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Conserved domains on  [gi|19112068|ref|NP_595276|]
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decaprenyl diphosphate synthase subunit Dps1 [Schizosaccharomyces pombe]

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 ...
28-376 1.68e-94

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: 285.10  E-value: 1.68e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068    28 TTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddl 107
Cdd:TIGR02749   1 ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATA-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   108 rsfSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTEL 187
Cdd:TIGR02749  61 ---EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   188 LATVIADLVRGEFLQLKNTMDPSsleikqSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQ 267
Cdd:TIGR02749 138 ISKVITDFAEGEIKQGLNQFDSD------LSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   268 LMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYI 347
Cdd:TIGR02749 212 VVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQA 291
                         330       340
                  ....*....|....*....|....*....
gi 19112068   348 KKAKDSLLCLPDSPARKALFALADKVITR 376
Cdd:TIGR02749 292 QLALQSLSFLPPSPPREALKELVHFVLSR 320
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
28-376 1.68e-94

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: 285.10  E-value: 1.68e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068    28 TTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddl 107
Cdd:TIGR02749   1 ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATA-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   108 rsfSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTEL 187
Cdd:TIGR02749  61 ---EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   188 LATVIADLVRGEFLQLKNTMDPSsleikqSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQ 267
Cdd:TIGR02749 138 ISKVITDFAEGEIKQGLNQFDSD------LSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   268 LMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYI 347
Cdd:TIGR02749 212 VVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQA 291
                         330       340
                  ....*....|....*....|....*....
gi 19112068   348 KKAKDSLLCLPDSPARKALFALADKVITR 376
Cdd:TIGR02749 292 QLALQSLSFLPPSPPREALKELVHFVLSR 320
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
54-376 2.42e-88

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: 267.11  E-value: 2.42e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  54 SNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddlrsfstGQILPSQLRLAQITEMIHIAS 133
Cdd:cd00685   1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALG-------------------------GPELEAALRLAAAIELLHTAS 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 134 LLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQ---VTELLATVIADLVRGEFLQLKNTMDPs 210
Cdd:cd00685  56 LVHDDVMDNSDLRRGKPTVHKVFGNATAILAGDYLLARAFELLARLGNPYyprALELFSEAILELVEGQLLDLLSEYDT- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 211 sleikQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADL 290
Cdd:cd00685 135 -----DVTEEEYLRIIRLKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDL 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 291 KLGLATAPVLFAWKKYpelgamivnrfnhpsdiqrarslvectdaieqtitwAKEYIKKAKDSLLCLPDSPARKALFALA 370
Cdd:cd00685 210 REGKCTLPVLLALREL------------------------------------AREYEEKALEALKALPESPAREALRALA 253

                ....*.
gi 19112068 371 DKVITR 376
Cdd:cd00685 254 DFILER 259
preA CHL00151
prenyl transferase; Reviewed
29-376 1.01e-86

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 265.50  E-value: 1.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   29 TNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddlr 108
Cdd:CHL00151   3 TNSNLLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATG--------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  109 sfSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELL 188
Cdd:CHL00151  62 --GNMEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  189 ATVIADLVRGEFLQLKNTMDPSsLEIkqsnfDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQL 268
Cdd:CHL00151 140 SKVITDFAEGEIRQGLVQFDTT-LSI-----LNYIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQI 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  269 MDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIK 348
Cdd:CHL00151 214 IDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCETKDISQALQIIKETNGIEKAKDLALEHMQ 293
                        330       340
                 ....*....|....*....|....*...
gi 19112068  349 KAKDSLLCLPDSPARKALFALADKVITR 376
Cdd:CHL00151 294 AAIQCLKFLPPSSAKDSLIEIANFIINR 321
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
35-378 1.76e-86

