G2QJR6 (CIP2_THIHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Thielavia heterothallica (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Myceliophthora thermophila) [Complete proteome]

Taxonomic identifier

573729 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › mitosporic Chaetomiaceae › Myceliophthora › Thielavia heterothallica

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lignin degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 397

379

4-O-methyl-glucuronoyl methylesterase

PRO_0000419176

Regions

Motif

211 – 216

6

GXSYXG catalytic site motif

Sites

Active site

213

1

Nucleophile Ref.2 Ref.3

Active site

346

1

Proton donor/acceptor Ref.2 Ref.3

Binding site

217

1

Substrate

Binding site

259

1

Substrate

Binding site

267

1

Substrate

Binding site

310

1

Substrate

Amino acid modifications

Disulfide bond

31 ↔ 65

Ref.3

Disulfide bond

212 ↔ 347

Ref.3

Disulfide bond

244 ↔ 319

Ref.3

Experimental info

Mutagenesis

213

1

S → A: Abolishes catalytic activity. Ref.2

Secondary structure

1

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397

Helix Strand Turn

Details...

Helix

60 – 77

18

Beta strand

87 – 93

7

Beta strand

95 – 104

10

Beta strand

107 – 116

10

Beta strand

119 – 121

3

Beta strand

124 – 131

8

Beta strand

141 – 146

6

Helix

148 – 151

4

Helix

157 – 159

3

Helix

164 – 169

6

Helix

177 – 195

19

Helix

197 – 200

4

Beta strand

202 – 212

11

Helix

214 – 225

12

Beta strand

230 – 236

7

Turn

239 – 242

4

Helix

245 – 253

9

Helix

261 – 264

4

Turn

265 – 267

3

Turn

273 – 275

3

Helix

276 – 278

3

Helix

282 – 284

3

Helix

289 – 291

3

Helix

292 – 296

5

Beta strand

299 – 305

7

Turn

309 – 311

3

Helix

313 – 330

18

Helix

333 – 335

3

Beta strand

336 – 340

5

Helix

351 – 353

3

Helix

354 – 364

11

Beta strand

375 – 379

5

Helix

383 – 386

4

Sequences

	Sequence		Length	Mass (Da)
	G2QJR6 [UniParc]. Last modified November 16, 2011. Version 1. Checksum: 69B2B5298F3C2043	FASTA	397	41,752
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

RefSeq

XP_003665709.1. XM_003665661.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

11507096.

KEGG

mtm:MYCTH_55568.

Family and domain databases

ProtoNet

Search...

Entry information

Entry name

CIP2_THIHA

Accession

Primary (citable) accession number: G2QJR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2012
Last sequence update:	November 16, 2011
Last modified:	April 3, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program