ID B8NGM1_ASPFN Unreviewed; 564 AA.
AC B8NGM1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Xylosidase: arabinofuranosidase {ECO:0000313|EMBL:EED50885.1};
GN ORFNames=AFLA_136480 {ECO:0000313|EMBL:EED50885.1}, G4B84_005552
GN {ECO:0000313|EMBL:QMW30217.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED50885.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED50885.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED50885.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW30217.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW30217.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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; EQ963478; EED50885.1; -; Genomic_DNA.
DR EMBL; CP059868; QMW30217.1; -; Genomic_DNA.
DR RefSeq; XP_002379661.1; XM_002379620.1.
DR AlphaFoldDB; B8NGM1; -.
DR STRING; 332952.B8NGM1; -.
DR EnsemblFungi; EED50885; EED50885; AFLA_136480.
DR VEuPathDB; FungiDB:AFLA_006013; -.
DR eggNOG; ENOG502SIVT; Eukaryota.
DR HOGENOM; CLU_016508_3_0_1; -.
DR OMA; YWRYPKT; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 3.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18833; GH43_PcXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..564
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035142811"
FT DOMAIN 348..557
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT SITE 152
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 564 AA; 62048 MW; C2D09706FB47B9ED CRC64;
MWTPGVSALS FLALATSALC QPIGLSPYTN PILPGWHSDP SCAYVEEDDT IFCVTSTFIA
FPGLPIYATK DLQNWKQVSN VFNRPSQIPS LSNTTNQQGG IYAPTLRYHD GTFYLIVSFL
GPEIKGLVFT SSDPYSDAAW SEPLEFSVRG IDPDIFWDDD GTVYVTSADD ARIQHYSLDL
QTGETGPVTY LWNGTGGASP EGPHLYRKDD FYYLMIAEGG TELNHAETMV RSKNRTGPWE
LCPHNPILTN RNTTQYFQTV GHADLFQDGT GNWWAVALST RSGPEWKNYP MGRETVLAPA
TWEEGEWLVV QPVRGQMQGP LPRENKDGIK GDGSFVNEPD HVTFAPGDSI PSHFLYWRYP
ETSNFAVSPQ DHPNTLRLTP SLYNITGNAS STPEEGITLL TRRQTDTLFT YSVDIAFDPQ
VPDEEAGVTL FLTQLQHVDL GLVLLESQNG TSSPALQLRT EGHGNYEGSL PGSIVSVPEG
WRGEPIRFQI QAVSDTQYEF SVASVKTPAQ RAVVGYADSR IVSGDTGRFT GTLVGVYATS
NGGSGTTDAY ISNWRYEGQG QKII
//
