GCE1_SODAL
ID GCE1_SODAL Reviewed; 496 AA.
AC A0A1D8EJG8;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase 1 {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:27397104, ECO:0000269|PubMed:28429057};
DE AltName: Full=Glucuronoyl esterase 1;
DE Short=GE1;
DE Flags: Precursor;
OS Sodiomyces alcalophilus (Acremonium alcalophilum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=398408;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 90507 / BCRC 33522 / CBS 114.92 / JCM 7366 / KCTC 16719;
RX PubMed=27397104; DOI=10.1002/1873-3468.12290;
RA Arnling Baath J., Giummarella N., Klaubauf S., Lawoko M., Olsson L.;
RT "A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-
RT carbohydrate ester bonds.";
RL FEBS Lett. 590:2611-2618(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28429057; DOI=10.1007/s00253-017-8266-9;
RA Huettner S., Klaubauf S., de Vries R.P., Olsson L.;
RT "Characterisation of three fungal glucuronoyl esterases on glucuronic acid
RT ester model compounds.";
RL Appl. Microbiol. Biotechnol. 101:5301-5311(2017).
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 (PubMed:27397104). Cleaves native lignin-
CC carbohydrate (LC) ester bonds from LC complex preparations of spruce
CC (softwood) and birch (hardwood), containing mainly hemicelluloses with
CC partially acetylated glucomannans in spruce and partially acetylated
CC xylan in birch (PubMed:27397104). Can hydrolyze benzyl glucuronic acid
CC (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree
CC methyl glucuronic acid (MeGlcA) in vitro (PubMed:28429057).
CC {ECO:0000269|PubMed:27397104, ECO:0000269|PubMed:28429057}.
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:27397104,
CC ECO:0000269|PubMed:28429057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:27397104, ECO:0000305|PubMed:28429057};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for benzyl glucuronic acid {ECO:0000269|PubMed:28429057};
CC Vmax=0.9 umol/min/mg enzyme for benzyl glucuronic acid
CC {ECO:0000269|PubMed:28429057};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0CT87}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KX898021; AOT21131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8EJG8; -.
DR SMR; A0A1D8EJG8; -.
DR ESTHER; acram-a0a1d8ejg8; Glucuronoyl_esterase.
DR BRENDA; 3.1.1.117; 16450.
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 Disulfide bond; Hydrolase; Lignin degradation; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..496
FT /note="4-O-methyl-glucuronoyl methylesterase 1"
FT /id="PRO_5009106681"
FT DOMAIN 20..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 57..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 306..311
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT COMPBIAS 57..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 442
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 129..163
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 307..443
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 339..415
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 496 AA; 51568 MW; D15C40976605389F CRC64;
MKSTVASALL VLAGTAVQAQ SGPWQQCGGI GWQGPFTCVS GHTCQVLNDW YHQCVPGGGP
SPPPTSPPPT TPPPTSPPPT SPPPTSPPPT SPPPTSPPPT SPPPTSPPPT SPPPTSPPPT
SPPPSSGSCP STPGGLGSGN QRLPDPFTFH NGNTVTSAAD FQCRQREVSS LIQQYELGQF
PAPPQSVTSS YSGNTLSITV SDQGRSISFS VSISGGSGSK SPAIIAYGAP SIPVPNGVAT
IRFNNDDIAA QQSGSSRGQG KFYNLYGSGH SAGAMTAWAW GVARIIDALE KTPAAGIDPT
RVGVTGCSRN GKGAMVAGAL EPRIALTIPQ ESGSGGSACW RISNWQGQQG QNVQTPAQII
TENVWLGPVF NNHANNVNAL PFDHHQLAGL IAPRALYVIE NSDMEWLGWT ATYGCMAAAR
TQWEALGALD NFGFSQVGGN QHCSFNSGKQ SAELNAFINK FLLQSGGGTT SILRTERNHG
SFNLAEWTPW NVPNLR
