ID A0A1M2VWM2_TRAPU Unreviewed; 241 AA.
AC A0A1M2VWM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=TRAPUB_11447 {ECO:0000313|EMBL:OJT12005.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT12005.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT12005.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT12005.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) 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:OJT12005.1}.
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DR EMBL; MNAD01000539; OJT12005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2VWM2; -.
DR STRING; 154538.A0A1M2VWM2; -.
DR OMA; CERVGAI; -.
DR OrthoDB; 1602034at2759; -.
DR Proteomes; UP000184267; 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:UP000184267}.
FT DOMAIN 54..239
FT /note="Dienelactone hydrolase"
FT /evidence="ECO:0000259|Pfam:PF01738"
SQ SEQUENCE 241 AA; 25500 MW; 965ABC7DF17DE40A CRC64;
MSIQTGLLAP AAIYVAASSS QATGQIARIS TTSYMSSARH PPLLQTSPSS PSLADAFARN
GFKVYLPDLF AGDALPEAEL NSGNFDLMGW LGKHPAADIP GIVRPVLSAL KAEGITKIAA
VGYCYGGRPA FDLAIGDEVD VVAVSHPSLL KSPDDLETYL GKSKAPILIN SCENDFQFGT
DAQAKADEIL GDGKFAPGYE HRYWEGCTHG FAVRGDISDP KIKAGKEGAF KATVEFLIKH
L
//
