ID A0A2G8RPZ0_9APHY Unreviewed; 579 AA.
AC A0A2G8RPZ0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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_14874 {ECO:0000313|EMBL:PIL23561.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL23561.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL23561.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL23561.1,
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:PIL23561.1}.
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DR EMBL; AYKW01000068; PIL23561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RPZ0; -.
DR STRING; 1077348.A0A2G8RPZ0; -.
DR OrthoDB; 1697614at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..366
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 411..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 63235 MW; C127B792E011BADF CRC64;
MPRSRKHPYQ ADMPYAKQPL KAIYVVQRLF TSIVMCIWWA AYYSIMPRRY RPRPSWTIKC
ILAVNFTRRI YKVTELAGVT WGTRDPEKEC DERSLKHTRF EWVDPMPQEL RTGIIADPQV
PFRRVGCFVW PKERPSFPCH DLDSGLSSSS PSQDVLMDFE AAAGDVPVIG IFMHGGGYCH
MSAHENAPTS QIPGRLIKDG AFKEIHSVEY RLLQHAPFPA AVQDAATVYA HLSGDLDFLD
VEGWSPERVK NRKENEEIHA RVSEAAAHVA CKIILIGDSA GGNLVLALAR WIRDEGVLPP
PDGLLLLSPS CDPSHAFPET PSSYIPRPHA STDYLVDTPE PRALLQRTFL GHNPLETMHS
PYVSPASMRV LAAFYGDAFA SSVADLSIAQ LDDDGHREFL RTMVSAPVTP VPMASRANTN
TDTDMSTSLG PFLVGPGPPV MNASPDTSNS NSSSGSGLGH DAGANVPGPG PGPGPGPGAG
VGAGAEGGRS PTSLAQPVIA SPRGLSLFSE FARTCVVLGD AERLEREVAK LVGAMERDGT
EVRAIWVRDA PHDVLQMKWW DERVRDGVWA QIEEWVVGV
//
