AGUA_ASPCL
ID AGUA_ASPCL Reviewed; 840 AA.
AC A1CC12;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=ACLA_017270;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
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DR EMBL; DS027049; EAW13280.1; -; Genomic_DNA.
DR RefSeq; XP_001274706.1; XM_001274705.1.
DR AlphaFoldDB; A1CC12; -.
DR SMR; A1CC12; -.
DR STRING; 5057.CADACLAP00001216; -.
DR EnsemblFungi; EAW13280; EAW13280; ACLA_017270.
DR GeneID; 4706795; -.
DR KEGG; act:ACLA_017270; -.
DR VEuPathDB; FungiDB:ACLA_017270; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OMA; DNNGWGQ; -.
DR OrthoDB; 127527at2759; -.
DR Proteomes; UP000006701; 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..840
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_0000393485"
FT CARBOHYD 222
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 682
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; 93928 MW; 9283A30F8B73E698 CRC64;
MRSVITTLTL VASVGLAVAE NGFDGWLRYA PVSCHGACQK SLPSHIVTLD PTESSPISVA
GQEIQDGLQR MFKMHATVEP KGCSTRSSVI IGTLDAYNHA CKDADPVPEL EEDGFWLNTK
DGKVQIIGQS ERGALYGAYE YLSMLSQGNF APVSYTTSPH APIRWVNQWD NMDGSMEHGY
GGLSIFFKDG VIPQDLSRVK QYARLLASIR INGIIVNNVN ANASLLKPEN MDGLARIADI
FRPYGVKVGI SLNFASPSTL GGLNTYDPLD ESVISWWGGI TDELYKRVPD MAGYLVKANS
EGQPGPTTYN RTLAEGANLF ARALKPHGGI VMFRAFVYDH HISEENWYND RANAAVDFFK
PLDGKFEENV VVQIKYGPID FQVREPVSPL FANLYKTNTA IELQVTQEYL GQQSHLVYLP
PLWQTILGFD LRVDGKPSPT RDIISGQRFN RPLGGWAAVV NVGTNTTWLG SHLALSNLYA
YGRLAWEPTL DSQDILQDWI RMTFGLDRRV LDTITKMSME SWPAYENYSG NLGIQTLTDI
LYTHYGPNPA SQDGNGWGQW TRADHEAIGM DRTIKNGTKF TGQYPAEVAQ VYENIETTPD
DLLLWFHHVP YTQRLQSGKT VIQHFYDAHY AGADTAQTFV SQWESLRGKI DPERYEHVLT
RLIYQAGHSI VWRDAINEFY HNLSGIADEK QRVGHHPWRI EAEDMKLDGY VPYDVNPFET
ASNTKAIVTA TNSTTGTAST QLDFKTGKYD LGINYYDFYG GKSQWTAYLN DRLVGQWQGN
NEDVLSHELS VYLDGHSATR ITFRDVKIHK GDRLKIVGKP DGMEPAPLDY VVLLPQGIVD
