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Conserved domains on  [gi|182891376|gb|AAI64398|]
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Fdps protein [Danio rerio]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
48-309 2.62e-104

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 306.74  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376   48 LREVLQYNA-PGGKRNRGLSVIGSLRELVSPselptEEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKea 126
Cdd:pfam00348   4 LYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  127 IGLD-AINDAFLLEGSIYRLLRRHCRgqpyYVHLLELFTETSFQTELGQALDLMTAppHKIDLNRfTMERYKAIVKYKTA 205
Cdd:pfam00348  77 FGNAiAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC-TEEEYLEIVKYKTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  206 fYSFYLPVAAAMYMAGIENEIeHHNAKTILLEMGEFFQIQDDYLDCFGDPAVTGKI-GTDIQDNKCSWLVVTALGiMTPE 284
Cdd:pfam00348 150 -YLFALAVKLGAILSGADDEV-IEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALE-RTPE 226
                         250       260
                  ....*....|....*....|....*
gi 182891376  285 QRAELEACYGRsDAESVERVKALYD 309
Cdd:pfam00348 227 QRKILLEIYGK-RPEDVEKVKEAYE 250
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
48-309 2.62e-104

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 306.74  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376   48 LREVLQYNA-PGGKRNRGLSVIGSLRELVSPselptEEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKea 126
Cdd:pfam00348   4 LYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  127 IGLD-AINDAFLLEGSIYRLLRRHCRgqpyYVHLLELFTETSFQTELGQALDLMTAppHKIDLNRfTMERYKAIVKYKTA 205
Cdd:pfam00348  77 FGNAiAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC-TEEEYLEIVKYKTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  206 fYSFYLPVAAAMYMAGIENEIeHHNAKTILLEMGEFFQIQDDYLDCFGDPAVTGKI-GTDIQDNKCSWLVVTALGiMTPE 284
Cdd:pfam00348 150 -YLFALAVKLGAILSGADDEV-IEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALE-RTPE 226
                         250       260
                  ....*....|....*....|....*
gi 182891376  285 QRAELEACYGRsDAESVERVKALYD 309
Cdd:pfam00348 227 QRKILLEIYGK-RPEDVEKVKEAYE 250
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
47-354 1.79e-79

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: 243.61  E-value: 1.79e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  47 RLREVLQYN-APGGKRNRGLSVIGSLRELVSPselpteEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKE 125
Cdd:cd00685    5 LLREALRYLlLAGGKRLRPLLVLLAARALGGP------ELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 126 AIGLdAINDAFLLEGSIYRLLRRHCRgqPYYVHLLELFTETSFQTELGQALDLMTApphkiDLNRFTMERYKAIVKYKTA 205
Cdd:cd00685   79 GNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSE-----YDTDVTEEEYLRIIRLKTA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 206 FYSFYLPVAAAMYMAGIENEIEHhnAKTILLEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCSWLVVTALgimtpE 284
Cdd:cd00685  151 ALFAAAPLLGALLAGADEEEAEA--LKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL-----R 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 285 QRAeleacygrsdaesvervkalydtlempmryHQHEEESYHRLQKLIQlhakNLPHAVFLNFAKKIYKR 354
Cdd:cd00685  224 ELA------------------------------REYEEKALEALKALPE----SPAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
47-333 3.08e-33

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: 125.72  E-value: 3.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  47 RLREVLQY-NAPGGKRNRGLSVIGSLReLVSPSelpTEEVHRALLVgwcIELLQAFFLVADDIMDSSVTRRGQP-CWYK- 123
Cdd:COG0142   32 LLAEAMRYlLLAGGKRLRPLLVLLAAR-ALGGD---PEAALRAAAA---VELIHTASLVHDDVMDDDDLRRGKPtVHARf 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 124 KEAIgldAIN--DAFLLEGsiYRLLRRHCRGQpYYVHLLELFTETSFQTELGQALDLMTAppHKIDLnrfTMERYKAIVK 201
Cdd:COG0142  105 GEAT---AILagDALLALA--FELLAELGDPE-RRLRALRILARAARGMCEGQALDLEAE--GRLDV---TLEEYLRVIR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 202 YKTAFYsfylpVAAAMYMAGI-----ENEIEHhnAKTILLEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCSWLVV 275
Cdd:COG0142  174 LKTAAL-----FAAALRLGAIlagadEEQVEA--LRRYGRNLGLAFQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLL 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 276 TALGIMTPEQRAELEACYGR--SDAESVERVKALydtlempMRYHQHEEESYHRLQKLIQ 333
Cdd:COG0142  247 LALERADPEERAELRELLGKpdLDEEDLAEVRAL-------LRESGALEYARELARELAE 299
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
48-272 2.29e-03

