FAEB_ASPCL
ID FAEB_ASPCL Reviewed; 526 AA.
AC A1CTK4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable feruloyl esterase B;
DE EC=3.1.1.73 {ECO:0000250|UniProtKB:Q8WZI8};
DE AltName: Full=Ferulic acid esterase B;
DE Short=FAEB;
DE Flags: Precursor;
GN Name=faeB; ORFNames=ACLA_083360;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06641.1; -; Genomic_DNA.
DR RefSeq; XP_001268067.1; XM_001268066.1.
DR AlphaFoldDB; A1CTK4; -.
DR SMR; A1CTK4; -.
DR ESTHER; aspcl-faeb; Tannase.
DR EnsemblFungi; EAW06641; EAW06641; ACLA_083360.
DR GeneID; 4700491; -.
DR KEGG; act:ACLA_083360; -.
DR VEuPathDB; FungiDB:ACLA_083360; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; LTPMAKN; -.
DR OrthoDB; 977166at2759; -.
DR Proteomes; UP000006701; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..526
FT /note="Probable feruloyl esterase B"
FT /id="PRO_0000394933"
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 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; 57522 MW; F4EDDAB9F4B65391 CRC64;
MARLSLLTLL ALGSAALAKK DTFQTKCAAL QHKVKLPNVH VNFVEYVPGG TNLDLPDNAP
SCGASSQAVS TDMCRIAMAV DTSDSSQITL EAWFPRDYTG RFLSTGNGGL SGCIQYYDLA
YAAGLGFATV GANNGHNGTS GEPFYQHPEV VEDFAHRSVH TGVVVGKQLT KLFYDKGFKK
SYYLGCSTGG RQGFKSVQKY PKDFDGIVAG APAFNFVNLI SWSAYFYSLT GSNTSESYLS
PAMWKIAHDE IVRQCDELDG AKDGIIEDTD LCHPRLETII CKPGAKDTAN CLTGAQAKTV
RDVLSPMYGV NGTLLYPRMQ PGSEVYAAGI MYNGEPFQYS TDWYRYVVYN NPDWDDTKWS
VEDAAAALAQ NPYDIQTFDA DISSFRGAGG KVLTYHGLQD QMISSDNSKL YYARVAETMK
LPPSELDEFY RFFPVSGMTH CAGGDGAYGI GNGLGSYNGV DPENNVLMAM VQWVEKGIAP
EFIRGAKFAE GPGSAVEYTR KHCRYPRRNV YKGPGNYTDE NAWECV
