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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Active sitei213Nucleophile1 Publication1 Publication1
    Binding sitei217Substrate1 Publication1
    Binding sitei259Substrate1 Publication1
    Binding sitei267Substrate1 Publication1
    Binding sitei310Substrate1 Publication1
    Active sitei346Proton donor/acceptor1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi213S → A: Abolishes catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 18Sequence analysisAdd BLAST18
    ChainiPRO_000041917619 – 3974-O-methyl-glucuronoyl methylesteraseAdd BLAST379

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi31 ↔ 651 Publication
    Disulfide bondi212 ↔ 3471 Publication
    Disulfide bondi244 ↔ 3191 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1397
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi60 – 77Combined sources18
    Beta strandi87 – 93Combined sources7
    Beta strandi95 – 104Combined sources10
    Beta strandi107 – 116Combined sources10
    Beta strandi119 – 121Combined sources3
    Beta strandi124 – 131Combined sources8
    Beta strandi141 – 146Combined sources6
    Helixi148 – 151Combined sources4
    Helixi157 – 159Combined sources3
    Helixi164 – 169Combined sources6
    Helixi177 – 195Combined sources19
    Helixi197 – 200Combined sources4
    Beta strandi202 – 212Combined sources11
    Helixi214 – 225Combined sources12
    Beta strandi230 – 236Combined sources7
    Turni239 – 242Combined sources4
    Helixi245 – 253Combined sources9
    Helixi261 – 264Combined sources4
    Turni265 – 267Combined sources3
    Turni273 – 275Combined sources3
    Helixi276 – 278Combined sources3
    Helixi282 – 284Combined sources3
    Helixi289 – 291Combined sources3
    Helixi292 – 296Combined sources5
    Beta strandi299 – 305Combined sources7
    Turni309 – 311Combined sources3
    Helixi313 – 330Combined sources18
    Helixi333 – 335Combined sources3
    Beta strandi336 – 340Combined sources5
    Helixi351 – 353Combined sources3
    Helixi354 – 364Combined sources11
    Beta strandi375 – 379Combined sources5
    Helixi383 – 386Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4G4GX-ray1.55A1-397[»]
    4G4IX-ray1.90A1-397[»]
    4G4JX-ray2.35A1-397[»]
    ProteinModelPortaliG2QJR6.
    SMRiG2QJR6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi211 – 216GXSYXG catalytic site motif1 Publication6

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4G4GX-ray1.55A1-397[»]
    4G4IX-ray1.90A1-397[»]
    4G4JX-ray2.35A1-397[»]
    ProteinModelPortaliG2QJR6.
    SMRiG2QJR6.
    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: November 2, 2016
    This is version 22 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.