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Conserved domains on  [gi|502863953|ref|WP_013098929|]
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MULTISPECIES: octaprenyl diphosphate synthase [Enterobacter]

Protein Classification

octaprenyl-diphosphate synthase( domain architecture ID 10793493)

octaprenyl-diphosphate synthase (all-trans) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
1-323 0e+00

octaprenyl diphosphate synthase; Provisional


:

Pssm-ID: 182813  Cd Length: 323  Bit Score: 660.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTAT 80
Cdd:PRK10888   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 241 LHAMHNGSADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888 241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 ...
gi 502863953 321 RDR 323
Cdd:PRK10888 321 RDR 323
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
1-323 0e+00

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 660.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTAT 80
Cdd:PRK10888   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 241 LHAMHNGSADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888 241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 ...
gi 502863953 321 RDR 323
Cdd:PRK10888 321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-323 4.93e-146

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: 414.23  E-value: 4.93e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLN-SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTA 79
Cdd:COG0142    1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  80 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 155
Cdd:COG0142   81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 156 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGK 235
Cdd:COG0142  161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 236 PTLPLLHAMHNGSADQAKMIREAIEQGN-GRHLLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGL 314
Cdd:COG0142  241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                 ....*....
gi 502863953 315 AHIAVQRDR 323
Cdd:COG0142  321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
27-321 2.34e-104

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: 306.01  E-value: 2.34e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  27 SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQG-KAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 105
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 106 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 182
Cdd:cd00685   81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 183 GILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMhngsadqakmireaieqg 262
Cdd:cd00685  161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502863953 263 ngrhllepvletmaicgslewtRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQR 321
Cdd:cd00685  223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
29-263 1.02e-99

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 293.64  E-value: 1.02e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   29 VQLINQLGYYIVSGGGKRIRPMIAILAARAVG--YQGKAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 106
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  107 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 183
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  184 ILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNgSADQAKMIREAIEQGN 263
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
13-322 5.57e-61

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: 197.25  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   13 DMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTATLLHDDVVDESDM 92
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  173 RLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNGSADQA 252
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  253 kmIREAIEQGNGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQRD 322
Cdd:TIGR02748 252 --IEQVLEETTAEE-MEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRK 318
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
1-323 0e+00

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 660.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTAT 80
Cdd:PRK10888   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888 161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 241 LHAMHNGSADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888 241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 ...
gi 502863953 321 RDR 323
Cdd:PRK10888 321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-323 4.93e-146

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: 414.23  E-value: 4.93e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLN-SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTA 79
Cdd:COG0142    1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  80 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 155
Cdd:COG0142   81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 156 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGK 235
Cdd:COG0142  161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 236 PTLPLLHAMHNGSADQAKMIREAIEQGN-GRHLLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGL 314
Cdd:COG0142  241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                 ....*....
gi 502863953 315 AHIAVQRDR 323
Cdd:COG0142  321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
27-321 2.34e-104

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: 306.01  E-value: 2.34e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  27 SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQG-KAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 105
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 106 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 182
Cdd:cd00685   81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 183 GILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMhngsadqakmireaieqg 262
Cdd:cd00685  161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502863953 263 ngrhllepvletmaicgslewtRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQR 321
Cdd:cd00685  223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
29-263 1.02e-99

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 293.64  E-value: 1.02e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   29 VQLINQLGYYIVSGGGKRIRPMIAILAARAVG--YQGKAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 106
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  107 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 183
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  184 ILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNgSADQAKMIREAIEQGN 263
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
47-321 3.12e-70

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: 217.98  E-value: 3.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  47 IRPMIAILAARAVGYQGKAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANA-AFGNAASVLVGDFIYTRAFQMMTS 125
Cdd:cd00867    1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLrRFGNALAILAGDYLLARAFQLLAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 126 LGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGT 205
Cdd:cd00867   81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 206 AFQLIDDLLDYSADGETLGKnVGDDLNEGKPTLPLLHAMhngsadqakmireaieqgngrhllepvletmaicgslewtr 285
Cdd:cd00867  161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILAR----------------------------------------- 198
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502863953 286 QRAEEEADKAIAALQVIPDSP--WRDALIGLAHIAVQR 321
Cdd:cd00867  199 ERAAEYAEEAYAALEALPPSLprARRALIALADFLYRR 236
preA CHL00151
prenyl transferase; Reviewed
20-323 7.84e-64

