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test.xml
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<?xml version="1.0" encoding="UTF-8" standalone="no" ?>
<uniprot xmlns="http://uniprot.org/uniprot" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://uniprot.org/uniprot http://www.uniprot.org/docs/uniprot.xsd">
<entry dataset="Swiss-Prot" created="2019-01-16" modified="2025-02-05" version="56" xmlns="http://uniprot.org/uniprot">
<accession>E9P8D2</accession>
<name>MPR1_YEASX</name>
<protein>
<recommendedName>
<fullName>N-acetyltransferase MPR1</fullName>
<ecNumber>2.3.1.271</ecNumber>
</recommendedName>
<alternativeName>
<fullName>(S)-1-pyrroline-5-carboxylate acetyltransferase</fullName>
</alternativeName>
<alternativeName>
<fullName>L-azetidine-2-carboxylate acetyltransferase</fullName>
<shortName>AZC acetyltransferase</shortName>
</alternativeName>
<alternativeName>
<fullName>Sigma1278b gene for proline-analog resistance 1</fullName>
</alternativeName>
</protein>
<gene>
<name evidence="9" type="primary">MPR1</name>
</gene>
<organism>
<name type="scientific">Saccharomyces cerevisiae</name>
<name type="common">Baker's yeast</name>
<dbReference type="NCBI Taxonomy" id="4932"/>
<lineage>
<taxon>Eukaryota</taxon>
<taxon>Fungi</taxon>
<taxon>Dikarya</taxon>
<taxon>Ascomycota</taxon>
<taxon>Saccharomycotina</taxon>
<taxon>Saccharomycetes</taxon>
<taxon>Saccharomycetales</taxon>
<taxon>Saccharomycetaceae</taxon>
<taxon>Saccharomyces</taxon>
</lineage>
</organism>
<reference key="1">
<citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="4249" last="4256">
<title>Saccharomyces cerevisiae sigma 1278b has novel genes of the N-acetyltransferase gene superfamily required for L-proline analogue resistance.</title>
<authorList>
<person name="Takagi H."/>
<person name="Shichiri M."/>
<person name="Takemura M."/>
<person name="Mohri M."/>
<person name="Nakamori S."/>
</authorList>
<dbReference type="PubMed" id="10894734"/>
<dbReference type="DOI" id="10.1128/jb.182.15.4249-4256.2000"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
<scope>VARIANT GLU-85</scope>
<source>
<strain>Sigma 1278B</strain>
</source>
</reference>
<reference key="2">
<citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="41998" last="42002">
<title>A novel acetyltransferase found in Saccharomyces cerevisiae Sigma1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid.</title>
<authorList>
<person name="Shichiri M."/>
<person name="Hoshikawa C."/>
<person name="Nakamori S."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="11555637"/>
<dbReference type="DOI" id="10.1074/jbc.c100487200"/>
</citation>
<scope>FUNCTION</scope>
<scope>SUBCELLULAR LOCATION</scope>
<scope>MUTAGENESIS OF ARG-145; GLY-146; GLN-147; LYS-148; VAL-149 AND GLY-150</scope>
</reference>
<reference key="3">
<citation type="journal article" date="2003" name="J. Biochem." volume="133" first="67" last="74">
<title>Characterization of novel acetyltransferases found in budding and fission yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid.</title>
<authorList>
<person name="Nomura M."/>
<person name="Nakamori S."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="12761200"/>
<dbReference type="DOI" id="10.1093/jb/mvg003"/>
</citation>
<scope>FUNCTION</scope>
<scope>SUBUNIT</scope>
<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
</reference>
<reference key="4">
<citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="12616" last="12621">
<title>Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate.</title>
<authorList>
<person name="Nomura M."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="15308773"/>
<dbReference type="DOI" id="10.1073/pnas.0403349101"/>
</citation>
<scope>FUNCTION</scope>
<scope>CATALYTIC ACTIVITY</scope>
<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
</reference>
<reference key="5">
<citation type="journal article" date="2010" name="FEMS Yeast Res." volume="10" first="687" last="698">
<title>An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1: oxidative stress-induced arginine synthesis and its physiological role.</title>
