FAEB1_ASPFN
ID FAEB1_ASPFN Reviewed; 526 AA.
AC B8NPA4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=AFLA_128870;
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; EQ963481; EED48664.1; -; Genomic_DNA.
DR RefSeq; XP_002382080.1; XM_002382039.1.
DR AlphaFoldDB; B8NPA4; -.
DR SMR; B8NPA4; -.
DR ESTHER; aspor-q2umx6; Tannase.
DR EnsemblFungi; EED48664; EED48664; AFLA_128870.
DR VEuPathDB; FungiDB:AFLA_128870; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; LTPMAKN; -.
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..526
FT /note="Probable feruloyl esterase B-1"
FT /id="PRO_0000394922"
FT ACT_SITE 188
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 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 BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
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 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
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 490
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 28..75
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 63..114
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 187..441
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 256..273
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 282..291
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 503..525
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 526 AA; 57748 MW; 3B4DE68DEA9D83E7 CRC64;
MPSLRRLLPF LAAGSAALAS QDTFQGKCTG FADKINLPDV RVNFVNYVPG GTNLSLPDNP
TSCGTTSQVV SEDVCRIAMA VATSNSSEIT LEAWLPQNYT GRFLSTGNGG LSGCIQYYDL
AYTSGLGFAT VGANSGHNGT SGEPFYHHPE VLEDFVHRSV HTGVVVGKQL TKLFYEEGFK
KSYYLGCSTG GRQGFKSVQK YPNDFDGVVA GAPAFNMINL MSWSAHFYSI TGPVGSDTYL
SPDLWNITHK EILRQCDGID GAEDGIIEDP SLCSPVLEAI ICKPGQNTTE CLTGKQAHTV
REIFSPLYGV NGTLLYPRMQ PGSEVMASSI MYNGQPFQYS ADWYRYVVYE NPNWDATKFS
VRDAAVALKQ NPFNLQTWDA DISSFRKAGG KVLTYHGLMD QLISSENSKL YYARVAETMN
VPPEELDEFY RFFQISGMAH CSGGDGAYGI GNQLVTYNDA NPENNVLMAM VQWVEKGIAP
ETIRGAKFTN GTGSAVEYTR KHCRYPRRNV YKGPGNYTDE NAWQCV
