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Conserved domains on  [gi|743518677|ref|WP_039036097|]
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MULTISPECIES: (2E,6E)-farnesyl diphosphate synthase [Shewanella]

Protein Classification

isoprenoid biosynthesis enzyme family protein( domain architecture ID 89)

isoprenoid biosynthesis enzyme family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Isoprenoid_Biosyn_C1 super family cl00210
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
3-291 3.68e-109

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.


The actual alignment was detected with superfamily member PRK10581:

Pssm-ID: 469660  Cd Length: 299  Bit Score: 318.25  E-value: 3.68e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   3 TQAINQYQQRVNQRIATILDTLDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIH 82
Cdd:PRK10581   4 PQQLQACVQQANQALSRFIAPLPFQNTPVVEAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  83 DDLPAMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELIS-SDIEGLSDRQHLRLVQALAKASGYRGMCGGQAQDLN 161
Cdd:PRK10581  84 DDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSdAPMPEVSDRDRISMISELASASGIAGMCGGQALDLE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 162 ATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLE-YADAVGLAFQVQDDILDITGSTEELGKPQGSDL 240
Cdd:PRK10581 164 AEGKQVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDrYAESIGLAFQVQDDILDVVGDTATLGKRQGADQ 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743518677 241 DANKSTYPKLLGLEGAKTTAQKLLEDALSALAKL---PYNSQLIAEFARYIVER 291
Cdd:PRK10581 244 QLGKSTYPALLGLEQARKKARDLIDDARQSLDQLaaqSLDTSALEALANYIIQR 297
 
Name Accession Description Interval E-value
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
3-291 3.68e-109

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 318.25  E-value: 3.68e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   3 TQAINQYQQRVNQRIATILDTLDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIH 82
Cdd:PRK10581   4 PQQLQACVQQANQALSRFIAPLPFQNTPVVEAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  83 DDLPAMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELIS-SDIEGLSDRQHLRLVQALAKASGYRGMCGGQAQDLN 161
Cdd:PRK10581  84 DDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSdAPMPEVSDRDRISMISELASASGIAGMCGGQALDLE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 162 ATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLE-YADAVGLAFQVQDDILDITGSTEELGKPQGSDL 240
Cdd:PRK10581 164 AEGKQVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDrYAESIGLAFQVQDDILDVVGDTATLGKRQGADQ 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743518677 241 DANKSTYPKLLGLEGAKTTAQKLLEDALSALAKL---PYNSQLIAEFARYIVER 291
Cdd:PRK10581 244 QLGKSTYPALLGLEQARKKARDLIDDARQSLDQLaaqSLDTSALEALANYIIQR 297
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
2-292 2.58e-106

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: 312.16  E-value: 2.58e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   2 LTQAINQYQQRVNQRIATILDtlDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLI 81
Cdd:COG0142    6 LLALLAEDLARVEAALEELLA--RSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  82 HDDLpaMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELISsdiEGLSDRQHLRLVQALAKASgyRGMCGGQAQDL- 160
Cdd:COG0142   84 HDDV--MDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLA---ELGDPERRLRALRILARAA--RGMCEGQALDLe 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 161 NATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDL 240
Cdd:COG0142  157 AEGRLDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 241 DANKSTYPKLLGLEGAKTT--------------------------------------AQKLLEDALSALAKLPYNS--QL 280
Cdd:COG0142  237 REGKPTLPLLLALERADPEeraelrellgkpdldeedlaevrallresgaleyarelARELAEEALAALAALPDSEarEA 316
                        330
                 ....*....|..
gi 743518677 281 IAEFARYIVERR 292
Cdd:COG0142  317 LRALADYVVERD 328
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
26-291 2.74e-86

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: 258.64  E-value: 2.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  26 DTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVP-LERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAF 104
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPeLEAALRLAAAIELLHTASLVHDDV--MDNSDLRRGKPTVHKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 105 NEATAILAGDALQTLAFELISSdiegLSDRQHLRLVQALAKASgyRGMCGGQAQDL-NATDKEISLEQLTALHRLKTGAL 183
Cdd:cd00685   79 GNATAILAGDYLLARAFELLAR----LGNPYYPRALELFSEAI--LELVEGQLLDLlSEYDTDVTEEEYLRIIRLKTAAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 184 IRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLEgakTTAQKL 263
Cdd:cd00685  153 FAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR---ELAREY 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 743518677 264 LEDALSALAKLPYNS--QLIAEFARYIVER 291
Cdd:cd00685  230 EEKALEALKALPESParEALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
28-265 2.33e-67

