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G2QJR6 (CIP2_THIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-O-methyl-glucuronoyl methylesterase

EC=3.1.1.-
Alternative name(s):
Glucuronoyl esterase 2
Short name=GE2
Gene names
Name:ge2
ORF Names:MYCTH_55568
OrganismThielavia heterothallica (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Myceliophthora thermophila) [Complete proteome]
Taxonomic identifier573729 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the carbohydrate esterase 15 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.2

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 3973794-O-methyl-glucuronoyl methylesterase
PRO_0000419176

Regions

Motif211 – 2166GXSYXG catalytic site motif

Sites

Active site2131Nucleophile Ref.2 Ref.3
Active site3461Proton donor/acceptor Ref.2 Ref.3
Binding site2171Substrate
Binding site2591Substrate
Binding site2671Substrate
Binding site3101Substrate

Amino acid modifications

Disulfide bond31 ↔ 65 Ref.3
Disulfide bond212 ↔ 347 Ref.3
Disulfide bond244 ↔ 319 Ref.3

Experimental info

Mutagenesis2131S → A: Abolishes catalytic activity. Ref.2

Secondary structure

.............................................................. 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
G2QJR6 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 69B2B5298F3C2043

FASTA39741,752
        10         20         30         40         50         60 
MVHLTSALLV AGAAFAAAAP MNHIFERQDT CSVSDNYPTV NSAKLPDPFT TASGEKVTTK 

        70         80         90        100        110        120 
DQFECRRAEI NKILQQYELG EYPGPPDSVE ASLSGNSITV RVTVGSKSIS FSASIRKPSG 

       130        140        150        160        170        180 
AGPFPAIIGI GGASIPIPSN VATITFNNDE FGAQMGSGSR GQGKFYDLFG RDHSAGSLTA 

       190        200        210        220        230        240 
WAWGVDRLID GLEQVGAQAS GIDTKRLGVT GCSRNGKGAF ITGALVDRIA LTIPQESGAG 

       250        260        270        280        290        300 
GAACWRISDQ QKAAGANIQT AAQIITENPW FSRNFDPHVN SITSVPQDHH LLAALIVPRG 

       310        320        330        340        350        360 
LAVFENNIDW LGPVSTTGCM AAGRLIYKAY GVPNNMGFSL VGGHNHCQFP SSQNQDLNSY 

       370        380        390 
INYFLLGQGS PSGVEHSDVN VNVAEWAPWG AGAPTLA 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genomic analysis of the thermophilic biomass-degrading fungi Myceliophthora thermophila and Thielavia terrestris."
Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P. expand/collapse author list , Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., Tsang A.
Nat. Biotechnol. 29:922-927(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003006 Genomic DNA. Translation: AEO60464.1.
RefSeqXP_003665709.1. XM_003665661.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G4GX-ray1.55A1-397[»]
4G4IX-ray1.90A1-397[»]
4G4JX-ray2.35A1-397[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11507096.
KEGGmtm:MYCTH_55568.

Phylogenomic databases

OrthoDBEOG76DV35.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMSSF53474. SSF53474. 2 hits.
ProtoNetSearch...

Entry information

Entry nameCIP2_THIHA
AccessionPrimary (citable) accession number: G2QJR6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: November 16, 2011
Last modified: June 11, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references