ID   FAEB_TALFU              Reviewed;         353 AA.
AC   Q9HE18;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Feruloyl esterase B;
DE            EC=3.1.1.73;
DE   AltName: Full=Cinnamoyl esterase;
DE   AltName: Full=Ferulic acid esterase B;
DE            Short=FAEB;
DE   Flags: Precursor;
GN   Name=FAEB;
OS   Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium
OS   funiculosum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=28572 {ECO:0000312|EMBL:CAC14144.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-68; 90-97;
RP   163-167; 212-241 AND 259-274, FUNCTION, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RC   STRAIN=IMI 134756;
RX   PubMed=11082184; DOI=10.1046/j.1432-1033.2000.01742.x;
RA   Kroon P.A., Williamson G., Fish N.M., Archer D.B., Belshaw N.J.;
RT   "A modular esterase from Penicillium funiculosum which releases ferulic
RT   acid from plant cell walls and binds crystalline cellulose contains a
RT   carbohydrate binding module.";
RL   Eur. J. Biochem. 267:6740-6752(2000).
CC   -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC       feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC       galactose and feruloyl-arabinose ester bonds in pectin. Binds strongly
CC       to cellulose. {ECO:0000269|PubMed:11082184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73; Evidence={ECO:0000269|PubMed:11082184};
CC   -!- ACTIVITY REGULATION: Inhibited by the specific serine esterase
CC       inhibitor AEBSF. {ECO:0000269|PubMed:11082184}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11082184}.
CC   -!- INDUCTION: Repressed by glucose, probably via the carbon catabolite
CC       repressor protein CreA. {ECO:0000269|PubMed:11082184,
CC       ECO:0000303|PubMed:11082184}.
CC   -!- PTM: Glycosylated. {ECO:0000303|PubMed:11082184, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family.
CC       Feruloyl esterase type B subfamily. {ECO:0000305}.
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DR   EMBL; AJ291496; CAC14144.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HE18; -.
DR   SMR; Q9HE18; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   ESTHER; penfn-faeb; Esterase_phb.
DR   BRENDA; 3.1.1.73; 4616.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
DR   GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR010126; Esterase_phb.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Hydrolase; Polysaccharide degradation; Secreted; Serine esterase; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:11082184"
FT   CHAIN           19..353
FT                   /note="Feruloyl esterase B"
FT                   /id="PRO_0000021229"
FT   DOMAIN          317..353
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          19..291
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  37334 MW;  4AD08FEDDA29B2D9 CRC64;
     MAIPLVLVLA WLLPVVLAAS LTQVNNFGDN PGSLQMYIYV PNKLASKPAI IVAMHPCGGS
     ATEYYGMYDY HSPADQYGYI LIYPSATRDY NCFDAYSSAS LTHNGGSDSL SIVNMVKYVI
     STYGADSSKV YMTGSSSGAI MTNVLAGAYP DVFAAGSAFS GMPYACLYGA GAADPIMSNQ
     TCSQGQIQHT GQQWAAYVHN GYPGYTGQYP RLQMWHGTAD NVISYADLGQ EISQWTTIMG
     LSFTGNQTNT PLSGYTKMVY GDGSKFQAYS AAGVGHFVPT DVSVVLDWFG ITSGTTTTTT
     PTTTPTTSTS PSSTGGCTAA HWAQCGGIGY SGCTACASPY TCQKANDYYS QCL