ID A0A0L8G5U4_OCTBM Unreviewed; 445 AA. AC A0A0L8G5U4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-MAR-2024, entry version 24. DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687}; GN ORFNames=OCBIM_22039473mg {ECO:0000313|EMBL:KOF72407.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF72407.1}; RN [1] {ECO:0000313|EMBL:KOF72407.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF72407.1}; RC TISSUE=Gonad {ECO:0000313|EMBL:KOF72407.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine; CC Xref=Rhea:RHEA:51312, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:58095, ChEBI:CHEBI:134022; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z- CC octadecenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51300, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58095, CC ChEBI:CHEBI:134020; Evidence={ECO:0000256|ARBA:ARBA00034630}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301; CC Evidence={ECO:0000256|ARBA:ARBA00034630}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302; CC Evidence={ECO:0000256|ARBA:ARBA00034630}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z- CC octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; CC Evidence={ECO:0000256|ARBA:ARBA00034640}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; CC Evidence={ECO:0000256|ARBA:ARBA00034640}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L- CC phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L- CC phenylalanine; Xref=Rhea:RHEA:64132, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58095, ChEBI:CHEBI:77016, ChEBI:CHEBI:149701; CC Evidence={ECO:0000256|ARBA:ARBA00034635}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133; CC Evidence={ECO:0000256|ARBA:ARBA00034635}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:59002; Evidence={ECO:0000256|ARBA:ARBA00034637}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; CC Evidence={ECO:0000256|ARBA:ARBA00034637}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110; CC Evidence={ECO:0000256|ARBA:ARBA00034637}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:149697; Evidence={ECO:0000256|ARBA:ARBA00034616}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; CC Evidence={ECO:0000256|ARBA:ARBA00034616}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118; CC Evidence={ECO:0000256|ARBA:ARBA00034616}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + CC L-asparagine; Xref=Rhea:RHEA:64136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58048, ChEBI:CHEBI:149730; CC Evidence={ECO:0000256|ARBA:ARBA00034627}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137; CC Evidence={ECO:0000256|ARBA:ARBA00034627}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + CC L-glutamine; Xref=Rhea:RHEA:51356, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58359, ChEBI:CHEBI:134033; CC Evidence={ECO:0000256|ARBA:ARBA00034643}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357; CC Evidence={ECO:0000256|ARBA:ARBA00034643}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L- CC leucine; Xref=Rhea:RHEA:51360, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:57427, ChEBI:CHEBI:134035; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L- CC lysine; Xref=Rhea:RHEA:64192, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:32551, ChEBI:CHEBI:149731; CC Evidence={ECO:0000256|ARBA:ARBA00034633}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193; CC Evidence={ECO:0000256|ARBA:ARBA00034633}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + CC L-methionine; Xref=Rhea:RHEA:64144, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57844, ChEBI:CHEBI:149732; CC Evidence={ECO:0000256|ARBA:ARBA00034645}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145; CC Evidence={ECO:0000256|ARBA:ARBA00034645}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L- CC serine; Xref=Rhea:RHEA:51352, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:33384, ChEBI:CHEBI:134031; CC Evidence={ECO:0000256|ARBA:ARBA00034646}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353; CC Evidence={ECO:0000256|ARBA:ARBA00034646}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + CC L-tryptophan; Xref=Rhea:RHEA:64176, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57912, ChEBI:CHEBI:149733; CC Evidence={ECO:0000256|ARBA:ARBA00034619}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177; CC Evidence={ECO:0000256|ARBA:ARBA00034619}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L- CC tyrosine; Xref=Rhea:RHEA:64184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:58315, ChEBI:CHEBI:149734; CC Evidence={ECO:0000256|ARBA:ARBA00034625}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185; CC Evidence={ECO:0000256|ARBA:ARBA00034625}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L- CC phenylalanine; Xref=Rhea:RHEA:64124, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:149699; CC Evidence={ECO:0000256|ARBA:ARBA00034620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125; CC Evidence={ECO:0000256|ARBA:ARBA00034620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + CC octadecanoate; Xref=Rhea:RHEA:64128, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:25629, ChEBI:CHEBI:58095, ChEBI:CHEBI:149700; CC Evidence={ECO:0000256|ARBA:ARBA00034641}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129; CC Evidence={ECO:0000256|ARBA:ARBA00034641}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha- CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824, CC ChEBI:CHEBI:138093; EC=3.5.1.114; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR036696-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036696- CC 2}; CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000256|ARBA:ARBA00034698}. CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC {ECO:0000256|ARBA:ARBA00004872}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. CC {ECO:0000256|ARBA:ARBA00006247}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KQ423675; KOF72407.1; -; Genomic_DNA. DR RefSeq; XP_014783801.1; XM_014928315.1. DR AlphaFoldDB; A0A0L8G5U4; -. DR EnsemblMetazoa; Ocbimv22039474m; Ocbimv22039474m.p; Ocbimv22039473m.g. DR EnsemblMetazoa; XM_014928315.1; XP_014783801.1; LOC106878941. DR GeneID; 106878941; -. DR OrthoDB; 3672990at2759; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.900; -; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR047177; Pept_M20A. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1. DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF036696; ACY-1; 2. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR036696-2}; Protease {ECO:0000256|ARBA:ARBA00022670}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}. FT DOMAIN 184..325 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" FT ACT_SITE 70 FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1" FT ACT_SITE 134 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" FT BINDING 406 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2" SQ SEQUENCE 445 AA; 50429 MW; 4FFBB77CBF93E6E0 CRC64; MYVSVCLSKY RQRITDFKKR LSLETIYEAY PTVHKSPFVK YEVVANYSML YTVEGSDKKL LPYLLTSHLD VVPVTEENWK FDPFAAKLYQ GYIYGRGTLD VKCSVIGIME ALEHALKSGF KPKRSFFIAF GHDEEVTGYD GAYHIAQTLE SRGVQLEYLL DEGLAIVKDF FKGLHPVAMI GVVEKGQAIV KLSVNGTAGH SAIPPPESVI GILSTAIRRI ESNPQPDLFG TGAERAMFEH LAPKLPFLPR MVLSNLWLFR PVVSWVLSRQ PQTNALIRTV NAVTKFNAGI KDNVLSDSAE AVIDYRIHPS QTLEQLFDFH LKIINDDRVK TTLKNYIAPS LISPYDDASF GYHTVKNSIR EVFLDVLVVP GVTVGNTDTH HYKHLTKSIY RFTPSVLTPE STNMIHGDNE KISIWNYEKV VNFYHHVILN SDRDKMNFIN KHVEL //