<authorList>
<person name="Nishimura A."/>
<person name="Kotani T."/>
<person name="Sasano Y."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="20550582"/>
<dbReference type="DOI" id="10.1111/j.1567-1364.2010.00650.x"/>
</citation>
<scope>FUNCTION</scope>
</reference>
<reference key="6">
<citation type="journal article" date="2012" name="FEBS Lett." volume="586" first="2411" last="2416">
<title>The proline metabolism intermediate Delta1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast.</title>
<authorList>
<person name="Nishimura A."/>
<person name="Nasuno R."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="22698729"/>
<dbReference type="DOI" id="10.1016/j.febslet.2012.05.056"/>
</citation>
<scope>FUNCTION</scope>
</reference>
<reference evidence="12 13 14" key="7">
<citation type="journal article" date="2013" name="Proc. Natl. Acad. Sci. U.S.A." volume="110" first="11821" last="11826">
<title>Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism.</title>
<authorList>
<person name="Nasuno R."/>
<person name="Hirano Y."/>
<person name="Itoh T."/>
<person name="Hakoshima T."/>
<person name="Hibi T."/>
<person name="Takagi H."/>
</authorList>
<dbReference type="PubMed" id="23818613"/>
<dbReference type="DOI" id="10.1073/pnas.1300558110"/>
</citation>
<scope>X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND SUBSTRATE</scope>
<scope>SUBUNIT</scope>
<scope>MUTAGENESIS OF ASN-135 AND ASN-178</scope>
</reference>
<comment type="function">
<text evidence="3 4 5 6 7">N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been shown to increase the levels of reactive oxygen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress (PubMed:15308773, PubMed:20550582, PubMed:22698729). Also acetylates and thereby detoxifies the proline analog azetidine-2-carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family (PubMed:11555637). Does not acetylate proline (PubMed:11555637, PubMed:12761200).</text>
</comment>
<comment type="catalytic activity">
<reaction evidence="5">
<text>L-glutamate 5-semialdehyde + acetyl-CoA = N-acetyl-L-glutamate 5-semialdehyde + CoA + H(+)</text>
<dbReference type="Rhea" id="RHEA:48232"/>
<dbReference type="ChEBI" id="CHEBI:15378"/>
<dbReference type="ChEBI" id="CHEBI:29123"/>
<dbReference type="ChEBI" id="CHEBI:57287"/>
<dbReference type="ChEBI" id="CHEBI:57288"/>
<dbReference type="ChEBI" id="CHEBI:58066"/>
<dbReference type="EC" id="2.3.1.271"/>
</reaction>
</comment>
<comment type="biophysicochemical properties">
<kinetics>
<KM evidence="8">20.9 mM for azetidine-2-carboxylate</KM>
<KM evidence="5">0.9 mM for azetidine-2-carboxylate</KM>
<KM evidence="5">7.019 mM for (S)-1-pyrroline-5-carboxylate</KM>
<KM evidence="8">4.3 mM for acetyl-CoA</KM>
<text evidence="5">kcat is 17.9 sec(-1) with azetidine-2-carboxylate as substrate and 121 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate.</text>
</kinetics>
<phDependence>
<text evidence="4 5">Optimum pH is 8.5-9 for azetidine-2-carboxylate and 6.5-7 for (S)-1-pyrroline-5-carboxylate.</text>
</phDependence>
<temperatureDependence>
<text evidence="4">Optimum temperature is 35 degrees Celsius.</text>
</temperatureDependence>
</comment>
<comment type="subunit">
<text evidence="4 8">Homodimer.</text>
</comment>
<comment type="subcellular location">
<subcellularLocation>
<location evidence="3 6">Cytoplasm</location>
</subcellularLocation>
<subcellularLocation>
<location evidence="6">Mitochondrion</location>
</subcellularLocation>
</comment>
<comment type="PTM">
<text evidence="3">Not glycosylated.</text>
</comment>
<comment type="similarity">
<text evidence="10">Belongs to the acetyltransferase family.</text>
</comment>
<dbReference type="EC" id="2.3.1.271"/>
<dbReference type="EMBL" id="AB031349">
<property type="protein sequence ID" value="BAA95611.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="PDB" id="3W6S">
<property type="method" value="X-ray"/>
<property type="resolution" value="1.90 A"/>
<property type="chains" value="A/B/C=1-229"/>
