FAEB2_ASPTN
ID FAEB2_ASPTN Reviewed; 527 AA.
AC Q0CI21;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 56.
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=ATEG_06663;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU33207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476602; EAU33207.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215841.1; XM_001215841.1.
DR AlphaFoldDB; Q0CI21; -.
DR SMR; Q0CI21; -.
DR ESTHER; asptn-faeb2; Tannase.
DR GeneID; 4322286; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
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..527
FT /note="Probable feruloyl esterase B-2"
FT /id="PRO_0000394931"
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 180
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 355
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 527 AA; 57504 MW; 5AB89D56E04EE3CC CRC64;
MAPIHYLLPI ITLGSAALAR QDAFEAKCHS FANKIHLPNV HVNFASYVPG GTNLTLADNP
SSCGATSQSV SADVCRVAMA VATSNSSEIT LEAWFPRNYT GRFLSTGNGG LSGCIQYYDM
AYTTGFGFAT VGANNGHNGT SGEPFYHHPE VLEDFAYRSI HTGVVIGKKL TKMFYEEGFN
KSYYLGCSTG GRQGFKSVQK YPNDFDGVVA GAPAFNFANL ISWSAHFYPI TGPPGSDTYL
SPAMWKVAHD EIIRQCDQID GAKDGIIEDP SLCNPIMETI ICKPGASSDN CLSAAQAKTV
REVLYPLYGV NGTLLYPRMQ PGSEVLAAPI MYNGQPFAYS TDWYRYVVYN DPNWNGTTFD
VQDAAAALAQ NPYNIQTWDA DLTPFRKSGG KVLTYHGLQD QLISSENSKL YYARVAETMG
MPPEELDEFY RFFQISGMGH CGGGDGAYGI GNGLATYSGK DPENNVLMAM VQWVEKGIAP
ETVRGAKFAN GPGSTVEYSR KHCRYPRRNV FKGPGNYTDE NAWECVV
