GCE_PHACS
ID GCE_PHACS Reviewed; 406 AA.
AC K5XDZ6; I6TB92;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:22924998, ECO:0000269|PubMed:24997793};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:22924998};
DE Short=GCE {ECO:0000303|PubMed:22924998};
DE Short=GE;
DE Flags: Precursor;
GN ORFNames=PHACADRAFT_247750;
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22924998; DOI=10.1111/j.1467-7652.2012.00735.x;
RA Tsai A.Y., Canam T., Gorzsas A., Mellerowicz E.J., Campbell M.M.,
RA Master E.R.;
RT "Constitutive expression of a fungal glucuronoyl esterase in Arabidopsis
RT reveals altered cell wall composition and structure.";
RL Plant Biotechnol. J. 10:1077-1087(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp;
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24997793; DOI=10.1016/j.phytochem.2014.06.002;
RA Latha Gandla M., Derba-Maceluch M., Liu X., Gerber L., Master E.R.,
RA Mellerowicz E.J., Joensson L.J.;
RT "Expression of a fungal glucuronoyl esterase in Populus: effects on wood
RT properties and saccharification efficiency.";
RL Phytochemistry 112:210-220(2015).
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:22924998,
CC ECO:0000269|PubMed:24997793}.
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:22924998,
CC ECO:0000269|PubMed:24997793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:22924998, ECO:0000305|PubMed:24997793};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:22924998};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:22924998};
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; JQ972915; AFM93784.1; -; mRNA.
DR EMBL; JH930468; EKM61262.1; -; Genomic_DNA.
DR RefSeq; XP_007390689.1; XM_007390627.1.
DR AlphaFoldDB; K5XDZ6; -.
DR SMR; K5XDZ6; -.
DR ESTHER; phacs-gce; Glucuronoyl_esterase.
DR EnsemblFungi; EKM61262; EKM61262; PHACADRAFT_247750.
DR GeneID; 18914176; -.
DR KEGG; pco:PHACADRAFT_247750; -.
DR HOGENOM; CLU_028869_1_1_1; -.
DR InParanoid; K5XDZ6; -.
DR OrthoDB; 941049at2759; -.
DR BRENDA; 3.1.1.117; 16451.
DR Proteomes; UP000008370; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..406
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_5003886404"
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 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
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 406 AA; 44170 MW; EFCB1735157B7EF1 CRC64;
MAFRWLSFLL LALPVLALPQ TSSKEAQSFG CSTPANIPFN DDKLPDPFLF NDGTPVRSLT
DWSCRRQQLA SLIQGYEAGT LPPKPPIVTS TFSQNGLTGN LTVTAGFPGN TTTFSSPVTF
PNGTVPTEGW PLLIAYSGLS IPIPDGIAVL TYDNSAIGEQ NDQTSRGVGQ FFDVYGHNAT
ASAMSAWVWG VSRIIDVLEV TPAAHVNTAK IAVTGCSRDG KGALMAGAFE ERIALTIPQE
SGSGGDTCWR LSKFEQDSGD VVQQATEIVQ ENVWFSTNFD NFVFNISVLP YDHHSLAGLI
APRPMISYEN TDFEWLSPLS GFGCMTAAHP IWEAMGVPDN HGFVQVGNHS HCEFPSDLNP
TLFAFFDKFL LGKEANTTIF ETNEVFNGTV WNPSQWINWT TPTLSH
