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Conserved domains on  [gi|665410656|ref|NP_001287138|]
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decaprenyl diphosphate synthase subunit 2, isoform B [Drosophila melanogaster]

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 ...
86-441 6.44e-36

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 CHL00151:

Pssm-ID: 469660  Cd Length: 323  Bit Score: 134.92  E-value: 6.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  86 SLRWLLSDEIANVALHLRKLVGSAHPLM-KTAKHLL-YNGKNTMQAwglIVLLVSKAAGhapsvpdveqdKSAGVLHSQR 163
Cdd:CHL00151   6 NLLTPIEEELLILEDNLKKLIGSGHPILyAAAKHLFsAGGKRIRPA---IVLLVAKATG-----------GNMEIKTSQQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 164 ALAEVTEMIRISHLVHNSVVNlQSSTQAGqdVDTYDDMsFGNKIGLLTGDYLLGHSSAELANLRNQEVVELISSAVRDFS 243
Cdd:CHL00151  72 RLAEITEIIHTASLVHDDVID-ECSIRRG--IPTVHKI-FGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 244 ESEFigerdeqnnplpyKPGTFQ-RPSLSVgVDFNEhdvmtpmpiaqvlgnpeeewecRNILNAGSLLGKSCQASLKLAG 322
Cdd:CHL00151 148 EGEI-------------RQGLVQfDTTLSI-LNYIE----------------------KSFYKTASLIAASCKAAALLSD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 323 QSEELQRHAYRFGKHLALAWQACLDAepfqcpqlpLDVTFSLVS---------------APVLFHLEHDPGMYSQLEagK 387
Cdd:CHL00151 192 ADEKDHNDFYLYGKHLGLAFQIIDDV---------LDITSSTESlgkpigsdlkngnltAPVLFALTQNSKLAKLIE--R 260
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665410656 388 QSVDNIDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDARQALENI 441
Cdd:CHL00151 261 EFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEI 314
 
Name Accession Description Interval E-value
preA CHL00151
prenyl transferase; Reviewed
86-441 6.44e-36

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 134.92  E-value: 6.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  86 SLRWLLSDEIANVALHLRKLVGSAHPLM-KTAKHLL-YNGKNTMQAwglIVLLVSKAAGhapsvpdveqdKSAGVLHSQR 163
Cdd:CHL00151   6 NLLTPIEEELLILEDNLKKLIGSGHPILyAAAKHLFsAGGKRIRPA---IVLLVAKATG-----------GNMEIKTSQQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 164 ALAEVTEMIRISHLVHNSVVNlQSSTQAGqdVDTYDDMsFGNKIGLLTGDYLLGHSSAELANLRNQEVVELISSAVRDFS 243
Cdd:CHL00151  72 RLAEITEIIHTASLVHDDVID-ECSIRRG--IPTVHKI-FGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 244 ESEFigerdeqnnplpyKPGTFQ-RPSLSVgVDFNEhdvmtpmpiaqvlgnpeeewecRNILNAGSLLGKSCQASLKLAG 322
Cdd:CHL00151 148 EGEI-------------RQGLVQfDTTLSI-LNYIE----------------------KSFYKTASLIAASCKAAALLSD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 323 QSEELQRHAYRFGKHLALAWQACLDAepfqcpqlpLDVTFSLVS---------------APVLFHLEHDPGMYSQLEagK 387
Cdd:CHL00151 192 ADEKDHNDFYLYGKHLGLAFQIIDDV---------LDITSSTESlgkpigsdlkngnltAPVLFALTQNSKLAKLIE--R 260
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665410656 388 QSVDNIDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDARQALENI 441
Cdd:CHL00151 261 EFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEI 314
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
83-445 6.78e-13

