ID B8P280_POSPM Unreviewed; 354 AA.
AC B8P280;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=(4-O-methyl)-D-glucuronate--lignin esterase {ECO:0000256|ARBA:ARBA00026105};
DE EC=3.1.1.117 {ECO:0000256|ARBA:ARBA00026105};
DE Flags: Fragment;
GN ORFNames=POSPLDRAFT_24214 {ECO:0000313|EMBL:EED85070.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED85070.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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}.
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DR EMBL; EQ966242; EED85070.1; -; Genomic_DNA.
DR RefSeq; XP_002469803.1; XM_002469758.1.
DR AlphaFoldDB; B8P280; -.
DR ESTHER; pospm-b8p280; Epoxide_hydrolase.
DR KEGG; ppl:POSPLDRAFT_24214; -.
DR HOGENOM; CLU_020336_7_4_1; -.
DR InParanoid; B8P280; -.
DR OMA; NWYRVRT; -.
DR OrthoDB; 369876at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProt.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR PANTHER; PTHR43329:SF43; HYDROLASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 17..136
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED85070.1"
FT NON_TER 354
FT /evidence="ECO:0000313|EMBL:EED85070.1"
SQ SEQUENCE 354 AA; 39848 MW; 98203C46141E21F9 CRC64;
VNDLNMHIHE AGDRSNPLIL FLHGFPELAY SWRKVILPVA HMGYHVVAPD QRGFGRTTMT
QCSGDQIRYE DDWRSFHVQS LVRDILALAF ALGHRTVAAV VGHDLGSIVA AQCALIRPDV
FHSVVMMSAP FPGPPSLPFD IDATSPPPPP ITIFSPLIQN QLAGLNKPLK YYMTYFAGPD
ANHDLLNAPE GLHQFLRAYF HTKSADWSGN NPHPLLSVEV SEMAKLPCYY MMPLHSTMPQ
AVAPYTPSSQ EVAYNRWLPD SELAVYTAEY QRTGFQGGLN WYRSWHPEVQ RELALFAERR
IDVPAMFLSG EKDWGVFQHP GAMEKMKQRA CSRMDDEDVV VIEGAGHWVQ QEQP
//
