ID B8PCH3_POSPM Unreviewed; 439 AA.
AC B8PCH3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
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_32089 {ECO:0000313|EMBL:EED81412.1};
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:EED81412.1, 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; EQ966312; EED81412.1; -; Genomic_DNA.
DR RefSeq; XP_002473398.1; XM_002473353.1.
DR AlphaFoldDB; B8PCH3; -.
DR KEGG; ppl:POSPLDRAFT_32089; -.
DR HOGENOM; CLU_019364_3_0_1; -.
DR InParanoid; B8PCH3; -.
DR OMA; EDYAMLN; -.
DR OrthoDB; 1697614at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 122..289
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 327..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED81412.1"
FT NON_TER 439
FT /evidence="ECO:0000313|EMBL:EED81412.1"
SQ SEQUENCE 439 AA; 48946 MW; 76285DA4D4BE3E81 CRC64;
VLPRSFRPRR SWSIKQIVAV NFTRRIYKVT ERAGVTWGTR DPEEACDNRA LKETRFEWVD
PLPERLRTGI VADRQVPCKR VGVFLWPKEG SEGSMQRKES GIALTSPSDV EARAGNKPII
GIFLHGGGYC HMSAHESSST SKIPRQLIKD KAFDQIYAVE YRLLQHAPFP AAVQDAAAVY
AHIRVARATQ SKQCKVVLIG DSAGGNLVLA LARWIRDEGV LPPPDGLLLL SPSCDPSHAF
PESPSSYIPR PHGNTDYLVD TPEPRALLQR TFLGHNPLET MHSPYVSPAS MRVLRAYYGD
AFAYSVQDLT IKQMDTAARK RLREMTSVPG TPAIGPETPF EPSTNSEVNG LKPSPTSLAR
PQISSPRGLS LFSEFPRACI VLGDAERLER EVMKLVGGME RDGVDVRTIW VEDGVHDVLM
MGWWDERVRA KVWGEVEDW
//