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: 69.48  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  83 SFLSLRWLLSDEIANVALHLRKLVGSAHP--LMKTAKHLLYNGkntmqawG-----LIVLLVSKAAGhapsvpdveqDKS 155
Cdd:COG0142    2 TLKDLLALLAEDLARVEAALEELLARSEPplLAEAMRYLLLAG-------GkrlrpLLVLLAARALG----------GDP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 156 AGVLHsqraLAEVTEMIrisH---LVHNSVVnlqsstqagqdvdtyDD-----------MSFGNKIGLLTGDYLLGHSSA 221
Cdd:COG0142   65 EAALR----AAAAVELI---HtasLVHDDVM---------------DDddlrrgkptvhARFGEATAILAGDALLALAFE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 222 ELANL----RNQEVVELISSAVRDFSESEFIgerdeqnnplpykpgtfqrpslsvgvdfnehDVMtpmpiAQVLGNPEEE 297
Cdd:COG0142  123 LLAELgdpeRRLRALRILARAARGMCEGQAL-------------------------------DLE-----AEGRLDVTLE 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 298 wECRNILNA--GSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQacL--DAepfqcpqlpLDVTFSL--------- 364
Cdd:COG0142  167 -EYLRVIRLktAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQ--IrdDI---------LDVTGDPevlgkpags 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 365 ------VSAPVLFHLEH-DPGMYSQLEA--GKQSVDNIDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDAR 435
Cdd:COG0142  235 dlregkPTLPLLLALERaDPEERAELREllGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAR 314
                        410
                 ....*....|
gi 665410656 436 QALENIILAM 445
Cdd:COG0142  315 EALRALADYV 324
polyprenyl_synt pfam00348
Polyprenyl synthetase;
112-398 7.16e-09

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 56.36  E-value: 7.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  112 LMKTAKHLLYN-GKntmQAWGLIVLLVSKAAGHAPSvpdveqdksagvLHSQRALAEVTEMIRISHLVHNSVVNlQSSTQ 190
Cdd:pfam00348   4 LYEPLDYLVSAgGK---RIRPLLVLLSAEALGGPED------------LEKAIVLAWAVELLHAASLVHDDIMD-NSDLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  191 AGQDVdTYDdmSFGNKIGLLTGDYLLGHSSAELANL-RNQEVVELISSAVRDFSESEFIgerdeqnnplpykpgtfqrps 269
Cdd:pfam00348  68 RGQPT-WHR--IFGNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGL--------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  270 lsvgvD-FNEHDVMTPmpiaqvlgNPEEEWECRNILNAGSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQ----- 343
Cdd:pfam00348 124 -----DlLWRNDDDLS--------CTEEEYLEIVKYKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQiqddy 190
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  344 -------------ACLDAEPFQCpqlpldvtfslvSAPVLFHLEHDPGMYSQLEA--GKQSVDNIDYDKI 398
Cdd:pfam00348 191 ldlfgdpevlgkpAGTDITEGKC------------TWPVIHALERTPEQRKILLEiyGKRPEDVEKVKEA 248
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
131-442 1.49e-07

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: 52.55  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 131 GLIVLLVSKAAGhapsvpdveqdksAGVLHSQRALAEVTEMIRISHLVHNSVVNlQSSTQAGQDVDTYDdmsFGNKIGLL 210
Cdd:cd00685   23 PLLVLLAARALG-------------GPELEAALRLAAAIELLHTASLVHDDVMD-NSDLRRGKPTVHKV---FGNATAIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 211 TGDYLLGHSSAELANLRNQ---EVVELISSAVRDFSESEFIGERDEQNNPlpykpgtfqrpslsvgVDFNEHDVMTpmpi 287
Cdd:cd00685   86 AGDYLLARAFELLARLGNPyypRALELFSEAILELVEGQLLDLLSEYDTD----------------VTEEEYLRII---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 288 aqvlgnpeeewecrnILNAGSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQACLDAepfqcpqlpLDVTfslvsa 367
Cdd:cd00685  146 ---------------RLKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDI---------LDLF------ 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410656 368 pvlfhleHDPGmysqlEAGKQSVDniDydkihkaILAG----PALAKTKELQRKHTAAALAVLQHFPATDARQALENII 442
Cdd:cd00685  196 -------GDPE-----TLGKPVGS--D-------LREGkctlPVLLALRELAREYEEKALEALKALPESPAREALRALA 253
 
Name Accession Description Interval E-value
preA CHL00151
prenyl transferase; Reviewed
86-441 6.44e-36

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 134.92  E-value: 6.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  86 SLRWLLSDEIANVALHLRKLVGSAHPLM-KTAKHLL-YNGKNTMQAwglIVLLVSKAAGhapsvpdveqdKSAGVLHSQR 163
Cdd:CHL00151   6 NLLTPIEEELLILEDNLKKLIGSGHPILyAAAKHLFsAGGKRIRPA---IVLLVAKATG-----------GNMEIKTSQQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 164 ALAEVTEMIRISHLVHNSVVNlQSSTQAGqdVDTYDDMsFGNKIGLLTGDYLLGHSSAELANLRNQEVVELISSAVRDFS 243
Cdd:CHL00151  72 RLAEITEIIHTASLVHDDVID-ECSIRRG--IPTVHKI-FGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 244 ESEFigerdeqnnplpyKPGTFQ-RPSLSVgVDFNEhdvmtpmpiaqvlgnpeeewecRNILNAGSLLGKSCQASLKLAG 322
Cdd:CHL00151 148 EGEI-------------RQGLVQfDTTLSI-LNYIE----------------------KSFYKTASLIAASCKAAALLSD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 323 QSEELQRHAYRFGKHLALAWQACLDAepfqcpqlpLDVTFSLVS---------------APVLFHLEHDPGMYSQLEagK 387
Cdd:CHL00151 192 ADEKDHNDFYLYGKHLGLAFQIIDDV---------LDITSSTESlgkpigsdlkngnltAPVLFALTQNSKLAKLIE--R 260
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665410656 388 QSVDNIDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDARQALENI 441
Cdd:CHL00151 261 EFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEI 314
PLN02857 PLN02857
octaprenyl-diphosphate synthase
81-443 1.70e-27

