ID PIMT2_SYNFM Reviewed; 247 AA.
AC A0LM89;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 01-MAY-2013, entry version 44.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 2;
DE EC=2.1.1.77;
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 2;
DE AltName: Full=Protein L-isoaspartyl methyltransferase 2;
DE AltName: Full=Protein-beta-aspartate methyltransferase 2;
DE Short=PIMT 2;
GN Name=pcm2; OrderedLocusNames=Sfum_2864;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl
CC residues in peptides and proteins that result from spontaneous
CC decomposition of normal L-aspartyl and L-asparaginyl residues. It
CC plays a role in the repair and/or degradation of damaged proteins
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC alpha-methyl ester.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
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DR EMBL; CP000478; ABK18541.1; -; Genomic_DNA.
DR RefSeq; YP_846976.1; NC_008554.1.
DR ProteinModelPortal; A0LM89; -.
DR STRING; 335543.Sfum_2864; -.
DR EnsemblBacteria; ABK18541; ABK18541; Sfum_2864.
DR GeneID; 4458796; -.
DR KEGG; sfu:Sfum_2864; -.
DR PATRIC; 23851703; VBISynFum78438_3408.
DR eggNOG; COG2518; -.
DR HOGENOM; HOG000257189; -.
DR KO; K00573; -.
DR OMA; GDGYHGW; -.
DR ProtClustDB; CLSK773872; -.
DR BioCyc; SFUM335543:GH6P-2925-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0030091; P:protein repair; IEA:HAMAP.
DR HAMAP; MF_00090; PIMT; 1; -.
DR InterPro; IPR000682; PCMT.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR Pfam; PF01135; PCMT; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 247 Protein-L-isoaspartate O-
FT methyltransferase 2.
FT /FTId=PRO_0000351945.
FT ACT_SITE 97 97 By similarity.
SQ SEQUENCE 247 AA; 26797 MW; B4D30E32216DDF67 CRC64;
MSRKSTGAFL VILLLSMAAG GAVGAADDPY GAARAKMVRE IEEDARRTSE RIGKTALDPR
VMEIMARVPR HEFVPAAERA YAYENRPLPI GYGQTISQPY IVAVMTDLLK VGSESTVLEV
GTGSGYQAAI LAEFVRSVYS IEIIEALAET AAERLKRLGY DNVRVRTGDG YHGWKEHAPF
DGIVVTAAAG HIPPPLLDQL KPGGRMIIPV GGPFFVQQLM LVEKDEQGRT RTRQILPVAF
VPLTGGH
//
