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Conserved domains on  [gi|2500425595|ref|WP_281277246|]
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octaprenyl diphosphate synthase [Kinneretia asaccharophila]

Protein Classification

isoprenoid biosynthesis enzyme family protein( domain architecture ID 89)

isoprenoid biosynthesis enzyme family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Isoprenoid_Biosyn_C1 super family cl00210
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
13-327 3.96e-132

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.


The actual alignment was detected with superfamily member PRK10888:

Pssm-ID: 469660  Cd Length: 323  Bit Score: 379.19  E-value: 3.96e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATLLHDDVV 92
Cdd:PRK10888    8 ELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  93 DESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVI 172
Cdd:PRK10888   88 DESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 173 RYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERG 252
Cdd:PRK10888  168 YSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHG 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500425595 253 SPKDRALIRQAIQNGEVQGLTE-IIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCAQSVDRSF 327
Cdd:PRK10888  248 TPEQAAMIRTAIEQGNGRHLLEpVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRDR 323
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
13-327 3.96e-132

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 379.19  E-value: 3.96e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATLLHDDVV 92
Cdd:PRK10888    8 ELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  93 DESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVI 172
Cdd:PRK10888   88 DESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 173 RYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERG 252
Cdd:PRK10888  168 YSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHG 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500425595 253 SPKDRALIRQAIQNGEVQGLTE-IIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCAQSVDRSF 327
Cdd:PRK10888  248 TPEQAAMIRTAIEQGNGRHLLEpVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
8-327 1.41e-130

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: 375.33  E-value: 1.41e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595   8 IVEAQALLDAEMREVDAVIARRLD-SDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATL 86
Cdd:COG0142     3 LKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  87 LHDDVVDESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSV----QRMRVLDVLADATNVIAEGEVLQLMNMHDPD 162
Cdd:COG0142    83 VHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELgdpeRRLRALRILARAARGMCEGQALDLEAEGRLD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 163 IAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPT 242
Cdd:COG0142   163 VTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 243 LPLLVAMERGSPKDRALIRQAIQNGEVQG--LTEIIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCA 320
Cdd:COG0142   243 LPLLLALERADPEERAELRELLGKPDLDEedLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALAD 322

                  ....*..
gi 2500425595 321 QSVDRSF 327
Cdd:COG0142   323 YVVERDR 329
polyprenyl_synt pfam00348
Polyprenyl synthetase;
34-267 1.31e-102

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 301.35  E-value: 1.31e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  34 VALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDR--FEMAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGNA 111
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEkaIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 112 AAVLVGDFLYSRAFQMMVSV-QRMRVLDVLADATNVIAEGEVLQLMNMHDPDI--AVEQYLRVIRYKTAKLFEASARLGA 188
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500425595 189 ILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERgSPKDRALIRQAIQNG 267
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKR 238
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
32-325 3.56e-98

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: 290.22  E-value: 3.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  32 SDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRF-EMAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGN 110
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPELEAAlRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 111 AAAVLVGDFLYSRAFQMMV---SVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLG 187
Cdd:cd00685    81 ATAILAGDYLLARAFELLArlgNPYYPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 188 AILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERgspKDRALIRQAIQng 267
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE---LAREYEEKALE-- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2500425595 268 evqglteiidivgrtgaldatreaaraeaesaraCLQSLPPSIWRETLLEFCAQSVDR 325
Cdd:cd00685   236 ----------------------------------ALKALPESPAREALRALADFILER 259
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
13-317 3.10e-62

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: 200.72  E-value: 3.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYIVQAGGKRIRPKLVLLfANALGHSKSDRFEMAAV-VEFIHTATLLHDDV 91
Cdd:TIGR02748   7 SFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLL-AGKFGDYDLDAIKHVAVaLELIHMASLVHDDV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  92 VDESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRV 171
Cdd:TIGR02748  86 IDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 172 IRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMEr 251
Cdd:TIGR02748 166 IKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAME- 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500425595 252 gSPKDRALIRQAIQNGEVQGLTEIIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLE 317
Cdd:TIGR02748 245 -DPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQE 309
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
13-327 3.96e-132

