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

 GCE_HYPJQ               Reviewed;         460 AA.
G0RV93; Q7Z9N1;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
25-OCT-2017, entry version 35.
RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
EC=3.1.1.- {ECO:0000269|PubMed:17678650};
AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:17678650};
Short=GE {ECO:0000303|PubMed:17678650};
Flags: Precursor;
Name=cip2 {ECO:0000303|PubMed:12788920}; ORFNames=TRIREDRAFT_123940;
Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
Trichoderma.
NCBI_TaxID=431241;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, AND DOMAIN.
STRAIN=QM6a;
PubMed=12788920; DOI=10.1074/jbc.M304750200;
Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S.,
Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J.,
Kelley A.S., Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A.,
Teunissen P.J.M., Yao J., Ward M.;
"Transcriptional regulation of biomass-degrading enzymes in the
filamentous fungus Trichoderma reesei.";
J. Biol. Chem. 278:31988-31997(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=QM6a;
PubMed=18454138; DOI=10.1038/nbt1403;
Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M.,
Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D.,
Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P.,
Han C.S., Ho I., Larrondo L.F., de Leon A.L., Magnuson J.K.,
Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A.,
Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L.,
Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R.,
Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M.,
Dunn-Coleman N., Ward M., Brettin T.S.;
"Genome sequencing and analysis of the biomass-degrading fungus
Trichoderma reesei (syn. Hypocrea jecorina).";
Nat. Biotechnol. 26:553-560(2008).
[3]
PROTEIN SEQUENCE OF 19-28, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND PYROGLUTAMATE FORMATION
AT GLN-18.
PubMed=17678650; DOI=10.1016/j.febslet.2007.07.041;
Li X.L., Spanikova S., de Vries R.P., Biely P.;
"Identification of genes encoding microbial glucuronoyl esterases.";
FEBS Lett. 581:4029-4035(2007).
[4]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 90-460, PUTATIVE ACTIVE
SITE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-447.
PubMed=21661060; DOI=10.1002/prot.23088;
Pokkuluri P.R., Duke N.E., Wood S.J., Cotta M.A., Li X.L., Biely P.,
Schiffer M.;
"Structure of the catalytic domain of glucuronoyl esterase Cip2 from
Hypocrea jecorina.";
Proteins 79:2588-2592(2011).
-!- 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. Does not hydrolyze substrates of
other carbohydrate esterases such as acetylxylan esterase, acetyl
esterase and feruloyl esterase. {ECO:0000269|PubMed:12788920,
ECO:0000269|PubMed:17678650}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.5 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
glucopyranosyluronate)-beta-D-xylopyranoside
{ECO:0000269|PubMed:17678650};
Vmax=5.5 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-
O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
{ECO:0000269|PubMed:17678650};
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:17678650};
Temperature dependence:
Optimum temperature is 40-60 degrees Celsius.
{ECO:0000269|PubMed:17678650};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- INDUCTION: Induced in the presence of lactose or sophorose.
{ECO:0000269|PubMed:12788920}.
-!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
{ECO:0000305}.
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EMBL; AY281368; AAP57749.1; -; mRNA.
EMBL; GL985083; EGR44948.1; -; Genomic_DNA.
RefSeq; XP_006969119.1; XM_006969057.1.
PDB; 3PIC; X-ray; 1.90 A; A/B/C=90-460.
PDBsum; 3PIC; -.
ProteinModelPortal; G0RV93; -.
SMR; G0RV93; -.
CAZy; CBM1; Carbohydrate-Binding Module Family 1.
ESTHER; hypjq-cip2; Glucuronoyl_esterase.
iPTMnet; G0RV93; -.
EnsemblFungi; EGR44948; EGR44948; TRIREDRAFT_123940.
GeneID; 18483767; -.
KEGG; tre:TRIREDRAFT_123940; -.
EuPathDB; FungiDB:TRIREDRAFT_123940; -.
OrthoDB; EOG092C1YHO; -.
Proteomes; UP000008984; 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:0030248; F:cellulose binding; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR035971; CBD_sf.
InterPro; IPR000254; Cellulose-bd_dom_fun.
Pfam; PF00734; CBM_1; 1.
ProDom; PD001821; CBD_fun; 1.
SMART; SM00236; fCBD; 1.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF57180; SSF57180; 1.
PROSITE; PS00562; CBM1_1; 1.
PROSITE; PS51164; CBM1_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lignin degradation;
Pyrrolidone carboxylic acid; Reference proteome; Secreted;
Serine esterase; Signal.
