FAEB2_ASPFN
ID FAEB2_ASPFN Reviewed; 521 AA.
AC B8NPT0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=AFLA_001440;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963482; EED47503.1; -; Genomic_DNA.
DR RefSeq; XP_002382345.1; XM_002382304.1.
DR AlphaFoldDB; B8NPT0; -.
DR SMR; B8NPT0; -.
DR ESTHER; aspor-q2ubd6; Tannase.
DR EnsemblFungi; EED47503; EED47503; AFLA_001440.
DR VEuPathDB; FungiDB:AFLA_001440; -.
DR eggNOG; ENOG502SHYE; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; IDGCIKY; -.
DR Proteomes; UP000001875; 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..521
FT /note="Probable feruloyl esterase B-2"
FT /id="PRO_0000394928"
FT ACT_SITE 188
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 258
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 BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
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 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..75
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 63..114
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 187..440
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 257..274
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 283..291
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 506..520
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 521 AA; 57299 MW; 851947143547945A CRC64;
MKVSLWLTLL GVNLSLALAV GTDFPASCQA FSPDTRAANA HREFTEYVPA GTNLSLPYND
ATCARPNQVV TVDLCRVALY VETSNRSSVT TEIWLPRNWT GRFLGTGNGG IDGCIKYEDL
AYGAANGFAV VGSNNGHNGT TAASFYQNSD VLADFAWRAL HLSTVIGKEI TQAFYGEPHR
KSYYLGCSLG GRQGINSAVE FPDDFDGIIA GSPAVDFNSL VSWRASFFPI TGSANSTDFI
SVSTWKDLIH AEVLTQCDTL DCVNDGIIED PSLCNFCPEA LKCTDDRINN CLSPAQVEIV
RKVFSPMYGE DGQLIFPAMQ PGSELEAADQ LYTGKPFRYS KEWFQYVVYN PSWDPAEFDI
HDAKVADDLN PQNIRTWPND LSNYEKRGGK IITFHGQQDG KITSFNTERF YNHLATAMNM
SSSELDNFFR FFRISGMSHC SSGPGAWAFG QGGSPAPAMT PFNGNENILA ALVAWVEHGV
APETITGTKY VDDNPELGIS IRRSHCRFVI QLNHGRHELC Y
