GUS79_ASPNC
ID GUS79_ASPNC Reviewed; 541 AA.
AC A2QEQ6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Beta-glucuronidase {ECO:0000303|PubMed:18377882};
DE Short=GlcAase {ECO:0000303|PubMed:18377882};
DE EC=3.2.1.31 {ECO:0000269|PubMed:18377882};
DE AltName: Full=Beta-D-glucuronoside glucuronosohydrolase {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=An02g11890;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000312|Proteomes:UP000006706};
RN [1] {ECO:0000312|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RX PubMed=18377882; DOI=10.1016/j.carres.2008.03.004;
RA Konishi T., Kotake T., Soraya D., Matsuoka K., Koyama T., Kaneko S.,
RA Igarashi K., Samejima M., Tsumuraya Y.;
RT "Properties of family 79 beta-glucuronidases that hydrolyze beta-
RT glucuronosyl and 4-O-methyl-beta-glucuronosyl residues of arabinogalactan-
RT protein.";
RL Carbohydr. Res. 343:1191-1201(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22443316; DOI=10.1021/pr201157b;
RA Krijgsheld P., Altelaar A.F., Post H., Ringrose J.H., Mueller W.H.,
RA Heck A.J., Woesten H.A.;
RT "Spatially resolving the secretome within the mycelium of the cell factory
RT Aspergillus niger.";
RL J. Proteome Res. 11:2807-2818(2012).
CC -!- FUNCTION: Beta-glucuronidase that hydrolyzes beta-glucuronosyl and 4-O-
CC methyl-beta-glucuronosyl residues of arabinogalactan-protein.
CC Hydrolyzed heparan sulfate only very weakly. Has no activity on xylan
CC from birchwood. Able to catalyze the transglycosylation of glucuronic
CC acid (GlcA) residues from p-nitrophenyl-beta-glucuronic acid (PNP beta-
CC GlcA) to various monosaccharide acceptors such as glucose, galactose
CC and xylose. {ECO:0000269|PubMed:18377882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30.4 uM for p-nitrophenyl-beta-glucuronic acid (when expressed in
CC P.pastoris) {ECO:0000269|PubMed:18377882};
CC KM=422 uM for p-nitrophenyl-beta-galacturonic acid (when expressed in
CC P.pastoris) {ECO:0000269|PubMed:18377882};
CC pH dependence:
CC Optimum pH is 3.0-4.0. {ECO:0000269|PubMed:18377882};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:18377882};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22443316}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18377882}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
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; AM270032; CAK96418.1; -; Genomic_DNA.
DR RefSeq; XP_001400317.1; XM_001400280.1.
DR AlphaFoldDB; A2QEQ6; -.
DR SMR; A2QEQ6; -.
DR CAZy; GH79; Glycoside Hydrolase Family 79.
DR CLAE; GUS79A_ASPNG; -.
DR PaxDb; A2QEQ6; -.
DR EnsemblFungi; CAK96418; CAK96418; An02g11890.
DR GeneID; 4979726; -.
DR KEGG; ang:ANI_1_3090024; -.
DR VEuPathDB; FungiDB:An02g11890; -.
DR HOGENOM; CLU_022148_0_0_1; -.
DR BioCyc; MetaCyc:MON-20549; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR InterPro; IPR031728; GlcAase_C.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF16862; Glyco_hydro_79C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..541
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000219654"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 541 AA; 58859 MW; DCB0F15FD332755E CRC64;
MHHHPITLLS LLLGAAQSIA AHPTAHDERR SSSSIGVSAS VPDDAALPVL HPFVSFSIEF
AFFPDFAGNL SHPNLFSNQL LDNLADLQGA KPYIRVGGNT QDFALYDPKL RAATNATYIT
SISTDYPLIL SFGPAFFESY FTWPGTKFIH GFNLGKNSSS DIELMLESVP LACKALEGGK
LAYWELGNEP DLYKTSAQGI RRPASWTEQD YVDEWLNKTA RIEKRLVEAC PELAESKYIA
PSFAGVTNSL NPVVTWEKGL DKSRNIALNS EHNYIGGATQ PGVTLQNTLM NHTKTVESVA
QQVNVSRILS KDNLTPGIPY ILGETNSLYN EGAPGLSNSF GAALWGVDFN LYCASQNIRR
THMHQGSNYN YISWQPVGTN RTTIGTKAPY YGNAMVAAML HGGDDVRIVN LPLAADTEAA
YAAYVNETLV RVAVINLVEF NYTSTDSTAE KVESRPSAKY TFQLPSSESV YAGSVSVQRL
MANGSNAITG ITWDGWSYNY ELAQGKPVRL QNVTTGEAIS VGDDGVVEIE IPYSSAAILS
L