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 39.37  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  48 LREVLQYNAP-GGKRNRGLSVIGSLREL-VSPSELPTEEVhrallvgwCIELLQAFFLVADDI--MDSSVTRRGQPCWYK 123
Cdd:PRK10581  32 VVEAMQYGALlGGKRLRPFLVYATGQMFgVSTNTLDAPAA--------AVECIHAYSLIHDDLpaMDDDDLRRGLPTCHV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 124 K--EAIGLDAiNDAflLEGSIYRLLRRHCRGQPYYVHLLELFTETSFQTEL-----GQALDLmTAPPHKIDLNrfTMERy 196
Cdd:PRK10581 104 KfgEANAILA-GDA--LQTLAFSILSDAPMPEVSDRDRISMISELASASGIagmcgGQALDL-EAEGKQVPLD--ALER- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 197 kaIVKYKTAFYsfylpVAAAMYMAGIENEIEHHNAKTIL----LEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCS 271
Cdd:PRK10581 177 --IHRHKTGAL-----IRAAVRLGALSAGDKGRRALPVLdryaESIGLAFQVQDDILDVVGDTATLGKrQGADQQLGKST 249

                 .
gi 182891376 272 W 272
Cdd:PRK10581 250 Y 250
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
48-309 2.62e-104

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 306.74  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376   48 LREVLQYNA-PGGKRNRGLSVIGSLRELVSPselptEEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKea 126
Cdd:pfam00348   4 LYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  127 IGLD-AINDAFLLEGSIYRLLRRHCRgqpyYVHLLELFTETSFQTELGQALDLMTAppHKIDLNRfTMERYKAIVKYKTA 205
Cdd:pfam00348  77 FGNAiAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWR--NDDDLSC-TEEEYLEIVKYKTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  206 fYSFYLPVAAAMYMAGIENEIeHHNAKTILLEMGEFFQIQDDYLDCFGDPAVTGKI-GTDIQDNKCSWLVVTALGiMTPE 284
Cdd:pfam00348 150 -YLFALAVKLGAILSGADDEV-IEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALE-RTPE 226
                         250       260
                  ....*....|....*....|....*
gi 182891376  285 QRAELEACYGRsDAESVERVKALYD 309
Cdd:pfam00348 227 QRKILLEIYGK-RPEDVEKVKEAYE 250
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
47-354 1.79e-79

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: 243.61  E-value: 1.79e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  47 RLREVLQYN-APGGKRNRGLSVIGSLRELVSPselpteEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKE 125
Cdd:cd00685    5 LLREALRYLlLAGGKRLRPLLVLLAARALGGP------ELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 126 AIGLdAINDAFLLEGSIYRLLRRHCRgqPYYVHLLELFTETSFQTELGQALDLMTApphkiDLNRFTMERYKAIVKYKTA 205
Cdd:cd00685   79 GNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSE-----YDTDVTEEEYLRIIRLKTA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 206 FYSFYLPVAAAMYMAGIENEIEHhnAKTILLEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCSWLVVTALgimtpE 284
Cdd:cd00685  151 ALFAAAPLLGALLAGADEEEAEA--LKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL-----R 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 285 QRAeleacygrsdaesvervkalydtlempmryHQHEEESYHRLQKLIQlhakNLPHAVFLNFAKKIYKR 354
Cdd:cd00685  224 ELA------------------------------REYEEKALEALKALPE----SPAREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
78-354 4.11e-56

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: 4.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  78 SELPTEEVHRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKEAIGLDAINDAFLLEGSIYRLLRRHCrgqpyYV 157
Cdd:cd00867   10 ARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLLARAFQLLARLG-----YP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 158 HLLELFTETSFQTELGQALDLMTApphkiDLNRFTMERYKAIVKYKTAFYSFYLPVAAAMYMAGIENEIEHhnAKTILLE 237
Cdd:cd00867   85 RALELFAEALRELLEGQALDLEFE-----RDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEA--LKDYGRA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 238 MGEFFQIQDDYLDCFGDPAVTGKIGTDIQDNKCSWLVVTALGimtpeqraeleacygrsdaesvervkalydtlempmRY 317
Cdd:cd00867  158 LGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARE------------------------------------RA 201
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 182891376 318 HQHEEESYHRLQKLIQlhAKNLPHAVFLNFAKKIYKR 354
Cdd:cd00867  202 AEYAEEAYAALEALPP--SLPRARRALIALADFLYRR 236
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
86-353 1.83e-34

