ID G1MVZ3_MELGA Unreviewed; 470 AA.
AC G1MVZ3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Peptidase M20 domain containing 1 {ECO:0000313|Ensembl:ENSMGAP00000002865.3};
GN Name=PM20D1 {ECO:0000313|Ensembl:ENSMGAP00000002865.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000002865.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000002865.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000002865.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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}.
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DR AlphaFoldDB; G1MVZ3; -.
DR Ensembl; ENSMGAT00000003553.3; ENSMGAP00000002865.3; ENSMGAG00000003150.3.
DR GeneTree; ENSGT00940000156659; -.
DR InParanoid; G1MVZ3; -.
DR TreeFam; TF328688; -.
DR Proteomes; UP000001645; Chromosome 28.
DR Bgee; ENSMGAG00000003150; Expressed in liver and 17 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:Ensembl.
DR GO; GO:0043605; P:amide catabolic process; IEA:Ensembl.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
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 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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 206..349
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 470 AA; 52359 MW; 3E06CC84A3F08247 CRC64;
RRGGTAAFSI EERLEMKETL RGAVKIPTVS VSPEDLNATA MAEFGDYIQK VFPAVFSSKF
IQHEIVGEYS HLFTVQGSDS EMMPYMLLAH MDVVPAPLEG WDFPPFSAAE HEGFIYGRGT
LDNKNSAIGI LQALEFLLRR NYRPRRSFYV GIGHDEEVFG RKGAVKIAAL LESRGVKLSF
LLDEGSAILD GIIAGMKKPV ALIAVTEKGS ITLNFTVEKE PGHSSFPPKE TSIGILATAM
SRLEQNPMRN LFGHGPELMT MEHLASEFNF PLNLIMSNLW LFSPIVSRVL AWKPSTNALI
RTTTAVTMFN AGIKLNVIPS SARATVNFRI HSAEKAREVL ETVRNTIADD RVKIDVVEAF
DPLPISPWDD QTFGVHVFQR TILDTFPNVD SVVPGTCIGN TDSRHFTNVT DAIYRFNPVL
LKSDDLPRIH GLNERISVES YEKQVEFLFQ LIKNCDVDEL PEPHANSHEL
//
