ID A0A2R6NU27_9APHY Unreviewed; 287 AA.
AC A0A2R6NU27;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
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_2v8288 {ECO:0000313|EMBL:PSR76691.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSR76691.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSR76691.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSR76691.1,
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 -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. LDAH family.
CC {ECO:0000256|ARBA:ARBA00008300}.
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:PSR76691.1}.
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DR EMBL; MLYV02000837; PSR76691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6NU27; -.
DR STRING; 98765.A0A2R6NU27; -.
DR Proteomes; UP000186601; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR019363; LDAH.
DR PANTHER; PTHR13390; LIPASE; 1.
DR PANTHER; PTHR13390:SF0; LIPID DROPLET-ASSOCIATED HYDROLASE; 1.
DR Pfam; PF10230; LIDHydrolase; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW Reference proteome {ECO:0000313|Proteomes:UP000186601}.
SQ SEQUENCE 287 AA; 32676 MW; EE7F07B391361F49 CRC64;
MSNLPAFLEP LQQTLPGQPS TEPVHYVNAL FRHKRFPSLA HVLYWPSKGE SKTCMVFIPG
NPGLLDFYTP FLAGIHEKAH DKMHILAHAF VGHTPGIIRG SEHPAATSLD AQIEHVIELI
DTIKPVYNKI IAIGHSVGTW VVLQWAFKLP RMISYASVFT RLMPLKMLSV LFPEWPEAQL
RVLRSFLDSP SAIYSSLSMA DDEMKQIQDL DGAALQQYHH RLHMYFAEKD DWVHDHKTEI
LDVLQPDPGS VRYIHGPEDI PHAFCINHGE ELAEQCYRWL VEGDFVD
//
