ID   FAEB1_ASPFU             Reviewed;         528 AA.
AC   Q4W8Z9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable feruloyl esterase B-1;
DE            EC=3.1.1.73 {ECO:0000250|UniProtKB:Q8WZI8};
DE   AltName: Full=Ferulic acid esterase B-1;
DE            Short=FAEB-1;
DE   Flags: Precursor;
GN   Name=faeB-1; ORFNames=AFUA_6G00450;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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.
CC       {ECO:0000250|UniProtKB:Q8WZI8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73; Evidence={ECO:0000250|UniProtKB:Q8WZI8};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
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DR   EMBL; AAHF01000018; EAL84220.1; -; Genomic_DNA.
DR   RefSeq; XP_731510.1; XM_726417.1.
DR   AlphaFoldDB; Q4W8Z9; -.
DR   SMR; Q4W8Z9; -.
DR   ESTHER; aspfu-faeb1; Tannase.
DR   EnsemblFungi; EAL84220; EAL84220; AFUA_6G00450.
DR   GeneID; 3503636; -.
DR   KEGG; afm:AFUA_6G00450; -.
DR   VEuPathDB; FungiDB:Afu6g00450; -.
DR   eggNOG; ENOG502QPXZ; Eukaryota.
DR   HOGENOM; CLU_014819_1_0_1; -.
DR   InParanoid; Q4W8Z9; -.
DR   OMA; INLISWG; -.
DR   OrthoDB; 977166at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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   Gene3D; 3.40.50.1820; -; 1.
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   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Polysaccharide degradation; Reference proteome; Secreted;
KW   Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..528
FT                   /note="Probable feruloyl esterase B-1"
FT                   /id="PRO_0000394923"
FT   ACT_SITE        191
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   ACT_SITE        404
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   ACT_SITE        444
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   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..78
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   DISULFID        64..117
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   DISULFID        190..445
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   DISULFID        259..276
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   DISULFID        285..295
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT   DISULFID        505..527
FT                   /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ   SEQUENCE   528 AA;  57676 MW;  B32E5FB7A29DFA58 CRC64;
     MMWWFLLIGL ASAAATASSA SSASFESRCQ HFHKEIHLQN VHVLSTTYVP IGSNIPMVYN
     PPICGGTASS SISTIQFCQV ALNVTTSDKS QFFMEAWLPS NYTGRFLSTG NGGLNGCVSY
     ADMVYATQYG FATIGTNNGH FGDTGQYFLN NPEVIEDFAY RALHTGTVVG KALTKLFYPQ
     GYKNSYYLGC STGGRQGWKS IQRFPDDFDG VVAGAPAINF VNLCSWGSRF LKITGPPGSE
     TFVTSAQWSA VHNEILRQCD ALDGAVDGII EDTDLCQPVF ETLLCNSTAV DKTSCLTGVQ
     ANTVNEVFSA MYGLDGKWLY PRMQPGSELA ASFIYYSGNG FKYSDDWYKY VVYNDSNWGH
     STWTLADAAA AAAQDPFQIS SFDGNISGFQ KAGGKVLHYH GLEDAIITSD SSKAYYKHVA
     DTMGLSPSEL DHFYRLFPIS GMGHCSPGTG AASIGQGSST YAGDDPQDNV LMAIVQWVEK
     GIAPEYVRGS KMSRDGTIDY RRKHCKYPKR NRYVGPGKYT DENAWKCV