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 379.19  E-value: 3.96e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATLLHDDVV 92
Cdd:PRK10888    8 ELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  93 DESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVI 172
Cdd:PRK10888   88 DESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 173 RYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERG 252
Cdd:PRK10888  168 YSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHG 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500425595 253 SPKDRALIRQAIQNGEVQGLTE-IIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCAQSVDRSF 327
Cdd:PRK10888  248 TPEQAAMIRTAIEQGNGRHLLEpVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQRDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
8-327 1.41e-130

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: 375.33  E-value: 1.41e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595   8 IVEAQALLDAEMREVDAVIARRLD-SDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATL 86
Cdd:COG0142     3 LKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  87 LHDDVVDESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSV----QRMRVLDVLADATNVIAEGEVLQLMNMHDPD 162
Cdd:COG0142    83 VHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELgdpeRRLRALRILARAARGMCEGQALDLEAEGRLD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 163 IAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPT 242
Cdd:COG0142   163 VTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 243 LPLLVAMERGSPKDRALIRQAIQNGEVQG--LTEIIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCA 320
Cdd:COG0142   243 LPLLLALERADPEERAELRELLGKPDLDEedLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRALAD 322

                  ....*..
gi 2500425595 321 QSVDRSF 327
Cdd:COG0142   323 YVVERDR 329
polyprenyl_synt pfam00348
Polyprenyl synthetase;
34-267 1.31e-102

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 301.35  E-value: 1.31e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  34 VALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDR--FEMAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGNA 111
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEkaIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 112 AAVLVGDFLYSRAFQMMVSV-QRMRVLDVLADATNVIAEGEVLQLMNMHDPDI--AVEQYLRVIRYKTAKLFEASARLGA 188
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500425595 189 ILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERgSPKDRALIRQAIQNG 267
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKR 238
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
32-325 3.56e-98

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: 290.22  E-value: 3.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  32 SDVALINQIGAYIVQAGGKRIRPKLVLLFANALGHSKSDRF-EMAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGN 110
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPELEAAlRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 111 AAAVLVGDFLYSRAFQMMV---SVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLG 187
Cdd:cd00685    81 ATAILAGDYLLARAFELLArlgNPYYPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 188 AILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERgspKDRALIRQAIQng 267
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLALRE---LAREYEEKALE-- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2500425595 268 evqglteiidivgrtgaldatreaaraeaesaraCLQSLPPSIWRETLLEFCAQSVDR 325
Cdd:cd00685   236 ----------------------------------ALKALPESPAREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
52-268 6.28e-69

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: 214.90  E-value: 6.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  52 IRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATLLHDDVVDESSLRRGKPTANAL-FGNAAAVLVGDFLYSRAFQMMVS 130
Cdd:cd00867     1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLARAFQLLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 131 VQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGT 210
Cdd:cd00867    81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2500425595 211 AFQLIDDALDYSGDTQALGKnVGDDLREGKPTLPLLVAMERgspkDRALIRQAIQNGE 268
Cdd:cd00867   161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARER----AAEYAEEAYAALE 213
preA CHL00151
prenyl transferase; Reviewed
42-325 1.23e-66

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 211.96  E-value: 1.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  42 AYIVQAGGKRIRPKLVLLFANALG---HSKSDRFEMAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGNAAAVLVGD 118
Cdd:CHL00151   38 KHLFSAGGKRIRPAIVLLVAKATGgnmEIKTSQQRLAEITEIIHTASLVHDDVIDECSIRRGIPTVHKIFGTKIAVLAGD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 119 FLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIE 198
Cdd:CHL00151  118 FLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYKTASLIAASCKAAALLSDADEKDH 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 199 EACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERGSPKDRALIRQAIQNgevQGLTEIIDI 278
Cdd:CHL00151  198 NDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFALTQNSKLAKLIEREFCET---KDISQALQI 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2500425595 279 VGRTGALDATREAARAEAESARACLQSLPPSIWRETLLEFCAQSVDR 325
Cdd:CHL00151  275 IKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINR 321
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
13-317 3.10e-62

