XYNB_ASPFN
ID XYNB_ASPFN Reviewed; 221 AA.
AC B8NJ86;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE AltName: Full=Endo-1,4-beta-xylanase G1;
DE Short=Xylanase G1;
DE Flags: Precursor;
GN Name=xlnB; Synonyms=xynB, xynG1; ORFNames=AFLA_065190;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
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).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; EQ963479; EED49697.1; -; Genomic_DNA.
DR RefSeq; XP_002380078.1; XM_002380037.1.
DR AlphaFoldDB; B8NJ86; -.
DR SMR; B8NJ86; -.
DR STRING; 5059.CADAFLAP00007943; -.
DR EnsemblFungi; EED49697; EED49697; AFLA_065190.
DR VEuPathDB; FungiDB:AFLA_065190; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR OMA; WSVRRQK; -.
DR BRENDA; 3.2.1.8; 506.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..221
FT /note="Probable endo-1,4-beta-xylanase B"
FT /id="PRO_0000393167"
FT DOMAIN 33..221
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 23746 MW; C010E11E5F53C77E CRC64;
MVSFSSLLLA VSAVSGALAA PGDSTLVELA KRAITSSETG TNNGYYYSFW TNGGGDVEYT
NGNGGQYSVK WTNCDNFVAG KGWNPGSAKT VTYSGEWESN SNSYVSLYGW TQNPLVEYYI
VDKYGDYDPS TGATELGTVE SDGGTYKIYK TTRENAPSIE GTSTFNQYWS VRQSGRVGGT
ITAQNHFDAW ANVGLQLGTH NYMILATEGY KSSGSATITV E