FAEB1_ASPFC
ID FAEB1_ASPFC Reviewed; 528 AA.
AC B0YDW9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=AFUB_097070;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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; DS499602; EDP47853.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YDW9; -.
DR SMR; B0YDW9; -.
DR ESTHER; aspfu-faeb1; Tannase.
DR EnsemblFungi; EDP47853; EDP47853; AFUB_097070.
DR VEuPathDB; FungiDB:AFUB_097070; -.
DR HOGENOM; CLU_014819_1_0_1; -.
DR PhylomeDB; B0YDW9; -.
DR Proteomes; UP000001699; 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 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; Secreted; Serine esterase;
KW 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_0000394921"
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; 57734 MW; 28425386DAC2C55B 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 VVYNDSNWDH
STWTLADAAA AAAQDPFQIS SFDGNISGFQ KAGGKVLHYH GLEDAIITSD SSKAYYKHVA
DTMGLSPSEL DHFYRLFPIS GMGHCSPGTG AASIGQGSST YAGDDPQDNV LMAIVQWVEK
GIAPEYVRGS KMSRDGTIDY RRKHCKYPKR NRYVGPGKYT DENAWKCV
