NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622829926|ref|XP_028684048|]
View 

farnesyl pyrophosphate synthase isoform X3 [Macaca mulatta]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
42-310 3.99e-95

Polyprenyl synthetase;


:

Pssm-ID: 459773  Cd Length: 251  Bit Score: 283.24  E-value: 3.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  42 IARLKEVLEYNA-IGGKYHRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQIC 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVEL---LHAASLVHDDIMDNSDLRRGQPT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 121 WYQKPGVGLdAINDAILLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLITAPQGNVDLgrfTEKRYKSIV 200
Cdd:pfam00348  73 WHRIFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 201 KYKTAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-VGTDIQDNKCSWLVVQCLQ 279
Cdd:pfam00348 145 KYKTA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGKCTWPVIHALE 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622829926 280 RaTPEQYQILKENYGQKeAEKVARVKALYEE 310
Cdd:pfam00348 223 R-TPEQRKILLEIYGKR-PEDVEKVKEAYEL 251
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
42-310 3.99e-95

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 283.24  E-value: 3.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  42 IARLKEVLEYNA-IGGKYHRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQIC 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVEL---LHAASLVHDDIMDNSDLRRGQPT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 121 WYQKPGVGLdAINDAILLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLITAPQGNVDLgrfTEKRYKSIV 200
Cdd:pfam00348  73 WHRIFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 201 KYKTAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-VGTDIQDNKCSWLVVQCLQ 279
Cdd:pfam00348 145 KYKTA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGKCTWPVIHALE 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622829926 280 RaTPEQYQILKENYGQKeAEKVARVKALYEE 310
Cdd:pfam00348 223 R-TPEQRKILLEIYGKR-PEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
40-354 4.52e-71

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: 222.04  E-value: 4.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  40 DAIARLKEVLEYN-AIGGKYHRGLTVVVAFRELVEPRkqdadsLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQ 118
Cdd:cd00685     1 SEVELLREALRYLlLAGGKRLRPLLVLLAARALGGPE------LEAALRLAAAIEL---LHTASLVHDDVMDNSDLRRGK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 119 ICWYQKPGVGLdAINDAILLEACIYRLLKLYCReqPYYLNLIELFLQSSYQTEIGQTLDLITAPQGNvdlgrFTEKRYKS 198
Cdd:cd00685    72 PTVHKVFGNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYDTD-----VTEEEYLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 199 IVKYKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-VGTDIQDNKCSWLVVQC 277
Cdd:cd00685   144 IIRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLA 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622829926 278 lqratpeqyqilkenygqkeaekvarvkalyeeldLQAVFLQYEEDSYSHIMALIEQYAAPLppaiFLGLARKIYKR 354
Cdd:cd00685   222 -----------------------------------LRELAREYEEKALEALKALPESPAREA----LRALADFILER 259
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
40-356 7.21e-30

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: 116.48  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  40 DAIARLKEVLEY--NAiGGKYHRGLTVVVAFRELveprkqdADSLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRG 117
Cdd:COG0142    28 SEPPLLAEAMRYllLA-GGKRLRPLLVLLAARAL-------GGDPEAALRAAAAVEL---IHTASLVHDDVMDDDDLRRG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 118 qicwyqKP------GVGLdAIN--DAILLEAciYRLLkLYCREQPYYLNLIELFLQSSYQTEIGQTLDLITAPQGNVdlg 189
Cdd:COG0142    97 ------KPtvharfGEAT-AILagDALLALA--FELL-AELGDPERRLRALRILARAARGMCEGQALDLEAEGRLDV--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 190 rfTEKRYKSIVKYKTAFYsfylpIAAAMYMAGI--DGEKEHANAkkilleMGEF-------FQIQDDYLDLFGDPSVTGK 260
Cdd:COG0142   164 --TLEEYLRVIRLKTAAL-----FAAALRLGAIlaGADEEQVEA------LRRYgrnlglaFQIRDDILDVTGDPEVLGK 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 261 -VGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKE--AEKVARVKALYEELdlqavflqyeeDSYSHIMALIEQYA- 336
Cdd:COG0142   231 pAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRES-----------GALEYARELARELAe 299
                         330       340       350
                  ....*....|....*....|....*....|
gi 1622829926 337 ------APLPP----AIFLGLARKIYKRKK 356
Cdd:COG0142   300 ealaalAALPDsearEALRALADYVVERDR 329
 
Name Accession Description Interval E-value
polyprenyl_synt pfam00348
Polyprenyl synthetase;
42-310 3.99e-95

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 283.24  E-value: 3.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  42 IARLKEVLEYNA-IGGKYHRGLTVVVAFRELVEPrkqdaDSLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQIC 120
Cdd:pfam00348   1 EKLLYEPLDYLVsAGGKRIRPLLVLLSAEALGGP-----EDLEKAIVLAWAVEL---LHAASLVHDDIMDNSDLRRGQPT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 121 WYQKPGVGLdAINDAILLEACIYRLLKLYCReqpyYLNLIELFLQSSYQTEIGQTLDLITAPQGNVDLgrfTEKRYKSIV 200
Cdd:pfam00348  73 WHRIFGNAI-AINDGDYLYALAFQLLAKLFP----NPELLELFSEVTLQTAEGQGLDLLWRNDDDLSC---TEEEYLEIV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 201 KYKTAfYSFYLPIAAAMYMAGIDgEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-VGTDIQDNKCSWLVVQCLQ 279
Cdd:pfam00348 145 KYKTA-YLFALAVKLGAILSGAD-DEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKpAGTDITEGKCTWPVIHALE 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622829926 280 RaTPEQYQILKENYGQKeAEKVARVKALYEE 310
Cdd:pfam00348 223 R-TPEQRKILLEIYGKR-PEDVEKVKEAYEL 251
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
40-354 4.52e-71

