FAEB2_NEOFI
ID FAEB2_NEOFI Reviewed; 526 AA.
AC A1DMV3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=NFIA_054700;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027698; EAW16124.1; -; Genomic_DNA.
DR RefSeq; XP_001258021.1; XM_001258020.1.
DR AlphaFoldDB; A1DMV3; -.
DR SMR; A1DMV3; -.
DR ESTHER; neofi-faeb2; Tannase.
DR EnsemblFungi; EAW16124; EAW16124; NFIA_054700.
DR GeneID; 4584536; -.
DR KEGG; nfi:NFIA_054700; -.
DR VEuPathDB; FungiDB:NFIA_054700; -.
DR eggNOG; ENOG502QPXZ; Eukaryota.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; LTPMAKN; -.
DR OrthoDB; 977166at2759; -.
DR Proteomes; UP000006702; 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-2"
FT /id="PRO_0000394932"
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 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 57575 MW; 9FD05AAE37AD7F6F CRC64;
MTKLSLLPLL ALASAVLAKQ DAFQAKCASF GHRIKLPNVH VNFVEYVPGG TNLTLPDNHV
TCGASSQIVS ADMCRVAMAV DTSKSSQITL EAWFPRNYTG RFLSTGNGGL SGCIQYYDLA
YTAGLGFATV GANNGHNGTS GKPFYQHPEV IEDFAYRSIH TGVVVGKQLI KMFYSEGFDK
SYYLGCSTGG RQGFKSIQKY PNDFDGVVAG APAFNFVNLI SWSIHFYSIT GSNTSDTYLS
PASWKVVHDE IVRQCDGIDG AKDGIIEDTD LCHPILETII CKPGASSTTN CITGTQAKTV
RNVLSPFYGV NGTLLYPRMQ PGSELFASSI MYNGQPFSYS TDWYRYVVYN NPNWDATKWT
VEDAAVALAQ NPYNIQTWDA DISSFQKAGG KVLTYHGIQD QLISSDNSKL YYARVAETMG
LGPEELDDFY RFFPVSGMAH CSGGDGAYGI GNGLRTYNGA EPENNVLMAM VQWVEKGVAP
EFIRGAKFSN GVGSPVEYTR KHCKYPRRNV YKGPGNYSDE NAWECV
