GUS79_NEUCR
ID GUS79_NEUCR Reviewed; 559 AA.
AC Q7SFB0;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=NCU00937;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
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 Evidence={ECO:0000269|PubMed:18377882};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.3 uM for p-nitrophenyl-beta-glucuronic acid (when expressed in
CC P.pastoris) {ECO:0000269|PubMed:18377882};
CC KM=378 uM for p-nitrophenyl-beta-galacturonic acid (when expressed in
CC P.pastoris) {ECO:0000269|PubMed:18377882};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:18377882};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:18377882};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A2QEQ6}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
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DR EMBL; CM002236; EAA35527.1; -; Genomic_DNA.
DR RefSeq; XP_964763.1; XM_959670.3.
DR AlphaFoldDB; Q7SFB0; -.
DR SMR; Q7SFB0; -.
DR STRING; 5141.EFNCRP00000000758; -.
DR CLAE; GUS79A_NEUCR; -.
DR EnsemblFungi; EAA35527; EAA35527; NCU00937.
DR GeneID; 3880916; -.
DR KEGG; ncr:NCU00937; -.
DR VEuPathDB; FungiDB:NCU00937; -.
DR HOGENOM; CLU_022148_0_0_1; -.
DR InParanoid; Q7SFB0; -.
DR BRENDA; 3.2.1.31; 3627.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..559
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432746"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 559 AA; 60235 MW; F913D3F85D605813 CRC64;
MKRILGLIAY ASVPTVINAV QISVDETAPS NPVFDAYVSY SIEFSSFPDY AGNNSRPNTF
SENLLDNLGK ITGTKPYIRV GGNTQDYALY NASLPYSLNG TIDPKRSSDY PTTIFIGPSF
FESYNSFKNT RFIHGFNLGL GGNRTSGWQT LLDTVPLACK ALGGGKLFAW TYGNEPDLFS
TSAQGPVRPP SWNEAEYVDQ WLNGTRKIHE LLERNCPDLA KNGTYGYIAP SFAGVGNKLK
APKAWGEGLN EDKNIKLFAT HNYISGATSP GVTLQGTLMN HSMTKASVDA HIVEYNQVKA
IDAAAPPLIF GETNSLYNQG RPGLSNTFGA ALWGVDFNLY SASVGFKRVH MHMGTNYRYA
SWQPIATNKA TIGTKAPYYG NIAVASFLAP PPSSPYDSPA TSLATVKHLP ISSTPFLSAY
AAYHSSNLTR LILINLQSYN TTASGEGLAP LPPSSLTPRP SVTFNFTLPA AYLLTDGGKE
KQVVVKRLMA NGSDAITGIT WDGWSYNWEL DGGRPVRLPN VTRTSESERA WVGEGTSDGG
KAGLGVVVEA GSAALVEFV
