ID   AGUA_ASPFU              Reviewed;         840 AA.
AC   Q4WW45;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=AFUA_5G14380;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000003; EAL91181.1; -; Genomic_DNA.
DR   RefSeq; XP_753219.1; XM_748126.1.
DR   AlphaFoldDB; Q4WW45; -.
DR   SMR; Q4WW45; -.
DR   STRING; 746128.CADAFUBP00006065; -.
DR   EnsemblFungi; EAL91181; EAL91181; AFUA_5G14380.
DR   GeneID; 3511012; -.
DR   KEGG; afm:AFUA_5G14380; -.
DR   VEuPathDB; FungiDB:Afu5g14380; -.
DR   eggNOG; ENOG502QWS4; Eukaryota.
DR   HOGENOM; CLU_007125_2_0_1; -.
DR   InParanoid; Q4WW45; -.
DR   OMA; DNNGWGQ; -.
DR   OrthoDB; 127527at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IDA:AspGD.
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_0000393488"
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;  93659 MW;  D8A8565BDFBC272F CRC64;
     MWSGIPIFAL LSSIGIAAAE TGLDGWLRYA SVPCNGNCQR ALPSHIVTLN STRSSPVYVA
     GQELQDGLHQ ILGKHASVKS TGCSTDSSII VGTVEAYRQV CNAGRQVPQF 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