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

 GCE_PHACS               Reviewed;         406 AA.
K5XDZ6; I6TB92;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
09-JAN-2013, sequence version 1.
07-JUN-2017, entry version 19.
RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
EC=3.1.1.- {ECO:0000269|PubMed:22924998, ECO:0000269|PubMed:24997793};
AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:22924998};
Short=GCE {ECO:0000303|PubMed:22924998};
Short=GE;
Flags: Precursor;
ORFNames=PHACADRAFT_247750;
Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus)
(Peniophora carnosa).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
NCBI_TaxID=650164;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22924998; DOI=10.1111/j.1467-7652.2012.00735.x;
Tsai A.Y., Canam T., Gorzsas A., Mellerowicz E.J., Campbell M.M.,
Master E.R.;
"Constitutive expression of a fungal glucuronoyl esterase in
Arabidopsis reveals altered cell wall composition and structure.";
Plant Biotechnol. J. 10:1077-1087(2012).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HHB-10118-sp;
PubMed=22937793; DOI=10.1186/1471-2164-13-444;
Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
Grigoriev I.V., Master E.R.;
"Comparative genomics of the white-rot fungi, Phanerochaete carnosa
and P. chrysosporium, to elucidate the genetic basis of the distinct
wood types they colonize.";
BMC Genomics 13:444-444(2012).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24997793; DOI=10.1016/j.phytochem.2014.06.002;
Latha Gandla M., Derba-Maceluch M., Liu X., Gerber L., Master E.R.,
Mellerowicz E.J., Joensson L.J.;
"Expression of a fungal glucuronoyl esterase in Populus: effects on
wood properties and saccharification efficiency.";
Phytochemistry 112:210-220(2015).
-!- 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:22924998,
ECO:0000269|PubMed:24997793}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6. {ECO:0000269|PubMed:22924998};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:22924998};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; JQ972915; AFM93784.1; -; mRNA.
EMBL; JH930468; EKM61262.1; -; Genomic_DNA.
RefSeq; XP_007390689.1; XM_007390627.1.
SMR; K5XDZ6; -.
ESTHER; phacs-gce; Glucuronoyl_esterase.
EnsemblFungi; EKM61262; EKM61262; PHACADRAFT_247750.
GeneID; 18914176; -.
KEGG; pco:PHACADRAFT_247750; -.
InParanoid; K5XDZ6; -.
OrthoDB; EOG092C1YHO; -.
Proteomes; UP000008370; Unassembled WGS sequence.
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; 2.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Lignin degradation; Reference proteome; Secreted; Serine esterase;
Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 406 4-O-methyl-glucuronoyl methylesterase.
/FTId=PRO_5003886404.
MOTIF 215 220 GXSYXG catalytic site motif.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 217 217 Nucleophile.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 351 351 Proton donor/acceptor.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 221 221 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 263 263 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 271 271 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 315 315 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 31 64 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 216 352 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 248 324 {ECO:0000250|UniProtKB:G2QJR6}.
SEQUENCE 406 AA; 44170 MW; EFCB1735157B7EF1 CRC64;
MAFRWLSFLL LALPVLALPQ TSSKEAQSFG CSTPANIPFN DDKLPDPFLF NDGTPVRSLT
DWSCRRQQLA SLIQGYEAGT LPPKPPIVTS TFSQNGLTGN LTVTAGFPGN TTTFSSPVTF
PNGTVPTEGW PLLIAYSGLS IPIPDGIAVL TYDNSAIGEQ NDQTSRGVGQ FFDVYGHNAT
ASAMSAWVWG VSRIIDVLEV TPAAHVNTAK IAVTGCSRDG KGALMAGAFE ERIALTIPQE
SGSGGDTCWR LSKFEQDSGD VVQQATEIVQ ENVWFSTNFD NFVFNISVLP YDHHSLAGLI
APRPMISYEN TDFEWLSPLS GFGCMTAAHP IWEAMGVPDN HGFVQVGNHS HCEFPSDLNP
TLFAFFDKFL LGKEANTTIF ETNEVFNGTV WNPSQWINWT TPTLSH


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