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: 264.78  E-value: 1.76e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  35 HLIKNELEQISPGIRQMLN-SNSEFLEECSKYYTIAQGKQMRPSLVLLMSKAtslCHGidrsvvgdkyiDDDDLrsfstg 113
Cdd:COG0142   8 ALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARA---LGG-----------DPEAA------ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 114 qilpsqLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNP----QVTELLA 189
Cdd:COG0142  68 ------LRAAAAVELIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 190 TVIADLVRGEFLQLKNTMDPssleikQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLM 269
Cdd:COG0142 142 RAARGMCEGQALDLEAEGRL------DVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIR 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 270 DDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYP-----ELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAK 344
Cdd:COG0142 216 DDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADpeeraELRELLGKPDLDEEDLAEVRALLRESGALEYARELAR 295
                       330       340       350
                ....*....|....*....|....*....|....
gi 19112068 345 EYIKKAKDSLLCLPDSPARKALFALADKVITRKK 378
Cdd:COG0142 296 ELAEEALAALAALPDSEAREALRALADYVVERDR 329
polyprenyl_synt pfam00348
Polyprenyl synthetase;
57-329 5.25e-76

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 235.48  E-value: 5.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068    57 EFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRsvvgdkyiddddlrsfstgqilpsQLRLAQITEMIHIASLLH 136
Cdd:pfam00348   2 KLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEK------------------------AIVLAWAVELLHAASLVH 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   137 DDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARL-RNPQVTELLATVIADLVRGEFLQLKNTMDPSsleiK 215
Cdd:pfam00348  58 DDIMDNSDLRRGQPTWHRIFGNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDD----L 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   216 QSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLA 295
Cdd:pfam00348 134 SCTEEEYLEIVKYKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKC 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 19112068   296 TAPVLFAWKKYPE----LGAMIVNRFNHPSDIQRARSL 329
Cdd:pfam00348 214 TWPVIHALERTPEqrkiLLEIYGKRPEDVEKVKEAYEL 251
hexpp_archaea NF040936
hexaprenyl pyrophosphate synthase;
48-279 1.85e-09

hexaprenyl pyrophosphate synthase;


Pssm-ID: 468868  Cd Length: 275  Bit Score: 58.15  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   48 IRQMLNSNSEF-LEECSKYyTIAQGKQMRPSLVLLMSKATslchgidrsvvgdkyiddddlrsfstGQILPSQLRLAQIT 126
Cdd:NF040936  18 VEKFLNDVKDWeLLEMSKY-IMKDGKRFRGTLMFLFTEAL--------------------------GGEEKDAYKGALAT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  127 EMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARA----STAMARLRNPQVTELLATVIAdlvrgeflQ 202
Cdd:NF040936  71 EILHSASLALDDIVDYDLTRRGDKSAWAVYTNRRVIFVSNYLIPTAlniiSSYGEDALKISIELWKDTAVG--------A 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  203 LKNTMDPSSleikqsnfDYY--IEksfLKTASLIskscKASTILGqcsptvATAAG---------EYGRCIGTAFQLMDD 271
Cdd:NF040936 143 LKDMYGNKE--------DYFktIE---LKTASLF----KLSTMLA------SFSSRreelldellDAGKYLGIIYQLIDD 201

                 ....*...
gi 19112068  272 VLDYTSKD 279
Cdd:NF040936 202 YVDCVKYE 209
 
Name Accession Description Interval E-value
prenyl_cyano TIGR02749
solanesyl diphosphate synthase; Members of this family all are from cyanobacteria or ...
28-376 1.68e-94

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: 285.10  E-value: 1.68e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068    28 TTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddl 107
Cdd:TIGR02749   1 ASATSLFAPVEDDLYLLTDNLKSLVGARHPILYAAAEHLFSAGGKRLRPAIVLLVSRATA-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   108 rsfSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTEL 187
Cdd:TIGR02749  61 ---EQQELTPRHRRLAEITEMIHTASLVHDDVIDESDTRRGIETVHSLFGTRVAVLAGDFLFAQASWYLANLENLEVVKL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   188 LATVIADLVRGEFLQLKNTMDPSsleikqSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQ 267
Cdd:TIGR02749 138 ISKVITDFAEGEIKQGLNQFDSD------LSLEDYLEKSFYKTASLVAASSKAAAVLSDVPSQVANDLYEYGKHLGLAFQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   268 LMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYI 347
Cdd:TIGR02749 212 VVDDILDFTGSTEQLGKPAGSDLMKGNLTAPVLFALEEEPKLSELIEREFSQKGDLEQALSLVRKSGGIKKARELAKEQA 291
                         330       340
                  ....*....|....*....|....*....
gi 19112068   348 KKAKDSLLCLPDSPARKALFALADKVITR 376
Cdd:TIGR02749 292 QLALQSLSFLPPSPPREALKELVHFVLSR 320
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
54-376 2.42e-88

