ID   XGEA_ASPNG              Reviewed;         241 AA.
AC   A1XP58;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase A;
DE            EC=3.2.1.151;
DE   AltName: Full=Xyloglucanase A;
DE   AltName: Full=Xyloglucanendohydrolase A;
DE   Flags: Precursor;
GN   Name=xgeA; Synonyms=XEG12A;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 9089 / N402;
RX   PubMed=18072936; DOI=10.1042/bj20070819;
RA   Master E.R., Zheng Y., Storms R., Tsang A., Powlowski J.;
RT   "A xyloglucan-specific family 12 glycosyl hydrolase from Aspergillus niger:
RT   recombinant expression, purification and characterization.";
RL   Biochem. J. 411:161-170(2008).
CC   -!- FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in
CC       xyloglucan with retention of the beta-configuration of the glycosyl
CC       residues. Specific for xyloglucan and does not hydrolyze other cell
CC       wall components (Probable). {ECO:0000305|PubMed:18072936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:18072936};
CC       Temperature dependence:
CC         Optimum temperature is between 50 and 60 degrees Celsius.
CC         {ECO:0000269|PubMed:18072936};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC       {ECO:0000305}.
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DR   EMBL; DQ486529; ABF46829.1; -; mRNA.
DR   AlphaFoldDB; A1XP58; -.
DR   SMR; A1XP58; -.
DR   STRING; 5061.CADANGAP00000317; -.
DR   CAZy; GH12; Glycoside Hydrolase Family 12.
DR   CLAE; XEG12A_ASPNG; -.
DR   VEuPathDB; FungiDB:An01g03340; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1142168; -.
DR   VEuPathDB; FungiDB:ATCC64974_20420; -.
DR   VEuPathDB; FungiDB:M747DRAFT_334034; -.
DR   eggNOG; ENOG502RW43; Eukaryota.
DR   BioCyc; MetaCyc:MON-16908; -.
DR   BRENDA; 3.2.1.151; 518.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR002594; GH12.
DR   PANTHER; PTHR34002; PTHR34002; 1.
DR   Pfam; PF01670; Glyco_hydro_12; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..241
FT                   /note="Xyloglucan-specific endo-beta-1,4-glucanase A"
FT                   /id="PRO_5000214050"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   241 AA;  25456 MW;  FE4E5CD2B9CB46A2 CRC64;
     MKVLALSALL SLASAASISR RSDFCGQWDT ATAGDFILYN DLWGEDNASS GSQCTGVDSA
     SGSEIAWHTS WSWEGGSSDV KSYANAALQF TGTQLSSISS IPSTWKWTYS GSDIVADVAY
     DMFLGSTADA SSDEYEIMVW LAALGGAGPI SSTGSTIATP TINGVTWDLY TGPNGDTTVY
     SFVAQSTTED FSGDLNDFFT YLVDNEGVSD SLYLTTLEAG TEPFTGSDAE LKVSEYSVSI
     E