AGUA_ASPOR
ID AGUA_ASPOR Reviewed; 835 AA.
AC Q2UFP4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=AO090026000127;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007159; BAE59621.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UFP4; -.
DR SMR; Q2UFP4; -.
DR STRING; 510516.Q2UFP4; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR EnsemblFungi; BAE59621; BAE59621; AO090026000127.
DR VEuPathDB; FungiDB:AO090026000127; -.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OMA; DNNGWGQ; -.
DR Proteomes; UP000006564; Chromosome 3.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..835
FT /note="Probable alpha-glucuronidase A"
FT /id="PRO_0000393489"
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 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 835 AA; 93450 MW; 9E9E78FCD47455E9 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
LDGQFEDNIK YGPIDFQVRE PVSPLFANLY KTNMAIELQV TQEYLGQQDH LVYLSPLWKE
LLDFDLRVDH QPSLVRDIVS GQRFDRQLGG WAAVVNVGTN TTWLGSHLAM SNLYAYGRLA
WSPTDDSQGI LQDWIRLTFG RDQNVLDAIT DMSMASWPAY ENYTGNLGIQ TLTDILYTHY
GPNPASQDNN GWGQWTRADH DTIGMDRTVK NGTGNAGQYP AEIAQVYEDL DSTPDDLLLW
FHHVPYTHRL HSGKTVIQHF YDAHYDGAET AHRFLSQWES LKGRIDQQRY NEVLSRLVYQ
AGHSLVWRDA INNFYWNMSG ISDEKNRLGH HPWRVEAESM TLDGYEPYTV SPFETASNYK
AVVTTSNSTT GTAQTKLQFP SGTYDLGVNY YDMYGGKSEW TVYVNDRVVG QWEGNSENTL
GHTPSIYIDG HSATRITFRG VEIENGDQLK IVGVPDGVEP APLDYVVLLP PDVVD
