Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

G2QJR6

- CIP2_THIHA

UniProt

G2QJR6 - CIP2_THIHA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. carboxylic ester 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 Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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:
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

InParanoidiG2QJR6.
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

        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:
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

InParanoidi G2QJR6.
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: October 29, 2014
This is version 15 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