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Conserved domains on  [gi|479538617|gb|ENR12175|]
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hypothetical protein C068_00296 [Brucella sp. UK38/05]

Protein Classification

polyprenyl synthetase family protein( domain architecture ID 10000639)

polyprenyl synthetase family protein such as farnesyl/geranylgeranyl diphosphate synthase, which is a key enzyme in isoprenoid biosynthesis, catalyzing the formation of farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), respectively

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
16-338 6.34e-134

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: 384.19  E-value: 6.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  16 SVQPLVDLTRADMARVNELILSR-AGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTAT 94
Cdd:COG0142    2 TLKDLLALLAEDLARVEAALEELlARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  95 LLHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGS----LDALDVLATSASIIAEGEVMQLAAAKNM 170
Cdd:COG0142   82 LVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 171 ETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKI 250
Cdd:COG0142  162 DVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 251 TLPVILSYRRGTDEERAFWKGAIEGGASDDASLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVV 330
Cdd:COG0142  242 TLPLLLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALA 321

                 ....*...
gi 479538617 331 DFCISRVN 338
Cdd:COG0142  322 DYVVERDR 329
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
16-338 6.34e-134

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: 384.19  E-value: 6.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  16 SVQPLVDLTRADMARVNELILSR-AGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTAT 94
Cdd:COG0142    2 TLKDLLALLAEDLARVEAALEELlARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  95 LLHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGS----LDALDVLATSASIIAEGEVMQLAAAKNM 170
Cdd:COG0142   82 LVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 171 ETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKI 250
Cdd:COG0142  162 DVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 251 TLPVILSYRRGTDEERAFWKGAIEGGASDDASLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVV 330
Cdd:COG0142  242 TLPLLLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALA 321

                 ....*...
gi 479538617 331 DFCISRVN 338
Cdd:COG0142  322 DYVVERDR 329
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
16-336 2.19e-105

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 311.39  E-value: 2.19e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  16 SVQPLVDLTRADMARVNELILSRAGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTATL 95
Cdd:PRK10888   2 NLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  96 LHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTED 175
Cdd:PRK10888  82 LHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 176 EYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVI 255
Cdd:PRK10888 162 NYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 256 LSYRRGTDEERAFWKGAIEGGASDDAsLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVVDFCIS 335
Cdd:PRK10888 242 HAMHHGTPEQAAMIRTAIEQGNGRHL-LEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 .
gi 479538617 336 R 336
Cdd:PRK10888 321 R 321
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
41-336 1.55e-93

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: 279.05  E-value: 1.55e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  41 SDVEMIPEVANHLISSGGKRLRPMMTLASARMFGY-EGDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGN 119
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGpELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 120 QASVLVGDFLLGQAFKMMVDVGS---LDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVG 196
Cdd:cd00685   81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 197 PIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYRrgtdeerafwkgaiegg 276
Cdd:cd00685  161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR----------------- 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 277 asddaslqkaiglmmkhgaiadtvQRARHFGEIARDALAPLKASPQKDALIEVVDFCISR 336
Cdd:cd00685  224 ------------------------ELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
43-287 2.43e-86

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 260.13  E-value: 2.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617   43 VEMIPEVANHLISSGGKRLRPMMTLASARMFG--YEGDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGNQ 120
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  121 ASVLVGDFLLGQAFKMMVDV-GSLDALDVLATSASIIAEGEVMQLAAAKNME--TTEDEYLAVIKAKTAALFSAAAEVGP 197
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDlsCTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  198 IIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYRRgTDEERAFWKGAIEGGA 277
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
                         250
                  ....*....|
gi 479538617  278 SDDASLQKAI 287
Cdd:pfam00348 240 EDVEKVKEAY 249
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
25-332 9.91e-52

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: 173.75  E-value: 9.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617   25 RADMARVNELILSRAGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTATLLHDDVVDES 104
Cdd:TIGR02748  10 QKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  105 DLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAK 184
Cdd:TIGR02748  90 DLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  185 TAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYrrgtde 264
Cdd:TIGR02748 170 TALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAM------ 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479538617  265 ERAFWKGAIEGGASDDASLQKAIglMMKHGAIADTVQRARHFGEI----ARDALAPLKASPQKDALIEVVDF 332
Cdd:TIGR02748 244 EDPFLKKRIEQVLEETTAEEMEP--LIEEVKKSDAIEYAYAVSDRylkkALELLDGLPDGRAKKPLQEIAKY 313
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
16-338 6.34e-134