SIGNAL 1 17 {ECO:0000305|PubMed:17678650}.
CHAIN 18 460 4-O-methyl-glucuronoyl methylesterase.
/FTId=PRO_0000419175.
DOMAIN 18 53 CBM1. {ECO:0000255|PROSITE-
ProRule:PRU00597}.
MOTIF 276 281 GXSYXG catalytic site motif.
{ECO:0000305|PubMed:21661060}.
COMPBIAS 65 83 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
ACT_SITE 278 278 Nucleophile.
{ECO:0000305|PubMed:21661060}.
ACT_SITE 411 411 Proton donor/acceptor.
{ECO:0000305|PubMed:21661060}.
BINDING 282 282 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 324 324 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 332 332 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 375 375 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
MOD_RES 18 18 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:17678650}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21661060}.
DISULFID 96 131 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 277 412 {ECO:0000269|PubMed:21661060}.
DISULFID 309 384 {ECO:0000269|PubMed:21661060}.
HELIX 126 143 {ECO:0000244|PDB:3PIC}.
STRAND 153 160 {ECO:0000244|PDB:3PIC}.
STRAND 163 170 {ECO:0000244|PDB:3PIC}.
STRAND 173 182 {ECO:0000244|PDB:3PIC}.
STRAND 185 187 {ECO:0000244|PDB:3PIC}.
STRAND 189 197 {ECO:0000244|PDB:3PIC}.
STRAND 209 213 {ECO:0000244|PDB:3PIC}.
HELIX 215 218 {ECO:0000244|PDB:3PIC}.
HELIX 224 226 {ECO:0000244|PDB:3PIC}.
HELIX 231 236 {ECO:0000244|PDB:3PIC}.
HELIX 244 261 {ECO:0000244|PDB:3PIC}.
HELIX 263 265 {ECO:0000244|PDB:3PIC}.
STRAND 267 277 {ECO:0000244|PDB:3PIC}.
HELIX 279 290 {ECO:0000244|PDB:3PIC}.
STRAND 294 301 {ECO:0000244|PDB:3PIC}.
TURN 304 307 {ECO:0000244|PDB:3PIC}.
HELIX 310 318 {ECO:0000244|PDB:3PIC}.
HELIX 326 329 {ECO:0000244|PDB:3PIC}.
TURN 330 332 {ECO:0000244|PDB:3PIC}.
HELIX 338 342 {ECO:0000244|PDB:3PIC}.
TURN 343 345 {ECO:0000244|PDB:3PIC}.
HELIX 347 349 {ECO:0000244|PDB:3PIC}.
HELIX 354 359 {ECO:0000244|PDB:3PIC}.
STRAND 364 369 {ECO:0000244|PDB:3PIC}.
HELIX 374 376 {ECO:0000244|PDB:3PIC}.
HELIX 378 394 {ECO:0000244|PDB:3PIC}.
HELIX 398 400 {ECO:0000244|PDB:3PIC}.
STRAND 401 404 {ECO:0000244|PDB:3PIC}.
HELIX 416 418 {ECO:0000244|PDB:3PIC}.
HELIX 419 429 {ECO:0000244|PDB:3PIC}.
HELIX 448 451 {ECO:0000244|PDB:3PIC}.
SEQUENCE 460 AA; 48296 MW; D889B2C9199C0962 CRC64;
MASRFFALLL LAIPIQAQSP VWGQCGGIGW SGPTTCVGGA TCVSYNPYYS QCIPSTQASS
SIASTTLVTS FTTTTATRTS ASTPPASSTG AGGATCSALP GSITLRSNAK LNDLFTMFNG
DKVTTKDKFS CRQAEMSELI QRYELGTLPG RPSTLTASFS GNTLTINCGE AGKSISFTVT
ITYPSSGTAP YPAIIGYGGG SLPAPAGVAM INFNNDNIAA QVNTGSRGQG KFYDLYGSSH
SAGAMTAWAW GVSRVIDALE LVPGARIDTT KIGVTGCSRN GKGAMVAGAF EKRIVLTLPQ
ESGAGGSACW RISDYLKSQG ANIQTASEII GEDPWFSTTF NSYVNQVPVL PFDHHSLAAL
IAPRGLFVID NNIDWLGPQS CFGCMTAAHM AWQALGVSDH MGYSQIGAHA HCAFPSNQQS
QLTAFVQKFL LGQSTNTAIF QSDFSANQSQ WIDWTTPTLS


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