ID A0A2G8SNG9_9APHY Unreviewed; 289 AA.
AC A0A2G8SNG9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=GSI_02039 {ECO:0000313|EMBL:PIL35314.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL35314.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL35314.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL35314.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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:PIL35314.1}.
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DR EMBL; AYKW01000003; PIL35314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8SNG9; -.
DR STRING; 1077348.A0A2G8SNG9; -.
DR OrthoDB; 2676839at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF2; PEROXISOMAL MEMBRANE PROTEIN LPX1; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT DOMAIN 37..281
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
SQ SEQUENCE 289 AA; 30297 MW; 2388DDEA66429751 CRC64;
MTKVEPTCTT KLIDLPHGVI LHTERHRVGT DAPSMTVVCI HGLGSTSTAF YPIIKHILTA
LPAAHLIAYD WAGSGSSPRP SSVSDRTVAD HVSDLDALIG AEAPSGPLVI LAHSAGTHLA
SRWLLTPSPH VTRVTHAIYL GGPINIPLSP EVTTMQLDLA TTIAAGGPAA VVDSLAPMLL
GATSMVERPV AVTALRAIML AQSAEGYAAA IRAFSKNMGE GDAPVDWAAI RDKVKILVVA
GEEDVLLGQT EVAGFLERAV VKKIARAGHT LTLEAPEETA KMIVEFLQN
//