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: 222.04  E-value: 4.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  40 DAIARLKEVLEYN-AIGGKYHRGLTVVVAFRELVEPRkqdadsLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQ 118
Cdd:cd00685     1 SEVELLREALRYLlLAGGKRLRPLLVLLAARALGGPE------LEAALRLAAAIEL---LHTASLVHDDVMDNSDLRRGK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 119 ICWYQKPGVGLdAINDAILLEACIYRLLKLYCReqPYYLNLIELFLQSSYQTEIGQTLDLITAPQGNvdlgrFTEKRYKS 198
Cdd:cd00685    72 PTVHKVFGNAT-AILAGDYLLARAFELLARLGN--PYYPRALELFSEAILELVEGQLLDLLSEYDTD-----VTEEEYLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 199 IVKYKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK-VGTDIQDNKCSWLVVQC 277
Cdd:cd00685   144 IIRLKTAALFAAAPLLGALLAGA--DEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKpVGSDLREGKCTLPVLLA 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622829926 278 lqratpeqyqilkenygqkeaekvarvkalyeeldLQAVFLQYEEDSYSHIMALIEQYAAPLppaiFLGLARKIYKR 354
Cdd:cd00685   222 -----------------------------------LRELAREYEEKALEALKALPESPAREA----LRALADFILER 259
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
60-354 2.87e-50

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: 167.91  E-value: 2.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  60 RGLTVVVAFRELVEPrkqdadsLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQICWYQKPGVGLDAINDAILLE 139
Cdd:cd00867     2 RPLLVLLLARALGGD-------LEAALRLAAAVEL---LHAASLVHDDIVDDSDLRRGKPTAHLRRFGNALAILAGDYLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 140 ACIYRLLKLYCreqpyYLNLIELFLQSSYQTEIGQTLDLITAPQGNvdlgrFTEKRYKSIVKYKTAFYSFYLPIAAAMYM 219
Cdd:cd00867    72 ARAFQLLARLG-----YPRALELFAEALRELLEGQALDLEFERDTY-----ETLDEYLEYCRYKTAGLVGLLCLLGAGLS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 220 AGIDgeKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLQRAtpeqyqilkenygqkeae 299
Cdd:cd00867   142 GADD--EQAEALKDYGRALGLAFQLTDDLLDVFGDAEELGKVGSDLREGRITLPVILARERA------------------ 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622829926 300 kvarvkalyeeldlqavfLQYEEDSYSHIMALIEQyaAPLPPAIFLGLARKIYKR 354
Cdd:cd00867   202 ------------------AEYAEEAYAALEALPPS--LPRARRALIALADFLYRR 236
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
84-353 4.72e-31

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: 117.60  E-value: 4.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  84 RAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRGQICWYQK--PGVGLDAINDAILLEACIYRLLklycrEQPYYLNLIE 161
Cdd:cd00385    11 EASRLRAAVEK---LHAASLVHDDIVDDSGTRRGLPTAHLAvaIDGLPEAILAGDLLLADAFEEL-----AREGSPEALE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 162 LFLQSSYQTEIGQTLDLITAPQGNvdlgrFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGidGEKEHANAKKILLEMGEF 241
Cdd:cd00385    83 ILAEALLDLLEGQLLDLKWRREYV-----PTLEEYLEYCRYKTAGLVGALCLLGAGLSGG--EAELLEALRKLGRALGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 242 FQIQDDYLDLFGDPSVTgkvgtdiqDNKCSWLVVQCLQRATPEQYQILkenygqkeaekvarVKALYEELDLQAVFLQYE 321
Cdd:cd00385   156 FQLTNDLLDYEGDAERG--------EGKCTLPVLYALEYGVPAEDLLL--------------VEKSGSLEEALEELAKLA 213
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1622829926 322 EDSYSHIMALIEQyaAPLPPAIFLGLARKIYK 353
Cdd:cd00385   214 EEALKELNELILS--LPDVPRALLALALNLYR 243
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
40-356 7.21e-30

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: 116.48  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926  40 DAIARLKEVLEY--NAiGGKYHRGLTVVVAFRELveprkqdADSLQRAWTVGWCVELvrgLQAFFLVTDDIMDSSLTRRG 117
Cdd:COG0142    28 SEPPLLAEAMRYllLA-GGKRLRPLLVLLAARAL-------GGDPEAALRAAAAVEL---IHTASLVHDDVMDDDDLRRG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 118 qicwyqKP------GVGLdAIN--DAILLEAciYRLLkLYCREQPYYLNLIELFLQSSYQTEIGQTLDLITAPQGNVdlg 189
Cdd:COG0142    97 ------KPtvharfGEAT-AILagDALLALA--FELL-AELGDPERRLRALRILARAARGMCEGQALDLEAEGRLDV--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 190 rfTEKRYKSIVKYKTAFYsfylpIAAAMYMAGI--DGEKEHANAkkilleMGEF-------FQIQDDYLDLFGDPSVTGK 260
Cdd:COG0142   164 --TLEEYLRVIRLKTAAL-----FAAALRLGAIlaGADEEQVEA------LRRYgrnlglaFQIRDDILDVTGDPEVLGK 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829926 261 -VGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKE--AEKVARVKALYEELdlqavflqyeeDSYSHIMALIEQYA- 336
Cdd:COG0142   231 pAGSDLREGKPTLPLLLALERADPEERAELRELLGKPDldEEDLAEVRALLRES-----------GALEYARELARELAe 299
                         330       340       350
                  ....*....|....*....|....*....|
gi 1622829926 337 ------APLPP----AIFLGLARKIYKRKK 356
Cdd:COG0142   300 ealaalAALPDsearEALRALADYVVERDR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH