GCE1_WOLCO
ID GCE1_WOLCO Reviewed; 408 AA.
AC P0CU53; A0A2H3JPZ0;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase 1 {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:28429057};
DE AltName: Full=Glucuronoyl esterase 1;
DE Short=GE1;
DE Flags: Precursor;
GN ORFNames=WOLCODRAFT_23632;
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Wolfiporia.
OX NCBI_TaxID=742152;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104;
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28429057; DOI=10.1007/s00253-017-8266-9;
RA Huettner S., Klaubauf S., de Vries R.P., Olsson L.;
RT "Characterisation of three fungal glucuronoyl esterases on glucuronic acid
RT ester model compounds.";
RL Appl. Microbiol. Biotechnol. 101:5301-5311(2017).
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. Can hydrolyze benzyl glucuronic acid (BnGlcA),
CC allyl glucuronic acid (allylGlcA) and to a lower degree methyl
CC glucuronic acid (MeGlcA) in vitro. {ECO:0000269|PubMed:28429057}.
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:28429057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:28429057};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for benzyl glucuronic acid {ECO:0000269|PubMed:28429057};
CC Vmax=1.91 umol/min/mg enzyme for benzyl glucuronic acid
CC {ECO:0000269|PubMed:28429057};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0CT87}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB468053; PCH39808.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CU53; -.
DR SMR; P0CU53; -.
DR EnsemblFungi; PCH39808; PCH39808; WOLCODRAFT_23632.
DR OMA; LSAYGCM; -.
DR OrthoDB; 941049at2759; -.
DR BRENDA; 3.1.1.117; 4987.
DR Proteomes; UP000218811; Unassembled WGS sequence.
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 Disulfide bond; Glycoprotein; Hydrolase; Lignin degradation;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..408
FT /note="4-O-methyl-glucuronoyl methylesterase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441411"
FT MOTIF 217..222
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 353
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..65
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 218..354
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 250..326
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 408 AA; 44123 MW; 91025084BE34D139 CRC64;
MASSSRFAAL LLLALPALAL PPSQVVPRAA CATPSTVPGY NNDRLPDPFL FDDGTAVTSS
ADWDCRRSQI AAVVQGYEAG YLPPQPPIVS ATFSSSDGTG TLTVTAGLSS DNTISFSEPI
TYPSGTAPAA GWPLVIAYDV LSIPVPDGIA VMVYNNDDIA QENDLSSRGV GLFYDLYGTD
ATASAMTAWV WGVSRIIDAL ETTPAANINT AKIAVTGCSR DGKGALMAGA FEPRVALTIP
QESGSGGDTC WRLSKYEQDS GDVVQQATEI VTENVWFSTN FDNYVNNLSV LPYDHHELAA
MVAPRPLLSY ENTEYEWLSP LSAYGCMSAA HTVYEALGIP DYHGFVQVGN HSHCYFPDTL
DDSLYAFFDR FLLDEDDVST DYFTTNYQFN GTVWNASYWI NWTTPQLD
