CPPS2_MAIZE
ID CPPS2_MAIZE Reviewed; 825 AA.
AC A0A1D6K6U5; Q672R4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Ent-copalyl diphosphate synthase 2, chloroplastic {ECO:0000305};
DE Short=Ent-CPP synthase 2 {ECO:0000303|PubMed:16307364};
DE Short=Ent-CPS 2 {ECO:0000303|PubMed:16307364};
DE EC=5.5.1.13 {ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898};
DE AltName: Full=Protein ANTHER EAR 2 {ECO:0000305};
DE Short=ZmAN2 {ECO:0000303|PubMed:29475898};
DE Flags: Precursor;
GN Name=CPPS2 {ECO:0000305}; Synonyms=AN2 {ECO:0000303|PubMed:16307364};
GN ORFNames=ZEAMMB73_Zm00001d029648 {ECO:0000312|EMBL:ONL99283.1};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16307364; DOI=10.1007/s11103-005-1674-8;
RA Harris L.J., Saparno A., Johnston A., Prisic S., Xu M., Allard S.,
RA Kathiresan A., Ouellet T., Peters R.J.;
RT "The maize An2 gene is induced by Fusarium attack and encodes an ent-
RT copalyl diphosphate synthase.";
RL Plant Mol. Biol. 59:881-894(2005).
RN [2]
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 [3]
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 gibberellin biosynthesis (PubMed:16307364).
CC Catalyzes the conversion of geranylgeranyl diphosphate to the
CC gibberellin precursor ent-copalyl diphosphate (ent-CPP)
CC (PubMed:16307364). Involved in the production of antifungal
CC dolabralexin phytoalexins in response to biotic and abiotic stresses
CC (PubMed:29475898). In response to fungal infection and in associtation
CC with KSL4, is involved in the production dolabradiene, a type of
CC antifungal phytoalexin (PubMed:29475898). {ECO:0000269|PubMed:16307364,
CC ECO:0000269|PubMed:29475898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl
CC diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553,
CC ChEBI:CHEBI:58756; EC=5.5.1.13;
CC Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q38802};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in tassels.
CC {ECO:0000269|PubMed:16307364}.
CC -!- INDUCTION: Induced by the fungal pathogens Fusarium graminearum and
CC Fusarium verticillioides. {ECO:0000269|PubMed:16307364}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity through binding to Mg(2+). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC {ECO:0000305}.
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DR EMBL; AY562490; AAT70083.1; -; Genomic_DNA.
DR EMBL; AY562491; AAT70084.1; -; mRNA.
DR EMBL; CM007647; ONL99283.1; -; Genomic_DNA.
DR RefSeq; NP_001105257.2; NM_001111787.2.
DR AlphaFoldDB; A0A1D6K6U5; -.
DR SMR; A0A1D6K6U5; -.
DR STRING; 4577.GRMZM2G044481_P01; -.
DR GeneID; 542165; -.
DR KEGG; zma:542165; -.
DR MaizeGDB; 85297; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; A0A1D6K6U5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IMP:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
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 GO; GO:0016102; P:diterpenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..825
FT /note="Ent-copalyl diphosphate synthase 2, chloroplastic"
FT /id="PRO_0000447770"
FT MOTIF 373..376
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 34
FT /note="A -> T (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="R -> RR (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="R -> L (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="D -> H (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="A -> G (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="V -> M (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="R -> K (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="P -> A (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="Q -> E (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="K -> R (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="D -> DI (in Ref. 1; AAT70083/AAT70084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 92762 MW; 1004925ED2C9A152 CRC64;
MVLSSSCTTV PHLSSLAVVQ LGPWSSRIKK KTDAVAVPAA AGRWRARARA QDTSESAAVA
KGSSLTPIVR TDAESRRTRW PTDDDDAEPL VDEIRAMLTS MSDGDISVSA YDTAWVGLVP
RLDGGEGPQF PAAVRWIRNN QLPDGSWGDA ALFSAYDRLI NTLACVVTLT RWSLEPEMRG
RGLSFLGRNM WKLATEDEES MPIGFELAFP SLIELAKSLG VHDFPYDHQA LQAIYSSREI
KVKRIPKEVM HTVPTSILHS LEGMPGLDWA RLLKLQSSDG SFLFSPAATA YALMNTGDDR
CFSYIDRTVK KFNGGVPNVY PVDLFEHIWA VDRLERLGIS RYFQKEIEQC MDYVNRHWTE
DGICWARNSD VKEVDDTAMA FRLLRLHGYS VSPDVFKNFE KDGEFFAFVG QSNQAVTGMY
NLNRASQISF PGEDVLHRAG PFSYEFLRRK QAEGALRDKW IISKDLPGEV VYTLDFPWYG
NLPRVEARDY LEQYGGGDDV WIGKTLYRMP LVNNDVYLEL ARMDFNHCQA LHQLEWQGLK
KWYTENRLMD FGVAQEDALR AYFLAAASVY EPCRAAERLA WARAAILANA VSTHLRNSPS
FRERLEHSLR CRPSEETDGS WFNSSSGSDA VLVKAVLRLT DSLAREAQPI HGGDPEDIHK
LLRSAWAEWV REKADAADSV CNGSSAVEQE GSRMVHDKQT CLLLARMIEI SAGRAAGEAA
SEDGDRRIIQ LTGSICDSLK QKMLVSQDPE KNEEMMSHVD DELKLRIREF VQYLLRLGEK
KTGSSETRQT FLSIVKSCYY AAHCPPHVVD RHISRVIFEP VSAAK