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: 126.84  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  86 HRALLVGWCIELLQAFFLVADDIMDSSVTRRGQPCWYKKEAIGL--DAINDAFLLEGSIYRLLRRHCRgqpyyVHLLELF 163
Cdd:cd00385   10 PEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGlpEAILAGDLLLADAFEELAREGS-----PEALEIL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 164 TETSFQTELGQALDLMTAPPHKidlnrFTMERYKAIVKYKTAFYSFYLPVAAAMYMAGIENEIEHhnAKTILLEMGEFFQ 243
Cdd:cd00385   85 AEALLDLLEGQLLDLKWRREYV-----PTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEA--LRKLGRALGLAFQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 244 IQDDYLDCFGDPAVTgkigtdiqDNKCSWLVVTAlgimtpeqraeLEACYGRSDAESVERVKALYDTLEmpmRYHQHEEE 323
Cdd:cd00385  158 LTNDLLDYEGDAERG--------EGKCTLPVLYA-----------LEYGVPAEDLLLVEKSGSLEEALE---ELAKLAEE 215
                        250       260       270
                 ....*....|....*....|....*....|
gi 182891376 324 SYHRLQKLIQlhAKNLPHAVFLNFAKKIYK 353
Cdd:cd00385  216 ALKELNELIL--SLPDVPRALLALALNLYR 243
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
47-333 3.08e-33

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: 125.72  E-value: 3.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  47 RLREVLQY-NAPGGKRNRGLSVIGSLReLVSPSelpTEEVHRALLVgwcIELLQAFFLVADDIMDSSVTRRGQP-CWYK- 123
Cdd:COG0142   32 LLAEAMRYlLLAGGKRLRPLLVLLAAR-ALGGD---PEAALRAAAA---VELIHTASLVHDDVMDDDDLRRGKPtVHARf 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 124 KEAIgldAIN--DAFLLEGsiYRLLRRHCRGQpYYVHLLELFTETSFQTELGQALDLMTAppHKIDLnrfTMERYKAIVK 201
Cdd:COG0142  105 GEAT---AILagDALLALA--FELLAELGDPE-RRLRALRILARAARGMCEGQALDLEAE--GRLDV---TLEEYLRVIR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 202 YKTAFYsfylpVAAAMYMAGI-----ENEIEHhnAKTILLEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCSWLVV 275
Cdd:COG0142  174 LKTAAL-----FAAALRLGAIlagadEEQVEA--LRRYGRNLGLAFQIRDDILDVTGDPEVLGKpAGSDLREGKPTLPLL 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 276 TALGIMTPEQRAELEACYGR--SDAESVERVKALydtlempMRYHQHEEESYHRLQKLIQ 333
Cdd:COG0142  247 LALERADPEERAELRELLGKpdLDEEDLAEVRAL-------LRESGALEYARELARELAE 299
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
48-272 2.29e-03

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 39.37  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376  48 LREVLQYNAP-GGKRNRGLSVIGSLREL-VSPSELPTEEVhrallvgwCIELLQAFFLVADDI--MDSSVTRRGQPCWYK 123
Cdd:PRK10581  32 VVEAMQYGALlGGKRLRPFLVYATGQMFgVSTNTLDAPAA--------AVECIHAYSLIHDDLpaMDDDDLRRGLPTCHV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 124 K--EAIGLDAiNDAflLEGSIYRLLRRHCRGQPYYVHLLELFTETSFQTEL-----GQALDLmTAPPHKIDLNrfTMERy 196
Cdd:PRK10581 104 KfgEANAILA-GDA--LQTLAFSILSDAPMPEVSDRDRISMISELASASGIagmcgGQALDL-EAEGKQVPLD--ALER- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891376 197 kaIVKYKTAFYsfylpVAAAMYMAGIENEIEHHNAKTIL----LEMGEFFQIQDDYLDCFGDPAVTGK-IGTDIQDNKCS 271
Cdd:PRK10581 177 --IHRHKTGAL-----IRAAVRLGALSAGDKGRRALPVLdryaESIGLAFQVQDDILDVVGDTATLGKrQGADQQLGKST 249

                 .
gi 182891376 272 W 272
Cdd:PRK10581 250 Y 250
 
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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