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 210.06  E-value: 2.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   28 EPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVP--LERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAFN 105
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPedLEKAIVLAWAVELLHAASLVHDDI--MDNSDLRRGQPTWHRIFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  106 EATAILAGDALQTLAFELISSDieglsdRQHLRLVQALAKASGyrGMCGGQAQDL---NATDKEISLEQLTALHRLKTGA 182
Cdd:pfam00348  79 NAIAINDGDYLYALAFQLLAKL------FPNPELLELFSEVTL--QTAEGQGLDLlwrNDDDLSCTEEEYLEIVKYKTAY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  183 LIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLEGAKTTAQK 262
Cdd:pfam00348 151 LFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEQRKI 230

                  ...
gi 743518677  263 LLE 265
Cdd:pfam00348 231 LLE 233
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
22-292 3.10e-29

heptaprenyl diphosphate synthase component II; Members of this family are component II of the heterodimeric heptaprenyl diphosphate synthase. The trusted cutoff was set such that all members identified are encoded near to a recognizable gene for component I (in pfam07307). This enzyme acts in menaquinone-7 isoprenoid side chain biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131795  Cd Length: 319  Bit Score: 113.27  E-value: 3.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   22 DTLDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVH 101
Cdd:TIGR02748  22 KAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDV--IDDADLRRGRPTIK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  102 IAFNEATAILAGDALQTLAFELISSdiegLSD-RQHLRLVQALAKasgyrgMCGGQAQDLNatDKeISLEQ--LTALHRL 178
Cdd:TIGR02748 100 SKWGNRIAMYTGDYLFAKSLETMTE----IKDpRAHQILSHTIVE------VCRGEIEQIK--DK-YNFDQnlRTYLRRI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  179 --KTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLE-- 254
Cdd:TIGR02748 167 krKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEdp 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743518677  255 ---------GAKTTAQKL-----------------------LEDALSALAKLPYNS--QLIAEFARYIVERR 292
Cdd:TIGR02748 247 flkkrieqvLEETTAEEMeplieevkksdaieyayavsdryLKKALELLDGLPDGRakKPLQEIAKYIGKRK 318
 
Name Accession Description Interval E-value
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
3-291 3.68e-109

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 318.25  E-value: 3.68e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   3 TQAINQYQQRVNQRIATILDTLDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIH 82
Cdd:PRK10581   4 PQQLQACVQQANQALSRFIAPLPFQNTPVVEAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  83 DDLPAMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELIS-SDIEGLSDRQHLRLVQALAKASGYRGMCGGQAQDLN 161
Cdd:PRK10581  84 DDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSdAPMPEVSDRDRISMISELASASGIAGMCGGQALDLE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 162 ATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLE-YADAVGLAFQVQDDILDITGSTEELGKPQGSDL 240
Cdd:PRK10581 164 AEGKQVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDrYAESIGLAFQVQDDILDVVGDTATLGKRQGADQ 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743518677 241 DANKSTYPKLLGLEGAKTTAQKLLEDALSALAKL---PYNSQLIAEFARYIVER 291
Cdd:PRK10581 244 QLGKSTYPALLGLEQARKKARDLIDDARQSLDQLaaqSLDTSALEALANYIIQR 297
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
2-292 2.58e-106

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: 312.16  E-value: 2.58e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   2 LTQAINQYQQRVNQRIATILDtlDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLI 81
Cdd:COG0142    6 LLALLAEDLARVEAALEELLA--RSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  82 HDDLpaMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELISsdiEGLSDRQHLRLVQALAKASgyRGMCGGQAQDL- 160
Cdd:COG0142   84 HDDV--MDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLA---ELGDPERRLRALRILARAA--RGMCEGQALDLe 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 161 NATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDL 240
Cdd:COG0142  157 AEGRLDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 241 DANKSTYPKLLGLEGAKTT--------------------------------------AQKLLEDALSALAKLPYNS--QL 280
Cdd:COG0142  237 REGKPTLPLLLALERADPEeraelrellgkpdldeedlaevrallresgaleyarelARELAEEALAALAALPDSEarEA 316
                        330
                 ....*....|..
gi 743518677 281 IAEFARYIVERR 292
Cdd:COG0142  317 LRALADYVVERD 328
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
26-291 2.74e-86

