ID R7SKP6_DICSQ Unreviewed; 631 AA.
AC R7SKP6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=DICSQDRAFT_93285 {ECO:0000313|EMBL:EJF56711.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF56711.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF56711.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56711.1,
RC ECO:0000313|Proteomes:UP000053319};
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 -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; JH719465; EJF56711.1; -; Genomic_DNA.
DR RefSeq; XP_007370574.1; XM_007370512.1.
DR AlphaFoldDB; R7SKP6; -.
DR GeneID; 18845007; -.
DR KEGG; dsq:DICSQDRAFT_93285; -.
DR HOGENOM; CLU_013364_5_1_1; -.
DR OMA; CNDVAWP; -.
DR OrthoDB; 50200at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..631
FT /note="(4-O-methyl)-D-glucuronate--lignin esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004444215"
FT DOMAIN 149..344
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 486..585
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 631 AA; 67161 MW; 4210F40DCA9512CE CRC64;
MALPRTAHTS QGLRFIGVCC AVLSLLAVGS NATGQWGLQS QELAVADDSG QSVAQMTLAE
QATATAWKHN VAALFAGGAL ALAGSTASVA PVQGSVGDLF FGNCTDNRAL PGAECGYAIV
PLDYTNSSAG VAKIALGRYN ATVSPRKGVV FVNPGGPGGP GVNLATEAGS FFQELIGEDY
DIIGFDPRGI GLSEPQTKCF PKNGSREAFI TNTVLDRGYD VSPNLTDPYN RFHLIETQRD
ANALYQAQFQ VCAQTMGETI KYAGTTSVVR DIDFITTLLE GTDSLINFYG FSYGTVMGQY
LVNVFPDRVG RVVIDGVVDA DSWANKAPYQ QLHQWLNSTD ATYEVFIAEC AKAGPASCAL
AQKDNEDPKD ILDRVERWID GLYDAPLAVP NATLPGILTN GRAHLFIEGG LESPTGWPQI
AAGLAEAMRG DGAVVLNVVN TRELVDLERS AVSCNDQRPF APPKPETIVD AGLEVLKHVS
RFFWSVIIAE PDSGCQYWPV TPPERYLGPW NKTLNNPILI ISNTHDPATP LVNGEAVHGY
LPNSSALLVQ NGPGHTSNAL TSRCTISLTR AYFANGTLPA AGTVCEVDQS PFPPPSDSTA
PATAAASAKM RVLDHIHRMS PNRLRMASGR S
//
