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Conserved domains on  [gi|665395515|ref|NP_001287619|]
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qless, isoform B [Drosophila melanogaster]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
138-387 5.86e-84

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 257.82  E-value: 5.86e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  138 QPELDTIASYYFDGQGKALRPMVTMLMAKAINyhlnneSHQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVN 217
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALG------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  218 ALWNHKKVTMAGDYILSIASIMIARLRSD-DVTIVLSQILTDLVQGEFMQLGSRETENER--FAHYLTKTYRKTASLIAN 294
Cdd:pfam00348  75 RIFGNAIAINDGDYLYALAFQLLAKLFPNpELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  295 ALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPE----LNPM 370
Cdd:pfam00348 155 AVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEI 234
                         250
                  ....*....|....*..
gi 665395515  371 VMRRFSEPGDVERAFEL 387
Cdd:pfam00348 235 YGKRPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
138-387 5.86e-84

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 257.82  E-value: 5.86e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  138 QPELDTIASYYFDGQGKALRPMVTMLMAKAINyhlnneSHQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVN 217
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALG------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  218 ALWNHKKVTMAGDYILSIASIMIARLRSD-DVTIVLSQILTDLVQGEFMQLGSRETENER--FAHYLTKTYRKTASLIAN 294
Cdd:pfam00348  75 RIFGNAIAINDGDYLYALAFQLLAKLFPNpELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  295 ALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPE----LNPM 370
Cdd:pfam00348 155 AVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEI 234
                         250
                  ....*....|....*..
gi 665395515  371 VMRRFSEPGDVERAFEL 387
Cdd:pfam00348 235 YGKRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
139-434 5.95e-83

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: 255.55  E-value: 5.95e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 139 PELDTIASYYFDGQGKALRPMVTMLMAKAINYhlnneshQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNA 218
Cdd:cd00685    4 ELLREALRYLLLAGGKRLRPLLVLLAARALGG-------PELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 219 LWNHKKVTMAGDYILSIASIMIARLRSD---DVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANA 295
Cdd:cd00685   77 VFGNATAILAGDYLLARAFELLARLGNPyypRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 296 LKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKypelnpmvmrrf 375
Cdd:cd00685  157 PLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE------------ 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665395515 376 sepgdverafelvhkshgleqtrfLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINR 434
Cdd:cd00685  225 ------------------------LAREYEEKALEALKALPESPAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
134-434 3.38e-82

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: 255.92  E-value: 3.38e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 134 SGTSQPELDTIASYYFDGQGKALRPMVTMLMAKAINYhlnnESHQLVHkqrqIALFSEMVHSASLVHDDVIDQSDFRRGK 213
Cdd:COG0142   26 ARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGG----DPEAALR----AAAAVELIHTASLVHDDVMDDDDLRRGK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 214 PSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTI----VLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTA 289
Cdd:COG0142   98 PTVHARFGEATAILAGDALLALAFELLAELGDPERRLralrILARAARGMCEGQALDLEAEGRLDVTLEEYLRVIRLKTA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 290 SLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYP---- 365
Cdd:COG0142  178 ALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADpeer 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 366 -ELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINR 434
Cdd:COG0142  258 aELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVER 327
PLN02890 PLN02890
geranyl diphosphate synthase
50-418 8.93e-82

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 257.93  E-value: 8.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  50 QQAMRLYHGLSFSMGKDYPDLLQSPHKCSQSLQYSQSSKANLRQHSSVHTQQPAGPVREfQIDPYIILDDDLKYFYDDVR 129
Cdd:PLN02890  22 GCSQSLASSRAALLGRHGHPLSQSTSKVVGCRGTYSVSSRWLHGFQYQVRHQSSSLVEE-QLDPFSLVADELSLLANKLR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 130 YLLKSGTsqPELDTIASYYFD--GQGKALRPMVTMLMAKAINYHLNNE---------SHQLVHKQRQIALFSEMVHSASL 198
Cdd:PLN02890 101 SMVVAEV--PKLASAAEYFFKvgVEGKRFRPTVLLLMATALNVPLPESteggvldivASELRTRQQNIAEITEMIHVASL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 199 VHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFA 278
Cdd:PLN02890 179 LHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 279 HYLTKTYRKTASLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVL 358
Cdd:PLN02890 259 YYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPIL 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 359 FACEKYPELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTES 418
Cdd:PLN02890 339 FAMEEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPET 398
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
153-436 3.76e-51

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


Pssm-ID: 131795  Cd Length: 319  Bit Score: 175.29  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  153 GKALRPMVTMLMAKAINYHLNneshqlvhKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYI 232
Cdd:TIGR02748  43 GKRIRPVFVLLAGKFGDYDLD--------AIKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  233 LSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEV 312
Cdd:TIGR02748 115 FAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTALLIAASCQLGAIASGANEAIVKK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  313 AFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEkypelNPMVMRRFSEPG------DVERAFE 386
Cdd:TIGR02748 195 LYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAME-----DPFLKKRIEQVLeettaeEMEPLIE 269
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 665395515  387 LVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVAdLVINRMK 436
Cdd:TIGR02748 270 EVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIA-KYIGKRK 318
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
138-387 5.86e-84

