FAEB2_ASPOR
ID FAEB2_ASPOR Reviewed; 526 AA.
AC Q2UMX6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=AO090001000582;
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).
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; AP007154; BAE57089.1; -; Genomic_DNA.
DR RefSeq; XP_001819091.1; XM_001819039.1.
DR PDB; 6G21; X-ray; 2.10 A; A/B=20-526.
DR PDBsum; 6G21; -.
DR AlphaFoldDB; Q2UMX6; -.
DR SMR; Q2UMX6; -.
DR ESTHER; aspor-q2umx6; Tannase.
DR EnsemblFungi; BAE57089; BAE57089; AO090001000582.
DR GeneID; 5991062; -.
DR KEGG; aor:AO090001000582; -.
DR VEuPathDB; FungiDB:AO090001000582; -.
DR HOGENOM; CLU_014819_1_0_1; -.
DR OMA; LTPMAKN; -.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..526
FT /note="Probable feruloyl esterase B-2"
FT /id="PRO_0000394930"
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"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 405..419
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:6G21"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6G21"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 481..491
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6G21"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:6G21"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:6G21"
SQ SEQUENCE 526 AA; 57747 MW; 72A258760523780A CRC64;
MPSLRRLLPF LAAGSAALAS QDTFQGKCTG FADKINLPNV 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