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: 384.19  E-value: 6.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  16 SVQPLVDLTRADMARVNELILSR-AGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTAT 94
Cdd:COG0142    2 TLKDLLALLAEDLARVEAALEELlARSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  95 LLHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGS----LDALDVLATSASIIAEGEVMQLAAAKNM 170
Cdd:COG0142   82 LVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 171 ETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKI 250
Cdd:COG0142  162 DVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 251 TLPVILSYRRGTDEERAFWKGAIEGGASDDASLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVV 330
Cdd:COG0142  242 TLPLLLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALA 321

                 ....*...
gi 479538617 331 DFCISRVN 338
Cdd:COG0142  322 DYVVERDR 329
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
16-336 2.19e-105

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 311.39  E-value: 2.19e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  16 SVQPLVDLTRADMARVNELILSRAGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTATL 95
Cdd:PRK10888   2 NLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  96 LHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTED 175
Cdd:PRK10888  82 LHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 176 EYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVI 255
Cdd:PRK10888 162 NYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 256 LSYRRGTDEERAFWKGAIEGGASDDAsLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVVDFCIS 335
Cdd:PRK10888 242 HAMHHGTPEQAAMIRTAIEQGNGRHL-LEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                 .
gi 479538617 336 R 336
Cdd:PRK10888 321 R 321
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
41-336 1.55e-93

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: 279.05  E-value: 1.55e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  41 SDVEMIPEVANHLISSGGKRLRPMMTLASARMFGY-EGDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGN 119
Cdd:cd00685    1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGpELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 120 QASVLVGDFLLGQAFKMMVDVGS---LDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVG 196
Cdd:cd00685   81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 197 PIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYRrgtdeerafwkgaiegg 276
Cdd:cd00685  161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALR----------------- 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 277 asddaslqkaiglmmkhgaiadtvQRARHFGEIARDALAPLKASPQKDALIEVVDFCISR 336
Cdd:cd00685  224 ------------------------ELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
43-287 2.43e-86

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 260.13  E-value: 2.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617   43 VEMIPEVANHLISSGGKRLRPMMTLASARMFG--YEGDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGNQ 120
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  121 ASVLVGDFLLGQAFKMMVDV-GSLDALDVLATSASIIAEGEVMQLAAAKNME--TTEDEYLAVIKAKTAALFSAAAEVGP 197
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDlsCTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  198 IIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYRRgTDEERAFWKGAIEGGA 277
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
                         250
                  ....*....|
gi 479538617  278 SDDASLQKAI 287
Cdd:pfam00348 240 EDVEKVKEAY 249
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
61-290 4.31e-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: 205.66  E-value: 4.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  61 LRPMMTLASARMFGYEGDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTI-WGNQASVLVGDFLLGQAFKMMVD 139
Cdd:cd00867    1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLARAFQLLAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 140 VGSLDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGL 219
Cdd:cd00867   81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479538617 220 AFQLVDDALDYGGSAADLGKnTGDDFREGKITLPVILSYRRGTDEERAFWKGAIEGGASDDASLQKAIGLM 290
Cdd:cd00867  161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARERAAEYAEEAYAALEALPPSLPRARRALIALA 230
preA CHL00151
prenyl transferase; Reviewed
50-338 3.92e-59

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 193.08  E-value: 3.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  50 ANHLISSGGKRLRPMMTLASARMFGYEGD---GHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGNQASVLVG 126
Cdd:CHL00151  37 AKHLFSAGGKRIRPAIVLLVAKATGGNMEiktSQQRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 127 DFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSD 206
Cdd:CHL00151 117 DFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTASLIAASCKAAALLSDADEKD 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 207 RAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYrrgtdEERAFWKGAIEGGASDDASLQKA 286
Cdd:CHL00151 197 HNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFAL-----TQNSKLAKLIEREFCETKDISQA 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 479538617 287 IGLMMKHGAIADTVQRARHFGEIARDALAPLKASPQKDALIEVVDFCISRVN 338
Cdd:CHL00151 272 LQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
PLN02857 PLN02857
octaprenyl-diphosphate synthase
3-337 8.61e-58

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 192.37  E-value: 8.61e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617   3 VVLNLDGKMKQEGSVQPLVDLTRADMARVNELILSRAGSDVEMIPEVANHLISSGGKRLRPMMTL----ASARMFGYE-- 76
Cdd:PLN02857  80 VALDLKAESKEPISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFlvsrATAELAGLKel 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  77 GDGHVRLATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDvgsLDALDVLATSASII 156
Cdd:PLN02857 160 TTEHRRLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLAN---LDNLEVIKLISQVI 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 157 ---AEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGS 233
Cdd:PLN02857 237 kdfASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQS 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 234 AADLGKNTGDDFREGKITLPVILSYRRGTdEERAFwkgaIEGGASDDASLQKAIGLMMKHGAIADTVQRARHFGEIARDA 313
Cdd:PLN02857 317 TEQLGKPAGSDLAKGNLTAPVIFALEKEP-ELREI----IESEFCEEGSLEEAIELVNEGGGIERAQELAKEKADLAIQN 391
                        330       340
                 ....*....|....*....|....
gi 479538617 314 LAPLKASPQKDALIEVVDFCISRV 337
Cdd:PLN02857 392 LECLPRGAFRSSLEDMVDYNLERI 415
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
25-332 9.91e-52

