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Conserved domains on  [gi|767959964|ref|XP_011517739|]
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all trans-polyprenyl-diphosphate synthase PDSS1 isoform X3 [Homo sapiens]

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 ...
2-290 2.50e-91

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 TIGR02749:

Pssm-ID: 469660  Cd Length: 322  Bit Score: 273.93  E-value: 2.50e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964    2 SEYYFDGKGKAFRPIIVALMARACNihhnNSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKA 81
Cdd:TIGR02749  36 AEHLFSAGGKRLRPAIVLLVSRATA----EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   82 VLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCP 161
Cdd:TIGR02749 112 VLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLNQFDSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  162 DPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRAR 241
Cdd:TIGR02749 192 PSQVANDLYEYGKHLGLAFQVVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQAL 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767959964  242 QYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:TIGR02749 272 SLVRKSGGIKKARELAKEQAQLALQSLSFLPPSPPREALKELVHFVLSR 320
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
2-290 2.50e-91

solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or plastid-containing eukaryotes. A member from Arabidopsis (where both plastoquinone and ubiquinone contain the C(45) prenyl moiety) was characterized by heterologous expression as a solanesyl diphosphate synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131796  Cd Length: 322  Bit Score: 273.93  E-value: 2.50e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964    2 SEYYFDGKGKAFRPIIVALMARACNihhnNSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKA 81
Cdd:TIGR02749  36 AEHLFSAGGKRLRPAIVLLVSRATA----EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   82 VLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCP 161
Cdd:TIGR02749 112 VLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLNQFDSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  162 DPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRAR 241
Cdd:TIGR02749 192 PSQVANDLYEYGKHLGLAFQVVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQAL 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767959964  242 QYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:TIGR02749 272 SLVRKSGGIKKARELAKEQAQLALQSLSFLPPSPPREALKELVHFVLSR 320
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
1-290 6.97e-89

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: 265.18  E-value: 6.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   1 MSEYYFDGKGKAFRPIIVALMARACnihhnnSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:cd00685    9 ALRYLLLAGGKRLRPLLVLLAARAL------GGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGNAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  81 AVLAGDLILSAASIALARIGNTT---VISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSV 157
Cdd:cd00685   83 AILAGDYLLARAFELLARLGNPYyprALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLGAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 158 LGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQfpemnamimrrfslpgdv 237
Cdd:cd00685  163 LAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE------------------ 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767959964 238 drarqyvlqsdgvqqttyLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:cd00685  225 ------------------LAREYEEKALEALKALPESPAREALRALADFILER 259
PLN02890 PLN02890
geranyl diphosphate synthase
2-292 8.36e-89

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 270.64  E-value: 8.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   2 SEYYFD--GKGKAFRPIIVALMARACNIHHNNS----------RHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGK 69
Cdd:PLN02890 114 AEYFFKvgVEGKRFRPTVLLLMATALNVPLPESteggvldivaSELRTRQQNIAEITEMIHVASLLHDDVLDDADTRRGV 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  70 HTVNKIWGEKKAVLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIA 149
Cdd:PLN02890 194 GSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLIS 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 150 NSCKAVSVLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMR 229
Cdd:PLN02890 274 NSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDR 353
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767959964 230 RFSLPGDVDRARQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERD------ALIQLSEIVLTRDK 292
Cdd:PLN02890 354 GFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETDDEDvltsrrALIDLTERVITRNK 422
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-292 1.35e-83

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: 254.38  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   1 MSEYYFDGKGKAFRPIIVALMARACNIhhNNSRHVQAsqrAIALiaEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:COG0142   36 AMRYLLLAGGKRLRPLLVLLAARALGG--DPEAALRA---AAAV--ELIHTASLVHDDVMDDDDLRRGKPTVHARFGEAT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  81 AVLAGDLILSAASIALARIGN----TTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVS 156
Cdd:COG0142  109 AILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRLDVTLEEYLRVIRLKTAALFAAALRLGA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 157 VLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQ-----QFPEMNAMIMRRF 231
Cdd:COG0142  189 ILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALEradpeERAELRELLGKPD 268
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767959964 232 SLPGDVDRARQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTRDK 292
Cdd:COG0142  269 LDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVERDR 329
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-243 2.11e-82

