ID A0A2R6QEP8_9APHY Unreviewed; 268 AA.
AC A0A2R6QEP8;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=PHLCEN_2v3657 {ECO:0000313|EMBL:PSS06599.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS06599.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSS06599.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSS06599.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSS06599.1}.
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DR EMBL; MLYV02000360; PSS06599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6QEP8; -.
DR STRING; 98765.A0A2R6QEP8; -.
DR Proteomes; UP000186601; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002925; Dienelactn_hydro.
DR PANTHER; PTHR17630; DIENELACTONE HYDROLASE; 1.
DR PANTHER; PTHR17630:SF44; PROTEIN AIM2; 1.
DR Pfam; PF01738; DLH; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000186601}.
FT DOMAIN 30..265
FT /note="Dienelactone hydrolase"
FT /evidence="ECO:0000259|Pfam:PF01738"
SQ SEQUENCE 268 AA; 29509 MW; 33F1AA85D669977E CRC64;
MACEHCTQGY IVPGQPQGKM VNGAYFHPAP QGSTTKSRAI VVFTDIFGLP LKNCKLIADA
LSSRVGCDVW VPDLFEGKPP FTTDELVPIL PDTGKPDDRM GLLRKLRLIL LGLSRALRLY
RARPAVVDAR AIAFLKSIRK ERMYETVGAV GYCFGGALAI RLGSGNILDS IVVCHPTHRS
LSTIQAINIP TSWVCAESDT SFTKDLRDES ERIFAARKNK PEYVDYEFKD YRGTVHGFAA
RPNIAISGLL EAYQGALEQA GAWFDKTL
//
