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Database: UniProt
Entry: A0A1M2VP95_TRAPU
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Original site: A0A1M2VP95_TRAPU 
ID   A0A1M2VP95_TRAPU        Unreviewed;       369 AA.
AC   A0A1M2VP95;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU367147};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU367147};
GN   ORFNames=TRAPUB_14136 {ECO:0000313|EMBL:OJT09388.1};
OS   Trametes pubescens (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT09388.1, ECO:0000313|Proteomes:UP000184267};
RN   [1] {ECO:0000313|EMBL:OJT09388.1, ECO:0000313|Proteomes:UP000184267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC735 {ECO:0000313|EMBL:OJT09388.1,
RC   ECO:0000313|Proteomes:UP000184267};
RA   Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA   Hilden K.;
RT   "Genome sequence of the basidiomycete white-rot fungus Trametes
RT   pubescens.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Esterase involved in the hydrolysis of xylan, a major
CC       structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. {ECO:0000256|RuleBase:RU367147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000256|ARBA:ARBA00001691};
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   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367147}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC       subfamily. {ECO:0000256|ARBA:ARBA00007052}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC       {ECO:0000256|ARBA:ARBA00010092}.
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:OJT09388.1}.
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DR   EMBL; MNAD01000923; OJT09388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M2VP95; -.
DR   STRING; 154538.A0A1M2VP95; -.
DR   OMA; MEWFGFA; -.
DR   OrthoDB; 1740325at2759; -.
DR   Proteomes; UP000184267; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR010126; Esterase_phb.
DR   NCBIfam; TIGR01840; esterase_phb; 1.
DR   PANTHER; PTHR43037:SF6; CARBOXYLIC ESTER HYDROLASE; 1.
DR   PANTHER; PTHR43037; UNNAMED PRODUCT-RELATED; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU367147};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367147};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU367147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW   Secreted {ECO:0000256|RuleBase:RU367147};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487,
KW   ECO:0000256|RuleBase:RU367147};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367147}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU367147"
FT   CHAIN           22..369
FT                   /note="Carboxylic ester hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU367147"
FT                   /id="PRO_5029036640"
FT   DOMAIN          19..55
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          61..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..84
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  38690 MW;  5B46177151A45F69 CRC64;
     MFSFSRTLSF VALAGLVAGQ AAEWGQCGGI GFTGATTCVA GTTCVTLNAY YSQCQPGAAA
     PAPTSAPQPS PTQPAGPAPS NPSTPTGPGL SSIPASTLHQ ITNFGANPNN IGMFVYKPAR
     VAANPPLIVA SHYCSGTAQA YFTGSKFAQL AETYGYVVLF PNSPHSGTCW DVSSDATLTH
     NGGGDSLGIA SAARFAIANW GVDANRVFAV GTSSGAMMTS VLAGAYPDIF KAGIVDSGVA
     FGCFAVPGQP DDSWNSQCST GEMILTGQQW AQKVYNAFPG YTGARPKMQV WHGTIDTTLY
     PQNFWEEIKQ WTTVFNYPST PISNVSEPYL PNGYSNATFG PMFQAILAQN VGHTVPLFEQ
     QYLQFFGIA
//
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