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 248.58  E-value: 2.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964    1 MSEYYFDGKGKAFRPIIVALMARACNIHHNNSRHvqasqRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:pfam00348   7 PLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEKA-----IVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   81 AVLAGDLILSAASIALARI-GNTTVISILTQVIEDLVRGEFLQLGSKENENER--FAHYLEKTFKKTASLIANSCKAVSV 157
Cdd:pfam00348  82 AINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFALAVKLGAI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  158 LGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPE----MNAMIMRRFSL 233
Cdd:pfam00348 162 LSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEIYGKRPED 241
                         250
                  ....*....|
gi 767959964  234 PGDVDRARQY 243
Cdd:pfam00348 242 VEKVKEAYEL 251
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
2-290 2.50e-91

solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or plastid-containing eukaryotes. A member from Arabidopsis (where both plastoquinone and ubiquinone contain the C(45) prenyl moiety) was characterized by heterologous expression as a solanesyl diphosphate synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131796  Cd Length: 322  Bit Score: 273.93  E-value: 2.50e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964    2 SEYYFDGKGKAFRPIIVALMARACNihhnNSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKA 81
Cdd:TIGR02749  36 AEHLFSAGGKRLRPAIVLLVSRATA----EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   82 VLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCP 161
Cdd:TIGR02749 112 VLAGDFLFAQASWYLANLENLEVVKLISKVITDFAEGEIKQGLNQFDSDLSLEDYLEKSFYKTASLVAASSKAAAVLSDV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  162 DPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRAR 241
Cdd:TIGR02749 192 PSQVANDLYEYGKHLGLAFQVVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQAL 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767959964  242 QYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:TIGR02749 272 SLVRKSGGIKKARELAKEQAQLALQSLSFLPPSPPREALKELVHFVLSR 320
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
1-290 6.97e-89

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: 265.18  E-value: 6.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   1 MSEYYFDGKGKAFRPIIVALMARACnihhnnSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:cd00685    9 ALRYLLLAGGKRLRPLLVLLAARAL------GGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGNAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  81 AVLAGDLILSAASIALARIGNTT---VISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSV 157
Cdd:cd00685   83 AILAGDYLLARAFELLARLGNPYyprALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLGAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 158 LGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQfpemnamimrrfslpgdv 237
Cdd:cd00685  163 LAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE------------------ 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767959964 238 drarqyvlqsdgvqqttyLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:cd00685  225 ------------------LAREYEEKALEALKALPESPAREALRALADFILER 259
PLN02890 PLN02890
geranyl diphosphate synthase
2-292 8.36e-89

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 270.64  E-value: 8.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   2 SEYYFD--GKGKAFRPIIVALMARACNIHHNNS----------RHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGK 69
Cdd:PLN02890 114 AEYFFKvgVEGKRFRPTVLLLMATALNVPLPESteggvldivaSELRTRQQNIAEITEMIHVASLLHDDVLDDADTRRGV 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  70 HTVNKIWGEKKAVLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIA 149
Cdd:PLN02890 194 GSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLIS 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 150 NSCKAVSVLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMR 229
Cdd:PLN02890 274 NSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDR 353
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767959964 230 RFSLPGDVDRARQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERD------ALIQLSEIVLTRDK 292
Cdd:PLN02890 354 GFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETDDEDvltsrrALIDLTERVITRNK 422
preA CHL00151
prenyl transferase; Reviewed
2-290 4.83e-85

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 257.80  E-value: 4.83e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   2 SEYYFDGKGKAFRPIIVALMARACNihhnNSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKA 81
Cdd:CHL00151  37 AKHLFSAGGKRIRPAIVLLVAKATG----GNMEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  82 VLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCP 161
Cdd:CHL00151 113 VLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTASLIAASCKAAALLSDA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 162 DPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRAR 241
Cdd:CHL00151 193 DEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCETKDISQAL 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767959964 242 QYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:CHL00151 273 QIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINR 321
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-292 1.35e-83

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: 254.38  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   1 MSEYYFDGKGKAFRPIIVALMARACNIhhNNSRHVQAsqrAIALiaEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:COG0142   36 AMRYLLLAGGKRLRPLLVLLAARALGG--DPEAALRA---AAAV--ELIHTASLVHDDVMDDDDLRRGKPTVHARFGEAT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  81 AVLAGDLILSAASIALARIGN----TTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVS 156
Cdd:COG0142  109 AILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRLDVTLEEYLRVIRLKTAALFAAALRLGA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 157 VLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQ-----QFPEMNAMIMRRF 231
Cdd:COG0142  189 ILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALEradpeERAELRELLGKPD 268
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767959964 232 SLPGDVDRARQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTRDK 292
Cdd:COG0142  269 LDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVERDR 329
polyprenyl_synt pfam00348
Polyprenyl synthetase;
1-243 2.11e-82

