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4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.-) (Glucuronoyl esterase) (GE)

 GCE_NEUCR               Reviewed;         394 AA.
Q7S1X0;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 2.
15-MAR-2017, entry version 58.
RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
EC=3.1.1.- {ECO:0000269|PubMed:27600355};
AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:27600355};
Short=GE {ECO:0000303|PubMed:27600355};
Flags: Precursor;
Name=Cip2 {ECO:0000303|PubMed:27600355}; Synonyms=ce15-1;
ORFNames=NCU09445;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=27600355; DOI=10.2323/jgam.2016.03.004;
Huynh H.H., Arioka M.;
"Functional expression and characterization of a glucuronoyl esterase
from the fungus Neurospora crassa: identification of novel consensus
sequences containing the catalytic triad.";
J. Gen. Appl. Microbiol. 62:217-224(2016).
-!- FUNCTION: Glucuronoyl esterase which may play a significant role
in biomass degradation, as it is considered to disconnect
hemicellulose from lignin through the hydrolysis of the ester bond
between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans
and aromatic alcohols of lignin. {ECO:0000269|PubMed:27600355}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 mM for 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-
D-glucopyranosiduronate {ECO:0000269|PubMed:27600355};
Note=kcat is 16.8 sec(-1) with 3-(4-methoxyphenyl) propyl methyl
4-O-methyl-alpha-D-glucopyranosiduronate.
{ECO:0000269|PubMed:27600355};
pH dependence:
Optimum pH is 7. Stable from pH 4 to pH 7.
{ECO:0000269|PubMed:27600355};
Temperature dependence:
Optimum temperature is 40-50 degrees Celsius.
{ECO:0000269|PubMed:27600355};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G0RV93}.
-!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
{ECO:0000305}.
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EMBL; CM002242; EAA29361.2; -; Genomic_DNA.
RefSeq; XP_958597.2; XM_953504.2.
SMR; Q7S1X0; -.
ESTHER; neucr-q7s1x0; Glucuronoyl_esterase.
EnsemblFungi; EAA29361; EAA29361; NCU09445.
GeneID; 3874744; -.
KEGG; ncr:NCU09445; -.
EuPathDB; FungiDB:NCU09445; -.
HOGENOM; HOG000217906; -.
InParanoid; Q7S1X0; -.
OrthoDB; EOG092C1YHO; -.
Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Hydrolase; Lignin degradation;
Reference proteome; Secreted; Serine esterase; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 394 4-O-methyl-glucuronoyl methylesterase.
{ECO:0000255}.
/FTId=PRO_5004291006.
MOTIF 209 214 GXSYXG catalytic site motif.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 211 211 Nucleophile.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 344 344 Proton donor/acceptor.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 215 215 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 257 257 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 265 265 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 308 308 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 29 63 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 210 345 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 242 317 {ECO:0000250|UniProtKB:G2QJR6}.
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


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