{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A2I1D2N1","uniProtkbId":"UNGD_ASPC2","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-02-28","entryVersion":23,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Aspergillus campestris (strain IBT 28561)","taxonId":1392248,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Circumdati"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36715406"}],"value":"Unguisins hydrolase ungD'"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"36715406"}],"value":"3.4.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36715406"}],"value":"Unguisins biosynthesis cluster protein D'"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36715406"}],"value":"ungD'"},"orfNames":[{"value":"P168DRAFT_297054"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36715406"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"36715406"}],"value":"Hydrolase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin I (PubMed:36715406). Within the pathway, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of the nonribosomal peptide synthetase (NRPS) ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"36715406"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase S12 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"Unguisins hydrolase ungD'","featureId":"PRO_0000458913"}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1F4QM13VP0TC3","citationType":"submission","authoringGroup":["DOE Joint Genome Institute"],"authors":["Vesth T.C.","Nybo J.","Theobald S.","Brandl J.","Frisvad J.C.","Nielsen K.F.","Lyhne E.K.","Kogle M.E.","Kuo A.","Riley R.","Clum A.","Nolan M.","Lipzen A.","Salamov A.","Henrissat B.","Wiebenga A.","De Vries R.P.","Grigoriev I.V.","Mortensen U.H.","Andersen M.R.","Baker S.E."],"title":"The genomes of Aspergillus section Nigri reveals drivers in fungal speciation.","publicationDate":"DEC-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"IBT 28561","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"36715406","citationType":"journal article","authors":["Wei X.","Chan T.K.","Kong C.T.D.","Matsuda Y."],"citationCrossReferences":[{"database":"PubMed","id":"36715406"},{"database":"DOI","id":"10.1021/acs.jnatprod.2c01065"}],"title":"Biosynthetic characterization, heterologous production, and genomics-guided discovery of GABA-containing fungal heptapeptides.","publicationDate":"2023","journal":"J. Nat. Prod.","firstPage":"416","lastPage":"422","volume":"86"},"referencePositions":["FUNCTION","PATHWAY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MSFM01000006","properties":[{"key":"ProteinId","value":"PKY04127.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2I1D2N1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A2I1D2N1","properties":[{"key":"Description","value":"-"}]},{"database":"VEuPathDB","id":"FungiDB:P168DRAFT_297054","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"5946976at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000234254","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"Gene3D","id":"3.40.710.10","properties":[{"key":"EntryName","value":"DD-peptidase/beta-lactamase superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050491","properties":[{"key":"EntryName","value":"AmpC-like"}]},{"database":"InterPro","id":"IPR001466","properties":[{"key":"EntryName","value":"Beta-lactam-related"}]},{"database":"InterPro","id":"IPR012338","properties":[{"key":"EntryName","value":"Beta-lactam/transpept-like"}]},{"database":"InterPro","id":"IPR021860","properties":[{"key":"EntryName","value":"Peptidase_S12_Pab87-rel_C"}]},{"database":"PANTHER","id":"PTHR46825:SF9","properties":[{"key":"EntryName","value":"BETA-LACTAMASE-RELATED DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46825","properties":[{"key":"EntryName","value":"D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00144","properties":[{"key":"EntryName","value":"Beta-lactamase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11954","properties":[{"key":"EntryName","value":"DUF3471"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56601","properties":[{"key":"EntryName","value":"beta-lactamase/transpeptidase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MISKTEDSGDPLDQDFAEVVKQTLDRWHIPGMSVAVVDGPDTWTKGYGLAQLPNTNVTPDTLFYTGSTTKAFTAAVLSLLVDDNKNYPQVQWNTPVNQLLRDDFVLSHEWDTNNITIEDILSHRTGMPRHEFAFGGDYDGHPASLRDIVRSVRYMQRSAPPRTTYQYSNLMFIVASYLIETLTGKWIGDVFREKIWRPLGMDSTYLSLEDARASGKELAQGYLYNSSLPGYEPVPLKNKPEVSGAGAAISNIKDYAKWATALLKRAPDVLSPAGYSAIWSARTVTPTHDPFITPSAYALAWNTQVYQGVEIVWHDGGIDGFGTEIALIPSLGFAVVTQANTTYSSNYAGTALVYHLIDKKLDVAPDKRFDWNKWYEDLERQMKEAVKNARQTFYPTVPSPAPPPTLPIGKYTGNYWHPAYRQLTILWDEERNLLYADRKDSTTPCQLTFIPVSREFFLVRLTVVGAEAMLPAEFRLGPDGTPSMVGILWEPSLGDEKIWLKKEGDTHFKEMYGGIVDSTAGKKRVPDTIHPIDL","length":534,"molWeight":59848,"crc64":"B8DD49F268A8B2D3","md5":"4EDAE60CCCB81B102CC6D7B46C6BDF5C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI000CB4F191"}}