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Conserved domains on  [gi|17137582|ref|NP_477380|]
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farnesyl pyrophosphate synthase [Drosophila melanogaster]

Protein Classification

FPP/GGPP synthase family protein( domain architecture ID 11092413)

FPP/GGPP synthase family protein such as farnesyl/geranylgeranyl diphosphate synthases, which are key enzymes in isoprenoid biosynthesis, catalyzing the formation of farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), respectively

CATH:  1.10.600.10
EC:  2.5.1.-
Gene Ontology:  GO:0004659|GO:0046872|GO:0008299
PubMed:  8003978|11111076
SCOP:  4001453

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
112-373 2.93e-96

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 288.64  E-value: 2.93e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   112 KWFAQVLQYNVPR-GKKNRGILTVLTYKNLVPtqdltPENIKLAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCWHKV 190
Cdd:pfam00348   2 KLLYEPLDYLVSAgGKRIRPLLVLLSAEALGG-----PEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   191 enVGL-TAINDALMIENAMYAILKKHFSHLDcyvaLMELFHEITYITTCGQSLDQLNSNRCVSEFTMENYKAIVENKTAy 269
Cdd:pfam00348  77 --FGNaIAINDGDYLYALAFQLLAKLFPNPE----LLELFSEVTLQTAEGQGLDLLWRNDDDLSCTEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   270 YSFYLPFALALHLAGYKDaEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGKI-GTDIQDNKCSWLAVVAMQRaNVEQ 348
Cdd:pfam00348 150 YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQ 227
                         250       260
                  ....*....|....*....|....*
gi 17137582   349 KQIMVDCYGKeEPAKVERVKELYKE 373
Cdd:pfam00348 228 RKILLEIYGK-RPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
112-373 2.93e-96

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 288.64  E-value: 2.93e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   112 KWFAQVLQYNVPR-GKKNRGILTVLTYKNLVPtqdltPENIKLAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCWHKV 190
Cdd:pfam00348   2 KLLYEPLDYLVSAgGKRIRPLLVLLSAEALGG-----PEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   191 enVGL-TAINDALMIENAMYAILKKHFSHLDcyvaLMELFHEITYITTCGQSLDQLNSNRCVSEFTMENYKAIVENKTAy 269
Cdd:pfam00348  77 --FGNaIAINDGDYLYALAFQLLAKLFPNPE----LLELFSEVTLQTAEGQGLDLLWRNDDDLSCTEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   270 YSFYLPFALALHLAGYKDaEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGKI-GTDIQDNKCSWLAVVAMQRaNVEQ 348
Cdd:pfam00348 150 YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQ 227
                         250       260
                  ....*....|....*....|....*
gi 17137582   349 KQIMVDCYGKeEPAKVERVKELYKE 373
Cdd:pfam00348 228 RKILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
109-417 2.96e-78

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 242.84  E-value: 2.96e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 109 DAAKWFAQVLQYNVPR-GKKNRGILTVLTYknlvptQDLTPENIKLAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCW 187
Cdd:cd00685   1 SEVELLREALRYLLLAgGKRLRPLLVLLAA------RALGGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 188 HKVENVGlTAINDALMIENAMYAILKKHFSHldCYVALMELFHEITYITTCGQSLDQLNSNRcvSEFTMENYKAIVENKT 267
Cdd:cd00685  75 HKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLDLLSEYD--TDVTEEEYLRIIRLKT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 268 AYYSFYLPFALALHLAGykDAEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGK-IGTDIQDNKCSWLAVVAMqranv 346
Cdd:cd00685 150 AALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL----- 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137582 347 eqkqimvdcygkeepakvervKELYKELglpstyaifEEESYNMIKTHIQQtsrgVPHQTFLQILNKIYQR 417
Cdd:cd00685 223 ---------------------RELAREY---------EEKALEALKALPES----PAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
161-397 2.39e-35

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 133.04  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 161 VEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGlTAIN--DALMIEnAMYAILKkhFSHLDCYVALMELFHEITYITTC 238
Cdd:COG0142  74 VELIHTASLVHDDVMDDDDLRRGKPTVHARFGEA-TAILagDALLAL-AFELLAE--LGDPERRLRALRILARAARGMCE 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 239 GQSLDQLNSNRcvSEFTMENYKAIVENKTAYYsfylpFALALHLAGY------KDAEAFRQsktILLEMGNFFQVQDDFL 312
Cdd:COG0142 150 GQALDLEAEGR--LDVTLEEYLRVIRLKTAAL-----FAAALRLGAIlagadeEQVEALRR---YGRNLGLAFQIRDDIL 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 313 DCFGNPEVTGK-IGTDIQDNKCSWLAVVAMQRANVEQKQIMVDCYGKEE--PAKVERVKELYKELGlpstyAIfeEESYN 389
Cdd:COG0142 220 DVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRESG-----AL--EYARE 292

                ....*...
gi 17137582 390 MIKTHIQQ 397
Cdd:COG0142 293 LARELAEE 300
preA CHL00151
prenyl transferase; Reviewed
125-396 9.20e-09

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 56.72  E-value: 9.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  125 GKKNRGILTVLTYKNLVPTQDLTPENIKLAQYLgwcvEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGLTAI-NDALM 203
Cdd:CHL00151  45 GKRIRPAIVLLVAKATGGNMEIKTSQQRLAEIT----EIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLaGDFLF 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  204 IENAMY-AILKKhfshldcyvalMELFHEIT-YITTCGQSLDQLNSNRCVSEFTMENYKAIVENKTAyysfYLPFALALH 281
Cdd:CHL00151 121 AQSSWYlANLNN-----------LEVVKLISkVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTA----SLIAASCKA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  282 LAGYKDAEAFRQSKTILL--EMGNFFQVQDDFLDCFGNPEVTGK-IGTDIQDNKCSWLAVVAMQRaNVEQKQIMVD--CY 356
Cdd:CHL00151 186 AALLSDADEKDHNDFYLYgkHLGLAFQIIDDVLDITSSTESLGKpIGSDLKNGNLTAPVLFALTQ-NSKLAKLIERefCE 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 17137582  357 GKEEPAKVERVKElykelglpsTYAIfeEESYNMIKTHIQ 396
Cdd:CHL00151 265 TKDISQALQIIKE---------TNGI--EKAKDLALEHMQ 293
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
112-373 2.93e-96

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 288.64  E-value: 2.93e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   112 KWFAQVLQYNVPR-GKKNRGILTVLTYKNLVPtqdltPENIKLAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCWHKV 190
Cdd:pfam00348   2 KLLYEPLDYLVSAgGKRIRPLLVLLSAEALGG-----PEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   191 enVGL-TAINDALMIENAMYAILKKHFSHLDcyvaLMELFHEITYITTCGQSLDQLNSNRCVSEFTMENYKAIVENKTAy 269
Cdd:pfam00348  77 --FGNaIAINDGDYLYALAFQLLAKLFPNPE----LLELFSEVTLQTAEGQGLDLLWRNDDDLSCTEEEYLEIVKYKTA- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582   270 YSFYLPFALALHLAGYKDaEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGKI-GTDIQDNKCSWLAVVAMQRaNVEQ 348
Cdd:pfam00348 150 YLFALAVKLGAILSGADD-EVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER-TPEQ 227
                         250       260
                  ....*....|....*....|....*
gi 17137582   349 KQIMVDCYGKeEPAKVERVKELYKE 373
Cdd:pfam00348 228 RKILLEIYGK-RPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
109-417 2.96e-78

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 242.84  E-value: 2.96e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 109 DAAKWFAQVLQYNVPR-GKKNRGILTVLTYknlvptQDLTPENIKLAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCW 187
Cdd:cd00685   1 SEVELLREALRYLLLAgGKRLRPLLVLLAA------RALGGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 188 HKVENVGlTAINDALMIENAMYAILKKHFSHldCYVALMELFHEITYITTCGQSLDQLNSNRcvSEFTMENYKAIVENKT 267
Cdd:cd00685  75 HKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLDLLSEYD--TDVTEEEYLRIIRLKT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 268 AYYSFYLPFALALHLAGykDAEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGK-IGTDIQDNKCSWLAVVAMqranv 346
Cdd:cd00685 150 AALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL----- 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137582 347 eqkqimvdcygkeepakvervKELYKELglpstyaifEEESYNMIKTHIQQtsrgVPHQTFLQILNKIYQR 417
Cdd:cd00685 223 ---------------------RELAREY---------EEKALEALKALPES----PAREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
128-344 6.43e-58

Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of class 1 isoprenoid biosynthesis enzymes which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, diterpenes, ubiquinone, and archaeal ether linked lipids; and are widely distributed among archaea, bacteria, and eukareya. The enzymes in this family share the same 'isoprenoid synthase fold' and include the head-to-tail (HT) IPPS which catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Mechanistically and structurally distinct, cis-IPPS are not included in this CD.


Pssm-ID: 173836  Cd Length: 236  Bit Score: 189.48  E-value: 6.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 128 NRGILTVLTYKNLVPTQDLtpeniklAQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGLTAINDALMIENA 207
Cdd:cd00867   1 SRPLLVLLLARALGGDLEA-------ALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLLAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 208 MYAILKKHFshldcYVALMELFHEITYITTCGQSLDQLNSNRcvSEFTMENYKAIVENKTAYYSFYLPFALALHLAGykD 287
Cdd:cd00867  74 AFQLLARLG-----YPRALELFAEALRELLEGQALDLEFERD--TYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGA--D 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17137582 288 AEAFRQSKTILLEMGNFFQVQDDFLDCFGNPEVTGKIGTDIQDNKCSWLAVVAMQRA 344
Cdd:cd00867 145 DEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERA 201
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
154-374 5.96e-36

Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases (IPPS) and class I terpene cyclases which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, and diterpenes; and are widely distributed among archaea, bacteria, and eukaryota.The enzymes in this superfamily share the same 'isoprenoid synthase fold' and include several subgroups. The head-to-tail (HT) IPPS catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. Cyclic monoterpenes, diterpenes, and sesquiterpenes, are formed from their respective linear isoprenoid diphosphates by class I terpene cyclases. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Cyclization of these 30- and 40-carbon linear forms are catalyzed by class II cyclases. Both the isoprenoid chain elongation reactions and the class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Generally, the enzymes in this family exhibit an all-trans reaction pathway, an exception, is the cis-trans terpene cyclase, trichodiene synthase. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD.


Pssm-ID: 173830 [Multi-domain]  Cd Length: 243  Bit Score: 132.23  E-value: 5.96e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 154 AQYLGWCVEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGL--TAINDALMIENAMYAILKKHFShldcyVALMELFHE 231
Cdd:cd00385  12 ASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGlpEAILAGDLLLADAFEELAREGS-----PEALEILAE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 232 ITYITTCGQSLDQLNSNRCVseFTMENYKAIVENKTAYYSFYLPFALALHLAGykDAEAFRQSKTILLEMGNFFQVQDDF 311
Cdd:cd00385  87 ALLDLLEGQLLDLKWRREYV--PTLEEYLEYCRYKTAGLVGALCLLGAGLSGG--EAELLEALRKLGRALGLAFQLTNDL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137582 312 LDCFGNPEVTgkigtdiqDNKCSWLAVVAMQRANVEQKQIMVDCYGKEEPAK---VERVKELYKEL 374
Cdd:cd00385 163 LDYEGDAERG--------EGKCTLPVLYALEYGVPAEDLLLVEKSGSLEEALeelAKLAEEALKEL 220
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
161-397 2.39e-35

