FAE1_ARTBC
ID FAE1_ARTBC Reviewed; 537 AA.
AC D4AS70;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Probable feruloyl esterase ARB_07085 {ECO:0000305};
DE EC=3.1.1.73 {ECO:0000250|UniProtKB:Q8WZI8};
DE Flags: Precursor;
GN ORFNames=ARB_07085;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans
CC as well as the feruloyl-galactose and feruloyl-arabinose ester bonds.
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:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
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DR EMBL; ABSU01000007; EFE34134.1; -; Genomic_DNA.
DR RefSeq; XP_003014523.1; XM_003014477.1.
DR AlphaFoldDB; D4AS70; -.
DR SMR; D4AS70; -.
DR EnsemblFungi; EFE34134; EFE34134; ARB_07085.
DR GeneID; 9520575; -.
DR KEGG; abe:ARB_07085; -.
DR eggNOG; ENOG502SH94; Eukaryota.
DR HOGENOM; CLU_014819_3_2_1; -.
DR OMA; TCELDAF; -.
DR Proteomes; UP000008866; 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 1: Evidence at protein level;
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..537
FT /note="Probable feruloyl esterase ARB_07085"
FT /id="PRO_5001370734"
FT ACT_SITE 197
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 419
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 458
FT /note="Charge relay system"
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 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 196..459
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 263..280
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 508..529
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 537 AA; 57777 MW; C70406061EAE9AFC CRC64;
MVTLPLLLSI LPLAAVFSSA ASLQVRENHD CASIQPPQVP GAEILSVIGV QRRVEVAPFP
PSPSKPNTTI DICSVNVTLS HMGVNDKVVV SVWLPLPDKW NGRFQATGGG GWAAGTFDLL
MGPAALEGYS TAGTDAGVTV DPGSADKWAL KEDGTVNYDL LENFASRSIH DMAIVGKAVT
ESYYKKPANY SYFYGCSNGG RQGMVEAQKY PDDFDGILAG APAIYWPQFL TSTEWPQVVM
QSEKVFPSQC VFEAFRKAGI AACDKLDGVE DGVVSNLDGC EFNPFALVGK KVKCGEESTT
ITLAQAWVAK KIYDGPKSTA KHALWDVLPV GASYVGLANS TIENGVPKIA PFVIGSSWIR
SFLKKDVNFD LSTITYADMP KLFQQSIDEF DKIAGGSNPD LSALKKSGTK LLSWHGLADE
LIHPQGSIKY RQAVEHRMGG GSEVDNYYRL FLAPGVTHCG IGVNDGAAPI DTLKVLVRWV
EKGEAPETMP ATATDASGTT TLFTRNLCRY PLVPRYKGGD KNSADSFECA KDFGSHH
