AGUA_ASPFN
ID AGUA_ASPFN Reviewed; 839 AA.
AC B8NGU1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=AFLA_138090;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963478; EED51045.1; -; Genomic_DNA.
DR RefSeq; XP_002379821.1; XM_002379780.1.
DR AlphaFoldDB; B8NGU1; -.
DR SMR; B8NGU1; -.
DR STRING; 5059.CADAFLAP00007686; -.
DR EnsemblFungi; EED51045; EED51045; AFLA_138090.
DR VEuPathDB; FungiDB:AFLA_138090; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OMA; DNNGWGQ; -.
DR Proteomes; UP000001875; 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; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..839
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_0000393487"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 839 AA; 93920 MW; CDE72379B43B295C CRC64;
MRWSFLTVLL WLVSLTGAEN GFNGWLRYAP VQCDKRCQRA LPSSIVTLNS TDSGPIGTAS
QELQAGLENI VGKQLSIKRS SCGSRSSILV ATLEQYRQAC NRSSEVPSLG IDGFWLRAYG
DTVQIVGENE RGALYGAFEY LSLLAQGNFS HVDYTTSAHA PVRWVNQWDN MDGSIERGYA
GPSIFFEDGH IVEDLSRVKQ YARLLASIRI NGVIVNNVNA NATLLTSQNM DGLARIANVF
RPYGIQIGIS LNFASPDTLG GLGTYDPLDP SVISWWANIT DSLYDRVPDM AGYLVKASSE
GQPGPDTYNR TLAEGANVFA KALQPHGGIL MFRTFVYDHH INESIWTNDR ANAQVDFFKE
LDGQFEDNVI LQIKYGPIDF QVREPVSPLF ANLYKTNMAI ELQVTQEYLG QQDHLVYLSP
LWKELLDFDL RVDHQPSLVR DIVSGQRFDR QLGGWAAVVN VGTNTTWLGS HLAMSNLYAY
GRLAWSPTDD SQGILQDWIR LTFGRDQNVL DTITDMSMAS WPAYENYTGN LGIQTLTDIL
YTHYGPNPAS QDNNGWGQWT RADHDTIGMD RTVKNGTGNA GQYPAEIAQV YEDLDSTPDD
LLLWFHHVPY THRLHSGKTV IQHFYDAHYD GAETAHRFLS QWESLKGRID QQRYNEVLSR
LVYQAGHSLV WRDAINNFYW NMSGISDEKN RVGHHPWRVE AESMTLDGYE PYTVSPFETA
SNYKAVVTTS NSTTGTAQTK LQFPSGTYDL GVNYYDMYGG KSEWTVYVND RVVGQWEGNS
ENTLGHTPSI YIDGHSATRI TFRGVEIENG DQLKIVGVPD GVEPAPLDYV VLLPPDVVD