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 113.40  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  81 PTSFLSLRWLLSDEIANVALHLRKLVGSAHP-LMKTAKHLLYNGKNTMQAwgLIVLLVSKAAGHAPSVPDVEQDksagvl 159
Cdd:PLN02857  91 PISLSELFEPVADDLQQLNDNLQSIVGAENPvLMSAAEQIFGAGGKRMRP--ALVFLVSRATAELAGLKELTTE------ 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 160 hsQRALAEVTEMIRISHLVHNSVVNlQSSTQAGQDvdTYDDMsFGNKIGLLTGDYLLGHSSAELANLRNQEVVELISSAV 239
Cdd:PLN02857 163 --HRRLAEITEMIHTASLIHDDVLD-ESDMRRGKE--TVHQL-YGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVI 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 240 RDFSESEFIgerdeqnnplpykpgtfQRPSLsvgvdFNEhDVMTpmpiaqvlgnpeEEWECRNILNAGSLLGKSCQASLK 319
Cdd:PLN02857 237 KDFASGEIK-----------------QASSL-----FDC-DVTL------------DEYLLKSYYKTASLIAASTKSAAI 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 320 LAGQSEELQRHAYRFGKHLALAWQACLD-------AEPFQCPQlPLDVTFSLVSAPVLFHLEHDPGMYSQLEAgkQSVDN 392
Cdd:PLN02857 282 FSGVDSSVKEQMYEYGKNLGLAFQVVDDildftqsTEQLGKPA-GSDLAKGNLTAPVIFALEKEPELREIIES--EFCEE 358
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665410656 393 IDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDARQALENIIL 443
Cdd:PLN02857 359 GSLEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLEDMVD 409
PLN02890 PLN02890
geranyl diphosphate synthase
90-441 1.19e-24

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 105.39  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  90 LLSDEIANVALHLRKLVGSAHPLMKTAKHLLYNGKNTMQAWGLIVLLVSKAAGHAPsVPDVEQDKSAGVLHS-----QRA 164
Cdd:PLN02890  87 LVADELSLLANKLRSMVVAEVPKLASAAEYFFKVGVEGKRFRPTVLLLMATALNVP-LPESTEGGVLDIVASelrtrQQN 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 165 LAEVTEMIRISHLVHNSVVNlqsstqagqDVDTYDDMS-----FGNKIGLLTGDYLLGHSSAELANLRNQEVVELISSAV 239
Cdd:PLN02890 166 IAEITEMIHVASLLHDDVLD---------DADTRRGVGslnvvMGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAV 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 240 rdfsESEFIGERDEQNNplpykpGTFQRPSLsvgvdfnehdvmtpmpiaqvlgnpeEEWECRNILNAGSLLGKSCQASLK 319
Cdd:PLN02890 237 ----EHLVTGETMQITS------SREQRRSM-------------------------DYYMQKTYYKTASLISNSCKAVAI 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 320 LAGQSEELQRHAYRFGKHLALAWQACLDAEPFQCPQLPL------DVTFSLVSAPVLFHLEHDPGMYSQLEAGKQSVDNI 393
Cdd:PLN02890 282 LAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLgkgslsDIRHGVITAPILFAMEEFPQLREVVDRGFDNPANV 361
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410656 394 D--YDKIHKAilagPALAKTKELQRKHTAAALAVLQHFPATD------ARQALENI 441
Cdd:PLN02890 362 DiaLEYLGKS----RGIQRTRELAREHANLAAAAIESLPETDdedvltSRRALIDL 413
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
83-445 6.78e-13

