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Conserved domains on  [gi|6322294|ref|NP_012368|]
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bifunctional (2E,6E)-farnesyl diphosphate synthase/dimethylallyltranstransferase [Saccharomyces cerevisiae S288C]

Protein Classification

FPP/GGPP synthase family protein( domain architecture ID 11092413)

FPP/GGPP synthase family protein such as farnesyl/geranylgeranyl diphosphate synthases, which are key enzymes 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
PubMed:  8003978|11111076
SCOP:  4001453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
38-304 6.25e-103

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 302.89  E-value: 6.25e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294     38 DWYAHSLNYNT-PGGKLNRGLSVVDTYAILSnktveqlGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWY 116
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    117 KVpeVGE-IAINDAFMLEAAIYKLLKSHFRnekyYIDITELFHEVTFQTELGQLMDLITapEDKVDLSKfSLKKHSFIVT 195
Cdd:pfam00348  75 RI--FGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLW--RNDDDLSC-TEEEYLEIVK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    196 FKTAyYSFYLPVALAMYVAGITDEkDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGKI-GTDIQDNKCSWVINKALEL 274
Cdd:pfam00348 146 YKTA-YLFALAVKLGAILSGADDE-VIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 6322294    275 aSAEQRKTLDENYGkKDSVAEAKCKKIFND 304
Cdd:pfam00348 224 -TPEQRKILLEIYG-KRPEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
38-304 6.25e-103

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 302.89  E-value: 6.25e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294     38 DWYAHSLNYNT-PGGKLNRGLSVVDTYAILSnktveqlGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWY 116
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    117 KVpeVGE-IAINDAFMLEAAIYKLLKSHFRnekyYIDITELFHEVTFQTELGQLMDLITapEDKVDLSKfSLKKHSFIVT 195
Cdd:pfam00348  75 RI--FGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLW--RNDDDLSC-TEEEYLEIVK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    196 FKTAyYSFYLPVALAMYVAGITDEkDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGKI-GTDIQDNKCSWVINKALEL 274
Cdd:pfam00348 146 YKTA-YLFALAVKLGAILSGADDE-VIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 6322294    275 aSAEQRKTLDENYGkKDSVAEAKCKKIFND 304
Cdd:pfam00348 224 -TPEQRKILLEIYG-KRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 35-350 1.08e-76

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: 236.29  E-value: 1.08e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   35 EACDWYAHSLNYNT-PGGKLNRGLSVVDTYailsnktvEQLGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQP 113
Cdd:cd00685   1 SEVELLREALRYLLlAGGKRLRPLLVLLAA--------RALGGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  114 CWYKVPEVGeIAINDAFMLEAAIYKLLKSHFRNekYYIDITELFHEVTFQTELGQLMDLITAPEdkvdlSKFSLKKHSFI 193
Cdd:cd00685  73 TVHKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLDLLSEYD-----TDVTEEEYLRI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  194 VTFKTAYYSFYLPVALAMYVAGitDEKDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGK-IGTDIQDNKCSWVINKAL 272
Cdd:cd00685 145 IRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322294  273 elasaeqrktldenygkkdsvaeakckkifndlkiEQLYHEYEESIAKDLKAKISQVdesrgfKADVLTAFLNKVYKR 350
Cdd:cd00685 223 -----------------------------------RELAREYEEKALEALKALPESP------AREALRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 89-352 9.44e-31

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: 118.79  E-value: 9.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   89 IELLQAYFLVADDMMDKSITRRGQPC----WykvpevGE-IAIN--DaFMLEAAiYKLLkSHFRNEKYYIDITELFHEVT 161
Cdd:COG0142  74 VELIHTASLVHDDVMDDDDLRRGKPTvharF------GEaTAILagD-ALLALA-FELL-AELGDPERRLRALRILARAA 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  162 FQTELGQLMDLitAPEDKVDLSkfsLKKHSFIVTFKTAYYsFYLPVALAMYVAGiTDEKDLKQARDVLIPLGEYFQIQDD 241
Cdd:COG0142 145 RGMCEGQALDL--EAEGRLDVT---LEEYLRVIRLKTAAL-FAAALRLGAILAG-ADEEQVEALRRYGRNLGLAFQIRDD 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  242 YLDCFGTPEQIGK-IGTDIQDNKCSWVINKALELASAEQRKTLDENYGKKDSVAE--AKCKKIFNDLKIEqlyhEYEESI 318
Cdd:COG0142 218 ILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDLDEEdlAEVRALLRESGAL----EYAREL 293

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6322294  319 AKDL--KAK--ISQVDESRGfkADVLTAFLNKVYKRSK 352
Cdd:COG0142 294 ARELaeEALaaLAALPDSEA--REALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
38-304 6.25e-103