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: 258.64  E-value: 2.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  26 DTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVP-LERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAF 104
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPeLEAALRLAAAIELLHTASLVHDDV--MDNSDLRRGKPTVHKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 105 NEATAILAGDALQTLAFELISSdiegLSDRQHLRLVQALAKASgyRGMCGGQAQDL-NATDKEISLEQLTALHRLKTGAL 183
Cdd:cd00685   79 GNATAILAGDYLLARAFELLAR----LGNPYYPRALELFSEAI--LELVEGQLLDLlSEYDTDVTEEEYLRIIRLKTAAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 184 IRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLEgakTTAQKL 263
Cdd:cd00685  153 FAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR---ELAREY 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 743518677 264 LEDALSALAKLPYNS--QLIAEFARYIVER 291
Cdd:cd00685  230 EEKALEALKALPESParEALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
28-265 2.33e-67

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 210.06  E-value: 2.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   28 EPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVP--LERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAFN 105
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPedLEKAIVLAWAVELLHAASLVHDDI--MDNSDLRRGQPTWHRIFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  106 EATAILAGDALQTLAFELISSDieglsdRQHLRLVQALAKASGyrGMCGGQAQDL---NATDKEISLEQLTALHRLKTGA 182
Cdd:pfam00348  79 NAIAINDGDYLYALAFQLLAKL------FPNPELLELFSEVTL--QTAEGQGLDLlwrNDDDLSCTEEEYLEIVKYKTAY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  183 LIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLEGAKTTAQK 262
Cdd:pfam00348 151 LFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEQRKI 230

                  ...
gi 743518677  263 LLE 265
Cdd:pfam00348 231 LLE 233
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
46-291 7.25e-57

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: 182.93  E-value: 7.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  46 IRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVH-IAFNEATAILAGDALQTLAFELi 124
Cdd:cd00867    1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDI--VDDSDLRRGKPTAHlRRFGNALAILAGDYLLARAFQL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 125 ssdiegLSDRQHLRLVQALAKASgyRGMCGGQAQDL-NATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQ 203
Cdd:cd00867   78 ------LARLGYPRALELFAEAL--RELLEGQALDLeFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 204 ALLEYADAVGLAFQVQDDILDITGSTEELGKPqGSDLDANKSTYPKLLGLEGAKTTAQKLLEDALSALAKLPYNSQLIAE 283
Cdd:cd00867  150 ALKDYGRALGLAFQLTDDLLDVFGDAEELGKV-GSDLREGRITLPVILARERAAEYAEEAYAALEALPPSLPRARRALIA 228

                 ....*...
gi 743518677 284 FARYIVER 291
Cdd:cd00867  229 LADFLYRR 236
preA CHL00151
prenyl transferase; Reviewed
13-291 4.95e-45

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 154.95  E-value: 4.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  13 VNQRIATILDTLDDTEPR----LKAAMRHGALLGGKRIRPFLVYSVGEMLG------VPLERLddcAAAIECIHAYSLIH 82
Cdd:CHL00151  11 IEEELLILEDNLKKLIGSghpiLYAAAKHLFSAGGKRIRPAIVLLVAKATGgnmeikTSQQRL---AEITEIIHTASLVH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  83 DDLpaMDDDALRRGQPTVHIAFNEATAILAGDALQTLAFELissdiegLSDRQHLRLVQALAK-----ASGYrgmcggQA 157
Cdd:CHL00151  88 DDV--IDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWY-------LANLNNLEVVKLISKvitdfAEGE------IR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 158 QDLNATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQG 237
Cdd:CHL00151 153 QGLVQFDTTLSILNYIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 238 SDLDANKSTYPKLLGL---------------------------------EGAKTTAQKLLEDALSALAKLPYNSQLIA-- 282
Cdd:CHL00151 233 SDLKNGNLTAPVLFALtqnsklaklierefcetkdisqalqiiketngiEKAKDLALEHMQAAIQCLKFLPPSSAKDSli 312

                 ....*....
gi 743518677 283 EFARYIVER 291
Cdd:CHL00151 313 EIANFIINR 321
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
46-290 5.11e-31

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: 116.06  E-value: 5.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  46 IRPFLVYsvgemlgvPLERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIA---FNEATAILAGDALQTLAFE 122
Cdd:cd00385    1 FRPLAVL--------LEPEASRLRAAVEKLHAASLVHDDI--VDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 123 LissdiegLSDRQHLRLVQALAKAsgYRGMCGGQAQDL-NATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKE 201
Cdd:cd00385   71 E-------LAREGSPEALEILAEA--LLDLLEGQLLDLkWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAEL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 202 EQALLEYADAVGLAFQVQDDILDITGSTEELgkpqgsdldANKSTYPKLL------------------GLEGAKTTAQKL 263
Cdd:cd00385  142 LEALRKLGRALGLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYaleygvpaedlllveksgSLEEALEELAKL 212
                        250       260       270
                 ....*....|....*....|....*....|.
gi 743518677 264 LEDALSALAKL----PYNSQLIAEFARYIVE 290
Cdd:cd00385  213 AEEALKELNELilslPDVPRALLALALNLYR 243
PLN02857 PLN02857
octaprenyl-diphosphate synthase
42-254 1.84e-30

