ID A0A177DKJ6_ALTAL Unreviewed; 836 AA.
AC A0A177DKJ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=CC77DRAFT_1061706 {ECO:0000313|EMBL:OAG20245.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG20245.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG20245.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG20245.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR029900,
CC 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; KV441479; OAG20245.1; -; Genomic_DNA.
DR RefSeq; XP_018385666.1; XM_018528459.1.
DR AlphaFoldDB; A0A177DKJ6; -.
DR STRING; 5599.A0A177DKJ6; -.
DR GeneID; 29114053; -.
DR KEGG; aalt:CC77DRAFT_1061706; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1061706; -.
DR OMA; IWRAFVY; -.
DR OrthoDB; 2783531at2759; -.
DR Proteomes; UP000077248; 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:UP000077248};
KW Secreted {ECO:0000256|PIRNR:PIRNR029900};
KW Signal {ECO:0000256|PIRNR:PIRNR029900, ECO:0000256|RuleBase:RU361198};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|PIRNR:PIRNR029900,
FT ECO:0000256|RuleBase:RU361198"
FT CHAIN 18..836
FT /note="Alpha-glucuronidase"
FT /evidence="ECO:0000256|PIRNR:PIRNR029900,
FT ECO:0000256|RuleBase:RU361198"
FT /id="PRO_5007949032"
FT DOMAIN 23..139
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 147..464
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 466..688
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 836 AA; 92201 MW; 167026AF9FD46C68 CRC64;
MRLTLTTLLC AVGVAVAEDG SKGWLRYAPI PDGPAAQSVP STIIALNSTR VSPVFTAGQE
LQKGVDGITG KKLNVSAVAD QSYSAIIVGT KDAYTAAFGN IDECENLDAD GFFLSTTTPG
KVIIVGQNER GALYGAFEYL SQLAQNNVTS GSTVFNPQVP IRWTNEWDNM DGSIERGYAG
PSLFFRDGFV VDNTTRVAEY ARLLASIRVN GAIINNVNAN ATLLNDRNVE GLGRLADAMR
PYGVQLGISL NFASPNATLG SFDPLDPRVD AWWANITNQI YSKVPDMAGY LVKANSEGQP
GPLTYNRTLA DGANMFARAA KPHGGVVMFR AFVYDNHINE TNWYNDRANA QLEFFQHLDG
KFDDNVVVQI KFGPIDFQVR EPASPLFGSL RQTSTAIELQ ITPEYLGQNC HLVYLAPQWK
EILEFDMRSE NQSSKVKDII TGERFKRPLG GYAGVTGVGS NATWLGSHLA MSNLYAYGRL
AWDASVDSEM ILQDWIRLTF GFDEDVLDTL TDMSMRSWPA YENYSGNLGI QTLTDILYTH
FGPNPASQDG NGWGQWTRAD AFSIGMDRTV KNGTGNAGQY PPEVAQIYEN IESTPDNLLL
WFHHVPYTQR LKSNKTVIQH FYDAHYEGAA TAQEFVGQWE SLKGKIDDER YEHVLFRQIF
QAGHSIVWRD AINEFYHNLS QIPDETKRVG NHPYRIEAED MMLDGFKTYA VSPFETASGY
TAIVTTSNST TGIATANVTF ASGTYDVAVN YYDLIGGKAK YELKLGDRTV GAWTGDLEDK
LGHAPSIYLD GHSATRITFR DVEVRQGDQV RLTGQADGIE PAPIDYLSFL PPGIVD
//
