{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"C0HLM5","uniProtkbId":"CARP_MUCTH","entryAudit":{"firstPublicDate":"2020-10-07","lastAnnotationUpdateDate":"2020-12-02","lastSequenceUpdateDate":"2020-10-07","entryVersion":2,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Mucor thermohyalospora","commonName":"Soil fungus","taxonId":2653441,"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31219401"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mucoromycota","Mucoromycotina","Mucoromycetes","Mucorales","Mucorineae","Mucoraceae","Mucor"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Mucorpepsin"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31219401"}],"value":"3.4.23.23"}]},"flag":"Fragment"},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.","ecNumber":"3.4.23.23","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31219401"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31219401"}],"value":"Optimum pH is 6 with hemoglobin as substrate. Activity decreases from pH 7, with a 36% decrease in activity when incubated at pH 10."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31219401"}],"value":"Optimum temperature is between 45-55 degrees Celsius with hemoglobin as substrate. Loses 50% of its activity at 65 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31219401"}],"value":"This enzyme is capable of clotting milk and thus can be used for cheese production"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase A1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"OUTSIDE"},"end":{"value":10,"modifier":"OUTSIDE"}},"description":"Mucorpepsin","featureId":"PRO_0000451150"},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31219401"}]},{"type":"Non-terminal residue","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31219401"}]}],"keywords":[{"id":"KW-0064","category":"Molecular function","name":"Aspartyl protease"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0645","category":"Molecular function","name":"Protease"}],"references":[{"referenceNumber":1,"citation":{"id":"31219401","citationType":"journal article","authors":["Chinmayee C.V.","Vidya C.","Rani A.","Singh S.A."],"citationCrossReferences":[{"database":"PubMed","id":"31219401"},{"database":"DOI","id":"10.1080/10826068.2019.1630647"}],"title":"Production of highly active fungal milk-clotting enzyme by solid-state fermentation.","publicationDate":"2019","journal":"Prep. Biochem. Biotechnol.","firstPage":"858","lastPage":"867","volume":"49"},"referencePositions":["PROTEIN SEQUENCE","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","BIOTECHNOLOGY"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"GO","id":"GO:0004190","properties":[{"key":"GoTerm","value":"F:aspartic-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22135901"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22135901"}]}],"sequence":{"value":"AEGDGSVDTP","length":10,"molWeight":947,"crc64":"3930AFB2D5B87AA8","md5":"61D16825625FE152E738B87B4EA19C47"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":2},"uniParcId":"UPI0015EE390D"}}]}