ID   AGUA_HYPJE              Reviewed;         847 AA.
AC   Q99024;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Alpha-glucuronidase;
DE            EC=3.2.1.139;
DE   AltName: Full=Alpha-glucosiduronase;
DE   AltName: Full=GLRI;
DE   Flags: Precursor;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=8654984; DOI=10.1016/0378-1119(96)00167-9;
RA   Margolles-Clark E., Saloheimo M., Siika-Aho M., Penttilae M.;
RT   "The alpha-glucuronidase-encoding gene of Trichoderma reesei.";
RL   Gene 172:171-172(1996).
CC   -!- FUNCTION: Releases 4-O-methylglucuronic acid from xylan.
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR   EMBL; Z68706; CAA92949.1; -; mRNA.
DR   PIR; JC4836; JC4836.
DR   AlphaFoldDB; Q99024; -.
DR   SMR; Q99024; -.
DR   CAZy; GH67; Glycoside Hydrolase Family 67.
DR   CLAE; AGU67A_TRIRE; -.
DR   VEuPathDB; FungiDB:TrQ_007137; -.
DR   OMA; DNNGWGQ; -.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..847
FT                   /note="Alpha-glucuronidase"
FT                   /id="PRO_0000012244"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        586
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        692
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   847 AA;  93424 MW;  214AAE487382FDB4 CRC64;
     MVIRSLLLLL LAAIVPVFAE SGIDAWLRYA RLPSSATRGH LTSFPDRIVV LNASKNGPLA
     SASSELHKGI KGILGLDLDV SSRGGKHCST QKSIVISTLD TYQSACGKLS PKLNLKEDGY
     WLSTKGGSVQ IIGQNERGAL YGAFQYLSYL GQGDFSGKAF ASNPSAPVRW SNQWDNLNAA
     TAAHGSIERG YGGPSIFFEN GLIKEDLSRV PLYGRLLASV GLNGIVINNV NADANLLNET
     NLQGLKRIAD LFRPWGVNVG ISLNFASPQV LGDLSTFDPL DDSVIKWWTD KTDRIYQLVP
     DLAGYLVKAN SEGQPGPLTY NRTLAEGANL FAKAVQPHGG IVVFRAFVYD QLNETDWKAD
     RANAAVDFFK SLDGQFDDNV LVQIKYGPID FQVREPASPL FANLPKTAVS IELEVTQEYL
     GQQSHLVYLP PLWQTVLGFD MRYNNRQSYV RDIISGEVFG HKLGGYAGVI NVGMDDTWLG
     SHLAMSNMFA YGRLAWNPRA DSRDIVEEWT RLTFGLDRDV VSTIADMSLK SWPAYEGYSG
     NLGIQTLTDI LYTHYGANPA SQDNNGWGQW TRADSKTIGM DRTVSNGTGN AGQYPKEVAA
     RFEHTQTTPD DLMLWFHHVP YTFRLHSGKS VIQHFYDAHY TGAATVQRFP AAWKSLKSKI
     DTERYNAVLY KLQYQTGHSL VWRDAITEFY RNLSSIPDQL NRVRNHPHRI EAEDMDLSGF
     TVVNVSPTEC ASKYKAIATN GTGTATTRLN VPSGKYTVAV NYYDVINGTA SYDVLLNGKS
     LGKWKGDSET HLGHDFSTFL DCHSAIRITF EGVRISRGDK LTIRGTGNAQ EQAAIDYVSI
     LPQGVVD