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 118.41  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  42 GGKRIRPFLVYSVG----EMLGVP--LERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAFNEATAILAGDA 115
Cdd:PLN02857 134 GGKRMRPALVFLVSrataELAGLKelTTEHRRLAEITEMIHTASLIHDDV--LDESDMRRGKETVHQLYGTRVAVLAGDF 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 116 LqtlaFELISSDIEGLSDRQHLRLVQALAK--ASGYRGmcggQAQDLnaTDKEISLEQLTALHRLKTGALIRCAVEFAVI 193
Cdd:PLN02857 212 M----FAQSSWYLANLDNLEVIKLISQVIKdfASGEIK----QASSL--FDCDVTLDEYLLKSYYKTASLIAASTKSAAI 281
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743518677 194 AADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLE 254
Cdd:PLN02857 282 FSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALE 342
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
22-292 3.10e-29

heptaprenyl diphosphate synthase component II; Members of this family are component II of the heterodimeric heptaprenyl diphosphate synthase. The trusted cutoff was set such that all members identified are encoded near to a recognizable gene for component I (in pfam07307). This enzyme acts in menaquinone-7 isoprenoid side chain biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131795  Cd Length: 319  Bit Score: 113.27  E-value: 3.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677   22 DTLDDTEPRLKAAMRHGALLGGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVH 101
Cdd:TIGR02748  22 KAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDV--IDDADLRRGRPTIK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  102 IAFNEATAILAGDALQTLAFELISSdiegLSD-RQHLRLVQALAKasgyrgMCGGQAQDLNatDKeISLEQ--LTALHRL 178
Cdd:TIGR02748 100 SKWGNRIAMYTGDYLFAKSLETMTE----IKDpRAHQILSHTIVE------VCRGEIEQIK--DK-YNFDQnlRTYLRRI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  179 --KTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLE-- 254
Cdd:TIGR02748 167 krKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEdp 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743518677  255 ---------GAKTTAQKL-----------------------LEDALSALAKLPYNS--QLIAEFARYIVERR 292
Cdd:TIGR02748 247 flkkrieqvLEETTAEEMeplieevkksdaieyayavsdryLKKALELLDGLPDGRakKPLQEIAKYIGKRK 318
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
42-268 3.28e-28

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 110.70  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  42 GGKRIRPFLVYSVGEMLGVPLERLDDCAAAIECIHAYSLIHDDLpaMDDDALRRGQPTVHIAFNEATAILAGDALQTLAF 121
Cdd:PRK10888  43 GGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDV--VDESDMRRGKATANAAFGNAASVLVGDFIYTRAF 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 122 ELissdiegLSDRQHLRLVQALAKASGYRGMcGGQAQDLNATDKEISLEQLTALHRLKTGALIRCAVEFAVIAADIDAKE 201
Cdd:PRK10888 121 QM-------MTSLGSLKVLEVMSEAVNVIAE-GEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQ 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743518677 202 EQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPKLLGLEGAKTTAQKLLEDAL 268
Cdd:PRK10888 193 EKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHGTPEQAAMIRTAI 259
PLN02890 PLN02890
geranyl diphosphate synthase
29-254 1.98e-14

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 73.04  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  29 PRLKAAMRHGALLG--GKRIRPFLVYSVGEMLGVPLE-----------------RLDDCAAAIECIHAYSLIHDDLpaMD 89
Cdd:PLN02890 108 PKLASAAEYFFKVGveGKRFRPTVLLLMATALNVPLPesteggvldivaselrtRQQNIAEITEMIHVASLLHDDV--LD 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677  90 DDALRRGQPTVHIAFNEATAILAGDALqtlafelISSDIEGLSDRQHLRLVQALAKASGYRgMCGGQAQDLNATDKEISL 169
Cdd:PLN02890 186 DADTRRGVGSLNVVMGNKLSVLAGDFL-------LSRACVALAALKNTEVVSLLATAVEHL-VTGETMQITSSREQRRSM 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743518677 170 EQLTALHRLKTGALIRCAVEFAVIAADIDAKEEQALLEYADAVGLAFQVQDDILDITGSTEELGKPQGSDLDANKSTYPK 249
Cdd:PLN02890 258 DYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPI 337

                 ....*
gi 743518677 250 LLGLE 254
Cdd:PLN02890 338 LFAME 342
 
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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