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Conserved domains on  [gi|2829443|sp|P55785|]
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RecName: Full=Heptaprenyl diphosphate synthase component 2; Short=HepPP synthase subunit 2

Protein Classification

heptaprenyl diphosphate synthase component 2( domain architecture ID 10798616)

heptaprenyl diphosphate synthase component 2 supplies heptaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinone menaquinone-7 (MQ-7)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
2-320 0e+00

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: 598.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443      2 KLKAMYSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMASL 81
Cdd:TIGR02748   1 KLADIYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     82 VHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLR 161
Cdd:TIGR02748  81 VHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    162 TYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVL 241
Cdd:TIGR02748 161 TYLRRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2829443    242 YALSDERVKAAIAAVGPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKRDY 320
Cdd:TIGR02748 241 YAMEDPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRKY 319
 
Name Accession Description Interval E-value
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
2-320 0e+00

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: 598.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443      2 KLKAMYSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMASL 81
Cdd:TIGR02748   1 KLADIYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     82 VHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLR 161
Cdd:TIGR02748  81 VHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    162 TYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVL 241
Cdd:TIGR02748 161 TYLRRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2829443    242 YALSDERVKAAIAAVGPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKRDY 320
Cdd:TIGR02748 241 YAMEDPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRKY 319
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-320 4.84e-133

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: 381.11  E-value: 4.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    1 MKLKAMYSFLSDDLAAVEEELERAVQ-SEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMA 79
Cdd:COG0142   1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   80 SLVHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNP----RAHQVLAKTIVEVCRGEIEQIKDKYR 155
Cdd:COG0142  81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILARAARGMCEGQALDLEAEGR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  156 FDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGN 235
Cdd:COG0142 161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  236 VTLPVLYAL--SDERVKAAIAAV--GPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDL 311
Cdd:COG0142 241 PTLPLLLALerADPEERAELRELlgKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                ....*....
gi 2829443  312 ALYIGKRDY 320
Cdd:COG0142 321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
27-318 1.34e-99

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: 293.69  E-value: 1.34e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   27 SEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYD-LERMKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWSN 105
Cdd:cd00685   1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPeLEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  106 RFAMYTGDYLFARSLERMAELGN---PRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRRIRRKTALLIAASCQLG 182
Cdd:cd00685  81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  183 ALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYALsdervkaaiaavgpetdv 262
Cdd:cd00685 161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2829443  263 aemaavisaikrtdaiersYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKR 318
Cdd:cd00685 223 -------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
32-271 4.79e-90

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 268.99  E-value: 4.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     32 LGEAALHLLQAGGKRIRPVFVLLAARF--GQYDLERMKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWSNRFAM 109
Cdd:pfam00348   4 LYEPLDYLVSAGGKRIRPLLVLLSAEAlgGPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAIAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    110 YTGDYLFARSLERMAEL-GNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQP--LRTYLRRIRRKTALLIAASCQLGALAA 186
Cdd:pfam00348  84 NDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFALAVKLGAILS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    187 GAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYAL--SDERVKAAIAAVGPET-DVA 263
Cdd:pfam00348 164 GADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALerTPEQRKILLEIYGKRPeDVE 243

                  ....*...
gi 2829443    264 EMAAVISA 271
Cdd:pfam00348 244 KVKEAYEL 251
preA CHL00151
prenyl transferase; Reviewed
10-320 3.81e-76

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 236.23  E-value: 3.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    10 LSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLE---RMKHVAVALELIHMASLVHDDV 86
Cdd:CHL00151  11 IEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATGGNMEiktSQQRLAEITEIIHTASLVHDDV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    87 IDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRR 166
Cdd:CHL00151  91 IDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   167 IRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYALSD 246
Cdd:CHL00151 171 SFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQ 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2829443   247 ERVKAAIAA--VGPETDVAEmaaVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKRDY 320
Cdd:CHL00151 251 NSKLAKLIEreFCETKDISQ---ALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
 
Name Accession Description Interval E-value
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
2-320 0e+00

