C7BL6_INUHU
ID C7BL6_INUHU Reviewed; 495 AA.
AC A0A2H4DGV8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Germacrene A acid 8-beta-hydroxylase {ECO:0000303|PubMed:29086444};
DE Short=Ih8H {ECO:0000303|PubMed:29086444};
DE Short=IhG8H {ECO:0000303|PubMed:29086444};
DE EC=1.14.14.168 {ECO:0000269|PubMed:29086444};
DE AltName: Full=Cytochrome P450 71BL6 {ECO:0000303|PubMed:29086444};
GN Name=CYP71BL6 {ECO:0000303|PubMed:29086444};
GN Synonyms=G8H {ECO:0000303|PubMed:29086444};
OS Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Inuleae;
OC Inulinae; Inula.
OX NCBI_TaxID=1805964;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND INDUCTION BY JASMONIC ACID.
RX PubMed=29086444; DOI=10.1111/tpj.13760;
RA Gou J., Hao F., Huang C., Kwon M., Chen F., Li C., Liu C., Ro D.K.,
RA Tang H., Zhang Y.;
RT "Discovery of a non-stereoselective cytochrome P450 catalyzing either
RT 8alpha- or 8beta-hydroxylation of germacrene A acid from the Chinese
RT medicinal plant, Inula hupehensis.";
RL Plant J. 93:92-106(2018).
CC -!- FUNCTION: Involved in the biosynthesis of germacrene-derived
CC sesquiterpene lactones (PubMed:29086444). Hydroxylates germacrene A
CC acid to 8-beta-hydroxy-germacrene A and 8-alpha-hydroxy-germacrene A
CC acids (PubMed:29086444). Unlike 8-alpha-hydroxy-germacrene A acid with
CC is spontaneously converted into inunolide (12, 8-alpha), 8-beta-
CC hydroxy-germacrene A cannot undergo spontaneous lactonization
CC (PubMed:29086444). {ECO:0000269|PubMed:29086444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 8beta-hydroxygermacra-1(10),4,11(13)-trien-
CC 12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:57964, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301,
CC ChEBI:CHEBI:142464; EC=1.14.14.168;
CC Evidence={ECO:0000269|PubMed:29086444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57965;
CC Evidence={ECO:0000269|PubMed:29086444};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 8alpha-hydroxygermacra-1(10),4,11(13)-trien-
CC 12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:58032, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301,
CC ChEBI:CHEBI:142490; Evidence={ECO:0000269|PubMed:29086444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58033;
CC Evidence={ECO:0000269|PubMed:29086444};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29086444}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in roots and stems. {ECO:0000269|PubMed:29086444}.
CC -!- INDUCTION: Induced by short jasmonic acid (MeJA) exposure (48 hours),
CC but repressed after a long exposure (120 hours).
CC {ECO:0000269|PubMed:29086444}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KR029572; AML23863.1; -; mRNA.
DR AlphaFoldDB; A0A2H4DGV8; -.
DR SMR; A0A2H4DGV8; -.
DR KEGG; ag:AML23863; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102614; F:germacrene A acid 8beta-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="Germacrene A acid 8-beta-hydroxylase"
FT /id="PRO_5014159214"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 433
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|UniProtKB:P04798"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 495 AA; 55963 MW; 5DA02C3608173A46 CRC64;
MEPFTTFSLV ASSLILLICW ALVKANKPAK NLPPGPPKLP IIGNMHQLES QSPHRVLRKL
SRKYGPIMHL QLGQVPTVVI STPRLVEEVV KHHDINFADR PTNTTSQIFY YNNQNVAWSS
YGNYWRQIKK IVTLELLSVK KVRSFSSIRA EELTRAVKSV EPSVGSTINF RDLTSQTVNN
MVSRATLGDV CKERHILLDT MNDILKTFNS FNVVNFFPSL QFLNVITGKK AKWLKIHKQL
DHILENILEE HKSKPKGNQD DEDLIDVLLR VKDAGGQELP ITNDNVKAIT LEMLTAGTSS
SSMTIEWAFC ELMRHPEVMK KVQSDVRSAV KGNKVTEDDI QNMHYLKLVV KETLRLHGVP
ILVPRQNRED CNVLGYHIPA KTKILINAWA CGTDPDTWED PESFIPERFE KSSVSYFGTD
FQLIPFGTGR RICPGVNFGI GTVEAVLSNF LYHFDWKLPD GVKPQDIDMT EVTGISTLPK
YPLHIVPVST VSQQK
