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Conserved domains on  [gi|1541646524|gb|RTN88609|]
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octaprenyl diphosphate synthase [Enterobacter bugandensis]

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: 659.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTAT 80
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 161 ENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 241 LHAMRNGTADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1541646524 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: 659.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTAT 80
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 161 ENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 241 LHAMRNGTADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1541646524 321 RDR 323
Cdd:PRK10888  321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-323 9.76e-147

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: 416.16  E-value: 9.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLN-SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTA 79
Cdd:COG0142     1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  80 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 155
Cdd:COG0142    81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 156 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGK 235
Cdd:COG0142   161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 236 PTLPLLHAMRNGTADQAKMIREAIEQGN-GRHLLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGL 314
Cdd:COG0142   241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                  ....*....
gi 1541646524 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 7.95e-106

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: 309.48  E-value: 7.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  27 SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQG-NAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 105
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 106 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 182
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 183 GILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMrngtadqakmireaieqg 262
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1541646524 263 ngrhllepvletmaicgslewtRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQR 321
Cdd:cd00685   223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
29-263 7.43e-101

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 296.73  E-value: 7.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  29 VQLINQLGYYIVSGGGKRIRPMIAILAARAVG--YQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 106
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 107 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 183
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 184 ILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNgTADQAKMIREAIEQGN 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 2.74e-63

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: 203.03  E-value: 2.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  13 DMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 92
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 173 RLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNGTADQA 252
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 253 kmIREAIEQGNGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQRD 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: 659.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTAT 80
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 161 ENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 241 LHAMRNGTADQAKMIREAIEQGNGRHLLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQ 320
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1541646524 321 RDR 323
Cdd:PRK10888  321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-323 9.76e-147

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: 416.16  E-value: 9.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLN-SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTA 79
Cdd:COG0142     1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  80 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 155
Cdd:COG0142    81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 156 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGK 235
Cdd:COG0142   161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 236 PTLPLLHAMRNGTADQAKMIREAIEQGN-GRHLLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGL 314
Cdd:COG0142   241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                  ....*....
gi 1541646524 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 7.95e-106

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: 309.48  E-value: 7.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  27 SDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQG-NAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 105
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 106 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 182
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 183 GILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMrngtadqakmireaieqg 262
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1541646524 263 ngrhllepvletmaicgslewtRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQR 321
Cdd:cd00685   223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
29-263 7.43e-101

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 296.73  E-value: 7.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  29 VQLINQLGYYIVSGGGKRIRPMIAILAARAVG--YQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 106
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 107 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 183
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 184 ILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNgTADQAKMIREAIEQGN 263
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
47-321 2.14e-71

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: 221.06  E-value: 2.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  47 IRPMIAILAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANA-AFGNAASVLVGDFIYTRAFQMMTS 125
Cdd:cd00867     1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLrRFGNALAILAGDYLLARAFQLLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 126 LGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGT 205
Cdd:cd00867    81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 206 AFQLIDDLLDYSADGETLGKnVGDDLNEGKPTLPLLHAMRngtadqakmireaieqgngrhllepvletmaicgslewtr 285
Cdd:cd00867   161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARE---------------------------------------- 199
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1541646524 286 qRAEEEADKAIEALQVIPDSP--WRDALIGLAHIAVQR 321
Cdd:cd00867   200 -RAAEYAEEAYAALEALPPSLprARRALIALADFLYRR 236
preA CHL00151
prenyl transferase; Reviewed
20-323 1.43e-63

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 203.87  E-value: 1.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  20 AILEQ-LNSDVQLINQLGY----YIVSGGGKRIRPMIAILAARAVGyqGNAHVT-----IAALIEFIHTATLLHDDVVDE 89
Cdd:CHL00151   16 LILEDnLKKLIGSGHPILYaaakHLFSAGGKRIRPAIVLLVAKATG--GNMEIKtsqqrLAEITEIIHTASLVHDDVIDE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  90 SDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYS 169
Cdd:CHL00151   94 CSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFY 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 170 KTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNgTA 249
Cdd:CHL00151  174 KTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQ-NS 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541646524 250 DQAKMI-REAIEQGNGRHLLEPVLETMAIcgslEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQRDR 323
Cdd:CHL00151  253 KLAKLIeREFCETKDISQALQIIKETNGI----EKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
13-322 2.74e-63

