GCE2_PHACR
ID GCE2_PHACR Reviewed; 407 AA.
AC P0CT88;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase 2 {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:18854978, ECO:0000269|PubMed:19897892};
DE AltName: Full=Glucuronoyl esterase 2 {ECO:0000303|PubMed:18854978};
DE Short=GE2 {ECO:0000303|PubMed:18854978};
DE Flags: Precursor;
GN ORFNames=e_gw1.11.1537.1, fgenesh1_pg.C_scaffold_11000167;
OS Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002)
OS (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia; Phanerodontia chrysosporium.
OX NCBI_TaxID=273507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=15122302; DOI=10.1038/nbt967;
RA Martinez D., Larrondo L.F., Putnam N., Gelpke M.D.S., Huang K., Chapman J.,
RA Helfenbein K.G., Ramaiya P., Detter J.C., Larimer F., Coutinho P.M.,
RA Henrissat B., Berka R., Cullen D., Rokhsar D.;
RT "Genome sequence of the lignocellulose degrading fungus Phanerochaete
RT chrysosporium strain RP78.";
RL Nat. Biotechnol. 22:695-700(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=16524749; DOI=10.1016/j.fgb.2006.01.003;
RA Vanden Wymelenberg A., Minges P., Sabat G., Martinez D., Aerts A.,
RA Salamov A., Grigoriev I., Shapiro H., Putnam N., Belinky P., Dosoretz C.,
RA Gaskell J., Kersten P., Cullen D.;
RT "Computational analysis of the Phanerochaete chrysosporium v2.0 genome
RT database and mass spectrometry identification of peptides in ligninolytic
RT cultures reveal complex mixtures of secreted proteins.";
RL Fungal Genet. Biol. 43:343-356(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=24853079; DOI=10.1016/j.fgb.2014.05.001;
RA Ohm R.A., Riley R., Salamov A., Min B., Choi I.-G., Grigoriev I.V.;
RT "Genomics of wood-degrading fungi.";
RL Fungal Genet. Biol. 72:82-90(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18854978; DOI=10.1007/s00203-008-0434-y;
RA Duranova M., Spanikova S., Woesten H.A., Biely P., de Vries R.P.;
RT "Two glucuronoyl esterases of Phanerochaete chrysosporium.";
RL Arch. Microbiol. 191:133-140(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19897892; DOI=10.1271/bbb.90486;
RA Duranova M., Hirsch J., Kolenova K., Biely P.;
RT "Fungal glucuronoyl esterases and substrate uronic acid recognition.";
RL Biosci. Biotechnol. Biochem. 73:2483-2487(2009).
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:18854978,
CC ECO:0000269|PubMed:19897892}.
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:18854978,
CC ECO:0000269|PubMed:19897892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:18854978, ECO:0000305|PubMed:19897892};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.82 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:19897892};
CC Vmax=88.4 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-
CC methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:19897892};
CC pH dependence:
CC Optimum pH is 5.0-6.0. {ECO:0000269|PubMed:19897892};
CC Temperature dependence:
CC Optimum temperature is 45-55 degrees Celsius.
CC {ECO:0000269|PubMed:19897892};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18854978}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; AADS01000151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CT88; -.
DR SMR; P0CT88; -.
DR ESTHER; phacr-gce2; Glucuronoyl_esterase.
DR VEuPathDB; FungiDB:AGR57_10612; -.
DR BRENDA; 3.1.1.117; 1380.
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; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..407
FT /note="4-O-methyl-glucuronoyl methylesterase 2"
FT /id="PRO_0000435848"
FT MOTIF 215..220
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 351
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..64
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 216..352
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 248..324
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 407 AA; 44294 MW; 6488B4CF722CC1C8 CRC64;
MAFSWLSFVL LALPVLALAR PSEHEARSLF CSTPSNIPFN DDKLPDPFKF NDGSPVRSFA
DWDCRRQQLS ALIQGYEAGT LPPRPPVVTS TFTKSGTTGN LTVTAGFPGK TITFSSPITF
PTGTAPFGGW PLVIAYGGVS IPIPDGIAVL TYDNSAMAEQ NDQSSRGVGL FFDVYGANAT
ASSMTAWVWG LSRIIDSLEV TPAAHINTAK IAVTGCSRNG KGALMAGAFE ERIALTIPQE
SGSGGDTCWR LSKFEQDSGD VVQQATEIVQ ENVWFSTNFD NYVFNISLLP YDHHELAALV
APRPLISYEN TDFEWLSPLS GFGCMTAAHT VWEAMGIPDK HGFVQVGNHS HCDFPSSLNP
TLFAFFDKFL LGKEANTSIF ETNGLFNGTE WVASQWINWT TPRFTLL
