BAGLU_SCUBA
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 03-AUG-2022, entry version 65.
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}.
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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:MON-15936; -.
DR BRENDA; 3.2.1.167; 5639.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0052748; F:baicalin beta-D-glucuronidase activity; IDA:UniProtKB.
DR InterPro; IPR005199; Glyco_hydro_79.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF03662; Glyco_hydro_79n; 1.
DR SUPFAM; SSF51445; SSF51445; 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