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 257.82  E-value: 5.86e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  138 QPELDTIASYYFDGQGKALRPMVTMLMAKAINyhlnneSHQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVN 217
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALG------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  218 ALWNHKKVTMAGDYILSIASIMIARLRSD-DVTIVLSQILTDLVQGEFMQLGSRETENER--FAHYLTKTYRKTASLIAN 294
Cdd:pfam00348  75 RIFGNAIAINDGDYLYALAFQLLAKLFPNpELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  295 ALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPE----LNPM 370
Cdd:pfam00348 155 AVKLGAILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALERTPEqrkiLLEI 234
                         250
                  ....*....|....*..
gi 665395515  371 VMRRFSEPGDVERAFEL 387
Cdd:pfam00348 235 YGKRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
139-434 5.95e-83

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: 255.55  E-value: 5.95e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 139 PELDTIASYYFDGQGKALRPMVTMLMAKAINYhlnneshQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNA 218
Cdd:cd00685    4 ELLREALRYLLLAGGKRLRPLLVLLAARALGG-------PELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 219 LWNHKKVTMAGDYILSIASIMIARLRSD---DVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANA 295
Cdd:cd00685   77 VFGNATAILAGDYLLARAFELLARLGNPyypRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 296 LKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKypelnpmvmrrf 375
Cdd:cd00685  157 PLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE------------ 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665395515 376 sepgdverafelvhkshgleqtrfLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINR 434
Cdd:cd00685  225 ------------------------LAREYEEKALEALKALPESPAREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
134-434 3.38e-82

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: 255.92  E-value: 3.38e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 134 SGTSQPELDTIASYYFDGQGKALRPMVTMLMAKAINYhlnnESHQLVHkqrqIALFSEMVHSASLVHDDVIDQSDFRRGK 213
Cdd:COG0142   26 ARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGG----DPEAALR----AAAAVELIHTASLVHDDVMDDDDLRRGK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 214 PSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTI----VLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTA 289
Cdd:COG0142   98 PTVHARFGEATAILAGDALLALAFELLAELGDPERRLralrILARAARGMCEGQALDLEAEGRLDVTLEEYLRVIRLKTA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 290 SLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYP---- 365
Cdd:COG0142  178 ALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPLLLALERADpeer 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 366 -ELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINR 434
Cdd:COG0142  258 aELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALADYVVER 327
PLN02890 PLN02890
geranyl diphosphate synthase
50-418 8.93e-82

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 257.93  E-value: 8.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  50 QQAMRLYHGLSFSMGKDYPDLLQSPHKCSQSLQYSQSSKANLRQHSSVHTQQPAGPVREfQIDPYIILDDDLKYFYDDVR 129
Cdd:PLN02890  22 GCSQSLASSRAALLGRHGHPLSQSTSKVVGCRGTYSVSSRWLHGFQYQVRHQSSSLVEE-QLDPFSLVADELSLLANKLR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 130 YLLKSGTsqPELDTIASYYFD--GQGKALRPMVTMLMAKAINYHLNNE---------SHQLVHKQRQIALFSEMVHSASL 198
Cdd:PLN02890 101 SMVVAEV--PKLASAAEYFFKvgVEGKRFRPTVLLLMATALNVPLPESteggvldivASELRTRQQNIAEITEMIHVASL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 199 VHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFA 278
Cdd:PLN02890 179 LHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 279 HYLTKTYRKTASLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVL 358
Cdd:PLN02890 259 YYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPIL 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 359 FACEKYPELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTES 418
Cdd:PLN02890 339 FAMEEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPET 398
preA CHL00151
prenyl transferase; Reviewed
135-436 5.90e-79

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 247.40  E-value: 5.90e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 135 GTSQPELDTIASYYFDGQGKALRPMVTMLMAKAINyhlnnESHQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKP 214
Cdd:CHL00151  27 GSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATG-----GNMEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRRGIP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 215 SVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIAN 294
Cdd:CHL00151 102 TVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTASLIAA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 295 ALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPELNPMVMRR 374
Cdd:CHL00151 182 SCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIERE 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665395515 375 FSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINRMK 436
Cdd:CHL00151 262 FCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
PLN02857 PLN02857
octaprenyl-diphosphate synthase
119-435 6.84e-78

