ID A0A401KIK1_ASPAW Unreviewed; 841 AA.
AC A0A401KIK1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=AAWM_02002 {ECO:0000313|EMBL:GCB19117.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB19117.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB19117.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB19117.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-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|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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB19117.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDHI01000002; GCB19117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KIK1; -.
DR STRING; 105351.A0A401KIK1; -.
DR Proteomes; UP000286921; 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:UP000286921};
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..20
FT /evidence="ECO:0000256|PIRNR:PIRNR029900,
FT ECO:0000256|RuleBase:RU361198"
FT CHAIN 21..841
FT /note="Alpha-glucuronidase"
FT /evidence="ECO:0000256|PIRNR:PIRNR029900,
FT ECO:0000256|RuleBase:RU361198"
FT /id="PRO_5018812648"
FT DOMAIN 26..141
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 147..468
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 470..692
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 301
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 841 AA; 93875 MW; 75112CB1389244A5 CRC64;
MRGLNLFQLI LALLLSMVAA EDGYDGWLRY APVSCDLHCQ QALPSHVVLL NSTKGSPIET
AGRELKAGLQ SILSTNLTSR PFQCNSSASI LVATLDEYRQ RCRDINVPEL DPDGFWLQSE
GDTVRILGKS ARGALYGAYE YLAMVAQRNF SRVAYATSPH APIRWVNQWD NMDGSIERGY
GGASIFFKDG TVVEDMAPVE QYARLLASIR INAIVVNNVN ANATLLLPEN MKGLGRIADA
CRPYGVQIGI SLNFASPEDL GGLNTYDPLD PGVIAWWQNI TDSLYTYVPD MAGYLVKADS
EGQPGPDTYN RTLSQGANLF ARALQPYGGV LMYRAFVYDD NLNESDWKAD RAKAAVEYFK
DLDGQFEENV VIQIKYGPID FQVREPTSPL FANLYHTNTA IELEVSQEYL GQQCHLVYLP
PLWKTVLDFD LRVDHKPSMV RDIISGQRFN RTLGGWAAVV NVGTNRTWLG SHLAMSNLYA
YGRLAWSPTD ESEQIFEDWT RLTFGQNHHV INTISEMSMT SWPAYENYTG NLGIQTLTDI
LYTHYGPNPA TQDNNGWGQW TRADHDSVGM DRTIWNGTGY TGQYPEEVAR VYESLESTPD
DLVLWFHHVP WTHRLHSGVT VIQHFYNAHY AGAEAAHGFV RQWESLEGLI DRERYEAMRS
RLVYQAGHSI VWRDAINNFY YNMTGIPDVA GRVGHHPWRI EAESMRLDGY QTYTVSPFEA
ASNTTAIITT SNSTTGTART SIKAPSGVYD IGVNYYDLYG GQSKWTLSVG DKVVGQWLGD
MEHNSLGHTP SIYLDGHSAT RITFHGVGIR QGDQLKIVGE ANGVEPAPLD YIVLLPPGVV
D
//