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: 598.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443      2 KLKAMYSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMASL 81
Cdd:TIGR02748   1 KLADIYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     82 VHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLR 161
Cdd:TIGR02748  81 VHDDVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    162 TYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVL 241
Cdd:TIGR02748 161 TYLRRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2829443    242 YALSDERVKAAIAAVGPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKRDY 320
Cdd:TIGR02748 241 YAMEDPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRKY 319
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-320 4.84e-133

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: 381.11  E-value: 4.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    1 MKLKAMYSFLSDDLAAVEEELERAVQ-SEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMA 79
Cdd:COG0142   1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   80 SLVHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNP----RAHQVLAKTIVEVCRGEIEQIKDKYR 155
Cdd:COG0142  81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDPerrlRALRILARAARGMCEGQALDLEAEGR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  156 FDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGN 235
Cdd:COG0142 161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  236 VTLPVLYAL--SDERVKAAIAAV--GPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDL 311
Cdd:COG0142 241 PTLPLLLALerADPEERAELRELlgKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                ....*....
gi 2829443  312 ALYIGKRDY 320
Cdd:COG0142 321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
27-318 1.34e-99

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: 293.69  E-value: 1.34e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   27 SEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYD-LERMKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWSN 105
Cdd:cd00685   1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPeLEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  106 RFAMYTGDYLFARSLERMAELGN---PRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRRIRRKTALLIAASCQLG 182
Cdd:cd00685  81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  183 ALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYALsdervkaaiaavgpetdv 262
Cdd:cd00685 161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2829443  263 aemaavisaikrtdaiersYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKR 318
Cdd:cd00685 223 -------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
32-271 4.79e-90

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 268.99  E-value: 4.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     32 LGEAALHLLQAGGKRIRPVFVLLAARF--GQYDLERMKHVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWSNRFAM 109
Cdd:pfam00348   4 LYEPLDYLVSAGGKRIRPLLVLLSAEAlgGPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNAIAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    110 YTGDYLFARSLERMAEL-GNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQP--LRTYLRRIRRKTALLIAASCQLGALAA 186
Cdd:pfam00348  84 NDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLSctEEEYLEIVKYKTAYLFALAVKLGAILS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    187 GAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYAL--SDERVKAAIAAVGPET-DVA 263
Cdd:pfam00348 164 GADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALerTPEQRKILLEIYGKRPeDVE 243

                  ....*...
gi 2829443    264 EMAAVISA 271
Cdd:pfam00348 244 KVKEAYEL 251
preA CHL00151
prenyl transferase; Reviewed
10-320 3.81e-76

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 236.23  E-value: 3.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    10 LSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLE---RMKHVAVALELIHMASLVHDDV 86
Cdd:CHL00151  11 IEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATGGNMEiktSQQRLAEITEIIHTASLVHDDV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    87 IDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRR 166
Cdd:CHL00151  91 IDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   167 IRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYALSD 246
Cdd:CHL00151 171 SFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQ 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2829443   247 ERVKAAIAA--VGPETDVAEmaaVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGKRDY 320
Cdd:CHL00151 251 NSKLAKLIEreFCETKDISQ---ALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
PLN02857 PLN02857
octaprenyl-diphosphate synthase
1-320 1.54e-71

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 227.42  E-value: 1.54e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     1 MKLKAMYSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAAR-----FGQYDL-ERMKHVAVALE 74
Cdd:PLN02857  92 ISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRataelAGLKELtTEHRRLAEITE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    75 LIHMASLVHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKY 154
Cdd:PLN02857 172 MIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLF 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   155 RFDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQG 234
Cdd:PLN02857 252 DCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKG 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   235 NVTLPVLYALSDE-RVKAAIaavgpETDVAE---MAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRD 310
Cdd:PLN02857 332 NLTAPVIFALEKEpELREII-----ESEFCEegsLEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLED 406
                        330
                 ....*....|
gi 2829443   311 LALYIGKRDY 320
Cdd:PLN02857 407 MVDYNLERIY 416
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
47-254 3.11e-65

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: 205.27  E-value: 3.11e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   47 IRPVFVLLAARFGQYDLERMKHVAVALELIHMASLVHDDVIDDADLRRGRPTI-KAKWSNRFAMYTGDYLFARSLERMAE 125
Cdd:cd00867   1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAhLRRFGNALAILAGDYLLARAFQLLAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  126 LGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGM 205
Cdd:cd00867  81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 2829443  206 SFQITDDILDFTGTEEQLGKpAGSDLLQGNVTLPVLYALSDERVKAAIA 254
Cdd:cd00867 161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARERAAEYAEEA 208
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
1-320 4.42e-51

