AGUA_ASPNG
ID AGUA_ASPNG Reviewed; 841 AA.
AC Q96WX9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 74.
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;
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 [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=12242504; DOI=10.1007/s00438-002-0729-7;
RA de Vries R.P., van de Vondervoort P.J.I., Hendriks L., van de Belt M.,
RA Visser J.V.;
RT "Regulation of the a-glucuronidase encoding gene (aguA) from Aspergillus
RT niger.";
RL Mol. Genet. Genomics 268:96-102(2002).
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 -!- INDUCTION: Expressed in the presence of D-xylose and L-arabinose and at
CC very low level in the presence of D-glucuronic acid. Expression is
CC under the control of the xylanolytic transcriptional activator xlnR and
CC the carbon catabolite repressor creA. {ECO:0000269|PubMed:12242504}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR EMBL; AJ290451; CAC38119.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96WX9; -.
DR SMR; Q96WX9; -.
DR STRING; 5061.CADANGAP00011295; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR VEuPathDB; FungiDB:An14g05800; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1161751; -.
DR VEuPathDB; FungiDB:ATCC64974_4680; -.
DR VEuPathDB; FungiDB:M747DRAFT_320051; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..841
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_5000066287"
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; 93950 MW; BAA43615A2B89B73 CRC64;
MRGLNLFQLI LALLLSMVAA EDGYDGWLRY APVSCDLRCR QALPSHVVLL NSTKGSPIET
AGRELKAGFQ SILSTNLTSR PFQCNSSTSI LVATLDEYRQ RCRDINVPEL DPDGFWLQSE
GDTVRILGKD ARGALYGAYE YLAMVAQRNF SRVAYATSPH APIRWVNQWD NMDGSIERGY
GGASIFFKDG TVVEDMAPVE QYARLLASIR INAIVVNNVN ANATLLLPEN MKGLGRIADA
CRPYGVQIGI SLNFASPEDL 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 DRTIRNGTGY TGQYPEEVAR VYESLESTPD
DLVLWFHHVP WTHRLHSGVT VIQHFYNAHY AGAEAAHGFV RQWESLEGLI DRERYEAMRS
RLVYQAGHSI VWRDAINNFY YNMTGIPDVA GRVGHHPWRI EAESMRLDGY QTYTVSPFEA
ASNTTAIITT SNSTTGTART SIKAPSGVYD IGVNYYDLYG GQSKWTLSVG DKVVGQWLGD
MEHNSLGHTP SIYLDGHSAT RITFHGVGIR QGDQLKIVGE ANGVEPAPLD YIVLLPPGLV
D
