ID A0A1H3NET1_9RHOB Unreviewed; 662 AA.
AC A0A1H3NET1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE EC=2.1.1.77 {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE Short=PIMT {ECO:0000256|HAMAP-Rule:MF_00090};
GN Name=pcm {ECO:0000256|HAMAP-Rule:MF_00090};
GN ORFNames=SAMN05444340_12313 {ECO:0000313|EMBL:SDY86965.1};
OS Citreimonas salinaria.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Citreimonas.
OX NCBI_TaxID=321339 {ECO:0000313|EMBL:SDY86965.1, ECO:0000313|Proteomes:UP000199286};
RN [1] {ECO:0000313|EMBL:SDY86965.1, ECO:0000313|Proteomes:UP000199286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26880 {ECO:0000313|EMBL:SDY86965.1,
RC ECO:0000313|Proteomes:UP000199286};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC in peptides and proteins that result from spontaneous decomposition of
CC normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC repair and/or degradation of damaged proteins. {ECO:0000256|HAMAP-
CC Rule:MF_00090}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00090};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|HAMAP-Rule:MF_00090}.
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DR EMBL; FNPF01000023; SDY86965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3NET1; -.
DR STRING; 321339.SAMN05444340_12313; -.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000199286; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd14728; Ere-like; 1.
DR Gene3D; 1.20.1440.30; Biosynthetic Protein domain; 1.
DR Gene3D; 3.40.1660.10; EreA-like (biosynthetic domain); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR007815; Emycin_Estase.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR31299; ESTERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05850)-RELATED; 1.
DR PANTHER; PTHR31299:SF0; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05139; Erythro_esteras; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF159501; EreA/ChaN-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW ECO:0000313|EMBL:SDY86965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199286};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:SDY86965.1}.
FT ACT_SITE 62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 662 AA; 73946 MW; 939F7780E7ED77D7 CRC64;
MADTAPARNH MVERQIESRG IRDRHVLDAM RLVPREVFVD PGMEEFAYDD SPLPIGEGQT
ISQPYIVALM IESAEVRPGD RVLEIGAGSG YAAALLSRIA DSVHAIERHE GLTKKAASRM
ERLGYDNVTL RTGDGTRGWP EEAPFDSILV AAGAPTAPES LKRQLAVGGS LVIPVQHDDQ
HQTLIRIRRT AEDAWDEEKL CAVRFVPLIG AEGWAEDGTR AATNHKPARE VPLPEMIAEA
AEPLPDVDDP AFGVLFERYG DRRVVLLGEA SHGTSEFYRA RAAITRHLIE NHGFNIVAVE
ADWPDAAAID RFARDLAPRD TGEPAFNRFP TWMWRNTVVE GFSHWLRSHN ARIPDPGARV
GFYGLDIYNM RGSIAAVLDY LETVDPEAAR IARERYSCLT PWQSDPATYG RAVLTQRYRD
CEAEVVAQLR ALLEKELDYE AADGAGFLDA AQNARLVRSA EQYYKVMYYG GAESWNLRDS
HMFETLEHVL ESRGPDAKAI VWAHNSHIGD ARATEMGAVR GEHNIGQLVR QRFGDEAGLI
GFGTHTGTVA AATDWGGEME IKRVRPSRED SYERLCHDAG GGRFLLDLSR DPALRRRLEK
QRLERFIGVI YRPETELASH YADASLPRQF DGWVWFDETS AITPLETEPD REGMPETWPF
GL
//