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 204.64  E-value: 7.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  20 AILEQ-LNSDVQLINQLGY----YIVSGGGKRIRPMIAILAARAVGYQGK---AHVTIAALIEFIHTATLLHDDVVDESD 91
Cdd:CHL00151  16 LILEDnLKKLIGSGHPILYaaakHLFSAGGKRIRPAIVLLVAKATGGNMEiktSQQRLAEITEIIHTASLVHDDVIDECS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  92 MRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKT 171
Cdd:CHL00151  96 IRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 172 ARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNgSADQ 251
Cdd:CHL00151 176 ASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQ-NSKL 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863953 252 AKMI-REAIEQGNGRHLLEPVLETMAIcgslEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQRDR 323
Cdd:CHL00151 255 AKLIeREFCETKDISQALQIIKETNGI----EKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
13-322 5.57e-61

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: 197.25  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   13 DMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTATLLHDDVVDESDM 92
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  173 RLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNGSADQA 252
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  253 kmIREAIEQGNGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGLAHIAVQRD 322
Cdd:TIGR02748 252 --IEQVLEETTAEE-MEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRK 318
PLN02857 PLN02857
octaprenyl-diphosphate synthase
1-321 2.01e-60

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 198.53  E-value: 2.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGK------AHVTIAALIE 74
Cdd:PLN02857  92 ISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAELAGlkelttEHRRLAEITE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  75 FIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVN 154
Cdd:PLN02857 172 MIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLF 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 155 DPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEG 234
Cdd:PLN02857 252 DCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKG 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 235 KPTLPLLHAMHNGSADQAKMIREAIEQGNgrhlLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDSPWRDALIGL 314
Cdd:PLN02857 332 NLTAPVIFALEKEPELREIIESEFCEEGS----LEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDM 407

                 ....*..
gi 502863953 315 AHIAVQR 321
Cdd:PLN02857 408 VDYNLER 414
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
47-316 2.26e-50

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: 167.29  E-value: 2.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  47 IRPMIAILAARAVgyqgkahvTIAALIEFIHTATLLHDDVVDESDMRRGKATANAA---FGNAASVLVGDFIYTRAFQMM 123
Cdd:cd00385    1 FRPLAVLLEPEAS--------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 124 TSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTAAQEKGLQDYGRYL 203
Cdd:cd00385   73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 204 GTAFQLIDDLLDYSADGETLgknvgddlnEGKPTLPLLHAMHNGSADQAKMIREAieqgngrhllepvletmaiCGSLEW 283
Cdd:cd00385  153 GLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYALEYGVPAEDLLLVEK-------------------SGSLEE 204
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 502863953 284 TRQRAEEEADKAIAALQVIPDSP--WRDALIGLAH 316
Cdd:cd00385  205 ALEELAKLAEEALKELNELILSLpdVPRALLALAL 239
PLN02890 PLN02890
geranyl diphosphate synthase
37-323 1.93e-47

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 164.71  E-value: 1.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  37 YYIVSGGGKRIRPMIAILAARAVGYQ-------GKAHV----------TIAALIEFIHTATLLHDDVVDESDMRRGKATA 99
Cdd:PLN02890 117 FFKVGVEGKRFRPTVLLLMATALNVPlpestegGVLDIvaselrtrqqNIAEITEMIHVASLLHDDVLDDADTRRGVGSL 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 100 NAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAA 179
Cdd:PLN02890 197 NVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISNSC 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 180 QCSGILAGCTAAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMhngsaDQAKMIREAI 259
Cdd:PLN02890 277 KAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAM-----EEFPQLREVV 351
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863953 260 EQG--NGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIAALQVIPDS------PWRDALIGLAHIAVQRDR 323
Cdd:PLN02890 352 DRGfdNPAN-VDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETddedvlTSRRALIDLTERVITRNK 422
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
43-260 3.21e-20

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 89.06  E-value: 3.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953  43 GGKRIRPMIAILAARAVGYQGKAHVTIAALIEFIHTATLLHDDV--VDESDMRRGKATANAAFGNAASVLVGDFIYTRAF 120
Cdd:PRK10581  43 GGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863953 121 QM-----MTSLGSLKVLEVMSE-----AVNVIAEGEVLQLmNVNDPDITEENYMRVIYSKTARLFEAAAQCsgilaGCTA 190
Cdd:PRK10581 123 SIlsdapMPEVSDRDRISMISElasasGIAGMCGGQALDL-EAEGKQVPLDALERIHRHKTGALIRAAVRL-----GALS 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863953 191 AQEKG------LQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHNGSADQAKMIREAIE 260
Cdd:PRK10581 197 AGDKGrralpvLDRYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQ 272
 
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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