ID A0A1M2VH67_TRAPU Unreviewed; 604 AA.
AC A0A1M2VH67;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_2155 {ECO:0000313|EMBL:OJT06954.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT06954.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT06954.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT06954.1,
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 -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:OJT06954.1}.
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DR EMBL; MNAD01001233; OJT06954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2VH67; -.
DR STRING; 154538.A0A1M2VH67; -.
DR OMA; CAEWRVR; -.
DR OrthoDB; 50200at2759; -.
DR Proteomes; UP000184267; 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; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267}.
FT DOMAIN 132..288
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 458..561
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 604 AA; 65649 MW; 8B2DD86DEAF9733B CRC64;
MDMNRDKIER PYVPYEPLAT VLPVVKPATS RSRKVKILLV LLTAAATFGL NHCWRGLDTD
LPSSTPSTRA DPPEFDWNAL EPAKTIRWTS CYSGQKCARL LLPLDYGTPD GPTTAIALRM
LPATDKVNYK GPMLINPGGP GGSGTDLVAR AGKNISAIVG PSFDILGFDP RGIGASTPSA
SCFESDSQRQ LWELQEDHRL LNASDGSVDI ARARQTLLGQ RCEQKIGGEW GIARFMSTPD
VARDMLEISQ QLGHEKLQYW GFSYGSILGQ YFSAIYPDKV GRVIIDGVYD GHNYRGALWN
SNLADTDAVI DSFFTFCHQA GPEKCALYDS TPAKIRARFF AVLHAVEAQP VSIPNAEPPV
LVTRKVLQSQ LFRATYKPLA QFVVVADTVY ALESGNQTAL AALAPKIVPP TECKCADLEP
WLASNEAFSP IACGDGDEIV YDREAYAKYY ENLVASSQLA GPLWANSYLK CAEWRVRPKW
RWTGPLGAKN TSHPLLLVSP RYDPVCPLSD AQAVQDRYAG SGLLIQESVG HCTLAAPSLC
TAKHIRAYME NGTLPKAGTV CGVDELPFVG AVQDVRALSV EDTELLEAMK GLSAAVPTFG
FGGL
//
