ID   FAEB_TALSN              Reviewed;         358 AA.
AC   B8M9H9;
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 B {ECO:0000303|PubMed:15006424};
DE            EC=3.1.1.73 {ECO:0000269|PubMed:15006424};
DE   AltName: Full=Ferulic acid esterase B;
DE            Short=FAE;
DE   Flags: Precursor;
GN   Name=faeB; ORFNames=TSTA_115370;
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 [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).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-56; 185-211 AND 266-295, FUNCTION, AND CATALYTIC
RP   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).
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 caffeate (MCA), but not sinapate (MSA)
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 carbohydrate esterase 1 (CE1) family.
CC       Feruloyl esterase type B subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ962655; EED17739.1; -; Genomic_DNA.
DR   RefSeq; XP_002481731.1; XM_002481686.1.
DR   AlphaFoldDB; B8M9H9; -.
DR   SMR; B8M9H9; -.
DR   STRING; 28564.XP_002481731.1; -.
DR   EnsemblFungi; EED17739; EED17739; TSTA_115370.
DR   GeneID; 8101347; -.
DR   VEuPathDB; FungiDB:TSTA_115370; -.
DR   eggNOG; ENOG502QTDU; Eukaryota.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   InParanoid; B8M9H9; -.
DR   OMA; RTRMQIW; -.
DR   OrthoDB; 1169544at2759; -.
DR   PhylomeDB; B8M9H9; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; Reference proteome; Secreted;
KW   Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:15006424"
FT   CHAIN           19..358
FT                   /note="Feruloyl esterase B"
FT                   /id="PRO_0000433997"
FT   DOMAIN          322..358
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          19..291
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WBW4"
FT   REGION          292..321
FT                   /note="Gly/Thr-rich linker"
FT                   /evidence="ECO:0000305"
FT   REGION          297..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   358 AA;  37584 MW;  47EBBB6321EF55E1 CRC64;
     MAIPLVLLLA WLLPTVFAAS LTQVSNFGDN PGSLQMYIYV PNNLASKPAI IVAMHPCGGS
     ATQYYGMYDY HTPADQYGYI LIYPSATRDL NCFDADTAAS LTHNGGSDSL SIVNMVKYTI
     SKYGADSSKV YMTGSSSGAI MTNVLAGTYP DVFAAGAAFS GMPFACLSGA GGADPAMSNQ
     TCSRGQINHT PQEWAAYVHN AYPGYTGQYP RLQVWHGTAD NVISYTDFNQ EISQWTTVMG
     LSFTSNQTNT PLSGYTKMIY GDGSRFQAFS ASGVGHFVPT DVSVVLDWFG ITGGGGGNGG
     GSGSTTTTTS ATTTSTGPTG GCTAAHWDQC GGNGYTGCTS CASPYTCQKV NDYYSQCL