GCE_SCHCM
ID GCE_SCHCM Reviewed; 393 AA.
AC D8QLP9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:16876163};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:16876163};
DE Short=GE {ECO:0000303|PubMed:17678650};
DE Flags: Precursor;
GN ORFNames=SCHCODRAFT_238770;
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210;
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
RN [2]
RP PROTEIN SEQUENCE OF 21-40 AND 214-228, AND PROBABLE PYROGLUTAMATE FORMATION
RP AT GLN-20.
RC STRAIN=ATCC 38548;
RX PubMed=17678650; DOI=10.1016/j.febslet.2007.07.041;
RA Li X.L., Spanikova S., de Vries R.P., Biely P.;
RT "Identification of genes encoding microbial glucuronoyl esterases.";
RL FEBS Lett. 581:4029-4035(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 38548;
RX PubMed=16876163; DOI=10.1016/j.febslet.2006.07.033;
RA Spanikova S., Biely P.;
RT "Glucuronoyl esterase--novel carbohydrate esterase produced by
RT Schizophyllum commune.";
RL FEBS Lett. 580:4597-4601(2006).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22844600; DOI=10.1155/2012/951267;
RA Wong D.W., Chan V.J., McCormack A.A., Hirsch J., Biely P.;
RT "Functional cloning and expression of the Schizophyllum commune glucuronoyl
RT esterase gene and characterization of the recombinant enzyme.";
RL Biotechnol. Res. Int. 2012:951267-951267(2012).
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:16876163}.
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:16876163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:16876163};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside (purified enzyme)
CC {ECO:0000269|PubMed:16876163};
CC KM=0.25 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside (recombinant enzyme)
CC {ECO:0000269|PubMed:22844600};
CC Vmax=4.4 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-
CC methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (purified
CC enzyme) {ECO:0000269|PubMed:16876163};
CC Vmax=16.3 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-
CC methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
CC (recombinant enzyme) {ECO:0000269|PubMed:22844600};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:16876163};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:16876163};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16876163}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; GL377318; EFI91386.1; -; Genomic_DNA.
DR RefSeq; XP_003026289.1; XM_003026243.1.
DR AlphaFoldDB; D8QLP9; -.
DR SMR; D8QLP9; -.
DR STRING; 578458.D8QLP9; -.
DR ESTHER; schcm-gce; Glucuronoyl_esterase.
DR EnsemblFungi; EFI91386; EFI91386; SCHCODRAFT_238770.
DR GeneID; 9589114; -.
DR KEGG; scm:SCHCODRAFT_238770; -.
DR eggNOG; ENOG502QS8Y; Eukaryota.
DR HOGENOM; CLU_028869_1_1_1; -.
DR InParanoid; D8QLP9; -.
DR OMA; GHAHCAW; -.
DR OrthoDB; 941049at2759; -.
DR BRENDA; 3.1.1.117; 5611.
DR SABIO-RK; D8QLP9; -.
DR Proteomes; UP000007431; 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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lignin degradation; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000305|PubMed:17678650"
FT CHAIN 20..393
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_5003121041"
FT MOTIF 203..208
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 339
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:17678650"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 22..56
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 204..340
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 236..312
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 393 AA; 41773 MW; 4AEFD7FE7DD53993 CRC64;
MKLSAALLAI AAFANVASAQ DCDTPATVSG YSNSALPDPF TFNDGSPVTT AEDWECRRSQ
ILALIQGYES GAAPPEPESV TGTASGNSLS VQVSYGGKSI TFNNSITYPS GTAPAEGWPV
IIAYEFPSLP IPSNVATLSF QNSAMGKQDS TSSRGQGLFY DLYGSSSNAS AMTAWAWGVS
RIIDAIESTP DAKLNPAAVG VTGCSRNGKG ALMAGALEPR VALTLPQESG SGGDACWRLS
RYEEQQGSQV QTATEIVGEN CWFSAGFDQY VNNLDSLPYD HHLLAALVAP RGLISYANTD
YVWLSGMSSF GCMTAAHAVY EALGVPENHG FEQVGGHSHC QWPSQLDGSL NAFINKFLLG
QDVSTDYFES NNQFNGVTWS ESQWINWETP TLN
