XGEA_ASPNC
ID XGEA_ASPNC Reviewed; 241 AA.
AC A2Q877;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable 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; ORFNames=An01g03340;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
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; AM269957; CAK36874.1; -; Genomic_DNA.
DR RefSeq; XP_001388766.1; XM_001388729.2.
DR AlphaFoldDB; A2Q877; -.
DR SMR; A2Q877; -.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR PaxDb; A2Q877; -.
DR EnsemblFungi; CAK36874; CAK36874; An01g03340.
DR GeneID; 4977580; -.
DR KEGG; ang:ANI_1_432014; -.
DR VEuPathDB; FungiDB:An01g03340; -.
DR HOGENOM; CLU_051064_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..241
FT /note="Probable xyloglucan-specific endo-beta-1,4-glucanase
FT A"
FT /id="PRO_5000219338"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 241 AA; 25483 MW; CE5355546B29B0DB CRC64;
MKVLALSALL SLASAASISR RSDFCGQWDT ATAGDFILYN DLWGEDNASS GSQCTGVDSA
SGNEIAWHTS WSWEGGSSDV KSYANAALQF TGTQLSSISS IPSTWKWTYS GSDIVADVAY
DMFLGSTADA SSDEYEIMVW LAALGGAGPI SSTGSTIATP TINGVTWDLY TGPNGDTTVY
SFVAQSTTED FSGDLNDFFT YLVDNEGVSD SLYLTTLEAG TEPFTGSDAE LKVSEYSVSI
E