AGUA_ASPTN
ID AGUA_ASPTN Reviewed; 841 AA.
AC Q0CJP9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=ATEG_06085;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476601; EAU33846.1; -; Genomic_DNA.
DR RefSeq; XP_001215263.1; XM_001215263.1.
DR AlphaFoldDB; Q0CJP9; -.
DR SMR; Q0CJP9; -.
DR STRING; 341663.Q0CJP9; -.
DR EnsemblFungi; EAU33846; EAU33846; ATEG_06085.
DR GeneID; 4321653; -.
DR VEuPathDB; FungiDB:ATEG_06085; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OMA; DNNGWGQ; -.
DR OrthoDB; 127527at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..841
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_0000393490"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 841 AA; 93769 MW; D57F2539FD082B5E CRC64;
MLRLPLVLVW SLWASLTVAE NGLNGWLRYA PIPCDGRCHK ALPSRIVALN STQGSPLETA
IEELQTGVRG MTGKRLSVAK ENNCNLHATA LIATVEEYRR TCRNSSDIPD LDVDGFWLRT
EGNNVQILGQ SERGALYGAF EYLSMLAQGD FSSVDYSTSP HAPVRWVNQW DNMDGSIERG
YAGPSIFFAQ GQIVPDLSRA KQYARLLASV RINGIIVNNV NANATLLTPQ NMDGLARIAN
VFRPYGIRIG IALNFASPDT LGGLGTYDPL DPSVISWWGN ITDSLYERIP DMAGYLVKAS
SEGQPGPDTY NRTLADGANL FARALKPHGG VMMFRAFVYD HHINESIWTN DRANAQVDFF
KKLDGQFEDN VIVQIKYGPI DFQVREPVSP LFANLYHTNT AIELQVTQEY LGQQCHLVYL
PPLWKTITDF DLRVDHSPSV VRDIISGERF NRPLGGWAAV VNVGTNDTWL GSHLSMSNLY
AYGRMAWSPT DDSVEILQDW IRLTFGRDQH VLDTITDMSM ASWPAYENYT GNLGIQTLTD
ILYTHYGPNP ASQDGNGWGQ WTRADHDSIG MDRTVKNGTG NAGQYPAEIA EIYEDIDKTP
DDLLLWFHHV PYTHRLDSGK TVIQHFYDAH YAGAETAQGF VPQWESLRGR IDPERYDAMR
TRLVYQAGHS IVWRDAINNF YWNLSGIADT NGRVGHHPWR VEAESMQLQG YQPYAVSPFE
TASNYTAVVT TSNSTTGTAS TTLDFPSGTY DVGVNYFDMY GGKSRWSLYL NDKVVGKWEG
NSEDVLGHTP SIYLDGHSAI RITFNGVKVR KGDRLKIVGV PDGVEPAPLD YVVFLPQGVI
D
