ID A0A2H3JKI0_WOLCO Unreviewed; 296 AA.
AC A0A2H3JKI0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=WOLCODRAFT_82182 {ECO:0000313|EMBL:PCH36507.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH36507.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH36507.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH36507.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043831};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC Class 3 subfamily. {ECO:0000256|ARBA:ARBA00043996}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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DR EMBL; KB467876; PCH36507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3JKI0; -.
DR STRING; 742152.A0A2H3JKI0; -.
DR OMA; HRWYTIY; -.
DR OrthoDB; 1102158at2759; -.
DR Proteomes; UP000218811; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45856; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR45856:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PCH36507.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..296
FT /note="(4-O-methyl)-D-glucuronate--lignin esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013581413"
FT DOMAIN 112..253
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 296 AA; 31179 MW; 7AFA47CDD146DCBF CRC64;
MFSSSLVALL PLLSFTPRTL AAPVPLFGIN LGEGSEATGN PTPISQSTIT DDLLRPALFA
RTAYCPSSTL TDWSCGAPCN ALPGVNVFTA GGDDGEIPFY YVASDPQTQT IVVAHEGTDP
ENFYSDLNDI KFSQVAINAT RFPQAGSNVQ VHDGFQETQG RTADTILSTV QSALASTGYT
NVLVTGHSLG AAVASLDAAM LKMALPSNIE IGSVVFGLPR VGNQEWADLV GSLLPSFTHV
TNQNDPVPRV PPRALSFVQP VGEAHITAVN NSTGDATMEE CPGQENEVRA FRRAVV
//
