(data stored in ACNUC14511 zone)

HOGENOM: MAIZE_9_PE3544

ID   MAIZE_9_PE3544                       STANDARD;      PRT;   350 AA.
AC   MAIZE_9_PE3544; P49353;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Farnesyl pyrophosphate synthase; Short=FPP synthase;
DE   Short=FPS; EC=2.5.1.10;AltName: Full=(2E,6E)-farnesyl diphosphate
DE   synthase;AltName: Full=Dimethylallyltranstransferase; EC=2.5.1 1;AltName:
DE   Full=Farnesyl diphosphate synthase;AltName: Full=Geranyltranstransferase;
DE   (MAIZE_9.PE3544).
GN   Name=FPS;
OS   ZEA MAYS.
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; Liliopsida; commelinids; Poales; Poaceae; Panicoideae;
OC   Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MAIZE_9.PE3544.
CC       Zea mays chromosome 8 AGPv2 full sequence 1..175793759 annotated by Ens
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:FPPS_MAIZE
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       pyrophosphate with the allylic pyrophosphates, dimethylallyl
CC       pyrophosphate, and then with the resultant geranylpyrophosphate to
CC       the ultimate product farnesyl pyrophosphate.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + (2E,6E)-farnesyl diphosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
CC       biosynthesis; farnesyl diphosphate from geranyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
CC       biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
CC       and isopentenyl diphosphate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC   -!- GENE_FAMILY: HOG000160912 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Zea_mays;GRMZM2G168681;GRMZM2G168681_T01;GRMZM2G168681_P01.
DR   UniProtKB/Swiss-Prot; P49353; -.
DR   EMBL; L39789; AAB39276.1; -; mRNA.
DR   PIR; T03291; T03291.
DR   RefSeq; NP_001105039.1; NM_001111569.1.
DR   UniGene; Zm.317; -.
DR   ProteinModelPortal; P49353; -.
DR   EnsemblPlants; GRMZM2G168681_T01; GRMZM2G168681_P01; GRMZM2G168681.
DR   GeneID; 541903; -.
DR   KEGG; zma:541903; -.
DR   Gramene; P49353; -.
DR   MaizeGDB; 86802; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; Terpenoid_synth; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   HOGENOMDNA; MAIZE_9.PE3544; -.
KW   GRMZM2G168681004965old_1320000031; GRMZM2G168681_P0181old_1320000031;
KW   C0P3X0; Q548K3;
KW   Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis;
KW   Lipid synthesis; Magnesium; Metal-binding; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
SQ   SEQUENCE   350 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAAGGNGAGG DTRAAFARIY KTLKEELLTD PAFEFTEESR QWIDRMVDYN VLGGKCNRGL
     SVVDSYKLLK GADALGEEET FLACTLGWCI EWLQAFFLVL DDIMDDSHTR RGQPCWFRVP
     QVGLIAANDG IILRNHISRI LRRHFKGKPY YADLLDLFNE VEFKTASGQL LDLITTHEGE
     KDLTKYNITV HGRIVQYKTA YYSFYLPVAC ALLLSGENLD NYGDVENILV EMGTYFQVQD
     DYLDCYGDPE FIGKIGTDIE DYKCSWLVVQ ALERADESQK RILFENYGKK DPACVAKVKN
     LYKELDLEAV FQEYENESYK KLIADIEAQP SIAVQKVLKS FLHKIYKRQK
//

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