AGUA_ASPTU
ID AGUA_ASPTU Reviewed; 841 AA.
AC O42814;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Alpha-glucuronidase A;
DE EC=3.2.1.139;
DE AltName: Full=Alpha-glucosiduronase A;
DE Flags: Precursor;
GN Name=aguA;
OS Aspergillus tubingensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NW756;
RX PubMed=9440512; DOI=10.1128/jb.180.2.243-249.1998;
RA de Vries R.P., Poulsen C.H., Madrid S., Visser J.;
RT "AguA, the gene encoding an extracellular alpha-glucuronidase from
RT Aspergillus tubingensis, is specifically induced on xylose and not on
RT glucuronic acid.";
RL J. Bacteriol. 180:243-249(1998).
RN [2]
RP FUNCTION.
RX PubMed=10779688; DOI=10.1016/s0304-4165(00)00029-5;
RA Biely P., de Vries R.P., Vrsanska M., Visser J.;
RT "Inverting character of alpha-glucuronidase A from Aspergillus
RT tubingensis.";
RL Biochim. Biophys. Acta 1474:360-364(2000).
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.
CC {ECO:0000269|PubMed:10779688, ECO:0000269|PubMed:9440512}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-6.0. {ECO:0000269|PubMed:9440512};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:9440512};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By xylan and xylose but not by glucuronic acid.
CC {ECO:0000269|PubMed:9440512}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y15405; CAA75605.1; -; Genomic_DNA.
DR AlphaFoldDB; O42814; -.
DR SMR; O42814; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR CLAE; AGU67A_ASPTU; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_194940; -.
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 1: Evidence at protein 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="Alpha-glucuronidase A"
FT /id="PRO_0000012243"
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 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; 93904 MW; 68F17219D1988309 CRC64;
MRGSNLFQLT LALLLSLVAA EDGYNGWLRY APVSCDLHCR QALPSHIVLL NSTKGSPIET
AGRELKAGFQ SILSTNLTFH PFQCDSSASI LVATLDEYRQ KCRDINLPEL DPDGFWLQSE
GDTVRILGNN ARGALYGAYE YLAMVAQRNF SRVAYTTNPH APIRWVNQWD NMDGSIERGY
GGASIFFKDG TVVEDMAPVE QYARLLASIR INAIVVNNVN ANATLLLPEN MKGLGRIADA
CRPYGVQIGI SLNFASPESL GGLETYDPLD PGVIAWWQNI TDSLYTYVPD MAGYLVKADS
EGQPGPDTYN RTLSQGANLF ARALQPHGGV LMYRAFVYND NLNESDWKAD RAKAAVEYFK
DLDGQFYENV VVQIKYGPID FQVREPTSPL FANLYQTNTA IELEVSQEYL GQQCHLVYLP
PLWKTVLDFD LRVDHKPSMV RDILSGQRFN RTLGGWAAVV NVGTNRTWLG SHLAMSNLYA
YGRLAWSPTD DSEQILKDWT RLTFGQNRQV IDTIADMPMT SWPAYENYTG NLGIQTLTDI
LYTHYGPNPA TQDNNGWGQW TRADHNSVGM DRTISNGTGY TGQYPEEVAR LYESLETTPD
DLVLWFHHVP WTHRLHSGLT VIQHFYNAHY AGSEAAHGFI RQWESLKGLI DRERYEAMRS
RLVYQAGHSI VWRDAINNFY YNMTGIPDVA GRVGHHPWRI EAESMRLDGY QTYTVSPFEA
ASNTTAIITT SNSTTGTART TIKAPSGVYD IGVNYYDLYG GQSKWTLSVG DKVVGQWLGD
MEHQSLGHTP SIYLDGHSAT RITFHGVVVR QGDQLKIVGE ANGVEPAPVD YVVLLPPGVV
D
