FAEB1_NEOFI
ID FAEB1_NEOFI Reviewed; 525 AA.
AC A1DKV3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=NFIA_047590;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027698; EAW15424.1; -; Genomic_DNA.
DR RefSeq; XP_001257321.1; XM_001257320.1.
DR AlphaFoldDB; A1DKV3; -.
DR SMR; A1DKV3; -.
DR ESTHER; neofi-faeb1; Tannase.
DR EnsemblFungi; EAW15424; EAW15424; NFIA_047590.
DR GeneID; 4583835; -.
DR KEGG; nfi:NFIA_047590; -.
DR VEuPathDB; FungiDB:NFIA_047590; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; INLISWG; -.
DR OrthoDB; 977166at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome; Secreted;
KW Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..525
FT /note="Probable feruloyl esterase B-1"
FT /id="PRO_0000394926"
FT ACT_SITE 188
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 441
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..75
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 61..114
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 187..442
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 256..273
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 282..292
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 502..524
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 525 AA; 57678 MW; 8576D39A5B5A740A CRC64;
MMRWFLLIGL ASAAATDSSA SFESRCQHFH KEIHLQNVHV HSTTYVPIGS NISMAYNPPI
CGGTSSSSIS TIEFCQVALN VTTSDKSQFF MEAWLPSNYT GRFLSTGNGG LNGCVGYGDM
IYASQYGFAT IGTNNGHFGD TGQYFLNNPE VIEDFAYRAL HTGTVVGKAL TKLFYPQGYK
NSYYLGCSTG GRQGWKSIQR FPDDFDGVVA GAPAFNFVNL CNWGSRFLKI TGPPDSDTFV
TSAQWSIIHN EIIRQCDALD GAVDGTIEDT DLCQPIFETL ICNSTAVNKT SCLTGVQANT
VNEVFSAMYG LDGKWLYPRM QPGSELAASF IYYSGNGFKY SDDWFKYVVY NDSNWDHSTW
TLADAAAADA QDPFQISTFD GDISGFQKAG GKVLHYHGLE DAIITSDSSK AYYKHVADTM
GLSPSDLDQF YRFFPISGMG HCSPGTGAAS IGQGSSTYAG DDPQDNVLMA MVQWVEKGIA
PEYVRGSKKS IDGQTEYRRK HCKYPKRNRY VGPGKYTDEN AWKCV
