GCE_HYPJQ
ID GCE_HYPJQ Reviewed; 460 AA.
AC G0RV93; Q7Z9N1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:17678650};
DE AltName: Full=Glucuronoyl esterase {ECO:0000303|PubMed:17678650};
DE Short=GE {ECO:0000303|PubMed:17678650};
DE Flags: Precursor;
GN Name=cip2 {ECO:0000303|PubMed:12788920}; ORFNames=TRIREDRAFT_123940;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, AND DOMAIN.
RC STRAIN=QM6a;
RX PubMed=12788920; DOI=10.1074/jbc.m304750200;
RA Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S.,
RA Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S.,
RA Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M.,
RA Yao J., Ward M.;
RT "Transcriptional regulation of biomass-degrading enzymes in the filamentous
RT fungus Trichoderma reesei.";
RL J. Biol. Chem. 278:31988-31997(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [3]
RP PROTEIN SEQUENCE OF 19-28, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PYROGLUTAMATE FORMATION AT GLN-18.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 90-460, PUTATIVE ACTIVE SITE,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-447.
RX PubMed=21661060; DOI=10.1002/prot.23088;
RA Pokkuluri P.R., Duke N.E., Wood S.J., Cotta M.A., Li X.L., Biely P.,
RA Schiffer M.;
RT "Structure of the catalytic domain of glucuronoyl esterase Cip2 from
RT Hypocrea jecorina.";
RL Proteins 79:2588-2592(2011).
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. Does not hydrolyze substrates of other carbohydrate
CC esterases such as acetylxylan esterase, acetyl esterase and feruloyl
CC esterase. {ECO:0000269|PubMed:12788920, ECO:0000269|PubMed:17678650}.
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:17678650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:17678650};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:17678650};
CC Vmax=5.5 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-
CC methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:17678650};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:17678650};
CC Temperature dependence:
CC Optimum temperature is 40-60 degrees Celsius.
CC {ECO:0000269|PubMed:17678650};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Induced in the presence of lactose or sophorose.
CC {ECO:0000269|PubMed:12788920}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; AY281368; AAP57749.1; -; mRNA.
DR EMBL; GL985083; EGR44948.1; -; Genomic_DNA.
DR RefSeq; XP_006969119.1; XM_006969057.1.
DR PDB; 3PIC; X-ray; 1.90 A; A/B/C=90-460.
DR PDBsum; 3PIC; -.
DR AlphaFoldDB; G0RV93; -.
DR SMR; G0RV93; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR ESTHER; hypjq-cip2; Glucuronoyl_esterase.
DR iPTMnet; G0RV93; -.
DR EnsemblFungi; EGR44948; EGR44948; TRIREDRAFT_123940.
DR GeneID; 18483767; -.
DR KEGG; tre:TRIREDRAFT_123940; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_123940; -.
DR eggNOG; ENOG502QS8Y; Eukaryota.
DR HOGENOM; CLU_028869_1_1_1; -.
DR BRENDA; 3.1.1.117; 6451.
DR Proteomes; UP000008984; 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:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lignin degradation; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000305|PubMed:17678650"
FT CHAIN 18..460
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_0000419175"
FT DOMAIN 18..53
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT MOTIF 276..281
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000305|PubMed:21661060"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:21661060"
FT ACT_SITE 411
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:21661060"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:17678650"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21661060"
FT DISULFID 96..131
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 277..412
FT /evidence="ECO:0000269|PubMed:21661060"
FT DISULFID 309..384
FT /evidence="ECO:0000269|PubMed:21661060"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:3PIC"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:3PIC"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:3PIC"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 378..394
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:3PIC"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:3PIC"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:3PIC"
SQ 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
