ID A0A165HRI7_9APHY Unreviewed; 383 AA.
AC A0A165HRI7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=LAESUDRAFT_740619 {ECO:0000313|EMBL:KZT12087.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12087.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12087.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12087.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427606; KZT12087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165HRI7; -.
DR STRING; 1314785.A0A165HRI7; -.
DR InParanoid; A0A165HRI7; -.
DR OrthoDB; 1054870at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR001375; Peptidase_S9.
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 Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KZT12087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 46..163
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 300..352
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 383 AA; 42156 MW; B917A17948E5331F CRC64;
MMPGDSQSPV PITLIYKHVD GLPLLLDVYL PNEVDQSGLV CYSSALVYFH GGGLTVGNRR
SWFPHWLYRR VTSADCIFIS ADYRLLPPST GHDLLADIKD VIDFVAHKLN QSLSESVSPV
TKIRVAVDSI AVAGTSSGGL CAYLAAIHAR PRPKAVLSMY GMGGMMLTPH YYYPKSSVFF
RGRELLDPTH FSEYLYPDCR QLSPISDSAL AYHPLTSPTP GYPANPRMLL ARLYLQLGVF
LDYYTGCHEL SLSKMLRSST AGERKAAQGQ EDAVPDIHQP PTGIESVIPR EHLPLFPHLN
ISSSWPPTLL VHGSIDSAIL PAESIHLHAM LQDAGVETNL VMIDGMEHSF DYQPGAENTY
GSHGGLFDQA AKFVIQHLRD NDL
//
