AN1_MAIZE
ID AN1_MAIZE Reviewed; 824 AA.
AC Q41771; A0A1D6KV47;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ent-copalyl diphosphate synthase AN1, chloroplastic {ECO:0000305};
DE Short=Ent-CPP synthase {ECO:0000303|PubMed:16307364};
DE Short=Ent-CPS {ECO:0000303|PubMed:16307364};
DE EC=5.5.1.13 {ECO:0000269|PubMed:16307364};
DE AltName: Full=Ent-kaurene synthase A {ECO:0000303|PubMed:7696880};
DE AltName: Full=Protein ANTHER EAR 1 {ECO:0000303|PubMed:7696880};
DE Flags: Precursor;
GN Name=AN1 {ECO:0000303|PubMed:7696880};
GN ORFNames=ZEAMMB73_Zm00001d032961 {ECO:0000312|EMBL:ONM06422.1};
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7696880; DOI=10.2307/3869839;
RA Bensen R.J., Johal G.S., Crane V.C., Tossberg J.T., Schnable P.S.,
RA Meeley R.B., Briggs S.P.;
RT "Cloning and characterization of the maize An1 gene.";
RL Plant Cell 7:75-84(1995).
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=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).
CC -!- FUNCTION: Involved in giberellin biosynthesis (Probable)
CC (PubMed:16307364). Catalyzes the conversion of geranylgeranyl
CC diphosphate to the gibberellin precursor ent-copalyl diphosphate
CC (Probable) (PubMed:16307364). {ECO:0000269|PubMed:16307364,
CC ECO:0000305|PubMed:7696880}.
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};
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 -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity through binding to Mg(2+). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype due to gibberellin-deficient
CC mutant, displaying reduced internode lengths, foreshortened broad
CC leaves, and unbranched tassel. {ECO:0000269|PubMed:7696880}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC {ECO:0000305}.
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DR EMBL; L37750; AAA73960.1; -; mRNA.
DR EMBL; CM007647; ONM06422.1; -; Genomic_DNA.
DR PIR; T02959; T02959.
DR RefSeq; NP_001105329.2; NM_001111859.2.
DR AlphaFoldDB; Q41771; -.
DR SMR; Q41771; -.
DR STRING; 4577.GRMZM2G081554_P01; -.
DR GeneID; 542253; -.
DR KEGG; zma:542253; -.
DR eggNOG; ENOG502QQN6; Eukaryota.
DR OrthoDB; 700680at2759; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q41771; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..824
FT /note="Ent-copalyl diphosphate synthase AN1, chloroplastic"
FT /id="PRO_0000447769"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 379..382
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 42..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
SQ SEQUENCE 824 AA; 95180 MW; B16A024358D307CA CRC64;
MPYPHPYPWQ SSRRRRRRRG RDGAPRQPQA RRVVERAAAG PGHATTTQQP DNVSSAKVFQ
TSRVETESEI AKWPGKPQDL EDEHQAEEAE LQPLIDQVRA MLRSMNDGDT SASAYDTAWV
AMVPKVGGDG GAQPQFPATV RWIVDHQLPD GSWGDSALFS AYDRMINTLA CVVALTKWSL
EPARCEAGLS FLHENMWRLA EEEAESMPIG FEIAFPSLIQ TARDLGVVDF PYGHPALQSI
YANREVKLKR IPRDMMHRVP TSILHSLEGM PDLDWPRLLN LQSCDGSFLF SPSATAYALM
QTGDKKCFEY IDRIVKKFNG GVPNVYPVDL FEHIWVVDRL ERLGISRYFQ REIEQCMDYV
NRHWTEDGIC WARKSNVKDV DDTAMAFRLL RLHGYNVSPS VFKNFEKDGE FFCFVGQSTQ
AVTGMYNLNR ASQISFQGED VLHRARVFSY EFLRQREEQG MIRDKWIVAK DLPGEVQYTL
DFPWYASLPR VEARTYLDQY GGKDDVWIGK TLYRMPLVNN DTYLELAIRD FNHCQALHQL
ECNGLQTWYK DNCLDAFGVE PQDVLRSYFL AAACIFEPSR AAERLAWART SMIANAISTH
LRDISEDKKR LECFVHCLYE ENDVSWLKRN PNDVILERAL RRLINLLAQE ALPIHEGQRF
IHSLLSLAWT EWMLQKANKE ENKYHKCSGI EPQYMVHDRQ TYLLLVQVIE ICAGRIGEAV
SMINNKDNDW FIQLTCATCD SLNHRMLLSQ DTMKNEARIN WIEKEIELNM QELAQSLLLR
CDEKTSNKKT KKTLWDVLRS LYYATHSPQH MIDRHVSRVI FEPV