</dbReference>
<dbReference type="PDB" id="3W6X">
<property type="method" value="X-ray"/>
<property type="resolution" value="2.30 A"/>
<property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L=1-229"/>
</dbReference>
<dbReference type="PDB" id="3W91">
<property type="method" value="X-ray"/>
<property type="resolution" value="2.10 A"/>
<property type="chains" value="A/B/C=1-229"/>
</dbReference>
<dbReference type="PDBsum" id="3W6S"/>
<dbReference type="PDBsum" id="3W6X"/>
<dbReference type="PDBsum" id="3W91"/>
<dbReference type="AlphaFoldDB" id="E9P8D2"/>
<dbReference type="SMR" id="E9P8D2"/>
<dbReference type="KEGG" id="ag:BAA95611"/>
<dbReference type="SGD" id="S000029666">
<property type="gene designation" value="MPR1"/>
</dbReference>
<dbReference type="VEuPathDB" id="FungiDB:YJL127C"/>
<dbReference type="BioCyc" id="MetaCyc:MONOMER-20450"/>
<dbReference type="BRENDA" id="2.3.1.271">
<property type="organism ID" value="984"/>
</dbReference>
<dbReference type="EvolutionaryTrace" id="E9P8D2"/>
<dbReference type="GO" id="GO:0005829">
<property type="term" value="C:cytosol"/>
<property type="evidence" value="ECO:0000314"/>
<property type="project" value="SGD"/>
</dbReference>
<dbReference type="GO" id="GO:0005739">
<property type="term" value="C:mitochondrion"/>
<property type="evidence" value="ECO:0000314"/>
<property type="project" value="SGD"/>
</dbReference>
<dbReference type="GO" id="GO:0005634">
<property type="term" value="C:nucleus"/>
<property type="evidence" value="ECO:0007669"/>
<property type="project" value="TreeGrafter"/>
</dbReference>
<dbReference type="GO" id="GO:0046941">
<property type="term" value="F:azetidine-2-carboxylic acid acetyltransferase activity"/>
<property type="evidence" value="ECO:0000314"/>
<property type="project" value="SGD"/>
</dbReference>
<dbReference type="GO" id="GO:0006526">
<property type="term" value="P:L-arginine biosynthetic process"/>
<property type="evidence" value="ECO:0000316"/>
<property type="project" value="SGD"/>
</dbReference>
<dbReference type="GO" id="GO:0006562">
<property type="term" value="P:proline catabolic process"/>
<property type="evidence" value="ECO:0000316"/>
<property type="project" value="SGD"/>
</dbReference>
<dbReference type="Gene3D" id="3.40.630.30">
<property type="match status" value="1"/>
</dbReference>
<dbReference type="InterPro" id="IPR016181">
<property type="entry name" value="Acyl_CoA_acyltransferase"/>
</dbReference>
<dbReference type="InterPro" id="IPR000182">
<property type="entry name" value="GNAT_dom"/>
</dbReference>
<dbReference type="InterPro" id="IPR052742">
<property type="entry name" value="Mito_N-acetyltransferase"/>
</dbReference>
<dbReference type="PANTHER" id="PTHR43138">
<property type="entry name" value="ACETYLTRANSFERASE, GNAT FAMILY"/>
<property type="match status" value="1"/>
</dbReference>
<dbReference type="PANTHER" id="PTHR43138:SF1">
<property type="entry name" value="N-ACETYLTRANSFERASE ACA1"/>
<property type="match status" value="1"/>
</dbReference>
<dbReference type="Pfam" id="PF00583">
<property type="entry name" value="Acetyltransf_1"/>
<property type="match status" value="1"/>
</dbReference>
<dbReference type="SUPFAM" id="SSF55729">
<property type="entry name" value="Acyl-CoA N-acyltransferases (Nat)"/>
<property type="match status" value="1"/>
</dbReference>
<proteinExistence type="evidence at protein level"/>
<keyword id="KW-0002">3D-structure</keyword>
<keyword id="KW-0012">Acyltransferase</keyword>
<keyword id="KW-0963">Cytoplasm</keyword>
<keyword id="KW-0496">Mitochondrion</keyword>
<keyword id="KW-0808">Transferase</keyword>
<feature type="chain" id="PRO_0000446015" description="N-acetyltransferase MPR1">
<location>
<begin position="1"/>
<end position="229"/>
</location>
</feature>
<feature type="domain" description="N-acetyltransferase" evidence="1">
<location>
<begin position="65"/>
<end position="219"/>
</location>
</feature>
<feature type="binding site" evidence="8 13">
<location>
<position position="135"/>
</location>
<ligand>
<name>substrate</name>
