FAEC_TALSN
ID FAEC_TALSN Reviewed; 530 AA.
AC B8LV47; Q70Y21;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Feruloyl esterase C {ECO:0000303|PubMed:15006424};
DE EC=3.1.1.73 {ECO:0000269|PubMed:15006424};
DE AltName: Full=Ferulic acid esterase C;
DE Short=FAE;
DE Flags: Precursor;
GN Name=faeC; ORFNames=TSTA_065520;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-44; 322-341;
RP 395-412; 476-487 AND 512-527, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=15006424; DOI=10.1016/j.jbiotec.2003.12.003;
RA Garcia-Conesa M.T., Crepin V.F., Goldson A.J., Williamson G.,
RA Cummings N.J., Connerton I.F., Faulds C.B., Kroon P.A.;
RT "The feruloyl esterase system of Talaromyces stipitatus: production of
RT three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a
RT broad substrate specificity.";
RL J. Biotechnol. 108:227-241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-
CC galactose and feruloyl-arabinose ester bonds in pectin (By similarity).
CC Active against methyl esters of sinapate (MSA) and caffeate (MCA)
CC (PubMed:15006424). {ECO:0000250|UniProtKB:O42807,
CC ECO:0000269|PubMed:15006424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:15006424};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42807}.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
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DR EMBL; AJ505939; CAD44531.1; -; Genomic_DNA.
DR EMBL; EQ962652; EED23097.1; -; Genomic_DNA.
DR RefSeq; XP_002340484.1; XM_002340443.1.
DR AlphaFoldDB; B8LV47; -.
DR SMR; B8LV47; -.
DR CLAE; FAE1C_TALST; -.
DR ESTHER; 9euro-q70y21; Tannase.
DR EnsemblFungi; EED23097; EED23097; TSTA_065520.
DR GeneID; 8109464; -.
DR VEuPathDB; FungiDB:TSTA_065520; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR InParanoid; B8LV47; -.
DR OMA; LTPMAKN; -.
DR OrthoDB; 977166at2759; -.
DR PhylomeDB; B8LV47; -.
DR BRENDA; 3.1.1.73; 4645.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011118; Tannase/feruloyl_esterase.
DR PANTHER; PTHR33938; PTHR33938; 1.
DR Pfam; PF07519; Tannase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Polysaccharide degradation;
KW Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..25
FT CHAIN 26..530
FT /note="Feruloyl esterase C"
FT /id="PRO_5001370416"
FT ACT_SITE 191
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 31..78
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 66..117
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 190..444
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 259..276
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 285..294
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 506..528
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 530 AA; 58020 MW; ADE064D3BA5634D5 CRC64;
MMLTSAILLL TLGVQLSHAD DSSRENFSNR CDQLAKEIHI PNVTVNFVEY VANGTNVTLA
DNPPSCGQSN QVVLADLCRV AMEVTTSNQS QITLEAWFPE NYTGRFLSTG NGGLAGCIQY
VDMAYASSMG FATVGANGGH NGTSGESFYH NPDIVEDLSW RSVHTGVVVG KELTKKFYHE
GFHKSYYLGC STGGRQGFKA VQEFVHDFDG VVAGCPAFNF VNLNSWSGHF YPITGNSSAD
TFLTTAQWTL VQQSVMEQCD SLDGAVDGVI EAIDQCHPVF EQLICRPGQN ASECLTGKQV
NTAQLVLSPI YGTKGEFLYP RMQPGVENVD MYITYNGDPF AYSTDWYKYV VFSDPNWDPA
TLNAQDYEIA LAQNPSNIQT FEGDLSAFRD AGAKVLTYHG TADPIITGET SKVYYRHVAE
TMNAAPEELD EFYRYFRIGG MSHCGGGTGA TAIGNVLSAQ WSNDPDANVL MAMVRWVEEG
VAPEYIRGAS LGSGPGAKVE YTRRHCKYPT RNVYVGPGNW TDENAWKCIL
