GCE1_PODAN
ID GCE1_PODAN Reviewed; 481 AA.
AC B2ABS0;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
DE EC=3.1.1.117 {ECO:0000269|PubMed:24531271};
DE AltName: Full=Glucuronoyl esterase 1 {ECO:0000303|PubMed:24531271};
DE Short=GE1 {ECO:0000303|PubMed:24531271};
DE Flags: Precursor;
GN Name=ge1 {ECO:0000303|PubMed:24531271}; OrderedLocusNames=Pa_0_910;
GN ORFNames=PODANS_0_910;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24531271; DOI=10.1007/s00253-014-5542-9;
RA Katsimpouras C., Benarouche A., Navarro D., Karpusas M., Dimarogona M.,
RA Berrin J.G., Christakopoulos P., Topakas E.;
RT "Enzymatic synthesis of model substrates recognized by glucuronoyl
RT esterases from Podospora anserina and Myceliophthora thermophila.";
RL Appl. Microbiol. Biotechnol. 98:5507-5516(2014).
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. {ECO:0000269|PubMed:24531271}.
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:24531271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000305|PubMed:24531271};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
CC glucopyranosyluronate)-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:24531271};
CC KM=2.66 mM for trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
CC {ECO:0000269|PubMed:24531271};
CC KM=0.94 mM for 3-phenyl-1-propyl D-glucopyranosyluronate
CC {ECO:0000269|PubMed:24531271};
CC KM=1.34 mM for 3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate
CC {ECO:0000269|PubMed:24531271};
CC Note=kcat is 16.2 min(-1) with 4-nitrophenyl 2-O-(methyl-4-O-methyl-
CC alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside, 315.3 min(-1)
CC with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate, 46.5 min(-
CC 1) with 3-phenyl-1-propyl D-glucopyranosyluronate and 11.4 min(-1)
CC with 3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate as
CC substrate. {ECO:0000269|PubMed:24531271};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000305}.
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DR EMBL; CU633446; CAP60908.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP24923.1; -; Genomic_DNA.
DR RefSeq; XP_001903136.1; XM_001903101.1.
DR AlphaFoldDB; B2ABS0; -.
DR SMR; B2ABS0; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR ESTHER; podan-b2abs0; Glucuronoyl_esterase.
DR EnsemblFungi; CAP60908; CAP60908; PODANS_0_910.
DR GeneID; 6187208; -.
DR KEGG; pan:PODANSg148; -.
DR VEuPathDB; FungiDB:PODANS_0_910; -.
DR eggNOG; ENOG502QS8Y; Eukaryota.
DR HOGENOM; CLU_028869_1_1_1; -.
DR OrthoDB; 941049at2759; -.
DR BRENDA; 3.1.1.117; 4930.
DR Proteomes; UP000001197; Chromosome 2.
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; Reference proteome;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..481
FT /note="4-O-methyl-glucuronoyl methylesterase"
FT /id="PRO_5002772631"
FT DOMAIN 23..59
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT MOTIF 291..296
FT /note="GXSYXG catalytic site motif"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT ACT_SITE 427
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 108..143
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 292..428
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
FT DISULFID 324..400
FT /evidence="ECO:0000250|UniProtKB:G2QJR6"
SQ SEQUENCE 481 AA; 50942 MW; FC713FA570BD406B CRC64;
MVSQTVVSSL LVVLGAAGVR AQQRQSLWGQ CGGSGWSGPT LCVDGAWCNP QNQWYHQCIP
GSGPTTAQPQ VPTTTARPTT TLVTSVVSST TSPSGPVVTN PPVNPGTCPN TPSGLGTPVA
NQLNDPFTFH NGNKVTSKAD WACRQREISE LLQRYELGTL PPKPSSVTAS FSGSTLSISV
SEGGKSISFT VSINNRPSGA GPHPAIINFG TFGASLPVPA GVATINFNND DIAQQQGGSS
RGRGKFYDLY GSSHSAGALT AWAWGVSRIV DALELTQAQT GIDPTRLGVT GCSRNGKGAI
VAGALEPRIA LTLPQESGAG GSGCWRIATW QKNNGQNVQD STQIVQENVW FSPNFNSYVN
NVNQLPFDHH LLAGLIAPRA LYVMENVDME WLGKISTYGC MGIARKQWEA LGALDNFGYS
QVGGNSHCSF PSSQQGSELN AFIEKFLLKR SGGNTNIFRS TQTHSSFNLN NWSPWAVPSL
N
