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G2QJR6

- CIP2_THIHA

UniProt

G2QJR6 - CIP2_THIHA

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Protein

4-O-methyl-glucuronoyl methylesterase

Gene
ge2, MYCTH_55568
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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei213 – 2131Nucleophile2 Publications
Binding sitei217 – 2171Substrate
Binding sitei259 – 2591Substrate
Binding sitei267 – 2671Substrate
Binding sitei310 – 3101Substrate
Active sitei346 – 3461Proton donor/acceptor2 Publications

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. lignin catabolic process Source: UniProtKB-KW
Complete GO annotation...

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 Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
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 – 1818 Reviewed predictionAdd
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[»]

Family & Domainsi

Motif

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

Sequence similaritiesi

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

« Hide

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 13 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

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

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