GCE_NEUCR
ID GCE_NEUCR Reviewed; 394 AA.
AC Q7S1X0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:27600355};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:27600355};
DE Short=GE {ECO:0000303|PubMed:27600355};
DE Flags: Precursor;
GN Name=Cip2 {ECO:0000303|PubMed:27600355}; Synonyms=ce15-1;
GN ORFNames=NCU09445;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27600355; DOI=10.2323/jgam.2016.03.004;
RA Huynh H.H., Arioka M.;
RT "Functional expression and characterization of a glucuronoyl esterase from
RT the fungus Neurospora crassa: identification of novel consensus sequences
RT containing the catalytic triad.";
RL J. Gen. Appl. Microbiol. 62:217-224(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. {ECO:0000269|PubMed:27600355}.
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:27600355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:27600355};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 mM for 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-
CC glucopyranosiduronate {ECO:0000269|PubMed:27600355};
CC Note=kcat is 16.8 sec(-1) with 3-(4-methoxyphenyl) propyl methyl 4-O-
CC methyl-alpha-D-glucopyranosiduronate. {ECO:0000269|PubMed:27600355};
CC pH dependence:
CC Optimum pH is 7. Stable from pH 4 to pH 7.
CC {ECO:0000269|PubMed:27600355};
CC Temperature dependence:
CC Optimum temperature is 40-50 degrees Celsius.
CC {ECO:0000269|PubMed:27600355};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G0RV93}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; CM002242; EAA29361.2; -; Genomic_DNA.
DR RefSeq; XP_958597.2; XM_953504.2.
DR AlphaFoldDB; Q7S1X0; -.
DR SMR; Q7S1X0; -.
DR ESTHER; neucr-q7s1x0; Glucuronoyl_esterase.
DR EnsemblFungi; EAA29361; EAA29361; NCU09445.
DR GeneID; 3874744; -.
DR KEGG; ncr:NCU09445; -.
DR VEuPathDB; FungiDB:NCU09445; -.
DR HOGENOM; CLU_028869_1_1_1; -.
DR InParanoid; Q7S1X0; -.
DR BRENDA; 3.1.1.117; 3627.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; Hydrolase; Lignin degradation; Reference proteome;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..394
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004291006"
FT MOTIF 209..214
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 344
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 29..63
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 210..345
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 242..317
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 394 AA; 41351 MW; 6ECA9F9B84C3D38D CRC64;
MVHLTPALLL ASAAFAAAAP ASQIFERQCS VAGNYPTAAV SKLPDPFTTA AGQKITTKAD
FDCRKAEISK ILQQYELGTY PGKPDKVEGS LSGNTLTVRI TVGSQTVSFS ASIKKPSSGS
GPFPAIIGIG GISIPIPSTV ATITFPNDDF AQQSGTSSRG RGKFYTLFGS SHSAGALIAW
AWGVDRLVDA LEQVQSTSGI DPKRLGVTGC SRNGKGAFVA GALVDRIALT IPQESGAGGA
ACWRISDSEK SAGKNIQTAS QIVTENVWFS PAFNAYTRQT TNIPADHHML AALTVPRGLI
AFENDIDWLG PVSTTACMQA GRLIYKAYGV SNHMGFSLVG GHGHCQFPSS QQSELTSYIN
YFLLKAGTAP GAVERSSAKV DLKSWAPWDV PALS
