C71Z6_MAIZE
ID C71Z6_MAIZE Reviewed; 506 AA.
AC A0A1D6GQ67;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Dolabradiene monooxygenase {ECO:0000305};
DE EC=1.14.14.159 {ECO:0000269|PubMed:29475898};
DE AltName: Full=Cytochrome P450 71Z16 {ECO:0000303|PubMed:29475898};
DE Short=ZmCYP71Z16 {ECO:0000303|PubMed:29475898};
GN Name=CYP71Z16 {ECO:0000303|PubMed:29475898};
GN ORFNames=ZEAMMB73_Zm00001d014136 {ECO:0000312|EMBL:AQK65314.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29475898; DOI=10.1104/pp.17.01351;
RA Mafu S., Ding Y., Murphy K.M., Yaacoobi O., Addison J.B., Wang Q., Shen Z.,
RA Briggs S.P., Bohlmann J., Castro-Falcon G., Hughes C.C., Betsiashvili M.,
RA Huffaker A., Schmelz E.A., Zerbe P.;
RT "Discovery, biosynthesis and stress-related accumulation of dolabradiene-
RT derived defenses in maize.";
RL Plant Physiol. 176:2677-2690(2018).
CC -!- FUNCTION: Involved in the production of antifungal dolabralexin
CC phytoalexins in response to biotic and abiotic stresses
CC (PubMed:29475898). Catalyzes the epoxidation of dolabradiene at C-16,
CC followed by hydroxylation at C-3, to yield the epoxides 15,16-
CC epoxydolabrene (epoxydolabrene) and 3b-hydroxy-15,16-epoxydolabrene
CC (epoxydolabranol) (PubMed:29475898). {ECO:0000269|PubMed:29475898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dolabradiene + O2 + reduced [NADPH--hemoprotein reductase] =
CC 15,16-epoxydolabrene + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:57516, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:141821,
CC ChEBI:CHEBI:141822; EC=1.14.14.159;
CC Evidence={ECO:0000269|PubMed:29475898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57517;
CC Evidence={ECO:0000269|PubMed:29475898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15,16-epoxydolabrene + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3beta-hydroxy-15,16-epoxydolabrene + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57520,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:141820, ChEBI:CHEBI:141821;
CC EC=1.14.14.159; Evidence={ECO:0000269|PubMed:29475898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57521;
CC Evidence={ECO:0000269|PubMed:29475898};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CM000781; AQK65314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6GQ67; -.
DR SMR; A0A1D6GQ67; -.
DR STRING; 4577.GRMZM2G067591_P01; -.
DR EnsemblPlants; Zm00001eb222680_T001; Zm00001eb222680_P001; Zm00001eb222680.
DR Gramene; Zm00001eb222680_T001; Zm00001eb222680_P001; Zm00001eb222680.
DR eggNOG; KOG0156; Eukaryota.
DR OMA; TYWNDAE; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-20517; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; A0A1D6GQ67; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051502; P:diterpene phytoalexin biosynthetic process; IDA:UniProtKB.
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 Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Dolabradiene monooxygenase"
FT /id="PRO_0000447766"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 443
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:Q96242"
SQ SEQUENCE 506 AA; 56314 MW; 2582D63BCC7F7065 CRC64;
MEDKVLLAVA MVALIAVLSK LKSLLETKPK LNLPPGPWTL PLIGSIHHLV SSPLPYRAMR
ELAHKHGPLM MLWLGEVPTL VVSSPEAAQA ITKTHDVTFA DRHMNSTVDI LTFNGNDIVF
GTYGEQWRQL RKLSVLELLS VARVQSFQRI REEEVARFMR NLAASAGAGA TVDLSKMISS
FINDTFVRES IGSRCKHQDE YLDALHTGIR VAAELSVANL FPSSRLLQSL STARRKAVAA
RDEMARILGQ IIRETKEAMD WGDKASNESM ISVLLRLQKE AGLPIELTDD IVMALMFDLF
GAGSDTSSTT LTWCMTEMIR YPATMAKAQA EVREAFKGKT TITEDDLSRA NLSYLKLVVK
EALRLHCPVP LLIPRKCRET CQIMGYDIPK DTCVLVNVWA ICRDSRYWED ADEFKPERFE
NSSLDYKGTS HEYLPFGSGR RMCPGGNLGV ANMELALASL LYHFDWKLPS GQEPKDVDVW
EAAGLVGRKN AGLVLHPVSR FAPVNA
