ID S7ZIW1_PENO1 Unreviewed; 823 AA.
AC S7ZIW1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alpha-glucuronidase {ECO:0000256|ARBA:ARBA00012271, ECO:0000256|PIRNR:PIRNR029900};
DE EC=3.2.1.139 {ECO:0000256|ARBA:ARBA00012271, ECO:0000256|PIRNR:PIRNR029900};
GN Name=aguA {ECO:0000256|RuleBase:RU361198};
GN ORFNames=PDE_03572 {ECO:0000313|EMBL:EPS28626.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS28626.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS28626.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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.
CC {ECO:0000256|ARBA:ARBA00024828, ECO:0000256|RuleBase:RU361198}.
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 Evidence={ECO:0000256|ARBA:ARBA00000762,
CC ECO:0000256|PIRNR:PIRNR029900, ECO:0000256|RuleBase:RU361198};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361198}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC ECO:0000256|RuleBase:RU361198}.
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DR EMBL; KB644411; EPS28626.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZIW1; -.
DR STRING; 933388.S7ZIW1; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OrthoDB; 2783531at2759; -.
DR PhylomeDB; S7ZIW1; -.
DR Proteomes; UP000019376; 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 CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361198};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361198};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 10..114
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 121..443
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 445..668
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 823 AA; 91511 MW; E1FD49571C9C4D90 CRC64;
MSTGETGLEA WLRYAPLPAD AAKQYPQYTD IVALTDSQSS PVYTAGKELQ DGLKKILNFS
ANLTNTIDSS ESLSPSAIVD DGFWLGTVSG EKGDKTQVVI VGQNERGALY GAMEFLMRLA
QNQPCPTSYA SSPSAPIRWI NQWDNLDGSI ERGYAGPSIF FKDGAVLDDL TRVEQYARLM
ASVRLNGIVV NNVNSHCNLL NPSNLKGLGR IADAMRPWGV RIGVALYFDT PIELGGLQTS
DPLDPDVVAF WNDITTQLYQ NVPDMLGYLI KANSEGQPGP LTYGRTLAEG ANLFARALKP
HGDGIVMYRA FVYNHHLDES NWKNDRANAA VEFFDGLDDV FDENVLVQIK YGPIDFQVRE
PPSPLLAHLR RTRTIIEFQV AQEYMGQQSH LCYLAPLWRT ILDFDLRIDG EPSLVKDVVS
GERFNWKYSG YAAVVNVGND STWLGSHLAM SNLYAYGRYC WDPSSDEAAV VQDWARLTFG
LNPTVVDTIT QLSMESWPTY ENYSGNLGIQ TLCDIVKTCH YGPSPAAMDG NGWGQWTRAD
AHAIGMDRTV ATGTGYSGQY PAEVARVFEH PETTPDELLL WFHHVPYTHR LKSGKTVIQH
FYDAHYEGAQ NAQTFPVRWA ALRGLVDEHR FQHILFHLTY QAGHALVWRD SVCTFYHAKC
GIPDEHNRVG NYQWRVKAQD MHLSGYKVVP VRPFEAAYGA EAIITESNTA PGTATWPVTF
PAGTYNVAVN YYDHLGGTSR YQLFLGSGSD EGKKRLVGEW AGDLGQHLLH DFSDLRDGHS
NTRITFKDVR VEDGDVLTIV GTPDGEELAP IDYVSFLPDG IID
//