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 248.58  E-value: 2.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964    1 MSEYYFDGKGKAFRPIIVALMARACNIHHNNSRHvqasqRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:pfam00348   7 PLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEKA-----IVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   81 AVLAGDLILSAASIALARI-GNTTVISILTQVIEDLVRGEFLQLGSKENENER--FAHYLEKTFKKTASLIANSCKAVSV 157
Cdd:pfam00348  82 AINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFALAVKLGAI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  158 LGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPE----MNAMIMRRFSL 233
Cdd:pfam00348 162 LSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEIYGKRPED 241
                         250
                  ....*....|
gi 767959964  234 PGDVDRARQY 243
Cdd:pfam00348 242 VEKVKEAYEL 251
PLN02857 PLN02857
octaprenyl-diphosphate synthase
2-290 3.62e-77

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 240.90  E-value: 3.62e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   2 SEYYFDGKGKAFRPIIVALMARA-CNIHHNNSRHVQasQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKK 80
Cdd:PLN02857 127 AEQIFGAGGKRMRPALVFLVSRAtAELAGLKELTTE--HRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRV 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  81 AVLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGC 160
Cdd:PLN02857 205 AVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSG 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 161 PDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRA 240
Cdd:PLN02857 285 VDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEA 364
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767959964 241 RQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTR 290
Cdd:PLN02857 365 IELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDMVDYNLER 414
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
13-290 6.61e-61

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: 193.33  E-value: 6.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  13 FRPIIVALMARACNIHHNnsrhvqaSQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKI-WGEKKAVLAGDLILSA 91
Cdd:cd00867    1 SRPLLVLLLARALGGDLE-------AALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  92 ASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDPVVHEIAYQ 171
Cdd:cd00867   74 AFQLLARLGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 172 YGKNVGIAFQLIDDVLDFTSCSDQMGKPTSaDLKLGLATGPVLFACQqfpemnamimrrfslpgdvdrarqyvlqsdgvq 251
Cdd:cd00867  154 YGRALGLAFQLTDDLLDVFGDAEELGKVGS-DLREGRITLPVILARE--------------------------------- 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767959964 252 qttyLAQQYCHEAIREISKLRPSP--ERDALIQLSEIVLTR 290
Cdd:cd00867  200 ----RAAEYAEEAYAALEALPPSLprARRALIALADFLYRR 236
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
4-291 2.53e-45

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 155.77  E-value: 2.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964   4 YYFDGKGKAFRPIIVALMARAcnIHHNNSRHVqasqrAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKAVL 83
Cdd:PRK10888  38 YIISGGGKRIRPMIAVLAARA--VGYQGNAHV-----TIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  84 AGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDP 163
Cdd:PRK10888 111 VGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTP 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 164 vVHEIAYQ-YGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQ-FPEMNAMImRRFSLPGDVDRAR 241
Cdd:PRK10888 191 -EQEKGLQdYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHgTPEQAAMI-RTAIEQGNGRHLL 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767959964 242 QYVL----QSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTRD 291
Cdd:PRK10888 269 EPVLeamnACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRD 322
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
13-288 1.54e-44

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: 151.49  E-value: 1.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  13 FRPIIVALMARACnihhnnsrhvqasqrAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNK---IWGEKKAVLAGDLIL 89
Cdd:cd00385    1 FRPLAVLLEPEAS---------------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLavaIDGLPEAILAGDLLL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  90 SAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDPVVHEIA 169
Cdd:cd00385   66 ADAFEELAREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEAL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964 170 YQYGKNVGIAFQLIDDVLDFTScsdqmgkptSADLKLGLATGPVLFACQQfpemnamimrrfslpGDVDRARQYVLQSDG 249
Cdd:cd00385  146 RKLGRALGLAFQLTNDLLDYEG---------DAERGEGKCTLPVLYALEY---------------GVPAEDLLLVEKSGS 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767959964 250 VQQTTYLAQQYCHEAIREISKL--RPSPERDALIQLSEIVL 288
Cdd:cd00385  202 LEEALEELAKLAEEALKELNELilSLPDVPRALLALALNLY 242
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
10-219 1.53e-11

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 63.64  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  10 GKAFRPIIVALMARACNIHhnnsrhvQASQRAIALIAEMIHTASLVHDDV--IDDASSRRGKHTVNKIWGEKKAVLAGDL 87
Cdd:PRK10581  44 GKRLRPFLVYATGQMFGVS-------TNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959964  88 -------ILSAASIA-LARIGNTTVISILTQV--IEDLVRGEFLQLGSKENENERFAhyLEKTFK-KTASLIANSCKaVS 156
Cdd:PRK10581 117 lqtlafsILSDAPMPeVSDRDRISMISELASAsgIAGMCGGQALDLEAEGKQVPLDA--LERIHRhKTGALIRAAVR-LG 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959964 157 VLGCPDPVVHEIAY--QYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQ 219
Cdd:PRK10581 194 ALSAGDKGRRALPVldRYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQ 258
 
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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