AGUA_ASPNC
ID AGUA_ASPNC Reviewed; 841 AA.
AC A2R3X3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable alpha-glucuronidase A;
DE EC=3.2.1.139;
DE AltName: Full=Alpha-glucosiduronase A;
DE Flags: Precursor;
GN Name=aguA; ORFNames=An14g05800;
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: Alpha-glucuronidase 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. Releases 4-O-methylglucuronic acid from xylan (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:20005, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:58899; EC=3.2.1.139;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR EMBL; AM270325; CAK42141.1; -; Genomic_DNA.
DR RefSeq; XP_001401203.1; XM_001401166.1.
DR AlphaFoldDB; A2R3X3; -.
DR SMR; A2R3X3; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR PaxDb; A2R3X3; -.
DR EnsemblFungi; CAK42141; CAK42141; An14g05800.
DR GeneID; 4987438; -.
DR KEGG; ang:ANI_1_792124; -.
DR VEuPathDB; FungiDB:An14g05800; -.
DR HOGENOM; CLU_007125_2_0_1; -.
DR Proteomes; UP000006706; Chromosome 1R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.379.10; -; 1.
DR Gene3D; 3.90.1330.10; -; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..841
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_5000220976"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 841 AA; 93732 MW; F0516EE6D27F190E CRC64;
MRGLNLFQLI LALLLSMVAA EDGYDGWLRY APVSCDLHCQ QALPSHVVLL NSTKGSPIET
AGRELKAGFQ SILSTNLTSR PFQCNSSASI LVATLDEYRQ RCRDINVPEL DPDGFWLQSE
GDTVRILGKD ARGALYGAYE YLAMVAQRNF SRVAYATSPH APIRWVNQWD NMDGSIERGY
GGASIFFKDG TVVEDMAPVE QYARLLASIR INAIVVNNVN ANATLLLPEN MKGLSRIADA
CRPYGVQIGI SLNFASPEAL GGLNTYDPLD PGVIAWWQNI TDSLYTYVPD MAGYLVKADS
EGQPGPDTYN RTLSQGANLF ARALQPYGGV LMYRAFVYDD NLNESDWKAD RAKAAVEYFK
DLDGQFEENV VIQIKYGPID FQVREPTSPL FANLYHTNTA IELEVSQEYL GQQCHLVYLP
PLWKTVLDFD LRVDHKPSMV RDIISGQRFN RTLGGWAAVV NVGTNRTWLG SHLAMSNLYA
YGRLAWSPTD ESEQILEDWT RLTFGQNHHV INTISDMSMT SWPAYENYTG NLGIQTLTDI
LYTHYGPNPA TQDNNGWGQW TRADHDSVGM DRTIWNGTGY TGQYPEEVAR VYESLESTPD
DLVLWFHHVP WTHRLHSGVT VIQHFYNAHY AGAEAAHGFV RQWESLEGLI DRERYEAMRS
RLVYQAGHSI VWRDAINNFY YNMTGIPDVA GRVGHHPWRI EAESMGLDGY QTYTVSPFEA
ASNTTAIITT SNSTTGTART SIKAPSGVYD IGVNYYDLYG GQSKWTLSVG DKVVGQWLGD
MEHNSLGHTP SIYLGGHSAT RITFHGVGIR QGDQLKIVGE ANGVEPAPLD YIVLLPPGLV
D
