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G2QJR6

- CIP2_THIHA

UniProt

G2QJR6 - CIP2_THIHA

Protein

4-O-methyl-glucuronoyl methylesterase

Gene

ge2

Organism
Thielavia heterothallica (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Myceliophthora thermophila)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 14 (01 Oct 2014)
      Sequence version 1 (16 Nov 2011)
      Previous versions | rss
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    Functioni

    Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin.1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei213 – 2131Nucleophile
    Binding sitei217 – 2171Substrate
    Binding sitei259 – 2591Substrate
    Binding sitei267 – 2671Substrate
    Binding sitei310 – 3101Substrate
    Active sitei346 – 3461Proton donor/acceptor

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW

    GO - Biological processi

    1. lignin catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Lignin degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-O-methyl-glucuronoyl methylesterase (EC:3.1.1.-)
    Alternative name(s):
    Glucuronoyl esterase 2
    Short name:
    GE2
    Gene namesi
    Name:ge2
    ORF Names:MYCTH_55568
    OrganismiThielavia heterothallica (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Myceliophthora thermophila)
    Taxonomic identifieri573729 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora
    ProteomesiUP000007322: Chromosome 5

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131S → A: Abolishes catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 3973794-O-methyl-glucuronoyl methylesterasePRO_0000419176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 651 Publication
    Disulfide bondi212 ↔ 3471 Publication
    Disulfide bondi244 ↔ 3191 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 7718
    Beta strandi87 – 937
    Beta strandi95 – 10410
    Beta strandi107 – 11610
    Beta strandi119 – 1213
    Beta strandi124 – 1318
    Beta strandi141 – 1466
    Helixi148 – 1514
    Helixi157 – 1593
    Helixi164 – 1696
    Helixi177 – 19519
    Helixi197 – 2004
    Beta strandi202 – 21211
    Helixi214 – 22512
    Beta strandi230 – 2367
    Turni239 – 2424
    Helixi245 – 2539
    Helixi261 – 2644
    Turni265 – 2673
    Turni273 – 2753
    Helixi276 – 2783
    Helixi282 – 2843
    Helixi289 – 2913
    Helixi292 – 2965
    Beta strandi299 – 3057
    Turni309 – 3113
    Helixi313 – 33018
    Helixi333 – 3353
    Beta strandi336 – 3405
    Helixi351 – 3533
    Helixi354 – 36411
    Beta strandi375 – 3795
    Helixi383 – 3864

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G4GX-ray1.55A1-397[»]
    4G4IX-ray1.90A1-397[»]
    4G4JX-ray2.35A1-397[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi211 – 2166GXSYXG catalytic site motif

    Sequence similaritiesi

    Belongs to the carbohydrate esterase 15 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OrthoDBiEOG76DV35.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    G2QJR6-1 [UniParc]FASTAAdd to Basket

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    MVHLTSALLV AGAAFAAAAP MNHIFERQDT CSVSDNYPTV NSAKLPDPFT    50
    TASGEKVTTK DQFECRRAEI NKILQQYELG EYPGPPDSVE ASLSGNSITV 100
    RVTVGSKSIS FSASIRKPSG AGPFPAIIGI GGASIPIPSN VATITFNNDE 150
    FGAQMGSGSR GQGKFYDLFG RDHSAGSLTA WAWGVDRLID GLEQVGAQAS 200
    GIDTKRLGVT GCSRNGKGAF ITGALVDRIA LTIPQESGAG GAACWRISDQ 250
    QKAAGANIQT AAQIITENPW FSRNFDPHVN SITSVPQDHH LLAALIVPRG 300
    LAVFENNIDW LGPVSTTGCM AAGRLIYKAY GVPNNMGFSL VGGHNHCQFP 350
    SSQNQDLNSY INYFLLGQGS PSGVEHSDVN VNVAEWAPWG AGAPTLA 397
    Length:397
    Mass (Da):41,752
    Last modified:November 16, 2011 - v1
    Checksum:i69B2B5298F3C2043
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003006 Genomic DNA. Translation: AEO60464.1.
    RefSeqiXP_003665709.1. XM_003665661.1.

    Genome annotation databases

    GeneIDi11507096.
    KEGGimtm:MYCTH_55568.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003006 Genomic DNA. Translation: AEO60464.1 .
    RefSeqi XP_003665709.1. XM_003665661.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4G4G X-ray 1.55 A 1-397 [» ]
    4G4I X-ray 1.90 A 1-397 [» ]
    4G4J X-ray 2.35 A 1-397 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 11507096.
    KEGGi mtm:MYCTH_55568.

    Phylogenomic databases

    OrthoDBi EOG76DV35.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42464 / BCRC 31852 / DSM 1799.
    2. "Functional expression of a thermophilic glucuronyl esterase from Sporotrichum thermophile: identification of the nucleophilic serine."
      Topakas E., Moukouli M., Dima rogona M., Vafiadi C., Christakopoulos P.
      Appl. Microbiol. Biotechnol. 87:1765-1772(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ACTIVE SITE, MUTAGENESIS OF SER-213.
    3. "The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst."
      Charavgi M.D., Dimarogona M., Topakas E., Christakopoulos P., Chrysina E.D.
      Acta Crystallogr. D 69:63-73(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH 4-O-METHYL-BETA-D-GLUCOPYRANURONATE, ACTIVE SITE, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCIP2_THIHA
    AccessioniPrimary (citable) accession number: G2QJR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 14 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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