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Q56308

- PIMT_THEMA

UniProt

Q56308 - PIMT_THEMA

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Protein
Protein-L-isoaspartate O-methyltransferase
Gene
pcm, TM_0704
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.UniRule annotation

Kineticsi

    Vmax=164 nmol/min/mg enzyme with KASA (isoD) LAKY as substrate at 85 degrees CelsiusUniRule annotation

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius. Highly thermostable, with no loss of activity after 60 min at 100 degrees Celsius. Enzyme activity is observed at temperatures as high as 93 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei59 – 591 By similarity

    GO - Molecular functioni

    1. protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein repair Source: UniProtKB-HAMAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-L-isoaspartate O-methyltransferase (EC:2.1.1.77)
    Alternative name(s):
    L-isoaspartyl protein carboxyl methyltransferase
    Protein L-isoaspartyl methyltransferase
    Protein-beta-aspartate methyltransferase
    Short name:
    PIMT
    Gene namesi
    Name:pcm
    Ordered Locus Names:TM_0704
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Subcellular locationi

    Cytoplasm By similarity UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Protein-L-isoaspartate O-methyltransferaseUniRule annotation
    PRO_0000111905Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi243274.TM0704.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1110
    Helixi16 – 249
    Helixi27 – 304
    Helixi37 – 404
    Beta strandi42 – 443
    Beta strandi46 – 505
    Beta strandi55 – 584
    Helixi61 – 7010
    Beta strandi78 – 825
    Helixi88 – 9710
    Beta strandi102 – 1087
    Helixi110 – 12213
    Beta strandi127 – 1337
    Helixi135 – 1373
    Helixi140 – 1423
    Beta strandi145 – 1506
    Beta strandi152 – 1554
    Helixi159 – 1646
    Beta strandi165 – 17511
    Helixi178 – 1803
    Beta strandi184 – 1918
    Beta strandi194 – 2029
    Helixi210 – 2123
    Helixi215 – 2206
    Beta strandi228 – 2336
    Helixi237 – 24812
    Beta strandi251 – 2544
    Beta strandi257 – 2615
    Beta strandi263 – 2708
    Beta strandi273 – 2786
    Helixi281 – 29212
    Turni293 – 2953
    Helixi298 – 3003
    Beta strandi301 – 3099
    Beta strandi312 – 3143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DL5X-ray1.80A/B1-317[»]
    ProteinModelPortaliQ56308.
    SMRiQ56308. Positions 1-317.

    Miscellaneous databases

    EvolutionaryTraceiQ56308.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2518.
    KOiK00573.
    OMAiPTQWRES.
    OrthoDBiEOG644ZP2.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    3.55.20.10. 1 hit.
    HAMAPiMF_00090. PIMT.
    InterProiIPR000682. PCMT.
    IPR009107. PIM_MeTrfase_C.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11579. PTHR11579. 1 hit.
    PfamiPF01135. PCMT. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 2 hits.
    SSF68930. SSF68930. 1 hit.
    PROSITEiPS01279. PCMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q56308-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREKLFWILK KYGVSDHIAK AFLEIPREEF LTKSYPLSYV YEDIVLVSYD    50
    DGEEYSTSSQ PSLMALFMEW VGLDKGMRVL EIGGGTGYNA AVMSRVVGEK 100
    GLVVSVEYSR KICEIAKRNV ERLGIENVIF VCGDGYYGVP EFSPYDVIFV 150
    TVGVDEVPET WFTQLKEGGR VIVPINLKLS RRQPAFLFKK KDPYLVGNYK 200
    LETRFITAGG NLGNLLERNR KLLREFPFNR EILLVRSHIF VELVDLLTRR 250
    LTEIDGTFYY AGPNGVVEFL DDRMRIYGDA PEIENLLTQW ESCGYRSFEY 300
    LMLHVGYNAF SHISCSI 317
    Length:317
    Mass (Da):36,400
    Last modified:November 1, 1996 - v1
    Checksum:i2FE6019571ADDF2C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30501 Genomic DNA. Translation: AAA96385.1.
    AE000512 Genomic DNA. Translation: AAD35786.1.
    PIRiG72342.
    RefSeqiNP_228513.1. NC_000853.1.
    YP_007977054.1. NC_021214.1.
    YP_008990327.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35786; AAD35786; TM_0704.
    GeneIDi898371.
    KEGGitma:TM0704.
    tmi:THEMA_01145.
    tmm:Tmari_0704.
    PATRICi23936326. VBITheMar51294_0716.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30501 Genomic DNA. Translation: AAA96385.1 .
    AE000512 Genomic DNA. Translation: AAD35786.1 .
    PIRi G72342.
    RefSeqi NP_228513.1. NC_000853.1.
    YP_007977054.1. NC_021214.1.
    YP_008990327.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DL5 X-ray 1.80 A/B 1-317 [» ]
    ProteinModelPortali Q56308.
    SMRi Q56308. Positions 1-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35786 ; AAD35786 ; TM_0704 .
    GeneIDi 898371.
    KEGGi tma:TM0704.
    tmi:THEMA_01145.
    tmm:Tmari_0704.
    PATRICi 23936326. VBITheMar51294_0716.

    Phylogenomic databases

    eggNOGi COG2518.
    KOi K00573.
    OMAi PTQWRES.
    OrthoDBi EOG644ZP2.

    Miscellaneous databases

    EvolutionaryTracei Q56308.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    3.55.20.10. 1 hit.
    HAMAPi MF_00090. PIMT.
    InterProi IPR000682. PCMT.
    IPR009107. PIM_MeTrfase_C.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11579. PTHR11579. 1 hit.
    Pfami PF01135. PCMT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 2 hits.
    SSF68930. SSF68930. 1 hit.
    PROSITEi PS01279. PCMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima."
      Swanson R.V., Sanna M.G., Simon M.I.
      J. Bacteriol. 178:484-489(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima."
      Ichikawa J.K., Clarke S.
      Arch. Biochem. Biophys. 358:222-231(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Crystal structure of protein isoaspartyl methyltransferase. A catalyst for protein repair."
      Skinner M.M., Puvathingal J.M., Walter R.L., Friedman A.M.
      Structure 8:1189-1201(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiPIMT_THEMA
    AccessioniPrimary (citable) accession number: Q56308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: July 9, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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