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: 203.03  E-value: 2.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  13 DMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 92
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 173 RLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNGTADQA 252
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 253 kmIREAIEQGNGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGLAHIAVQRD 322
Cdd:TIGR02748 252 --IEQVLEETTAEE-MEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRK 318
PLN02857 PLN02857
octaprenyl-diphosphate synthase
1-321 9.53e-62

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 202.00  E-value: 9.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524   1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAILAARAVGYQGN------AHVTIAALIE 74
Cdd:PLN02857   92 ISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAELAGlkelttEHRRLAEITE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  75 FIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVN 154
Cdd:PLN02857  172 MIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLF 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 155 DPDITEENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEG 234
Cdd:PLN02857  252 DCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKG 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 235 KPTLPLLHAMRNGTADQAKMIREAIEQGNgrhlLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDSPWRDALIGL 314
Cdd:PLN02857  332 NLTAPVIFALEKEPELREIIESEFCEEGS----LEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDM 407

                  ....*..
gi 1541646524 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 6.05e-51

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: 168.83  E-value: 6.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  47 IRPMIAILAARAVgyqgnahvTIAALIEFIHTATLLHDDVVDESDMRRGKATANAA---FGNAASVLVGDFIYTRAFQMM 123
Cdd:cd00385     1 FRPLAVLLEPEAS--------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 124 TSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCSEAQEKGLQDYGRYL 203
Cdd:cd00385    73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 204 GTAFQLIDDLLDYSADGETLgknvgddlnEGKPTLPLLHAMRNGTADQAKMIREAieqgngrhllepvletmaiCGSLEW 283
Cdd:cd00385   153 GLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYALEYGVPAEDLLLVEK-------------------SGSLEE 204
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1541646524 284 TRQRAEEEADKAIEALQVIPDSP--WRDALIGLAH 316
Cdd:cd00385   205 ALEELAKLAEEALKELNELILSLpdVPRALLALAL 239
PLN02890 PLN02890
geranyl diphosphate synthase
37-323 2.01e-45

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 159.32  E-value: 2.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  37 YYIVSGGGKRIRPMIAILAARAVGYQ-------GNAHV----------TIAALIEFIHTATLLHDDVVDESDMRRGKATA 99
Cdd:PLN02890  117 FFKVGVEGKRFRPTVLLLMATALNVPlpestegGVLDIvaselrtrqqNIAEITEMIHVASLLHDDVLDDADTRRGVGSL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 100 NAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAA 179
Cdd:PLN02890  197 NVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISNSC 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 180 QCSGILAGCSEAQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMrngtaDQAKMIREAI 259
Cdd:PLN02890  277 KAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAM-----EEFPQLREVV 351
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541646524 260 EQG--NGRHlLEPVLETMAICGSLEWTRQRAEEEADKAIEALQVIPDS------PWRDALIGLAHIAVQRDR 323
Cdd:PLN02890  352 DRGfdNPAN-VDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETddedvlTSRRALIDLTERVITRNK 422
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
43-260 8.36e-21

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 90.60  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524  43 GGKRIRPMIAILAARAVGYQGNAHVTIAALIEFIHTATLLHDDV--VDESDMRRGKATANAAFGNAASVLVGDFIYTRAF 120
Cdd:PRK10581   43 GGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAF 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541646524 121 QM-----MTSLGSLKVLEVMSE-----AVNVIAEGEVLQLmNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGcsE 190
Cdd:PRK10581  123 SIlsdapMPEVSDRDRISMISElasasGIAGMCGGQALDL-EAEGKQVPLDALERIHRHKTGALIRAAVRLGALSAG--D 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541646524 191 AQEKGLQDYGRY---LGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMRNGTADQAKMIREAIE 260
Cdd:PRK10581  200 KGRRALPVLDRYaesIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQ 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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