FAEB1_ASPTN
ID FAEB1_ASPTN Reviewed; 529 AA.
AC Q0CVS2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=ATEG_02212;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37174.1; -; Genomic_DNA.
DR RefSeq; XP_001211390.1; XM_001211390.1.
DR AlphaFoldDB; Q0CVS2; -.
DR SMR; Q0CVS2; -.
DR ESTHER; asptn-faeb1; Tannase.
DR EnsemblFungi; EAU37174; EAU37174; ATEG_02212.
DR GeneID; 4316909; -.
DR VEuPathDB; FungiDB:ATEG_02212; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; LTPMAKN; -.
DR OrthoDB; 977166at2759; -.
DR Proteomes; UP000007963; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..529
FT /note="Probable feruloyl esterase B-1"
FT /id="PRO_0000394925"
FT ACT_SITE 188
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 444
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 64
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 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..75
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 63..114
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 187..445
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 256..273
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 282..295
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 505..527
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 529 AA; 59051 MW; 8AE60FE1EDFA403D CRC64;
MKISYFFVAS LSYVSVARAS QSFEERCTDF RDSINSLPNV QATIVEYVAG SQNVSLPDND
PSCNQSSQFV TADICRAAMV VKTSNSSQIV MEAWFPRNYT GRFLATGNGG FGGCIRYPEL
DYTTRLGFAA VATNNGHNGT SAEAFLNSPE VLRDFADRSI HTAAKVGKEL TKRFYAEGFR
KSYYLGCSTG GRQGFKSVQQ YPHDFDGVVA GAPAVHEVNL ISWAGHIYEI TGNKSEETYL
PPALWNIVHS EVMRQCDGLD GAQDNLIEDP DLCHPTFENI MCPSDNKSNN GSLSCITEAQ
ANTVIQLMSP YYNTDGSMLF PGMQPGSETV SSALLYTGVP TPYAKEWFRY VVYNDTNWDP
TTFNIKDAQA ALKQNPFNIQ TWEGDLSRFQ NAGGKIITYH GMQDFLVSSF NSREYYKHVH
ETMGLAPDQL DEFYRYFRIS GMAHCYYGDG ASYIGGSAPS AYSDDPEDNV LMAMVEWVEK
GIAPEFIRGT KLDQDGHPQY TRKHCRYPRR NVYRGPGSYL DENAWECVL
