AGUA_ASPFC
ID AGUA_ASPFC Reviewed; 840 AA.
AC B0Y2K1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=AFUB_062100;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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; DS499597; EDP52172.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y2K1; -.
DR SMR; B0Y2K1; -.
DR EnsemblFungi; EDP52172; EDP52172; AFUB_062100.
DR VEuPathDB; FungiDB:AFUB_062100; -.
DR HOGENOM; CLU_007125_2_0_1; -.
DR PhylomeDB; B0Y2K1; -.
DR Proteomes; UP000001699; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..840
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_0000393486"
FT CARBOHYD 50
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 262
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 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 610
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 840 AA; 93625 MW; 9AD77161C2975EEE CRC64;
MWSGIPIFAL LSSIGIAAAE TGLDGWLRYA SVPCNGNCQR ALPSHIVTLN STRSSPVYVA
GQELQDGLHQ ILGKHASVKS TGCSTDSSII VGTVEAYRQV CNAGRQVPQL DVDGFWLSIR
EKSVLIVGQS ERGALYGAYE YLSMLAQGNF SQVSYATSPH APIRWVNQWD NMDGSIERGY
GGPSIFFKDG VIRQDLSRVQ QYARLLASVR INGIIVNNVN ANASLLMPSN MDGLARIADI
FRPYGIRVGI SLNFASPSTL GNLSTYDPFD SSVIAWWGNV TDQLYARIPD MAGYLVKANS
EGQPGPTTYN RTLADGANMF ARALKPYGGV VMFRAFVYDH HISEDNWYND RANAAVDFFK
PLDGKFDDNV VVQIKYGPID FQVREPASPL FANLYKTNTA IELQVTQEYL GQQSHLVYLP
PLWQTILGFD LRVDQKPSLV RDIISGQRFD RPLGGWAAVV NVGTNSTWLG SHLAMSNLYA
YGRLAWEPTL DSEDIVQDWI RLTFGLDRRI VDTLTQMSME SWPAYENYSG NLGIQTLTDI
LYTHYGPNPA SQDGNGWGQW TRADHLSIGM DRTVKNGTKF SGQYPAEVAA MYENIETTPD
NLLLWFHHVN YTQRLHSGKT VIQHFYDAHY TGAETAQTFV SQWESLRERI DAERYQHVLT
RLIYQAGHSI VWRDAINNFY HNLSGIADEK QRVGHHPWRV EAEDMQLDGY VPYAVSPFET
ASNYTAIVTA SNGTTGTASA TLDFKTGTYD LGINYYDMYG GKSHWTVYLN DRVVGQWQGN
SEDVLSHTPS IYLDGHSATR ITFRDVKIHK GDRLKIVGKP DGVEPAPLDY VVVLPPGIVD
