FAEB2_ASPFC
ID FAEB2_ASPFC Reviewed; 526 AA.
AC B0Y7U1;
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-2;
DE EC=3.1.1.73 {ECO:0000250|UniProtKB:Q8WZI8};
DE AltName: Full=Ferulic acid esterase B-2;
DE Short=FAEB-2;
DE Flags: Precursor;
GN Name=faeB-2; ORFNames=AFUB_074990;
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}.
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DR EMBL; DS499599; EDP49472.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y7U1; -.
DR SMR; B0Y7U1; -.
DR ESTHER; aspfu-q4wmr0; Tannase.
DR EnsemblFungi; EDP49472; EDP49472; AFUB_074990.
DR VEuPathDB; FungiDB:AFUB_074990; -.
DR HOGENOM; CLU_014819_1_0_1; -.
DR PhylomeDB; B0Y7U1; -.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..526
FT /note="Probable feruloyl esterase B-2"
FT /id="PRO_0000394927"
FT ACT_SITE 187
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 400
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 440
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 261
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 CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..74
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 62..113
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 186..441
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 255..272
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 281..291
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 503..525
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 526 AA; 57852 MW; 740A0F5765FC0713 CRC64;
MTKLSLLPLL TLASAVLAKQ DAFQAKCASF GRKIKLPNVH VNFVEYVPGG TNLTLPDNDV
TCGASSQVVS ADMCRVAMAV DTSKSSQITL EAWFPREYTG RFLSTGNGGL SGCIQYYDLA
YTAGLGFATV GANNGHNGTS GKPFYQHPEV IEDFAYRSIH TGVVVGKQLT KMFYKEGFDK
SYYLGCSTGG RQGFKSIQKY PNDFDGVVAG APAFNFVNLI SWSIHFYSIT GSNTSDTYLS
PESWKVVHDE IVRQCDEIDG AKDGIIEDTD LCQPVIETII CKPGASDKTN CITGAQAKTV
RNVLSPFYGV NGTLLYPRMQ PGSELFASSV VYNGQPFRYS TDWYRYVVYN NPDWDATKWT
VEDAAVALAQ NPYNIQTWDA DISSFQKAGG KVLTYHGMQD QLISSDNSKL YYARVAEEMG
LGPEELDDFY RFFPVSGMAH CTGGDGAYGI GNGLRTYNGA EPENNVLMAM VQWVEKGIAP
EFIRGAKFSN GVGSSVEYTR KHCRYPRRNV YKGPGNYSDE NAWECV