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: 69.48  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  83 SFLSLRWLLSDEIANVALHLRKLVGSAHP--LMKTAKHLLYNGkntmqawG-----LIVLLVSKAAGhapsvpdveqDKS 155
Cdd:COG0142    2 TLKDLLALLAEDLARVEAALEELLARSEPplLAEAMRYLLLAG-------GkrlrpLLVLLAARALG----------GDP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 156 AGVLHsqraLAEVTEMIrisH---LVHNSVVnlqsstqagqdvdtyDD-----------MSFGNKIGLLTGDYLLGHSSA 221
Cdd:COG0142   65 EAALR----AAAAVELI---HtasLVHDDVM---------------DDddlrrgkptvhARFGEATAILAGDALLALAFE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 222 ELANL----RNQEVVELISSAVRDFSESEFIgerdeqnnplpykpgtfqrpslsvgvdfnehDVMtpmpiAQVLGNPEEE 297
Cdd:COG0142  123 LLAELgdpeRRLRALRILARAARGMCEGQAL-------------------------------DLE-----AEGRLDVTLE 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 298 wECRNILNA--GSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQacL--DAepfqcpqlpLDVTFSL--------- 364
Cdd:COG0142  167 -EYLRVIRLktAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQ--IrdDI---------LDVTGDPevlgkpags 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 365 ------VSAPVLFHLEH-DPGMYSQLEA--GKQSVDNIDYDKIHKAILAGPALAKTKELQRKHTAAALAVLQHFPATDAR 435
Cdd:COG0142  235 dlregkPTLPLLLALERaDPEERAELREllGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAR 314
                        410
                 ....*....|
gi 665410656 436 QALENIILAM 445
Cdd:COG0142  315 EALRALADYV 324
polyprenyl_synt pfam00348
Polyprenyl synthetase;
112-398 7.16e-09

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 56.36  E-value: 7.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  112 LMKTAKHLLYN-GKntmQAWGLIVLLVSKAAGHAPSvpdveqdksagvLHSQRALAEVTEMIRISHLVHNSVVNlQSSTQ 190
Cdd:pfam00348   4 LYEPLDYLVSAgGK---RIRPLLVLLSAEALGGPED------------LEKAIVLAWAVELLHAASLVHDDIMD-NSDLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  191 AGQDVdTYDdmSFGNKIGLLTGDYLLGHSSAELANL-RNQEVVELISSAVRDFSESEFIgerdeqnnplpykpgtfqrps 269
Cdd:pfam00348  68 RGQPT-WHR--IFGNAIAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGL--------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  270 lsvgvD-FNEHDVMTPmpiaqvlgNPEEEWECRNILNAGSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQ----- 343
Cdd:pfam00348 124 -----DlLWRNDDDLS--------CTEEEYLEIVKYKTAYLFALAVKLGAILSGADDEVIEALKDYGLNLGLAFQiqddy 190
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656  344 -------------ACLDAEPFQCpqlpldvtfslvSAPVLFHLEHDPGMYSQLEA--GKQSVDNIDYDKI 398
Cdd:pfam00348 191 ldlfgdpevlgkpAGTDITEGKC------------TWPVIHALERTPEQRKILLEiyGKRPEDVEKVKEA 248
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
131-442 1.49e-07

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: 52.55  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 131 GLIVLLVSKAAGhapsvpdveqdksAGVLHSQRALAEVTEMIRISHLVHNSVVNlQSSTQAGQDVDTYDdmsFGNKIGLL 210
Cdd:cd00685   23 PLLVLLAARALG-------------GPELEAALRLAAAIELLHTASLVHDDVMD-NSDLRRGKPTVHKV---FGNATAIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 211 TGDYLLGHSSAELANLRNQ---EVVELISSAVRDFSESEFIGERDEQNNPlpykpgtfqrpslsvgVDFNEHDVMTpmpi 287
Cdd:cd00685   86 AGDYLLARAFELLARLGNPyypRALELFSEAILELVEGQLLDLLSEYDTD----------------VTEEEYLRII---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410656 288 aqvlgnpeeewecrnILNAGSLLGKSCQASLKLAGQSEELQRHAYRFGKHLALAWQACLDAepfqcpqlpLDVTfslvsa 367
Cdd:cd00685  146 ---------------RLKTAALFAAAPLLGALLAGADEEEAEALKRFGRNLGLAFQIQDDI---------LDLF------ 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410656 368 pvlfhleHDPGmysqlEAGKQSVDniDydkihkaILAG----PALAKTKELQRKHTAAALAVLQHFPATDARQALENII 442
Cdd:cd00685  196 -------GDPE-----TLGKPVGS--D-------LREGkctlPVLLALRELAREYEEKALEALKALPESPAREALRALA 253
 
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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