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| HAMAP annotation rule: MF_00090 |
| Accession |
MF_00090 |
| Dates |
1-JUN-2001 (Created)
25-NOV-2009 (Last updated, Version 20) |
| Protein name |
| RecName: |
Full=Protein-L-isoaspartate O-methyltransferase;
EC=2.1.1.77; |
| AltName: |
Full=Protein-beta-aspartate methyltransferase;
Short=PIMT; |
| AltName: |
Full=Protein L-isoaspartyl methyltransferase; |
| AltName: |
Full=L-isoaspartyl protein carboxyl methyltransferase; |
|
FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
GO:0004719; Molecular function: protein-L-isoaspartate (D-aspartate) O-methyltransferase activity.
GO:0006464; Biological process: protein modification process.
GO:0030091; Biological process: protein repair.
GO:0005737; Cellular component: cytoplasm.
| From: PIMT_ECOLI (P0A7A5) |
| Key |
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From |
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To |
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Description |
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Condition |
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FTGroup |
| ACT_SITE |
|
59 |
|
59 |
|
By similarity |
|
S |
|
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| Size range: |
198-327 amino acids |
| Related UniRules: |
None |
| Template: |
Q56308 (PIMT_THEMA); Q8TZR3 (PIMT_PYRFU): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: <Unknown> |
| Duplicate: |
in ANADF, ARCFU, GEOUR, MARAV, NITOC, NITMU, PELPD, POLSJ, RALEH, RHOP2, SHESH, SYNFM |
| Plasmid encoded: |
None |
| Comments: |
Possible wrong starts. Unknown C-terminal domain in THEMA. |
View rule in raw text format (no links)