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 302.89  E-value: 6.25e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294     38 DWYAHSLNYNT-PGGKLNRGLSVVDTYAILSnktveqlGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWY 116
Cdd:pfam00348   2 KLLYEPLDYLVsAGGKRIRPLLVLLSAEALG-------GPEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    117 KVpeVGE-IAINDAFMLEAAIYKLLKSHFRnekyYIDITELFHEVTFQTELGQLMDLITapEDKVDLSKfSLKKHSFIVT 195
Cdd:pfam00348  75 RI--FGNaIAINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLW--RNDDDLSC-TEEEYLEIVK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294    196 FKTAyYSFYLPVALAMYVAGITDEkDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGKI-GTDIQDNKCSWVINKALEL 274
Cdd:pfam00348 146 YKTA-YLFALAVKLGAILSGADDE-VIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPaGTDITEGKCTWPVIHALER 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 6322294    275 aSAEQRKTLDENYGkKDSVAEAKCKKIFND 304
Cdd:pfam00348 224 -TPEQRKILLEIYG-KRPEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
 35-350 1.08e-76

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: 236.29  E-value: 1.08e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   35 EACDWYAHSLNYNT-PGGKLNRGLSVVDTYailsnktvEQLGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQP 113
Cdd:cd00685   1 SEVELLREALRYLLlAGGKRLRPLLVLLAA--------RALGGPELEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  114 CWYKVPEVGeIAINDAFMLEAAIYKLLKSHFRNekYYIDITELFHEVTFQTELGQLMDLITAPEdkvdlSKFSLKKHSFI 193
Cdd:cd00685  73 TVHKVFGNA-TAILAGDYLLARAFELLARLGNP--YYPRALELFSEAILELVEGQLLDLLSEYD-----TDVTEEEYLRI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  194 VTFKTAYYSFYLPVALAMYVAGitDEKDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGK-IGTDIQDNKCSWVINKAL 272
Cdd:cd00685 145 IRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLAL 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322294  273 elasaeqrktldenygkkdsvaeakckkifndlkiEQLYHEYEESIAKDLKAKISQVdesrgfKADVLTAFLNKVYKR 350
Cdd:cd00685 223 -----------------------------------RELAREYEEKALEALKALPESP------AREALRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
 54-285 2.19e-56

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: 183.70  E-value: 2.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   54 NRGLSVVDTYAILSNKtveqlgqeeYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWYKVPEVGEIAINDAFMLE 133
Cdd:cd00867   1 SRPLLVLLLARALGGD---------LEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  134 AAIYKLLKSHFrnekyYIDITELFHEVTFQTELGQLMDLITAPEdkvdlSKFSLKKHSFIVTFKTAYYSFYLPVALAMYV 213
Cdd:cd00867  72 ARAFQLLARLG-----YPRALELFAEALRELLEGQALDLEFERD-----TYETLDEYLEYCRYKTAGLVGLLCLLGAGLS 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322294  214 AGitDEKDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGKIGTDIQDNKCSWVINKALELASAEQRKTLDE 285
Cdd:cd00867 142 GA--DDEQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERAAEYAEEAYAA 211
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
 85-325 1.02e-33

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: 124.91  E-value: 1.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   85 LGWCIELLQAYFLVADDMMDKSITRRGQPCWYKV--PEVGEIAINDAFMLEAAIYKLLKSHFRnekyyIDITELFHEVTF 162
Cdd:cd00385  15 LRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaIDGLPEAILAGDLLLADAFEELAREGS-----PEALEILAEALL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  163 QTELGQLMDLITAPEdkvdlSKFSLKKHSFIVTFKTAYYSFYLPVALAMYVAGitDEKDLKQARDVLIPLGEYFQIQDDY 242
Cdd:cd00385  90 DLLEGQLLDLKWRRE-----YVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGG--EAELLEALRKLGRALGLAFQLTNDL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  243 LDCFGTPEQIgkigtdiqDNKCSWVINKALELASAEQRKTLDENYGkkdsvAEAKCKKIFNDLkIEQLYHEYEESIAKDL 322
Cdd:cd00385 163 LDYEGDAERG--------EGKCTLPVLYALEYGVPAEDLLLVEKSG-----SLEEALEELAKL-AEEALKELNELILSLP 228


                ...
gi 6322294  323 KAK 325
Cdd:cd00385 229 DVP 231
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
 89-352 9.44e-31

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: 118.79  E-value: 9.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294   89 IELLQAYFLVADDMMDKSITRRGQPC----WykvpevGE-IAIN--DaFMLEAAiYKLLkSHFRNEKYYIDITELFHEVT 161
Cdd:COG0142  74 VELIHTASLVHDDVMDDDDLRRGKPTvharF------GEaTAILagD-ALLALA-FELL-AELGDPERRLRALRILARAA 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  162 FQTELGQLMDLitAPEDKVDLSkfsLKKHSFIVTFKTAYYsFYLPVALAMYVAGiTDEKDLKQARDVLIPLGEYFQIQDD 241
Cdd:COG0142 145 RGMCEGQALDL--EAEGRLDVT---LEEYLRVIRLKTAAL-FAAALRLGAILAG-ADEEQVEALRRYGRNLGLAFQIRDD 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322294  242 YLDCFGTPEQIGK-IGTDIQDNKCSWVINKALELASAEQRKTLDENYGKKDSVAE--AKCKKIFNDLKIEqlyhEYEESI 318
Cdd:COG0142 218 ILDVTGDPEVLGKpAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDLDEEdlAEVRALLRESGAL----EYAREL 293

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6322294  319 AKDL--KAK--ISQVDESRGfkADVLTAFLNKVYKRSK 352
Cdd:COG0142 294 ARELaeEALaaLAALPDSEA--REALRALADYVVERDR 329
 
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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