ID BAGLU_SCUBA Reviewed; 527 AA. AC Q9LRC8; DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 73. DE RecName: Full=Baicalin-beta-D-glucuronidase; DE EC=3.2.1.167; DE AltName: Full=Baicalinase; DE Flags: Precursor; GN Name=SGUS; OS Scutellaria baicalensis (Baical skullcap). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Lamiaceae; Scutellarioideae; Scutellaria. OX NCBI_TaxID=65409; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-55; 273-288; 410-423 AND RP 431-447, MUTAGENESIS OF GLU-194; GLU-212; GLU-225; GLU-272; TYR-281; RP GLU-329 AND TYR-376, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=10858442; DOI=10.1074/jbc.m004674200; RA Sasaki K., Taura F., Shoyama Y., Morimoto S.; RT "Molecular characterization of a novel beta-glucuronidase from Scutellaria RT baicalensis georgi."; RL J. Biol. Chem. 275:27466-27472(2000). RN [2] RP CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=8593473; DOI=10.1248/bpb.18.1531; RA Ikegami F., Matsunae K., Hisamitsu M., Kurihara T., Yamamoto T., RA Murakoshi I.; RT "Purification and properties of a plant beta-D-glucuronidase form RT Scutellaria root."; RL Biol. Pharm. Bull. 18:1531-1534(1995). RN [3] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RA Morimoto S., Harioka T., Shoyama Y.; RT "Purification and characterization of flavone-specific beta-glucuronidase RT from callus cultures of Scutellaria baicalensis Georgi."; RL Planta 195:535-540(1995). CC -!- FUNCTION: Beta-glucuronidase involved in the initiation of H(2)O(2) CC metabolism via the production of baicalein. Unable to use glycyrrhizin, CC gypsogenin-3-O-D-glucuronide, luteolin-7-O-D-glucoside and apigenin-7- CC O-D-glucoside as substrates. {ECO:0000269|PubMed:10858442}. CC -!- CATALYTIC ACTIVITY: CC Reaction=baicalin + H2O = baicalein + D-glucuronate + H(+); CC Xref=Rhea:RHEA:28130, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58720, ChEBI:CHEBI:61283, ChEBI:CHEBI:78324; CC EC=3.2.1.167; Evidence={ECO:0000269|PubMed:10858442, CC ECO:0000269|PubMed:8593473, ECO:0000269|Ref.3}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=9 uM for luteolin 3'-O-beta-D-glucuronide CC {ECO:0000269|PubMed:10858442, ECO:0000269|Ref.3}; CC KM=10 uM for baicalin {ECO:0000269|PubMed:10858442, CC ECO:0000269|Ref.3}; CC KM=30 uM for wogonin 7-O-beta-D-glucuronide CC {ECO:0000269|PubMed:10858442, ECO:0000269|Ref.3}; CC KM=40 uM for oroxlin 7-O-beta-D-glucuronide CC {ECO:0000269|PubMed:10858442, ECO:0000269|Ref.3}; CC KM=12 uM for baicalein 7-O-beta-D-glucuronide CC {ECO:0000269|PubMed:10858442, ECO:0000269|Ref.3}; CC Note=kcat is 639 sec(-1) for baicalein 7-O-beta-D-glucuronide.; CC pH dependence: CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:10858442, CC ECO:0000269|Ref.3}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8593473}. 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; AB040072; BAA97804.1; -; mRNA. DR AlphaFoldDB; Q9LRC8; -. DR SMR; Q9LRC8; -. DR CAZy; GH79; Glycoside Hydrolase Family 79. DR KEGG; ag:BAA97804; -. DR BioCyc; MetaCyc:MONOMER-15936; -. DR BRENDA; 3.2.1.167; 5639. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0009505; C:plant-type cell wall; IEA:TreeGrafter. DR GO; GO:0052748; F:baicalin beta-D-glucuronidase activity; IDA:UniProtKB. DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:TreeGrafter. DR FunFam; 3.20.20.80:FF:000549; Predicted protein; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR005199; Glyco_hydro_79. DR PANTHER; PTHR14363:SF17; HEPARANASE-LIKE PROTEIN 3; 1. DR PANTHER; PTHR14363; HEPARANASE-RELATED; 1. DR Pfam; PF03662; Glyco_hydro_79n; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Hydrolase; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:10858442" FT CHAIN 26..527 FT /note="Baicalin-beta-D-glucuronidase" FT /id="PRO_0000418918" FT ACT_SITE 212 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 329 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT MUTAGEN 194 FT /note="E->A: 14% reduction of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 212 FT /note="E->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 225 FT /note="E->A: 6% reduction of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 272 FT /note="E->A: 30% reduction of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 281 FT /note="Y->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 329 FT /note="E->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:10858442" FT MUTAGEN 376 FT /note="Y->A: 35% reduction of activity." FT /evidence="ECO:0000269|PubMed:10858442" SQ SEQUENCE 527 AA; 58772 MW; A5DE7C423F2A1E2B CRC64; MGFQVWQKGL CVLCFSLIFI CGVIGEETTI VKIEENPVAQ TDENYVCATL DLWPPTKCNY GNCPWGKSSF LNLDLNNNII RNAVKEFAPL KLRFGGTLQD RLVYQTSRDE PCDSTFYNNT NLILDFSHAC LSLDRWDEIN QFILETGSEA VFGLNALRGK TVEIKGIIKD GQYLGETTTA VGEWDYSNSK FLIEYSLKKG YKHIRGWTLG NELGGHTLFI GVSPEDYAND AKKLHELVKE IYQDQGTMPL IIAPGAIFDL EWYTEFIDRT PELHVATHHM YNLGSGGDDA LKDVLLTASF FDEATKSMYE GLQKIVNRPG TKAVAWIGEA GGAFNSGQDG ISNTFINGFW YLNMLGYSAL LDTKTFCRQT LTGGNYGLLQ TGTYIPNPDY YSALLWHRLM GSKVLKTEIV GTKNVYIYAH CAKKSNGITM LVLNHDGESS VKISLDPSKY GSKREEYHLT PVNNNLQSRL VKLNGELLHL DPSGVIPALN PVEKDNSKQL EVAPYSFMFV HLPGPTMFSA CEKPAGK //