C71Z8_MAIZE
ID C71Z8_MAIZE Reviewed; 505 AA.
AC B4FVP3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Zealexin A1 synthase {ECO:0000305};
DE EC=1.14.14.160 {ECO:0000269|PubMed:26471326};
DE AltName: Full=Cytochrome P450 71Z18 {ECO:0000303|PubMed:26471326};
GN Name=CYP71Z18 {ECO:0000303|PubMed:26471326};
GN ORFNames=ZEAMMB73_Zm00001d014134 {ECO:0000312|EMBL:AQK65312.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26471326; DOI=10.1016/j.phytochem.2015.10.003;
RA Mao H., Liu J., Ren F., Peters R.J., Wang Q.;
RT "Characterization of CYP71Z18 indicates a role in maize zealexin
RT biosynthesis.";
RL Phytochemistry 121:4-10(2016).
CC -!- FUNCTION: Involved in production of the antifungal phytoalexin zealexin
CC A1 (PubMed:26471326). The enzyme sequentially oxidizes(S)-beta-
CC macrocarpene via alcohol and aldehyde intermediates to form zealexin
CC A1, a maize phytoalexin that provides biochemical protection against
CC fungal infection (PubMed:26471326). {ECO:0000269|PubMed:26471326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-beta-macrocarpene + 3 O2 + 3 reduced [NADPH--hemoprotein
CC reductase] = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein
CC reductase] + zealexin A1; Xref=Rhea:RHEA:57544, 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:61344, ChEBI:CHEBI:141852; EC=1.14.14.160;
CC Evidence={ECO:0000269|PubMed:26471326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57545;
CC Evidence={ECO:0000269|PubMed:26471326};
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; AQK65312.1; -; Genomic_DNA.
DR EMBL; BT041181; ACF86186.1; -; mRNA.
DR RefSeq; NP_001141366.1; NM_001147894.1.
DR AlphaFoldDB; B4FVP3; -.
DR SMR; B4FVP3; -.
DR PRIDE; B4FVP3; -.
DR EnsemblPlants; Zm00001eb222660_T001; Zm00001eb222660_P001; Zm00001eb222660.
DR GeneID; 100273457; -.
DR Gramene; Zm00001eb222660_T001; Zm00001eb222660_P001; Zm00001eb222660.
DR KEGG; zma:100273457; -.
DR OMA; IANRDKM; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-20518; -.
DR BRENDA; 1.14.14.160; 6752.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; B4FVP3; 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..505
FT /note="Zealexin A1 synthase"
FT /id="PRO_0000447767"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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 505 AA; 56021 MW; 53324116A447E07D CRC64;
MEDKVLIAVG TVAVVAVLSK LKSAVTKPKL NLPPGPWTLP LIGSIHHIVS NPLPYRAMRE
LAHKHGPLMM LWLGEVPTLV VSSPEAAQAI TKTHDVSFAD RHINSTVDIL TFNGMDMVFG
SYGEQWRQLR KLSVLELLSA ARVQSFQRIR EEEVARFMRS LAASASAGAT VDLSKMISSF
INDTFVRESI GSRCKYQDEY LAALDTAIRV AAELSVGNIF PSSRVLQSLS TARRKAIASR
DEMARILGQI IRETKESMDQ GDKTSNESMI SVLLRLQKDA GLPIELTDNV VMALMFDLFG
AGSDTSSTTL TWCMTELVRY PATMAKAQAE VREAFKGKTT ITEDDLSTAN LRYLKLVVKE
ALRLHCPVPL LLPRKCREAC QVMGYDIPKG TCVFVNVWAI CRDPRYWEDA EEFKPERFEN
SNLDYKGTYY EYLPFGSGRR MCPGANLGVA NLELALASLL YHFDWKLPSG QEPKDVDVWE
AAGLVAKKNI GLVLHPVSHI APVNA
