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4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.-) (Glucuronoyl esterase 1) (GE1)

 GCE1_PODAN              Reviewed;         481 AA.
B2ABS0;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 1.
25-OCT-2017, entry version 47.
RecName: Full=4-O-methyl-glucuronoyl methylesterase {ECO:0000305};
EC=3.1.1.- {ECO:0000269|PubMed:24531271};
AltName: Full=Glucuronoyl esterase 1 {ECO:0000303|PubMed:24531271};
Short=GE1 {ECO:0000303|PubMed:24531271};
Flags: Precursor;
Name=ge1 {ECO:0000303|PubMed:24531271}; OrderedLocusNames=Pa_0_910;
ORFNames=PODANS_0_910;
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
(Pleurage anserina).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
Podospora.
NCBI_TaxID=515849;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
Anthouard V., Grossetete S., Khalili H., Coppin E.,
Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
Debuchy R., Wincker P., Weissenbach J., Silar P.;
"The genome sequence of the model ascomycete fungus Podospora
anserina.";
Genome Biol. 9:R77.1-R77.22(2008).
[2]
GENOME REANNOTATION.
STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
PubMed=24558260; DOI=10.1534/genetics.113.159988;
Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E.,
Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
"Maintaining two mating types: Structure of the mating type locus and
its role in heterokaryosis in Podospora anserina.";
Genetics 197:421-432(2014).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=24531271; DOI=10.1007/s00253-014-5542-9;
Katsimpouras C., Benarouche A., Navarro D., Karpusas M.,
Dimarogona M., Berrin J.G., Christakopoulos P., Topakas E.;
"Enzymatic synthesis of model substrates recognized by glucuronoyl
esterases from Podospora anserina and Myceliophthora thermophila.";
Appl. Microbiol. Biotechnol. 98:5507-5516(2014).
-!- 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:24531271}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.6 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-
glucopyranosyluronate)-beta-D-xylopyranoside
{ECO:0000269|PubMed:24531271};
KM=2.66 mM for trans-3-phenyl-2-propen-1-yl D-
glucopyranosyluronate {ECO:0000269|PubMed:24531271};
KM=0.94 mM for 3-phenyl-1-propyl D-glucopyranosyluronate
{ECO:0000269|PubMed:24531271};
KM=1.34 mM for 3-(4-hydroxyphenyl)-1-propyl D-
glucopyranosyluronate {ECO:0000269|PubMed:24531271};
Note=kcat is 16.2 min(-1) with 4-nitrophenyl 2-O-(methyl-4-O-
methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside,
315.3 min(-1) with trans-3-phenyl-2-propen-1-yl D-
glucopyranosyluronate, 46.5 min(-1) with 3-phenyl-1-propyl D-
glucopyranosyluronate and 11.4 min(-1) with 3-(4-hydroxyphenyl)-
1-propyl D-glucopyranosyluronate as substrate.
{ECO:0000269|PubMed:24531271};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
{ECO:0000305}.
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EMBL; CU633446; CAP60908.1; -; Genomic_DNA.
EMBL; FO904937; CDP24923.1; -; Genomic_DNA.
RefSeq; XP_001903136.1; XM_001903101.1.
ProteinModelPortal; B2ABS0; -.
SMR; B2ABS0; -.
CAZy; CBM1; Carbohydrate-Binding Module Family 1.
ESTHER; podan-b2abs0; Glucuronoyl_esterase.
PRIDE; B2ABS0; -.
EnsemblFungi; CAP60908; CAP60908; PODANS_0_910.
GeneID; 6187208; -.
KEGG; pan:PODANSg148; -.
eggNOG; ENOG410IFIE; Eukaryota.
eggNOG; ENOG410XRBM; LUCA.
OrthoDB; EOG092C1YHO; -.
Proteomes; UP000001197; Chromosome 2.
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; 2.
SUPFAM; SSF57180; SSF57180; 1.
PROSITE; PS00562; CBM1_1; 1.
PROSITE; PS51164; CBM1_2; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Hydrolase; Lignin degradation;
Reference proteome; Secreted; Serine esterase; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 481 4-O-methyl-glucuronoyl methylesterase.
/FTId=PRO_5002772631.
DOMAIN 23 59 CBM1. {ECO:0000255|PROSITE-
ProRule:PRU00597}.
MOTIF 291 296 GXSYXG catalytic site motif.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 293 293 Nucleophile.
{ECO:0000250|UniProtKB:G2QJR6}.
ACT_SITE 427 427 Proton donor/acceptor.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 297 297 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 339 339 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 347 347 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
BINDING 391 391 Substrate.
{ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 108 143 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 292 428 {ECO:0000250|UniProtKB:G2QJR6}.
DISULFID 324 400 {ECO:0000250|UniProtKB:G2QJR6}.
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


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