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 133.04  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 161 VEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGlTAIN--DALMIEnAMYAILKkhFSHLDCYVALMELFHEITYITTC 238
Cdd:COG0142  74 VELIHTASLVHDDVMDDDDLRRGKPTVHARFGEA-TAILagDALLAL-AFELLAE--LGDPERRLRALRILARAARGMCE 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 239 GQSLDQLNSNRcvSEFTMENYKAIVENKTAYYsfylpFALALHLAGY------KDAEAFRQsktILLEMGNFFQVQDDFL 312
Cdd:COG0142 150 GQALDLEAEGR--LDVTLEEYLRVIRLKTAAL-----FAAALRLGAIlagadeEQVEALRR---YGRNLGLAFQIRDDIL 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582 313 DCFGNPEVTGK-IGTDIQDNKCSWLAVVAMQRANVEQKQIMVDCYGKEE--PAKVERVKELYKELGlpstyAIfeEESYN 389
Cdd:COG0142 220 DVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRESG-----AL--EYARE 292

                ....*...
gi 17137582 390 MIKTHIQQ 397
Cdd:COG0142 293 LARELAEE 300
preA CHL00151
prenyl transferase; Reviewed
125-396 9.20e-09

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 56.72  E-value: 9.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  125 GKKNRGILTVLTYKNLVPTQDLTPENIKLAQYLgwcvEMLQSFFIISDDVMDNSTTRRGQPCWHKVENVGLTAI-NDALM 203
Cdd:CHL00151  45 GKRIRPAIVLLVAKATGGNMEIKTSQQRLAEIT----EIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLaGDFLF 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  204 IENAMY-AILKKhfshldcyvalMELFHEIT-YITTCGQSLDQLNSNRCVSEFTMENYKAIVENKTAyysfYLPFALALH 281
Cdd:CHL00151 121 AQSSWYlANLNN-----------LEVVKLISkVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTA----SLIAASCKA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  282 LAGYKDAEAFRQSKTILL--EMGNFFQVQDDFLDCFGNPEVTGK-IGTDIQDNKCSWLAVVAMQRaNVEQKQIMVD--CY 356
Cdd:CHL00151 186 AALLSDADEKDHNDFYLYgkHLGLAFQIIDDVLDITSSTESLGKpIGSDLKNGNLTAPVLFALTQ-NSKLAKLIERefCE 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 17137582  357 GKEEPAKVERVKElykelglpsTYAIfeEESYNMIKTHIQ 396
Cdd:CHL00151 265 TKDISQALQIIKE---------TNGI--EKAKDLALEHMQ 293
PLN02857 PLN02857
octaprenyl-diphosphate synthase
125-375 7.02e-04

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 41.76  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  125 GKKNRGILTVLTYK---NLVPTQDLTPENIKLAQylgwCVEMLQSFFIISDDVMDNSTTRRGQPCWHKvenvgLTAINDA 201
Cdd:PLN02857 135 GKRMRPALVFLVSRataELAGLKELTTEHRRLAE----ITEMIHTASLIHDDVLDESDMRRGKETVHQ-----LYGTRVA 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  202 LMIENAMYAILKKHFSHLDcYVALMELFHEITYITTCGQsLDQLnSNRCVSEFTMENYKAIVENKTAyysfylpfalALH 281
Cdd:PLN02857 206 VLAGDFMFAQSSWYLANLD-NLEVIKLISQVIKDFASGE-IKQA-SSLFDCDVTLDEYLLKSYYKTA----------SLI 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137582  282 LAGYKDAEAFRQSKTILLE--------MGNFFQVQDDFLDCFGNPEVTGK-IGTDIQDNKCSWLAVVAMQRaNVEQKQIM 352
Cdd:PLN02857 273 AASTKSAAIFSGVDSSVKEqmyeygknLGLAFQVVDDILDFTQSTEQLGKpAGSDLAKGNLTAPVIFALEK-EPELREII 351
                        250       260
                 ....*....|....*....|...
gi 17137582  353 VDCYgkEEPAKVERVKELYKELG 375
Cdd:PLN02857 352 ESEF--CEEGSLEEAIELVNEGG 372
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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