BAMO_GLYUR
ID BAMO_GLYUR Reviewed; 493 AA.
AC B5BSX1; A0A218KSA8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Beta-amyrin 11-oxidase {ECO:0000303|PubMed:18779566, ECO:0000303|PubMed:31138208};
DE EC=1.14.14.152 {ECO:0000269|PubMed:18779566};
DE AltName: Full=Cytochrome P450 88D6 {ECO:0000303|PubMed:18779566, ECO:0000303|PubMed:31138208};
GN Name=CYP88D6 {ECO:0000303|PubMed:18779566, ECO:0000303|PubMed:31138208};
OS Glycyrrhiza uralensis (Chinese licorice) (Glycyrrhiza shiheziensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Galegeae; Glycyrrhiza.
OX NCBI_TaxID=74613;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=18779566; DOI=10.1073/pnas.0803876105;
RA Seki H., Ohyama K., Sawai S., Mizutani M., Ohnishi T., Sudo H., Akashi T.,
RA Aoki T., Saito K., Muranaka T.;
RT "Licorice beta-amyrin 11-oxidase, a cytochrome P450 with a key role in the
RT biosynthesis of the triterpene sweetener glycyrrhizin.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14204-14209(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOTECHNOLOGY, AND REVIEW.
RX PubMed=31138208; DOI=10.1186/s12934-019-1138-5;
RA Wang C., Su X., Sun M., Zhang M., Wu J., Xing J., Wang Y., Xue J., Liu X.,
RA Sun W., Chen S.;
RT "Efficient production of glycyrrhetinic acid in metabolically engineered
RT Saccharomyces cerevisiae via an integrated strategy.";
RL Microb. Cell Fact. 18:95-95(2019).
CC -!- FUNCTION: Involved in the biosynthesis of Glycyrrhetinic acid (GA), a
CC natural product which exhibits anti-inflammatory activity
CC (PubMed:31138208). Catalyzes 2 successive oxidations of beta-amyrin,
CC producing a precursor of the triterpene sweetener glycyrrhizin
CC (PubMed:18779566). Unable to use 11-deoxoglycyrrhetinic acid or ent-
CC kaurenoic acid as substrates (PubMed:18779566).
CC {ECO:0000269|PubMed:18779566, ECO:0000269|PubMed:31138208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-amyrin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC = 11-oxo-beta-amyrin + 2 H(+) + 3 H2O + 2 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:31711, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:63184; EC=1.14.14.152;
CC Evidence={ECO:0000269|PubMed:18779566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC 11alpha-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:31715, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:63177;
CC Evidence={ECO:0000269|PubMed:18779566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11alpha-hydroxy-beta-amyrin + O2 + reduced [NADPH--hemoprotein
CC reductase] = 11-oxo-beta-amyrin + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:31719, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:63177, ChEBI:CHEBI:63184;
CC Evidence={ECO:0000269|PubMed:18779566};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stolons. Not detected in
CC leaves and stems. {ECO:0000269|PubMed:18779566}.
CC -!- BIOTECHNOLOGY: Saccharomyces cerevisiae expressing Glycyrrhiza
CC uralensis CYP88D6 and CYP72A154, combined with the expression of
CC Arabidopsis thaliana beta-amyrin synthase (beta-AS) and NADPH-
CC cytochrome P450 reductase 1 (ATR1), accumulates glycyrrhetinic acid
CC (GA) and, to lower levels, beta-amyrin; these GA production was
CC increased in the presence of G.uralensis cytochrome b5 (GuCYB5).
CC {ECO:0000269|PubMed:31138208}.
CC -!- MISCELLANEOUS: The CYP88D subfamily seems to be restricted to the
CC Fabaceae.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB433179; BAG68929.1; -; mRNA.
DR EMBL; KY499143; AQQ13664.1; -; mRNA.
DR AlphaFoldDB; B5BSX1; -.
DR SMR; B5BSX1; -.
DR KEGG; ag:BAG68929; -.
DR BioCyc; MetaCyc:MON-16879; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102291; F:11alpha-hydroxy-beta-amyrin dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102289; F:beta-amyrin 11-oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102290; F:beta-amyrin monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..493
FT /note="Beta-amyrin 11-oxidase"
FT /id="PRO_0000418848"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="S -> C (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..55
FT /note="IGD -> MGN (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..266
FT /note="PQEGS -> QQEGD (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..339
FT /note="TRTRF -> MRTRL (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> F (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> L (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="I -> V (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="I -> M (in Ref. 2; AQQ13664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 56372 MW; 5348A67F0617231B CRC64;
MEVHWVCMSA ATLLVCYIFG SKFVRNLNGW YYDVKLRRKE HPLPPGDMGW PLIGDLLSFI
KDFSSGHPDS FINNLVLKYG RSGIYKTHLF GNPSIIVCEP QMCRRVLTDD VNFKLGYPKS
IKELARCRPM IDVSNAEHRL FRRLITSPIV GHKALAMYLE RLEEIVINSL EELSSMKHPV
ELLKEMKKVS FKAIVHVFMG SSNQDIIKKI GSSFTDLYNG MFSIPINVPG FTFHKALEAR
KKLAKIVQPV VDERRLMIEN GPQEGSQRKD LIDILLEVKD ENGRKLEDED ISDLLIGLLF
AGHESTATSL MWSITYLTQH PHILKKAKEE QEEITRTRFS SQKQLSLKEI KQMVYLSQVI
DETLRCANIA FATFREATAD VNINGYIIPK GWRVLIWARA IHMDSEYYPN PEEFNPSRWD
DYNAKAGTFL PFGAGSRLCP GADLAKLEIS IFLHYFLRNY RLERINPECH VTSLPVSKPT
DNCLAKVIKV SCA
