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Q56308

- PIMT_THEMA

UniProt

Q56308 - PIMT_THEMA

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Protein

Protein-L-isoaspartate O-methyltransferase

Gene

pcm

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 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.

Catalytic activityi

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

Kineticsi

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

    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 – 591By 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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Protein-L-isoaspartate O-methyltransferasePRO_0000111905Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi243274.TM0704.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1110Combined sources
    Helixi16 – 249Combined sources
    Helixi27 – 304Combined sources
    Helixi37 – 404Combined sources
    Beta strandi42 – 443Combined sources
    Beta strandi46 – 505Combined sources
    Beta strandi55 – 584Combined sources
    Helixi61 – 7010Combined sources
    Beta strandi78 – 825Combined sources
    Helixi88 – 9710Combined sources
    Beta strandi102 – 1087Combined sources
    Helixi110 – 12213Combined sources
    Beta strandi127 – 1337Combined sources
    Helixi135 – 1373Combined sources
    Helixi140 – 1423Combined sources
    Beta strandi145 – 1506Combined sources
    Beta strandi152 – 1554Combined sources
    Helixi159 – 1646Combined sources
    Beta strandi165 – 17511Combined sources
    Helixi178 – 1803Combined sources
    Beta strandi184 – 1918Combined sources
    Beta strandi194 – 2029Combined sources
    Helixi210 – 2123Combined sources
    Helixi215 – 2206Combined sources
    Beta strandi228 – 2336Combined sources
    Helixi237 – 24812Combined sources
    Beta strandi251 – 2544Combined sources
    Beta strandi257 – 2615Combined sources
    Beta strandi263 – 2708Combined sources
    Beta strandi273 – 2786Combined sources
    Helixi281 – 29212Combined sources
    Turni293 – 2953Combined sources
    Helixi298 – 3003Combined sources
    Beta strandi301 – 3099Combined sources
    Beta strandi312 – 3143Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DL5X-ray1.80A/B1-317[»]
    ProteinModelPortaliQ56308.
    SMRiQ56308. Positions 1-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ56308.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2518.
    InParanoidiQ56308.
    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

            10         20         30         40         50
    MREKLFWILK KYGVSDHIAK AFLEIPREEF LTKSYPLSYV YEDIVLVSYD
    60 70 80 90 100
    DGEEYSTSSQ PSLMALFMEW VGLDKGMRVL EIGGGTGYNA AVMSRVVGEK
    110 120 130 140 150
    GLVVSVEYSR KICEIAKRNV ERLGIENVIF VCGDGYYGVP EFSPYDVIFV
    160 170 180 190 200
    TVGVDEVPET WFTQLKEGGR VIVPINLKLS RRQPAFLFKK KDPYLVGNYK
    210 220 230 240 250
    LETRFITAGG NLGNLLERNR KLLREFPFNR EILLVRSHIF VELVDLLTRR
    260 270 280 290 300
    LTEIDGTFYY AGPNGVVEFL DDRMRIYGDA PEIENLLTQW ESCGYRSFEY
    310
    LMLHVGYNAF SHISCSI
    Length:317
    Mass (Da):36,400
    Last modified:November 1, 1996 - v1
    Checksum:i2FE6019571ADDF2C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    GeneIDi18092085.
    898371.
    KEGGitma:TM0704.
    PATRICi23936326. VBITheMar51294_0716.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    PDBei
    RCSB PDBi
    PDBji
    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 18092085.
    898371.
    KEGGi tma:TM0704.
    PATRICi 23936326. VBITheMar51294_0716.

    Phylogenomic databases

    eggNOGi COG2518.
    InParanoidi Q56308.
    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: November 26, 2014
    This is version 108 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