ID A0A165GEC2_9APHY Unreviewed; 668 AA.
AC A0A165GEC2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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_755741 {ECO:0000313|EMBL:KZT10231.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10231.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10231.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10231.1,
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; KV427609; KZT10231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GEC2; -.
DR STRING; 1314785.A0A165GEC2; -.
DR ESTHER; 9aphy-a0a165gec2; Fungal_carboxylesterase_lipase.
DR InParanoid; A0A165GEC2; -.
DR OrthoDB; 1387367at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR PANTHER; PTHR43142; CARBOXYLIC ESTER HYDROLASE; 1.
DR PANTHER; PTHR43142:SF5; CARBOXYLIC ESTER HYDROLASE; 1.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 26..505
FT /note="Carboxylesterase type B"
FT /evidence="ECO:0000259|Pfam:PF00135"
FT REGION 544..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74379 MW; 63C8C09A833098F1 CRC64;
MPAMIPKLNP VQEPVVVHEA LDTTFTGIVH PISTPDAPVH QFRGIKYANI PARFRQSRLH
TSYPAQTDAT HFGPICPQPR YDGYEAELFG IPADELPHQN LKQSEFGCLN LNITRPGDAT
PDLNLPVMVW VHGGGNRGSG SSWVYDGGSL VQKSMIVGKP VIMVSFIYRL GLLGFAASPA
LREDNKAAGD EGVGNYGLRD QRRALEWVYH FIPEFGGDPS NITFFGESTG AADIVCHLHS
AANEKHPLFK RAIIQSAIVE CEVPTVHAAG AQLSKYMSAL CLHSIDDLRV VEVEKLVSVD
QHLRATNDGT FFCRHFTGSL VLDEQQEHHH HPYVHLSSNL RHDDHAIEDS RGLQVLRHSH
WLQSSNRLRV SSRSRSRPRH AHMCHQSIMI GDCSDESLLW SLTASLWSAT AVERRVRAIC
QSLSKANVLL RAYDIHPHLP PDELHARVLE LINDSRFAWP TECIAACAKR ERGGKGVWRY
VFDQEGPARG VPHHAVDLIY LFDNVPQPSP TPKCSSKPTC MPAICPAICD ADDEDEDAMR
LIPKRVEEPS DSDDAEASSS SDSDVSTDSG YFEDWGVPAV DTYAYTRVRD AVQERWITFA
YGESPWREDK VYVFGPEGEV GERSMSIFQG RRRTQLWKEA LEPLGMPIVQ KVGTELCNGP
PLPSCGRF
//