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: 173.75  E-value: 9.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617   25 RADMARVNELILSRAGSDVEMIPEVANHLISSGGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTATLLHDDVVDES 104
Cdd:TIGR02748  10 QKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  105 DLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAK 184
Cdd:TIGR02748  90 DLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  185 TAALFSAAAEVGPIIAGAQRSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVILSYrrgtde 264
Cdd:TIGR02748 170 TALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAM------ 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479538617  265 ERAFWKGAIEGGASDDASLQKAIglMMKHGAIADTVQRARHFGEI----ARDALAPLKASPQKDALIEVVDF 332
Cdd:TIGR02748 244 EDPFLKKRIEQVLEETTAEEMEP--LIEEVKKSDAIEYAYAVSDRylkkALELLDGLPDGRAKKPLQEIAKY 313
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
61-335 4.56e-44

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: 151.49  E-value: 4.56e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  61 LRPMMTLASARMfgyegdghVRLATSVEFMHTATLLHDDVVDESDLRRGKSTAR---TIWGNQASVLVGDFLLGQAFKMM 137
Cdd:cd00385    1 FRPLAVLLEPEA--------SRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHlavAIDGLPEAILAGDLLLADAFEEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 138 VDVGSLDALDVLATSASIIAEGEVMQLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQRSDRAALRDYGLNL 217
Cdd:cd00385   73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 218 GLAFQLVDDALDYGGSAADLgkntgddfrEGKITLPVILSYRRGTDEERafwkgaieggasddaslqkaIGLMMKHGAIA 297
Cdd:cd00385  153 GLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYALEYGVPAED--------------------LLLVEKSGSLE 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 479538617 298 DTVQRARHFGEIARDALA--PLKASPQKDALIEVVDFCIS 335
Cdd:cd00385  204 EALEELAKLAEEALKELNelILSLPDVPRALLALALNLYR 243
PLN02890 PLN02890
geranyl diphosphate synthase
83-336 2.19e-38

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 141.22  E-value: 2.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  83 LATSVEFMHTATLLHDDVVDESDLRRGKSTARTIWGNQASVLVGDFLLGQAFKMMVDVGSLDALDVLATSASIIAEGEVM 162
Cdd:PLN02890 166 IAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETM 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 163 QLAAAKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGaQRSDRAALR-DYGLNLGLAFQLVDDALDYGGSAADLGKNT 241
Cdd:PLN02890 246 QITSSREQRRSMDYYMQKTYYKTASLISNSCKAVAILAG-QTAEVAVLAfEYGRNLGLAFQLIDDVLDFTGTSASLGKGS 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 242 GDDFREGKITLPVILSYrrgtdEERAFWKGAIEGGASDDASLQKAIGLMMKHGAIADTVQRARHFGEIARDALAPLKASP 321
Cdd:PLN02890 325 LSDIRHGVITAPILFAM-----EEFPQLREVVDRGFDNPANVDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETD 399
                        250       260
                 ....*....|....*....|.
gi 479538617 322 QKD------ALIEVVDFCISR 336
Cdd:PLN02890 400 DEDvltsrrALIDLTERVITR 420
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
57-256 1.66e-24

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 101.00  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617  57 GGKRLRPMMTLASARMFGYEGDGHVRLATSVEFMHTATLLHDDV--VDESDLRRGKSTARTIWGNQASVLVGDFLLGQAF 134
Cdd:PRK10581  43 GGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479538617 135 KM-----MVDVGSLDALDVLA--TSASIIA---EGEVMQLAAaKNMETTEDEYLAVIKAKTAALFSAAAEVGPIIAGAQ- 203
Cdd:PRK10581 123 SIlsdapMPEVSDRDRISMISelASASGIAgmcGGQALDLEA-EGKQVPLDALERIHRHKTGALIRAAVRLGALSAGDKg 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 479538617 204 RSDRAALRDYGLNLGLAFQLVDDALDYGGSAADLGKNTGDDFREGKITLPVIL 256
Cdd:PRK10581 202 RRALPVLDRYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALL 254
 
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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