PIMT_DROME
ID PIMT_DROME Reviewed; 226 AA.
AC Q27869; Q9VND1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000305|PubMed:14596598};
DE Short=PIMT;
DE EC=2.1.1.77 {ECO:0000269|PubMed:14596598};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl/D-aspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
DE AltName: Full=dPIMT;
GN Name=Pcmt; Synonyms=PIAM; ORFNames=CG2152;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9061928; DOI=10.1016/s0965-1748(96)00071-9;
RA O'Connor M.B., Galus A., Hartenstine M., Magee M., Jackson F.R.,
RA O'Connor C.M.;
RT "Structural organization and developmental expression of the protein
RT isoaspartyl methyltransferase gene from Drosophila melanogaster.";
RL Insect Biochem. Mol. Biol. 27:49-54(1997).
RN [2]
RP SEQUENCE REVISION TO 124.
RA O'Connor C.M.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-221, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF SER-60.
RX PubMed=14596598; DOI=10.1021/bi034891+;
RA Bennett E.J., Bjerregaard J., Knapp J.E., Chavous D.A., Friedman A.M.,
RA Royer W.E. Jr., O'Connor C.M.;
RT "Catalytic implications from the Drosophila protein L-isoaspartyl
RT methyltransferase structure and site-directed mutagenesis.";
RL Biochemistry 42:12844-12853(2003).
CC -!- FUNCTION: Initiates the repair of damaged proteins by catalyzing methyl
CC esterification of L-isoaspartyl and D-aspartyl residues produced by
CC spontaneous isomerization and racemization of L-aspartyl and L-
CC asparaginyl residues in aging peptides and proteins.
CC {ECO:0000269|PubMed:14596598, ECO:0000269|PubMed:9061928}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC ChEBI:CHEBI:90598; EC=2.1.1.77;
CC Evidence={ECO:0000269|PubMed:14596598};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000305|PubMed:14596598};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14596598}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P22061}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, lowest in larvae
CC and highest in adults. {ECO:0000269|PubMed:9061928}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR EMBL; U43737; AAA86272.2; -; Genomic_DNA.
DR EMBL; U37432; AAA80540.2; -; mRNA.
DR EMBL; AE014297; AAF52012.1; -; Genomic_DNA.
DR EMBL; AY070630; AAL48101.1; -; mRNA.
DR EMBL; AY075527; AAL68334.1; -; mRNA.
DR RefSeq; NP_536756.1; NM_080508.4.
DR PDB; 1R18; X-ray; 2.20 A; A=1-221.
DR PDBsum; 1R18; -.
DR AlphaFoldDB; Q27869; -.
DR SMR; Q27869; -.
DR STRING; 7227.FBpp0078405; -.
DR PaxDb; Q27869; -.
DR PRIDE; Q27869; -.
DR EnsemblMetazoa; FBtr0078758; FBpp0078405; FBgn0086768.
DR GeneID; 40668; -.
DR KEGG; dme:Dmel_CG2152; -.
DR CTD; 30751; -.
DR FlyBase; FBgn0086768; Pcmt.
DR VEuPathDB; VectorBase:FBgn0086768; -.
DR eggNOG; KOG1661; Eukaryota.
DR GeneTree; ENSGT00950000183032; -.
DR HOGENOM; CLU_055432_0_4_1; -.
DR InParanoid; Q27869; -.
DR OMA; TISAIHM; -.
DR PhylomeDB; Q27869; -.
DR BRENDA; 2.1.1.77; 1994.
DR Reactome; R-DME-5676934; Protein repair.
DR BioGRID-ORCS; 40668; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Pcmt; fly.
DR EvolutionaryTrace; Q27869; -.
DR GenomeRNAi; 40668; -.
DR PRO; PR:Q27869; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086768; Expressed in eye disc (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q27869; baseline and differential.
DR Genevisible; Q27869; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..226
FT /note="Protein-L-isoaspartate(D-aspartate) O-
FT methyltransferase"
FT /id="PRO_0000111881"
FT ACT_SITE 60
FT /evidence="ECO:0000269|PubMed:14596598"
FT BINDING 57..60
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 65
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 89
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 115..116
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 147..148
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT BINDING 222
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P22061"
FT MUTAGEN 60
FT /note="S->A: Reduces catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:14596598"
FT MUTAGEN 60
FT /note="S->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:14596598"
FT MUTAGEN 60
FT /note="S->T: Reduces catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:14596598"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1R18"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1R18"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1R18"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:1R18"
SQ SEQUENCE 226 AA; 24590 MW; AA56803256DBD567 CRC64;
MAWRSVGANN EDLIRQLKDH GVIASDAVAQ AMKETDRKHY SPRNPYMDAP QPIGGGVTIS
APHMHAFALE YLRDHLKPGA RILDVGSGSG YLTACFYRYI KAKGVDADTR IVGIEHQAEL
VRRSKANLNT DDRSMLDSGQ LLIVEGDGRK GYPPNAPYNA IHVGAAAPDT PTELINQLAS
GGRLIVPVGP DGGSQYMQQY DKDANGKVEM TRLMGVMYVP LTDLRS
