Detail Information for IndEnz0002001146
IED ID IndEnz0002001146
Enzyme Type ID protease001146
Protein Name N-fatty-acyl-amino acid synthase/hydrolase PM20D1.1
EC 3.5.1.114
EC 3.5.1.14
Peptidase M20 domain-containing protein 1.1
Gene Name pm20d1.1 zgc:123113
Organism Danio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio)
Enzyme Sequence MKTKFTKKTVLKFFGILFAILLLSVLILFSVVIGRTFTFKVNRELGQWENTSTIYPYLSPEQREKLLDNFKVAVQIPTVSFSESDQNITALQEFDLLLRRVFPKVFSSSLVRHEVVGNYSHLFTVVGADAGLEPYMLLAHIDVVPANEAGGWDAPPFSAQEIDGFIYGRGTIDNKQSVMGILQALEYLLERGYTPRRTFYIGLGHDEEINGEEGAVKIVNLLKSRGVKLLYVLDEGLTIMDGVVDGLNEPAALIGVSEKGQTTVKLSVSTPPGHSSMPPRESSIGILASAVARLEKNRMPNLFGHGPERATFEHLAHKFGWSYRMIMSNLWLFSSLLSSVLEGQPDTNAFVRTTTAVTMFNSGVKINVMPAHAEAFVNFRIHSSQTVQGVLNRIESTVSDKRVKVEFINGFDPLPIGSYEDDTFGYQIIKKSVQDIFPQVTVTPGICVANTDSRHYTQLSPDIYRFAPSWYKPGDSARFHGVNERISIQNYEEIVLFYFQLMQNSDVRNLPTLRS
Enzyme Length 515
Uniprot Accession Number Q32LT9
Absorption
Active Site ACT_SITE 142; /evidence=ECO:0000250|UniProtKB:Q6GTS8; ACT_SITE 207; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q6GTS8
Activity Regulation ACTIVITY REGULATION: Lipoproteins are powerful coactivators of PM20D1 activity in vitro and NAA biosynthesis in vivo. {ECO:0000250|UniProtKB:Q8C165}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824, ChEBI:CHEBI:138093; EC=3.5.1.114; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, ChEBI:CHEBI:59002; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-phenylalanine; Xref=Rhea:RHEA:64124, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:149699; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + octadecanoate; Xref=Rhea:RHEA:64128, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:58095, ChEBI:CHEBI:149700; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-phenylalanine; Xref=Rhea:RHEA:64132, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:77016, ChEBI:CHEBI:149701; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + L-asparagine; Xref=Rhea:RHEA:64136, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58048, ChEBI:CHEBI:149730; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-lysine; Xref=Rhea:RHEA:64192, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:32551, ChEBI:CHEBI:149731; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + L-methionine; Xref=Rhea:RHEA:64144, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57844, ChEBI:CHEBI:149732; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-serine; Xref=Rhea:RHEA:51352, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:33384, ChEBI:CHEBI:134031; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + L-tryptophan; Xref=Rhea:RHEA:64176, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57912, ChEBI:CHEBI:149733; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-tyrosine; Xref=Rhea:RHEA:64184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58315, ChEBI:CHEBI:149734; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + L-glutamine; Xref=Rhea:RHEA:51356, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58359, ChEBI:CHEBI:134033; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, ChEBI:CHEBI:149697; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51312, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:58095, ChEBI:CHEBI:134022; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-leucine; Xref=Rhea:RHEA:51360, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57427, ChEBI:CHEBI:134035; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362; Evidence={ECO:0000250|UniProtKB:Q8C165}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-octadecenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51300, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58095, ChEBI:CHEBI:134020; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301; Evidence={ECO:0000250|UniProtKB:Q8C165};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302; Evidence={ECO:0000250|UniProtKB:Q8C165};
DNA Binding
EC Number 3.5.1.114; 3.5.1.14
Enzyme Function FUNCTION: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction. Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles. {ECO:0000250|UniProtKB:Q8C165}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Amino-acid metabolism. {ECO:0000250|UniProtKB:Q8C165}.; PATHWAY: Energy metabolism; electron transfer. {ECO:0000250|UniProtKB:Q8C165}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q8C165}.
nucleotide Binding
Features Active site (2); Chain (1); Glycosylation (3); Metal binding (6); Signal peptide (1)
Keywords Glycoprotein;Hydrolase;Lyase;Metal-binding;Protease;Reference proteome;Secreted;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8C165}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..34; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 57,640
Kinetics
Metal Binding METAL 140; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q6GTS8; METAL 173; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q6GTS8; METAL 173; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q6GTS8; METAL 208; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q6GTS8; METAL 234; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q6GTS8; METAL 480; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q6GTS8
Rhea ID RHEA:15565; RHEA:15566; RHEA:15567; RHEA:54184; RHEA:54185; RHEA:54186; RHEA:64108; RHEA:64109; RHEA:64110; RHEA:64124; RHEA:64125; RHEA:64128; RHEA:64129; RHEA:64132; RHEA:64133; RHEA:64136; RHEA:64137; RHEA:51316; RHEA:51318; RHEA:64192; RHEA:64193; RHEA:64144; RHEA:64145; RHEA:51352; RHEA:51353; RHEA:64176; RHEA:64177; RHEA:64184; RHEA:64185; RHEA:51356; RHEA:51357; RHEA:64116; RHEA:64117; RHEA:64118; RHEA:51312; RHEA:51313; RHEA:51314; RHEA:51360; RHEA:51361; RHEA:51362; RHEA:51300; RHEA:51301; RHEA:51302
Cross Reference Brenda