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: 200.72  E-value: 3.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYIVQAGGKRIRPKLVLLfANALGHSKSDRFEMAAV-VEFIHTATLLHDDV 91
Cdd:TIGR02748   7 SFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLL-AGKFGDYDLDAIKHVAVaLELIHMASLVHDDV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  92 VDESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRV 171
Cdd:TIGR02748  86 IDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 172 IRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMEr 251
Cdd:TIGR02748 166 IKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAME- 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500425595 252 gSPKDRALIRQAIQNGEVQGLTEIIDIVGRTGALDATREAARAEAESARACLQSLPPSIWRETLLE 317
Cdd:TIGR02748 245 -DPFLKKRIEQVLEETTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQE 309
PLN02857 PLN02857
octaprenyl-diphosphate synthase
44-315 5.07e-54

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 181.97  E-value: 5.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  44 IVQAGGKRIRPKLVLLFANA---LGHSKSDRFE---MAAVVEFIHTATLLHDDVVDESSLRRGKPTANALFGNAAAVLVG 117
Cdd:PLN02857  130 IFGAGGKRMRPALVFLVSRAtaeLAGLKELTTEhrrLAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAG 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 118 DFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILADSTPEI 197
Cdd:PLN02857  210 DFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSV 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 198 EEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERgSPKDRALIRQaiQNGEVQGLTEIID 277
Cdd:PLN02857  290 KEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEK-EPELREIIES--EFCEEGSLEEAIE 366
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2500425595 278 IVGRTGALDATREAARAEAESARACLQSLPPSIWRETL 315
Cdd:PLN02857  367 LVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSL 404
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
52-263 5.19e-46

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: 156.12  E-value: 5.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  52 IRPKLVLLFANALghsksdrfEMAAVVEFIHTATLLHDDVVDESSLRRGKPTANAL---FGNAAAVLVGDFLYSRAFQMM 128
Cdd:cd00385     1 FRPLAVLLEPEAS--------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 129 VSVQRMRVLDVLADATNVIAEGEVLQLMNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIEEACAGFGRAL 208
Cdd:cd00385    73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2500425595 209 GTAFQLIDDALDYSGDTQALgknvgddlrEGKPTLPLLVAMERGSPKDRALIRQA 263
Cdd:cd00385   153 GLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYALEYGVPAEDLLLVEK 198
PLN02890 PLN02890
geranyl diphosphate synthase
13-266 7.93e-42

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 150.08  E-value: 7.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  13 ALLDAEMREVDAVIARRLDSDVALINQIGAYivqagGKRIRPKLVLLFANALGHSKSDRFE-----------------MA 75
Cdd:PLN02890   93 SLLANKLRSMVVAEVPKLASAAEYFFKVGVE-----GKRFRPTVLLLMATALNVPLPESTEggvldivaselrtrqqnIA 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  76 AVVEFIHTATLLHDDVVDESSLRRGKPTANALFGNAAAVLVGDFLYSRAFQMMVSVQRMRVLDVLADATNVIAEGEVLQL 155
Cdd:PLN02890  168 EITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQI 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 156 MNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILADSTPEIEEACAGFGRALGTAFQLIDDALDYSGDTQALGKNVGDD 235
Cdd:PLN02890  248 TSSREQRRSMDYYMQKTYYKTASLISNSCKAVAILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSD 327
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2500425595 236 LREGKPTLPLLVAMERgSPKDRALIRQAIQN 266
Cdd:PLN02890  328 IRHGVITAPILFAMEE-FPQLREVVDRGFDN 357
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
48-265 4.82e-30

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 115.64  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595  48 GGKRIRPKLVLLFANALGHSKSDRFEMAAVVEFIHTATLLHDDV--VDESSLRRGKPTANALFGNAAAVLVGDFLYSRAF 125
Cdd:PRK10581   43 GGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAF 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500425595 126 QM-----MVSV---QRMRVLDVLADATNV--IAEGEVLQLmNMHDPDIAVEQYLRVIRYKTAKLFEASARLGAILA---- 191
Cdd:PRK10581  123 SIlsdapMPEVsdrDRISMISELASASGIagMCGGQALDL-EAEGKQVPLDALERIHRHKTGALIRAAVRLGALSAgdkg 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500425595 192 -DSTPEIEEacagFGRALGTAFQLIDDALDYSGDTQALGKNVGDDLREGKPTLPLLVAMERGSPKDRALIRQAIQ 265
Cdd:PRK10581  202 rRALPVLDR----YAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQ 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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