ID U7PJI3_SPOS1 Unreviewed; 855 AA.
AC U7PJI3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 03-MAY-2023, entry version 32.
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=HMPREF1624_07782 {ECO:0000313|EMBL:ERS95707.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS95707.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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|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; KI440852; ERS95707.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PJI3; -.
DR STRING; 1391915.U7PJI3; -.
DR eggNOG; ENOG502QWS4; Eukaryota.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OrthoDB; 2783531at2759; -.
DR Proteomes; UP000018087; 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:UP000018087};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 11..141
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 162..478
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 480..703
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 309
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 855 AA; 91468 MW; D9F18B93A61E97A2 CRC64;
MSPPDEDGVA AWLRYGELPA AARTAANSPA VDTVVVLGDG DDTSPVTVAG RELVDGFRTI
LGQSVTVVRS VPLSNASSGG LVLVIGTLKA YMKGGHTAPA DAAAAEVLSH EDGYWVGAST
SAQHVVLGHD ERGVLYGAFA YLSRLAQGTL SLSPGLGLGF GSRPSAPIRW VNQWDNMDGS
IERGYGGRSL FFADGQVRQT AAALARVRAY ARLLASVGLN GVVVNNVNAD ASLLTDANLA
GVQAVADTMR PYGVRVGLAL NFDAPRTLGG LATADPLDAG VEAFWADVTR RVYGRVPDLL
GYTIKANSEG QPGPLSYGRT LAEGANVLAR PLQPHGGLVL FRAFVYDHHL REEDPTSDRA
NAAVDFFAPL DGAFADNVVV QVKFGPIDFQ VREPPSPLLA RLRRTPAAIE FMVAQEYMGQ
QSHAVYLAPQ WQEILAFDMR VDGAPSRVRD LLAPDTTPFG WATTGYTAVV NVGSDPTWLG
HYLAMANLYA YGRLAWRPAD DARDILEDWI RLTFGAGDAA VVAAVSSLLM DSWPAYEGHS
GNLGVQTLCD ILYTHYGPSP ASQDGNGWGQ WTRADSQGIG MDRTVATGTG NAGQYHAAVA
AVFEDVRQTP DDLLLWFHHV PYTHVLRSGK TVIQHFYDAH YAGAATVQTF PARWAALRGK
IDDARFAHVA FKLAYQAGHA LVWRDSVCRF YRTLSGIDDA HGRVNNHMYR IPLAAPSPNV
VLDGYKVVDV TPPEAASHGR AVQTAPSTAT GTVTVTLAVD DGVYDMAVNY YDTSAGRATY
ELLLNSRPIG QWAGNLQDRL GHDFSAFVDG HSATRVYFRG VALKTGDSLA IVGHADGNER
APLDYVSILP EGVVD
//