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: 267.11  E-value: 2.42e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  54 SNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddlrsfstGQILPSQLRLAQITEMIHIAS 133
Cdd:cd00685   1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALG-------------------------GPELEAALRLAAAIELLHTAS 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 134 LLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQ---VTELLATVIADLVRGEFLQLKNTMDPs 210
Cdd:cd00685  56 LVHDDVMDNSDLRRGKPTVHKVFGNATAILAGDYLLARAFELLARLGNPYyprALELFSEAILELVEGQLLDLLSEYDT- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 211 sleikQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADL 290
Cdd:cd00685 135 -----DVTEEEYLRIIRLKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDL 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 291 KLGLATAPVLFAWKKYpelgamivnrfnhpsdiqrarslvectdaieqtitwAKEYIKKAKDSLLCLPDSPARKALFALA 370
Cdd:cd00685 210 REGKCTLPVLLALREL------------------------------------AREYEEKALEALKALPESPAREALRALA 253

                ....*.
gi 19112068 371 DKVITR 376
Cdd:cd00685 254 DFILER 259
preA CHL00151
prenyl transferase; Reviewed
29-376 1.01e-86

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 265.50  E-value: 1.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   29 TNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSlchgidrsvvgdkyiddddlr 108
Cdd:CHL00151   3 TNSNLLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATG--------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  109 sfSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELL 188
Cdd:CHL00151  62 --GNMEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  189 ATVIADLVRGEFLQLKNTMDPSsLEIkqsnfDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQL 268
Cdd:CHL00151 140 SKVITDFAEGEIRQGLVQFDTT-LSI-----LNYIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQI 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  269 MDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIK 348
Cdd:CHL00151 214 IDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCETKDISQALQIIKETNGIEKAKDLALEHMQ 293
                        330       340
                 ....*....|....*....|....*...
gi 19112068  349 KAKDSLLCLPDSPARKALFALADKVITR 376
Cdd:CHL00151 294 AAIQCLKFLPPSSAKDSLIEIANFIINR 321
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
35-378 1.76e-86

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: 264.78  E-value: 1.76e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  35 HLIKNELEQISPGIRQMLN-SNSEFLEECSKYYTIAQGKQMRPSLVLLMSKAtslCHGidrsvvgdkyiDDDDLrsfstg 113
Cdd:COG0142   8 ALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARA---LGG-----------DPEAA------ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 114 qilpsqLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNP----QVTELLA 189
Cdd:COG0142  68 ------LRAAAAVELIHTASLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 190 TVIADLVRGEFLQLKNTMDPssleikQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLM 269
Cdd:COG0142 142 RAARGMCEGQALDLEAEGRL------DVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIR 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 270 DDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYP-----ELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAK 344
Cdd:COG0142 216 DDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADpeeraELRELLGKPDLDEEDLAEVRALLRESGALEYARELAR 295
                       330       340       350
                ....*....|....*....|....*....|....
gi 19112068 345 EYIKKAKDSLLCLPDSPARKALFALADKVITRKK 378
Cdd:COG0142 296 ELAEEALAALAALPDSEAREALRALADYVVERDR 329
PLN02890 PLN02890
geranyl diphosphate synthase
36-378 1.70e-78

