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Protein

4-O-methyl-glucuronoyl methylesterase

Gene

ge2

Organism
Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Kineticsi

kcat is 115.9 min(-1) with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate and 166.4 with 3-phenyl-1-propyl D-glucopyranosyluronate as substrate.1 Publication

  1. KM=3.63 mM for trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate1 Publication
  2. KM=7.24 mM for 3-phenyl-1-propyl D-glucopyranosyluronate1 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 – 2131Nucleophile1 Publication1 Publication
    Binding sitei217 – 2171Substrate1 Publication
    Binding sitei259 – 2591Substrate1 Publication
    Binding sitei267 – 2671Substrate1 Publication
    Binding sitei310 – 3101Substrate1 Publication
    Active sitei346 – 3461Proton donor/acceptor1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Lignin degradation

    Protein family/group databases

    ESTHERithiha-cip2. Glucuronoyl_esterase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-O-methyl-glucuronoyl methylesteraseCurated (EC:3.1.1.-1 Publication)
    Alternative name(s):
    Glucuronoyl esterase 21 Publication
    Short name:
    GE21 Publication
    Gene namesi
    Name:ge2
    ORF Names:MYCTH_55568
    OrganismiMyceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile)
    Taxonomic identifieri573729 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora
    Proteomesi
    • UP000007322 Componenti: Chromosome 5

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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 – 7718Combined sources
    Beta strandi87 – 937Combined sources
    Beta strandi95 – 10410Combined sources
    Beta strandi107 – 11610Combined sources
    Beta strandi119 – 1213Combined sources
    Beta strandi124 – 1318Combined sources
    Beta strandi141 – 1466Combined sources
    Helixi148 – 1514Combined sources
    Helixi157 – 1593Combined sources
    Helixi164 – 1696Combined sources
    Helixi177 – 19519Combined sources
    Helixi197 – 2004Combined sources
    Beta strandi202 – 21211Combined sources
    Helixi214 – 22512Combined sources
    Beta strandi230 – 2367Combined sources
    Turni239 – 2424Combined sources
    Helixi245 – 2539Combined sources
    Helixi261 – 2644Combined sources
    Turni265 – 2673Combined sources
    Turni273 – 2753Combined sources
    Helixi276 – 2783Combined sources
    Helixi282 – 2843Combined sources
    Helixi289 – 2913Combined sources
    Helixi292 – 2965Combined sources
    Beta strandi299 – 3057Combined sources
    Turni309 – 3113Combined sources
    Helixi313 – 33018Combined sources
    Helixi333 – 3353Combined sources
    Beta strandi336 – 3405Combined sources
    Helixi351 – 3533Combined sources
    Helixi354 – 36411Combined sources
    Beta strandi375 – 3795Combined sources
    Helixi383 – 3864Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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 motif1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG410IE00. Eukaryota.
    ENOG410XRBM. LUCA.
    InParanoidiG2QJR6.
    OrthoDBiEOG092C1YHO.

    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

    « Hide

            10         20         30         40         50
    MVHLTSALLV AGAAFAAAAP MNHIFERQDT CSVSDNYPTV NSAKLPDPFT
    60 70 80 90 100
    TASGEKVTTK DQFECRRAEI NKILQQYELG EYPGPPDSVE ASLSGNSITV
    110 120 130 140 150
    RVTVGSKSIS FSASIRKPSG AGPFPAIIGI GGASIPIPSN VATITFNNDE
    160 170 180 190 200
    FGAQMGSGSR GQGKFYDLFG RDHSAGSLTA WAWGVDRLID GLEQVGAQAS
    210 220 230 240 250
    GIDTKRLGVT GCSRNGKGAF ITGALVDRIA LTIPQESGAG GAACWRISDQ
    260 270 280 290 300
    QKAAGANIQT AAQIITENPW FSRNFDPHVN SITSVPQDHH LLAALIVPRG
    310 320 330 340 350
    LAVFENNIDW LGPVSTTGCM AAGRLIYKAY GVPNNMGFSL VGGHNHCQFP
    360 370 380 390
    SSQNQDLNSY INYFLLGQGS PSGVEHSDVN VNVAEWAPWG AGAPTLA
    Length:397
    Mass (Da):41,752
    Last modified:November 16, 2011 - v1
    Checksum:i69B2B5298F3C2043
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP003006 Genomic DNA. Translation: AEO60464.1.
    RefSeqiXP_003665709.1. XM_003665661.1.

    Genome annotation databases

    EnsemblFungiiAEO60464; AEO60464; MYCTH_55568.
    GeneIDi11507096.
    KEGGimtm:MYCTH_55568.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP003006 Genomic DNA. Translation: AEO60464.1.
    RefSeqiXP_003665709.1. XM_003665661.1.

    3D structure databases

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

    Protein family/group databases

    ESTHERithiha-cip2. Glucuronoyl_esterase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiAEO60464; AEO60464; MYCTH_55568.
    GeneIDi11507096.
    KEGGimtm:MYCTH_55568.

    Phylogenomic databases

    eggNOGiENOG410IE00. Eukaryota.
    ENOG410XRBM. LUCA.
    InParanoidiG2QJR6.
    OrthoDBiEOG092C1YHO.

    Family and domain databases

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

    Entry informationi

    Entry nameiGCE2_MYCTT
    AccessioniPrimary (citable) accession number: G2QJR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: November 16, 2011
    Last modified: September 7, 2016
    This is version 21 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.