</ligand>
</feature>
<feature type="binding site" evidence="11">
<location>
<begin position="145"/>
<end position="150"/>
</location>
<ligand>
<name>CoA</name>
<dbReference type="ChEBI" id="CHEBI:57287"/>
</ligand>
</feature>
<feature type="binding site" evidence="8 13">
<location>
<begin position="172"/>
<end position="173"/>
</location>
<ligand>
<name>substrate</name>
</ligand>
</feature>
<feature type="sequence variant" description="Deletion">
<location>
<begin position="4"/>
<end position="5"/>
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<position position="85"/>
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<position position="135"/>
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<original>G</original>
<variation>A</variation>
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<feature type="mutagenesis site" description="No effect." evidence="3">
<original>Q</original>
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</feature>
<feature type="mutagenesis site" description="No effect." evidence="3">
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<variation>A</variation>
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<position position="150"/>
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<original>N</original>
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<location>
<begin position="7"/>
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<feature type="helix" evidence="15">
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<location>
<begin position="24"/>
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<feature type="strand" evidence="15">
<location>
<begin position="31"/>
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<feature type="strand" evidence="15">
<location>
<begin position="41"/>
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</feature>
<feature type="helix" evidence="15">
<location>
<begin position="50"/>
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</feature>
<feature type="helix" evidence="15">
<location>
<begin position="55"/>
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<feature type="strand" evidence="15">
<location>
<begin position="73"/>
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<location>
<begin position="83"/>
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<location>
<begin position="92"/>
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<feature type="helix" evidence="15">
<location>
<begin position="112"/>
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<location>
<begin position="116"/>
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<feature type="helix" evidence="15">
<location>
<begin position="128"/>
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<feature type="strand" evidence="15">
<location>
<begin position="133"/>
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<feature type="helix" evidence="15">
<location>
<begin position="142"/>
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<feature type="helix" evidence="15">
<location>
<begin position="149"/>
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</feature>
<feature type="helix" evidence="15">
<location>
<begin position="162"/>
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</feature>
<feature type="strand" evidence="15">
<location>
<begin position="168"/>
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<feature type="helix" evidence="15">
<location>
<begin position="180"/>
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<location>
<begin position="184"/>
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<location>
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<feature type="strand" evidence="15">
<location>
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<scope>VARIANT TRP-1036</scope>
<source>
<tissue>Brain</tissue>
<tissue>Lung</tissue>
<tissue>Pancreas</tissue>
<tissue>Urinary bladder</tissue>
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<scope>METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1107</scope>