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 171.56  E-value: 4.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     1 MKLKAMYSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMAS 80
Cdd:PRK10888   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    81 LVHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPL 160
Cdd:PRK10888  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   161 RTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPV 240
Cdd:PRK10888 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   241 LYAL---SDERVKAAIAAVGPETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLPMNEARGLLRDLALYIGK 317
Cdd:PRK10888 241 LHAMhhgTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 ...
gi 2829443   318 RDY 320
Cdd:PRK10888 321 RDR 323
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
47-317 3.62e-47

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: 159.20  E-value: 3.62e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   47 IRPVFVLLAARFGqydlermkHVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWS---NRFAMYTGDYLFARSLERM 123
Cdd:cd00385   1 FRPLAVLLEPEAS--------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAidgLPEAILAGDLLLADAFEEL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  124 AELGNPRAHQVLAKTIVEVCRGEIEQIKDKYRFDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYV 203
Cdd:cd00385  73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443  204 GMSFQITDDILDFTGTEEQlgkpagsdlLQGNVTLPVLYALsdervkaaiaavgpetDVAEMAAVISAIKRTDAIERSYA 283
Cdd:cd00385 153 GLAFQLTNDLLDYEGDAER---------GEGKCTLPVLYAL----------------EYGVPAEDLLLVEKSGSLEEALE 207
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 2829443  284 LSDRYLDKALHLLDGLPMNE--ARGLLRDLALYIGK 317
Cdd:cd00385 208 ELAKLAEEALKELNELILSLpdVPRALLALALNLYR 243
PLN02890 PLN02890
geranyl diphosphate synthase
7-300 3.04e-42

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 150.85  E-value: 3.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443     7 YSFLSDDLAAVEEELERAVQSEYGPLGEAALHLLQAG--GKRIRPVFVLLAARFGQYDLE-----------------RMK 67
Cdd:PLN02890  85 FSLVADELSLLANKLRSMVVAEVPKLASAAEYFFKVGveGKRFRPTVLLLMATALNVPLPesteggvldivaselrtRQQ 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    68 HVAVALELIHMASLVHDDVIDDADLRRGRPTIKAKWSNRFAMYTGDYLFARSLERMAELGNPRAHQVLAKTIVEVCRGEI 147
Cdd:PLN02890 165 NIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGET 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   148 EQIKDKYRFDQPLRTYLRRIRRKTALLIAASCQLGALAAGAPEPIVKRLYWFGHYVGMSFQITDDILDFTGTEEQLGKPA 227
Cdd:PLN02890 245 MQITSSREQRRSMDYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGS 324
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2829443   228 GSDLLQGNVTLPVLYALSDERVKAAIAAVGpETDVAEMAAVISAIKRTDAIERSYALSDRYLDKALHLLDGLP 300
Cdd:PLN02890 325 LSDIRHGVITAPILFAMEEFPQLREVVDRG-FDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLP 396
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
30-251 3.01e-25

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 102.54  E-value: 3.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443    30 GPLGEAALHLLQAGGKRIRPVFVLLAARFGQYDLERMKHVAVALELIHMASLVHDDV--IDDADLRRGRPTIKAKWSNRF 107
Cdd:PRK10581  30 TPVVEAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEAN 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2829443   108 AMYTGDYLFARSLERMAELGNPR----------AHQVLAKTIVEVCRGEIEQIKDKYRfdQPLRTYLRRIRR-KTALLIA 176
Cdd:PRK10581 110 AILAGDALQTLAFSILSDAPMPEvsdrdrismiSELASASGIAGMCGGQALDLEAEGK--QVPLDALERIHRhKTGALIR 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2829443   177 ASCQLGALAAGAPE----PIVKRlywFGHYVGMSFQITDDILDFTGTEEQLGKPAGSDLLQGNVTLPVLYALSDERVKA 251
Cdd:PRK10581 188 AAVRLGALSAGDKGrralPVLDR---YAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKA 263
 
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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