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Database: UniProt
Entry: J4H1Q9_9APHY
LinkDB: J4H1Q9_9APHY
Original site: J4H1Q9_9APHY 
ID   J4H1Q9_9APHY            Unreviewed;       202 AA.
AC   J4H1Q9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=(4-O-methyl)-D-glucuronate--lignin esterase {ECO:0000256|ARBA:ARBA00026105};
DE            EC=3.1.1.117 {ECO:0000256|ARBA:ARBA00026105};
GN   ORFNames=FIBRA_02232 {ECO:0000313|EMBL:CCM00204.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00204.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM00204.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00204.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
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:0000256|ARBA:ARBA00024511};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC         Evidence={ECO:0000256|ARBA:ARBA00024511};
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC       {ECO:0000256|ARBA:ARBA00010092}.
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DR   EMBL; HE796971; CCM00204.1; -; Genomic_DNA.
DR   RefSeq; XP_012179487.1; XM_012324097.1.
DR   AlphaFoldDB; J4H1Q9; -.
DR   STRING; 599839.J4H1Q9; -.
DR   GeneID; 24095115; -.
DR   HOGENOM; CLU_1354645_0_0_1; -.
DR   InParanoid; J4H1Q9; -.
DR   OrthoDB; 1776336at2759; -.
DR   Proteomes; UP000006352; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT   DOMAIN          64..159
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
SQ   SEQUENCE   202 AA;  22081 MW;  09B18B4A9E3B393C CRC64;
     MKFRTKEIID PNYPLLDVDR AANISVKRTT HVYGETDVHK LSSIKLDVYH FPIPSTDGRT
     HHILVFFYGG GFTKGSRLGQ SPPHDLVHAN LGAFFARRGI LTVVPDYHFV PSITYPQGSE
     DVRDALLWVV RHLHTAGDAS RVFVLAHSAG GVHAVSMLLL SSLFSCPFAP LSVGCASSAS
     HLRSATAPPP HFSKLQWDTT AA
//
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