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Database: UniProt
Entry: A0A2G8SMY9_9APHY
LinkDB: A0A2G8SMY9_9APHY
Original site: A0A2G8SMY9_9APHY 
ID   A0A2G8SMY9_9APHY        Unreviewed;       553 AA.
AC   A0A2G8SMY9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU361235};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361235};
GN   ORFNames=GSI_02923 {ECO:0000313|EMBL:PIL35134.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL35134.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL35134.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL35134.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
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 type-B carboxylesterase/lipase family.
CC       {ECO:0000256|ARBA:ARBA00005964, ECO:0000256|RuleBase:RU361235}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIL35134.1}.
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DR   EMBL; AYKW01000004; PIL35134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8SMY9; -.
DR   STRING; 1077348.A0A2G8SMY9; -.
DR   OrthoDB; 1446144at2759; -.
DR   Proteomes; UP000230002; 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; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   PANTHER; PTHR11559; CARBOXYLESTERASE; 1.
DR   PANTHER; PTHR11559:SF162; CARBOXYLIC ESTER HYDROLASE; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361235};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW   Signal {ECO:0000256|RuleBase:RU361235}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361235"
FT   CHAIN           20..553
FT                   /note="Carboxylic ester hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361235"
FT                   /id="PRO_5013431993"
FT   DOMAIN          29..517
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
SQ   SEQUENCE   553 AA;  59222 MW;  C3AC3334D594CECE CRC64;
     MLVRSSLSLL ALFAGAALGL PVEVEKRASP TVLLDQGTFV GSSDGTTNKF LGIPFGKAPV
     GNLRFSLPVA VDAYNGTQTV TSYGPACPQQ AFDFPQIPGL VGDVADWFVN TIYNVITPSA
     EDCLSLNVIV PAGTKAGANL PVAVWIFGGG FEIGGPDIYD GSVIVKRSIE LGEPVVYVSM
     NYRVSAYGFL ASQEVKDAGV GNLGLQDQRL ALRWVQKYIS TFGGDPSKVT IWGESAGAIS
     VALQMLTNGG NTEGLFRGAF MQSGSPIPVG DITHGQNDYD TLVSATGCSG AADTLQCLRE
     VPFATLKQAV DSSPGIFSPQ SLRLAWLPRV DGKFLVDAPQ KLVQQGSVAN IPFVNGDCDD
     EGTLFSLSNI NVTTEDEVRS YLSSNYISGI SSSDLDQLLT LYPSDITQGS PFDTGILNVV
     TPEFKRLASI QGDLVFQAPR RFFLQNTADK QPVWSYINKR LKVTPILGSA HGTDILNVYG
     GSDMADHVIN FVNNLDPNGA TVISWPKYTT ASPQLLEYYD TIIPGINGLQ LTTDDYRVDA
     MNFMTQLSLE FPI
//
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