ID A0A060STF7_PYCCI Unreviewed; 328 AA.
AC A0A060STF7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU367147};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU367147};
GN ORFNames=BN946_scf184969.g36 {ECO:0000313|EMBL:CDO77685.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77685.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77685.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77685.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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:CDO77685.1}.
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DR EMBL; CCBP010000462; CDO77685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060STF7; -.
DR STRING; 5643.A0A060STF7; -.
DR HOGENOM; CLU_027551_1_1_1; -.
DR OMA; GWNGPCA; -.
DR OrthoDB; 1740325at2759; -.
DR Proteomes; UP000029665; 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: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; 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; PF10503; Esterase_PHB; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
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:UP000029665};
KW Secreted {ECO:0000256|RuleBase:RU367147};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487,
KW ECO:0000256|RuleBase:RU367147}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REGION 20..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 328 AA; 34596 MW; 0459AFE62B950CFA CRC64;
MIVAGTTCVE LNAYYSQCQP GAAAPPPPPT STPSTPTSST PTGSAPTGLS SIPASTLHQI
TNFGTNPNNI GMFVYKPAKV APNPPLIVAS HYCSGTAQAY FSGSRFAQLA ETYGYVVLYP
NSPHSGTCWD VSSDETLTHN GGSDSLGIAS AARYAIANWG VDANRVFAVG TSSGAMMTSV
LAGAYPDIFK AGIVDSGVAF GCFALPGQPD DSWNSQCSTG ELILTGQQWA QKVFNAYPGY
TGARPKMQVW HGTADTTLYP QNFFEEIKQW TTVFGYSSTP ISNVSEPYLP SGYSNATYGP
QFQAILAQGV GHTVPLFEPQ YLQFLGIA
//
