GCE2_MYCTT
ID GCE2_MYCTT Reviewed; 397 AA.
AC G2QJR6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:20473662};
DE AltName: Full=Glucuronoyl esterase 2 {ECO:0000303|PubMed:20473662};
DE Short=GE2 {ECO:0000303|PubMed:20473662};
DE Flags: Precursor;
GN Name=ge2; ORFNames=MYCTH_55568;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ACTIVE
RP SITE, AND MUTAGENESIS OF SER-213.
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=20473662; DOI=10.1007/s00253-010-2655-7;
RA Topakas E., Moukouli M., Dima rogona M., Vafiadi C., Christakopoulos P.;
RT "Functional expression of a thermophilic glucuronyl esterase from
RT Sporotrichum thermophile: identification of the nucleophilic serine.";
RL Appl. Microbiol. Biotechnol. 87:1765-1772(2010).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24531271; DOI=10.1007/s00253-014-5542-9;
RA Katsimpouras C., Benarouche A., Navarro D., Karpusas M., Dimarogona M.,
RA Berrin J.G., Christakopoulos P., Topakas E.;
RT "Enzymatic synthesis of model substrates recognized by glucuronoyl
RT esterases from Podospora anserina and Myceliophthora thermophila.";
RL Appl. Microbiol. Biotechnol. 98:5507-5516(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH
RP 4-O-METHYL-BETA-D-GLUCOPYRANURONATE, ACTIVE SITE, AND DISULFIDE BONDS.
RX PubMed=23275164; DOI=10.1107/s0907444912042400;
RA Charavgi M.D., Dimarogona M., Topakas E., Christakopoulos P.,
RA Chrysina E.D.;
RT "The structure of a novel glucuronoyl esterase from Myceliophthora
RT thermophila gives new insights into its role as a potential biocatalyst.";
RL Acta Crystallogr. D 69:63-73(2013).
CC -!- FUNCTION: Glucuronoyl esterase which may play a significant role in
CC biomass degradation, as it is considered to disconnect hemicellulose
CC from lignin through the hydrolysis of the ester bond between 4-O-
CC methyl-D-glucuronic acid residues of glucuronoxylans and aromatic
CC alcohols of lignin. {ECO:0000269|PubMed:20473662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC EC=3.1.1.117; Evidence={ECO:0000269|PubMed:20473662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:20473662};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.63 mM for trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
CC {ECO:0000269|PubMed:24531271};
CC KM=7.24 mM for 3-phenyl-1-propyl D-glucopyranosyluronate
CC {ECO:0000269|PubMed:24531271};
CC Note=kcat is 115.9 min(-1) with trans-3-phenyl-2-propen-1-yl D-
CC glucopyranosyluronate and 166.4 with 3-phenyl-1-propyl D-
CC glucopyranosyluronate as substrate. {ECO:0000269|PubMed:24531271};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:20473662};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:20473662};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; CP003006; AEO60464.1; -; Genomic_DNA.
DR RefSeq; XP_003665709.1; XM_003665661.1.
DR PDB; 4G4G; X-ray; 1.55 A; A=1-397.
DR PDB; 4G4I; X-ray; 1.90 A; A=1-397.
DR PDB; 4G4J; X-ray; 2.35 A; A=1-397.
DR PDBsum; 4G4G; -.
DR PDBsum; 4G4I; -.
DR PDBsum; 4G4J; -.
DR AlphaFoldDB; G2QJR6; -.
DR SMR; G2QJR6; -.
DR ESTHER; thiha-cip2; Glucuronoyl_esterase.
DR EnsemblFungi; AEO60464; AEO60464; MYCTH_55568.
DR GeneID; 11507096; -.
DR KEGG; mtm:MYCTH_55568; -.
DR VEuPathDB; FungiDB:MYCTH_55568; -.
DR eggNOG; ENOG502QS8Y; Eukaryota.
DR HOGENOM; CLU_028869_1_1_1; -.
DR InParanoid; G2QJR6; -.
DR OrthoDB; 941049at2759; -.
DR BRENDA; 3.1.1.117; 13804.
DR Proteomes; UP000007322; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Lignin degradation;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..397
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_0000419176"
FT MOTIF 211..216
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000305|PubMed:20473662"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:20473662,
FT ECO:0000305|PubMed:23275164"
FT ACT_SITE 346
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23275164"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23275164"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23275164"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23275164"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23275164"
FT DISULFID 31..65
FT /evidence="ECO:0000269|PubMed:23275164"
FT DISULFID 212..347
FT /evidence="ECO:0000269|PubMed:23275164"
FT DISULFID 244..319
FT /evidence="ECO:0000269|PubMed:23275164"
FT MUTAGEN 213
FT /note="S->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20473662"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 177..195
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:4G4G"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4G4G"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:4G4G"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:4G4G"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:4G4G"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4G4G"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:4G4G"
SQ SEQUENCE 397 AA; 41752 MW; 69B2B5298F3C2043 CRC64;
MVHLTSALLV AGAAFAAAAP MNHIFERQDT CSVSDNYPTV NSAKLPDPFT TASGEKVTTK
DQFECRRAEI NKILQQYELG EYPGPPDSVE ASLSGNSITV RVTVGSKSIS FSASIRKPSG
AGPFPAIIGI GGASIPIPSN VATITFNNDE FGAQMGSGSR GQGKFYDLFG RDHSAGSLTA
WAWGVDRLID GLEQVGAQAS GIDTKRLGVT GCSRNGKGAF ITGALVDRIA LTIPQESGAG
GAACWRISDQ QKAAGANIQT AAQIITENPW FSRNFDPHVN SITSVPQDHH LLAALIVPRG
LAVFENNIDW LGPVSTTGCM AAGRLIYKAY GVPNNMGFSL VGGHNHCQFP SSQNQDLNSY
INYFLLGQGS PSGVEHSDVN VNVAEWAPWG AGAPTLA
