C7BL1_HELAN
ID C7BL1_HELAN Reviewed; 488 AA.
AC F8S1H3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Germacrene A acid 8-beta-hydroxylase {ECO:0000303|PubMed:21515683};
DE Short=HaG8H {ECO:0000303|PubMed:21515683};
DE EC=1.14.14.168 {ECO:0000269|PubMed:21515683, ECO:0000269|PubMed:29758164};
DE AltName: Full=Cytochrome P450 71BL1 {ECO:0000303|PubMed:21515683};
GN Name=CYP71BL1 {ECO:0000303|PubMed:21515683};
GN Synonyms=C12, G8H {ECO:0000303|PubMed:21515683};
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], FUNCTION, CATALYTIC ACTIVITY, AND 3D-STRUCTURE
RP MODELING.
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 PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
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:30468448). Hydroxylates germacrene A
CC acid to 8-beta-hydroxy-germacrene A acid (PubMed:21515683,
CC PubMed:29758164). Unlike 6-alpha-hydroxy-germacrene A acid, this
CC compound cannot undergo spontaneous lactonization (PubMed:21515683,
CC PubMed:29758164). {ECO:0000269|PubMed:21515683,
CC ECO:0000269|PubMed:29758164, ECO:0000303|PubMed:30468448}.
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:21515683, ECO:0000269|PubMed:29758164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57965;
CC Evidence={ECO:0000269|PubMed:21515683, 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, ECO:0000303|PubMed:30468448}.
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}.
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DR EMBL; HQ439590; AEI59773.1; -; mRNA.
DR AlphaFoldDB; F8S1H3; -.
DR SMR; F8S1H3; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr04g0180561; mRNA:HanXRQr2_Chr04g0180561; HanXRQr2_Chr04g0180561.
DR Gramene; mRNA:HanXRQr2_Chr04g0180561; mRNA:HanXRQr2_Chr04g0180561; HanXRQr2_Chr04g0180561.
DR KEGG; ag:AEI59773; -.
DR OMA; VMSFGQA; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-18648; -.
DR BRENDA; 1.14.14.168; 2597.
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: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..488
FT /note="Germacrene A acid 8-beta-hydroxylase"
FT /id="PRO_0000421930"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 429
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 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 488 AA; 55803 MW; FE139CAE10A1E4A8 CRC64;
MELFTIFSIV VSSLILFTFW SLKVPKNLPP GPPKLPIIGN IHLLDKIAPH RNLRNLARKY
GPIMHLRLGQ VSTVVISSPR LAHEIMKTQD LSFADRPTTT TSQIFFYKAS NIAWARYGNY
WRQMKKICTL ELLSAKKSRS FFYIREEELT RTYKFLDFSS GTPITLRDTI QEMVNNVVSR
ATLGDVSEDR QFIIDSTYTM LKSFNSFNLF NYYPSLSFIN VISGKQAQWL KMHKEVDVIL
EKILREHRSR PRGKNDHEDL VDVLIRIKET GDLDMAITDD NIKAIILEML TAGTSSSSMT
IEWAFTEMMR NPKIMKKAQT EVRSVVKGDR VTEADIQNLD YTKLVIKETL RLHGVPILVP
RENQEDCVVN GYDIPAKTRL LVNAWACATD PDSWEDPDSF IPERFENNSI GYSGADFEFI
PFGAGRRICP GMNFGMGTVE YVVANLLLHY DWKLPDGMKP HDIDMREITG ISTLPIHPLK
IVPISLSK
