C7DD6_HELAN
ID C7DD6_HELAN Reviewed; 491 AA.
AC F8S1H8; A0A251V7A7;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Eupatolide synthase {ECO:0000303|PubMed:29758164};
DE Short=HaES {ECO:0000303|PubMed:29758164};
DE EC=1.14.14.169 {ECO:0000269|PubMed:29758164};
DE AltName: Full=Cytochrome P450 71B4 {ECO:0000303|PubMed:28538728};
DE AltName: Full=Cytochrome P450 71DD6 {ECO:0000303|PubMed:29758164};
GN Name=CYP71DD6 {ECO:0000303|PubMed:29758164};
GN Synonyms=CYP71B4 {ECO:0000303|PubMed:28538728},
GN ES {ECO:0000303|PubMed:29758164};
GN OrderedLocusNames=HannXRQ_Chr03g0072541 {ECO:0000312|EMBL:OTG31169.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. HA300;
RX PubMed=21515683; DOI=10.1074/jbc.m110.216804;
RA Ikezawa N., Gopfert J.C., Nguyen D.T., Kim S.U., O'Maille P.E., Spring O.,
RA Ro D.K.;
RT "Lettuce costunolide synthase (CYP71BL2) and its homolog (CYP71BL1) from
RT sunflower catalyze distinct regio- and stereoselective hydroxylations in
RT sesquiterpene lactone metabolism.";
RL J. Biol. Chem. 286:21601-21611(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193;
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=29758164; DOI=10.1021/acschembio.8b00126;
RA Frey M., Schmauder K., Pateraki I., Spring O.;
RT "Biosynthesis of eupatolide-A metabolic route for sesquiterpene lactone
RT formation involving the P450 enzyme CYP71DD6.";
RL ACS Chem. Biol. 13:1536-1543(2018).
CC -!- FUNCTION: Involved in the biosynthesis of germacrene-derived
CC sesquiterpene lactones (PubMed:29758164). Hydroxylates 8-beta-hydroxy-
CC germacrene A acid to 6-alpha,8-beta-hydroxy-germacrene A acid, which,
CC in turn, undergo spontaneous lactonization to become eupatolide
CC (PubMed:29758164). {ECO:0000269|PubMed:29758164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + O2 +
CC reduced [NADPH--hemoprotein reductase] = eupatolide + 2 H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57972,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:4935,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:142464; EC=1.14.14.169;
CC Evidence={ECO:0000269|PubMed:29758164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57973;
CC Evidence={ECO:0000269|PubMed:29758164};
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:29758164}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf primordia.
CC {ECO:0000269|PubMed:29758164}.
CC -!- DEVELOPMENTAL STAGE: In developing leaves, expressed at very low levels
CC in young leaf primordia, but strongly induced after the fourth and
CC fifth days following leaf primordia initiation.
CC {ECO:0000269|PubMed:29758164}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OTG31169.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; HQ439596; AEI59778.1; -; mRNA.
DR EMBL; CM007892; OTG31169.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; F8S1H8; -.
DR SMR; F8S1H8; -.
DR STRING; 4232.F8S1H8; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr03g0100431; mRNA:HanXRQr2_Chr03g0100431; HanXRQr2_Chr03g0100431.
DR Gramene; mRNA:HanXRQr2_Chr03g0100431; mRNA:HanXRQr2_Chr03g0100431; HanXRQr2_Chr03g0100431.
DR OrthoDB; 702827at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000215914; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106244; F:eupatolide synthase 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Eupatolide synthase"
FT /id="PRO_0000448397"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 430
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"
SQ SEQUENCE 491 AA; 56027 MW; DB951E1BC2B7CC17 CRC64;
MDFLTYLPSW LLPAVVILTI SCILMLWTKP SKGASGLNLP PGPPSLPLIG NLHQLIGKSF
HETVYKLAEK YGPIMHIHMG SQPVVVISSS ALATEAFKTH DHILANRQYS NNLRRLTFDY
NDIAWAPYGD HSKHMRRVLV TEFLNSRMSK SFKKVLDMEV KSMLDNLPYG TETNLNKVFG
NFVCDFTSKV VTGKSYRDVK IRGKTMKEML DEMIILFSGS FSEIFPKYGW ILEDLSGWTR
RVDKHMANYN DLLELMIDEH LDHTSEDEKD MIDACRPLLN REEMKAIMSN VYNGAIDTSY
LTLVWAMSEI VKNPRVMHKL QDEIRSNAGN KARLDETDTS KMTYLKYVVK ETLRRHGPSP
FLIPRDCVSH IQIGGYDILP GTKVLINAWG IAKDPKVWTE NANEFHPDRF ENHVLEQFHM
VPFGGGRRAC PGYNFATLNI EVVLANLLYS IDWKLPPGLT LEDFNMEEEG SLLVTKKTPL
YLVPIKHNTQ A