GCE1_PHACR
ID GCE1_PHACR Reviewed; 472 AA.
AC P0CT87;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase 1 {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:18854978, ECO:0000269|PubMed:19897892, ECO:0000269|PubMed:28429057};
DE AltName: Full=Glucuronoyl esterase 1 {ECO:0000303|PubMed:18854978};
DE Short=GE1 {ECO:0000303|PubMed:18854978};
DE Flags: Precursor;
GN ORFNames=e_gw1.18.61.1, e_gwh2.18.77.1;
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).
RN [6]
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 (PubMed:18854978, PubMed:19897892). Can hydrolyze
CC benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and
CC to a lower degree methyl glucuronic acid (MeGlcA) in vitro
CC (PubMed:28429057). {ECO:0000269|PubMed:18854978,
CC ECO:0000269|PubMed:19897892, 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:18854978,
CC ECO:0000269|PubMed:19897892, ECO:0000269|PubMed:28429057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:18854978, ECO:0000305|PubMed:19897892,
CC ECO:0000305|PubMed:28429057};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.83 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:19897892};
CC KM=2.9 mM for benzyl glucuronic acid {ECO:0000269|PubMed:28429057};
CC Vmax=14.2 umol/min/mg enzyme for 4-nitrophenyl 2-O-(methyl-4-O-
CC methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:19897892};
CC Vmax=0.44 umol/min/mg enzyme for benzyl glucuronic acid
CC {ECO:0000269|PubMed:28429057};
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; AADS01000169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CT87; -.
DR SMR; P0CT87; -.
DR ESTHER; phacr-gce1; Glucuronoyl_esterase.
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: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 Disulfide bond; Glycoprotein; Hydrolase; Lignin degradation; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..472
FT /note="4-O-methyl-glucuronoyl methylesterase 1"
FT /id="PRO_0000435847"
FT DOMAIN 21..56
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 62..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 282..287
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT COMPBIAS 75..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 418
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 97..131
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 283..419
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 315..391
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 472 AA; 49192 MW; 7C3C6263A62B3980 CRC64;
MKSAAYLAAL AAVLPAYVNA QAQEWGQCGG IGWTGATTCV SGTVCTVLNP YYSQCLPGTA
TTAPPPPPPP PTSVSSSSSS STSSAPPSGP SGTSPTCSVA STIPGFSNAA LPNPFVFNDG
SPVQSKADFT CRQQQILALI QGYEAGALPG PPQSVTASFS KSGSTGTLSI TVTDNGKSIS
FAPTISIPSG TPPANGWPLV IAFEGGSIPI PAGIAKLTYS NSDMAQQTDT SSRGKGLFYN
LYGSGATASA MTAWAWGVSR IIDALEKTPS AQINTQRIAV TGCSRDGKGA LMAGALEPRI
ALTIPQESGS GGDTCWRLSK AESDQGHQVQ TATEIVTENV WFSTNFNNYV NNLNVLPYDH
HMLMALVAPR ALVSFENTDY TWLSPMSAWG CVNAAHTVFS ALGVADHHGF AQVGGHAHCA
WPDSLTPSLN AFFNRFLLDQ NVDTNVFTTN NQFGGATWTQ SSWINWSTPT LS