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 247.53  E-value: 1.70e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   36 LIKNELEQISPGIRQMLNSNSEFLEECSKYY--TIAQGKQMRPSLVLLMSKATSLcHGIDRSVVGDKYIDDDDLRSfstg 113
Cdd:PLN02890  87 LVADELSLLANKLRSMVVAEVPKLASAAEYFfkVGVEGKRFRPTVLLLMATALNV-PLPESTEGGVLDIVASELRT---- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  114 qilpSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIA 193
Cdd:PLN02890 162 ----RQQNIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVE 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  194 DLVRGEflqlknTMDPSSLEIKQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVL 273
Cdd:PLN02890 238 HLVTGE------TMQITSSREQRRSMDYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVL 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  274 DYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDS 353
Cdd:PLN02890 312 DFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAA 391
                        330       340       350
                 ....*....|....*....|....*....|.
gi 19112068  354 LLCLPDS------PARKALFALADKVITRKK 378
Cdd:PLN02890 392 IESLPETddedvlTSRRALIDLTERVITRNK 422
polyprenyl_synt pfam00348
Polyprenyl synthetase;
57-329 5.25e-76

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 235.48  E-value: 5.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068    57 EFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRsvvgdkyiddddlrsfstgqilpsQLRLAQITEMIHIASLLH 136
Cdd:pfam00348   2 KLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEK------------------------AIVLAWAVELLHAASLVH 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   137 DDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARL-RNPQVTELLATVIADLVRGEFLQLKNTMDPSsleiK 215
Cdd:pfam00348  58 DDIMDNSDLRRGQPTWHRIFGNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDD----L 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   216 QSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLA 295
Cdd:pfam00348 134 SCTEEEYLEIVKYKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKC 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 19112068   296 TAPVLFAWKKYPE----LGAMIVNRFNHPSDIQRARSL 329
Cdd:pfam00348 214 TWPVIHALERTPEqrkiLLEIYGKRPEDVEKVKEAYEL 251
PLN02857 PLN02857
octaprenyl-diphosphate synthase
36-376 4.63e-75

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 238.59  E-value: 4.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   36 LIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDrsvvgdkyiddddlrsfstgQI 115
Cdd:PLN02857 100 PVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAELAGLK--------------------EL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  116 LPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADL 195
Cdd:PLN02857 160 TTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDF 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  196 VRGEFLQLKNTMDpssLEIKqsnFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDY 275
Cdd:PLN02857 240 ASGEIKQASSLFD---CDVT---LDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDF 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  276 TSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDSLL 355
Cdd:PLN02857 314 TQSTEQLGKPAGSDLAKGNLTAPVIFALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNLE 393
                        330       340
                 ....*....|....*....|.
gi 19112068  356 CLPDSPARKALFALADKVITR 376
Cdd:PLN02857 394 CLPRGAFRSSLEDMVDYNLER 414
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
112-376 3.20e-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: 186.40  E-value: 3.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 112 TGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSN-VAFGNRRSILAGNFILARASTAMARLRNPQVTELLAT 190
Cdd:cd00867  13 LGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHlRRFGNALAILAGDYLLARAFQLLARLGYPRALELFAE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 191 VIADLVRGEFLQLKNTMDPssleikQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMD 270
Cdd:cd00867  93 ALRELLEGQALDLEFERDT------YETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGLAFQLTD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 271 DVLDYTSKDDTLGKaAGADLKLGLATAPVLFAWKKypelgamivnrfnhpsdiqrarslvectdaieqtitwAKEYIKKA 350
Cdd:cd00867 167 DLLDVFGDAEELGK-VGSDLREGRITLPVILARER-------------------------------------AAEYAEEA 208
                       250       260
                ....*....|....*....|....*...
gi 19112068 351 KDSLLCLPDSP--ARKALFALADKVITR 376
Cdd:cd00867 209 YAALEALPPSLprARRALIALADFLYRR 236
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
36-376 8.50e-55

