GCE_CERUI
ID GCE_CERUI Reviewed; 474 AA.
AC A0A0A7EQR3;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:25425346};
DE Short=GE {ECO:0000303|PubMed:25425346};
DE Flags: Precursor;
OS Cerrena unicolor (Canker rot fungus) (Daedalea unicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Cerrenaceae; Cerrena.
OX NCBI_TaxID=90312 {ECO:0000312|EMBL:AIY68500.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25425346; DOI=10.1002/bit.25508;
RA d'Errico C., Joergensen J.O., Krogh K.B., Spodsberg N., Madsen R.,
RA Monrad R.N.;
RT "Enzymatic degradation of lignin-carbohydrate complexes (LCCs): model
RT studies using a fungal glucuronoyl esterase from Cerrena unicolor.";
RL Biotechnol. Bioeng. 112:914-922(2015).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26712478; DOI=10.1016/j.jbiotec.2015.12.024;
RA d'Errico C., Boerjesson J., Ding H., Krogh K.B., Spodsberg N., Madsen R.,
RA Monrad R.N.;
RT "Improved biomass degradation using fungal glucuronoyl-esterases-hydrolysis
RT of natural corn fiber substrate.";
RL J. Biotechnol. 219:117-123(2016).
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 (PubMed:25425346, PubMed:26712478).
CC {ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478}.
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:25425346,
CC ECO:0000269|PubMed:26712478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:25425346, ECO:0000305|PubMed:26712478};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 mM for benzyl (methyl 4-O-methyl-alpha-D-glucopyranoside)
CC uronate {ECO:0000269|PubMed:25425346};
CC KM=80 mM for benzyl (methyl alpha-D-glucopyranoside) uronate
CC {ECO:0000269|PubMed:25425346};
CC KM=55 mM for phenylpropyl (methyl alpha-D-glucopyranoside) uronate
CC {ECO:0000269|PubMed:25425346};
CC KM=8.9 mM for phenyl (methyl alpha-D-glucopyranoside) uronate
CC {ECO:0000269|PubMed:25425346};
CC KM=4.6 mM for threo-l-[4-(benzyloxy)-3-methoxyphenyl]-3-hydroxy-
CC 2- (2-methoxyphenoxy) propyl (methyl 4-O-methyl-alpha-D-
CC glucopyranosid) uronate {ECO:0000269|PubMed:26712478};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25425346}.
CC -!- PTM: N-glycosylated (PubMed:25425346). {ECO:0000269|PubMed:25425346}.
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; KM875459; AIY68500.1; -; mRNA.
DR PDB; 6RTV; X-ray; 1.46 A; A/B=95-474.
DR PDB; 6RU1; X-ray; 1.39 A; A/B=95-474.
DR PDB; 6RU2; X-ray; 1.96 A; A/B=95-474.
DR PDB; 6RV7; X-ray; 1.73 A; A/B=95-474.
DR PDB; 6RV8; X-ray; 1.85 A; A/B=18-474.
DR PDB; 6RV9; X-ray; 1.64 A; A/B=95-474.
DR PDBsum; 6RTV; -.
DR PDBsum; 6RU1; -.
DR PDBsum; 6RU2; -.
DR PDBsum; 6RV7; -.
DR PDBsum; 6RV8; -.
DR PDBsum; 6RV9; -.
DR AlphaFoldDB; A0A0A7EQR3; -.
DR SASBDB; A0A0A7EQR3; -.
DR SMR; A0A0A7EQR3; -.
DR ESTHER; cerui-gce; Glucuronoyl_esterase.
DR BRENDA; 3.1.1.117; 8864.
DR SABIO-RK; A0A0A7EQR3; -.
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:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lignin degradation;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..474
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_5002038279"
FT DOMAIN 19..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 61..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 284..289
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT COMPBIAS 64..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 420
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 285..421
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 317..393
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:6RU1"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6RU1"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:6RU1"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 387..403
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6RU1"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:6RU1"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:6RU1"
SQ SEQUENCE 474 AA; 49910 MW; 7E1F16E59E5E3413 CRC64;
MFKPSFVALA LVSYATAQAS APQWGQCGGI GWTGPTACPS GWACQQLNAY YSQCLQGAAP
APARTTAAPP PPPATTAAPP PPTTSAPTGS SPVAGACGAI ASTVPNYNNA KLPDPFTFAN
GTALRTKADW SCRRAEISAL IQNYEAGTLP PKPPVVTASF SKSGNTGTLA ITAGLSNSQT
IKFSPTISYP SGTPPANGWP LIIAYEGGSI PIPAGVATLT YSNSDMAQQN SASSRGQGLF
YQLYGSTHSA SAMTAWVWGV SRIIDALEMT PTAQINTQRI GVTGCSRDGK GALMAGAFEE
RIALTIPQES GSGGDACWRL SKYEIDNGNQ VQDAVEIVGE NVWFSTNFNN YVQKLPTVPE
DHHLLAAMVA PRAMISFENT DYLWLSPMSS FGCMTAAHTV WQGLGIADSH GFAQVGGHAH
CAWPSSLTPQ LNAFINRFLL DQSATTNVFT TNNQFGKVQW NAANWITWTT PTLT
