FAEB1_ASPOR
ID FAEB1_ASPOR Reviewed; 540 AA.
AC Q2UP89;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=AO090001000066;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 19-540 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BOND, GLYCOSYLATION AT ASN-49; ASN-95; ASN-234; ASN-298 AND
RP ASN-367, ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF CYS-202 AND CYS-458.
RX PubMed=25066066; DOI=10.1002/prot.24649;
RA Suzuki K., Hori A., Kawamoto K., Thangudu R.R., Ishida T., Igarashi K.,
RA Samejima M., Yamada C., Arakawa T., Wakagi T., Koseki T., Fushinobu S.;
RT "Crystal structure of a feruloyl esterase belonging to the tannase family:
RT a disulfide bond near a catalytic triad.";
RL Proteins 82:2857-2867(2014).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25066066}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: The calcium ion seen in the crystal structure is located
CC far from the active site and appears to have a role in stabilization of
CC the lid domain. {ECO:0000305|PubMed:25066066}.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007154; BAE56626.1; -; Genomic_DNA.
DR RefSeq; XP_001818628.2; XM_001818576.2.
DR PDB; 3WMT; X-ray; 1.50 A; A/B=19-540.
DR PDBsum; 3WMT; -.
DR AlphaFoldDB; Q2UP89; -.
DR SMR; Q2UP89; -.
DR ESTHER; aspor-q2up89; Tannase.
DR iPTMnet; Q2UP89; -.
DR PRIDE; Q2UP89; -.
DR EnsemblFungi; BAE56626; BAE56626; AO090001000066.
DR GeneID; 5990599; -.
DR KEGG; aor:AO090001000066; -.
DR VEuPathDB; FungiDB:AO090001000066; -.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; INLISWG; -.
DR BRENDA; 3.1.1.73; 522.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:AspGD.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Polysaccharide degradation;
KW Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..540
FT /note="Probable feruloyl esterase B-1"
FT /id="PRO_0000394924"
FT ACT_SITE 203
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:25066066"
FT ACT_SITE 417
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:25066066"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:25066066"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25066066,
FT ECO:0007744|PDB:3WMT"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..90
FT /evidence="ECO:0000269|PubMed:25066066"
FT DISULFID 76..129
FT /evidence="ECO:0000269|PubMed:25066066"
FT DISULFID 202..458
FT /evidence="ECO:0000269|PubMed:25066066"
FT DISULFID 271..288
FT /evidence="ECO:0000269|PubMed:25066066"
FT DISULFID 297..308
FT /evidence="ECO:0000269|PubMed:25066066"
FT DISULFID 517..539
FT /evidence="ECO:0000269|PubMed:25066066"
FT MUTAGEN 202
FT /note="C->A: High decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:25066066"
FT MUTAGEN 458
FT /note="C->A: High decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:25066066"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 102..113
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:3WMT"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 173..189
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 422..436
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3WMT"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 483..493
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 498..506
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 509..517
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:3WMT"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:3WMT"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:3WMT"
SQ SEQUENCE 540 AA; 58419 MW; D9F39D10FEDBD265 CRC64;
MLVMQLLLPF LASTAAAAAA IDSTSSSNGS DHHGSSFQAE CESFKAKINV TNANVHSVTY
VPAGVNISMA DNPSICGGDE DPITSTFAFC RIALNVTTSS KSQIFMEAWL PSNYSGRFLS
TGNGGLGGCV KYDDMAYAAG YGFATVGTNN GHFGNNGVSF YQNTEVVEDF AYRALHTGVV
VGKELTKNFY PQGYNKSYYL GCSTGGRQGW KSVQTFPDDF DGVVAGAPAF NFINLTSWGA
RFLTLTGDSS AETFVTETQW TAVHNEIIRQ CDSLDGAKDG IIEDPDLCQP IIEALLCNAT
QSSTSGTCLT GAQVKTVNGV FSATYGLNGS FLYPRMQPGS ELAAYSSYYS GTPFAYAEDW
YRYVVFNNTN WDVATWTVQD AAIANAQDPY QISTWNGDLS PFQKKGGKVL HYHGMEDAII
SSESSKVYYK HVADTMNLSP SELDSFYRFF PISGMAHCAN ADGPSAIGQG TGTFAGNNPQ
DNVLLAMVQW VEEGVAPDFV RGAKLNGSTV EYRRKHCKYP KRNRYVGPGS YTDENAWECV