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 247.84  E-value: 6.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 119 DDLKYFYDDVRYLLksGTSQPELDTIASYYFDGQGKALRPMVTMLMAKAiNYHLNNEShQLVHKQRQIALFSEMVHSASL 198
Cdd:PLN02857 103 DDLQQLNDNLQSIV--GAENPVLMSAAEQIFGAGGKRMRPALVFLVSRA-TAELAGLK-ELTTEHRRLAEITEMIHTASL 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 199 VHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFA 278
Cdd:PLN02857 179 IHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLFDCDVTLD 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 279 HYLTKTYRKTASLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVL 358
Cdd:PLN02857 259 EYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVI 338
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665395515 359 FACEKYPELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINRM 435
Cdd:PLN02857 339 FALEKEPELREIIESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDMVDYNLERI 415
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
156-364 6.76e-55

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: 182.16  E-value: 6.76e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 156 LRPMVTMLMAKAINYHLnneshqlvHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNAL-WNHKKVTMAGDYILS 234
Cdd:cd00867    1 SRPLLVLLLARALGGDL--------EAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 235 IASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEVAF 314
Cdd:cd00867   73 RAFQLLARLGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALK 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 665395515 315 QYGRNIGLAFQLVDDMLDFVSSTEQMGKpTAADLKLGLATAPVLFACEKY 364
Cdd:cd00867  153 DYGRALGLAFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARERA 201
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
153-436 3.76e-51

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


Pssm-ID: 131795  Cd Length: 319  Bit Score: 175.29  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  153 GKALRPMVTMLMAKAINYHLNneshqlvhKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYI 232
Cdd:TIGR02748  43 GKRIRPVFVLLAGKFGDYDLD--------AIKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  233 LSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEV 312
Cdd:TIGR02748 115 FAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTALLIAASCQLGAIASGANEAIVKK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515  313 AFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEkypelNPMVMRRFSEPG------DVERAFE 386
Cdd:TIGR02748 195 LYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAME-----DPFLKKRIEQVLeettaeEMEPLIE 269
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 665395515  387 LVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVAdLVINRMK 436
Cdd:TIGR02748 270 EVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIA-KYIGKRK 318
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
147-434 1.41e-47

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 165.79  E-value: 1.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 147 YYFDGQGKALRPMVTMLMAKAINYHLNneshqlvhKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNALWNHKKVT 226
Cdd:PRK10888  38 YIISGGGKRIRPMIAVLAARAVGYQGN--------AHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 227 MAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQAD 306
Cdd:PRK10888 110 LVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 307 DNvAEVAFQ-YGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEK-YPELNPMVmRRFSEPGD---- 380
Cdd:PRK10888 190 PE-QEKGLQdYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHgTPEQAAMI-RTAIEQGNgrhl 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665395515 381 VERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINR 434
Cdd:PRK10888 268 LEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQR 321
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
156-419 6.32e-39

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: 140.32  E-value: 6.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 156 LRPMVTMLMAKAInyhlnneshqlvhkqrQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNAL---WNHKKVTMAGDYI 232
Cdd:cd00385    1 FRPLAVLLEPEAS----------------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 233 LSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEV 312
Cdd:cd00385   65 LADAFEELAREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 313 AFQYGRNIGLAFQLVDDMLDFVSSTEQMGkptaadlklGLATAPVLFACEKypelnpmvmrrfsepGDVERAFELVHKSH 392
Cdd:cd00385  145 LRKLGRALGLAFQLTNDLLDYEGDAERGE---------GKCTLPVLYALEY---------------GVPAEDLLLVEKSG 200
                        250       260
                 ....*....|....*....|....*..
gi 665395515 393 GLEQTRFLAKKHCNEAIRLAQELTESP 419
Cdd:cd00385  201 SLEEALEELAKLAEEALKELNELILSL 227
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
191-436 2.63e-14

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 73.27  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 191 EMVHSASLVHDDV--IDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIV--LSQIlTDLVQ----- 261
Cdd:PRK10581  74 ECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDAPMPEVSDRdrISMI-SELASasgia 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 262 ----GEFMQLgsrETENERFA-HYLTKTYR-KTASLIANALKATAVIAQADDNVAEVAF-QYGRNIGLAFQLVDDMLDFV 334
Cdd:PRK10581 153 gmcgGQALDL---EAEGKQVPlDALERIHRhKTGALIRAAVRLGALSAGDKGRRALPVLdRYAESIGLAFQVQDDILDVV 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395515 335 SSTEQMGKPTAADLKLGLATAPVLFacekypelnpmvmrrfsepgdverafelvhkshGLEQTRFLAKKHCNEAIRLAQE 414
Cdd:PRK10581 230 GDTATLGKRQGADQQLGKSTYPALL---------------------------------GLEQARKKARDLIDDARQSLDQ 276
                        250       260
                 ....*....|....*....|...
gi 665395515 415 LTESPYQKG-LQVVADLVINRMK 436
Cdd:PRK10581 277 LAAQSLDTSaLEALANYIIQRDK 299
 
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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