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 183.12  E-value: 8.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   36 LIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLchgidrsvVGDKYIddddlrsfstgqi 115
Cdd:PRK10888   9 LTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGY--------QGNAHV------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  116 lpsqlRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADL 195
Cdd:PRK10888  68 -----TIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  196 VRGEFLQLKNTMDPSSLEikqsnfDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDY 275
Cdd:PRK10888 143 AEGEVLQLMNVNDPDITE------ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDY 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  276 TSKDDTLGKAAGADLKLGLATAPVLFAWKK-YPELGAMI---VNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAK 351
Cdd:PRK10888 217 SADGETLGKNVGDDLNEGKPTLPLLHAMHHgTPEQAAMIrtaIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAI 296
                        330       340
                 ....*....|....*....|....*
gi 19112068  352 DSLLCLPDSPARKALFALADKVITR 376
Cdd:PRK10888 297 AALQVLPDTPWREALIGLAHIAVQR 321
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
116-374 6.47e-45

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: 154.96  E-value: 6.47e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 116 LPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVA---FGNRRSILAGNFILARASTAMARLRNPQVTELLATVI 192
Cdd:cd00385   9 EPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEELAREGSPEALEILAEAL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 193 ADLVRGEFLQLKNTMDPSSleikqsNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDV 272
Cdd:cd00385  89 LDLLEGQLLDLKWRREYVP------TLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRALGLAFQLTNDL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068 273 LDYTSKDDTLGkaagadlklGLATAPVLFAWKKYPELGAMIvnrfnhpsdiqrarsLVECTDAIEQTITWAKEYIKKAKD 352
Cdd:cd00385 163 LDYEGDAERGE---------GKCTLPVLYALEYGVPAEDLL---------------LVEKSGSLEEALEELAKLAEEALK 218
                       250       260
                ....*....|....*....|....
gi 19112068 353 SLLCLPDSP--ARKALFALADKVI 374
Cdd:cd00385 219 ELNELILSLpdVPRALLALALNLY 242
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
123-378 7.75e-18

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 82.90  E-value: 7.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  123 AQITEMIHIASLLHDDV--IDHANVRRGSPSSNVAFGNRRSILAGNF-------ILARASTAMARLRN--PQVTEL-LAT 190
Cdd:PRK10581  70 AAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDAlqtlafsILSDAPMPEVSDRDriSMISELaSAS 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  191 VIADLVRGEFLQLKntmdpssLEIKQSNFDYYIEKSFLKTASLIskscKASTILGqcsptvATAAGEYGR---------- 260
Cdd:PRK10581 150 GIAGMCGGQALDLE-------AEGKQVPLDALERIHRHKTGALI----RAAVRLG------ALSAGDKGRralpvldrya 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  261 -CIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLfawkkypeLGamivnrfnhpsdiqrarslvectdaIEQT 339
Cdd:PRK10581 213 eSIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPAL--------LG-------------------------LEQA 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 19112068  340 ITWAKEYIKKAKDSLLCLPDSPAR-KALFALADKVITRKK 378
Cdd:PRK10581 260 RKKARDLIDDARQSLDQLAAQSLDtSALEALANYIIQRDK 299
hexpp_archaea NF040936
hexaprenyl pyrophosphate synthase;
48-279 1.85e-09

hexaprenyl pyrophosphate synthase;


Pssm-ID: 468868  Cd Length: 275  Bit Score: 58.15  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068   48 IRQMLNSNSEF-LEECSKYyTIAQGKQMRPSLVLLMSKATslchgidrsvvgdkyiddddlrsfstGQILPSQLRLAQIT 126
Cdd:NF040936  18 VEKFLNDVKDWeLLEMSKY-IMKDGKRFRGTLMFLFTEAL--------------------------GGEEKDAYKGALAT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  127 EMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARA----STAMARLRNPQVTELLATVIAdlvrgeflQ 202
Cdd:NF040936  71 EILHSASLALDDIVDYDLTRRGDKSAWAVYTNRRVIFVSNYLIPTAlniiSSYGEDALKISIELWKDTAVG--------A 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112068  203 LKNTMDPSSleikqsnfDYY--IEksfLKTASLIskscKASTILGqcsptvATAAG---------EYGRCIGTAFQLMDD 271
Cdd:NF040936 143 LKDMYGNKE--------DYFktIE---LKTASLF----KLSTMLA------SFSSRreelldellDAGKYLGIIYQLIDD 201

                 ....*...
gi 19112068  272 VLDYTSKD 279
Cdd:NF040936 202 YVDCVKYE 209
 
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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