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Conserved domains on  [gi|1063729094|ref|NP_001318758|]
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Terpenoid cyclases/Protein prenyltransferases superfamily protein [Arabidopsis thaliana]

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 ...
3-335 2.95e-131

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 cd00684:

Pssm-ID: 469660 [Multi-domain]  Cd Length: 542  Bit Score: 385.01  E-value: 2.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094   3 REYIQFYEQETHHDETLLKFAKINFKFMQLHYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVAR 82
Cdd:cd00684   205 RWYIEFYEQEDDHNETLLELAKLDFNILQALHQEELKILSRWWKDLDLASKLP-FARDRLVECYFWAAGTYFEPQYSLAR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  83 IILSKSLVLWTIIDDLYDAYCTLPEAIAFTENMERWETDAIDM-PDHMKVLLRSLIDLMEDFKGEVRSEGRLYSVEYGID 161
Cdd:cd00684   284 IALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAIDQlPEYMKIVFKALLNTVNEIEEELLKEGGSYVVPYLKE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 162 EWKRLFRADLTISKWARTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDV 240
Cdd:cd00684   364 AWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDiLTEEAFEWLESRPKLVRASSTIGRLMNDI 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 241 ATYKDEMARGEIATGINCYMKQYKVTEEEAFLEFHRRIKHTSKLVNEEYFK--TTVPLKLVRIAFNVGRVIDTNYKHGDG 318
Cdd:cd00684   444 ATYEDEMKRGDVASSIECYMKEYGVSEEEAREEIKKMIEDAWKELNEEFLKpsSDVPRPIKQRFLNLARVIDVFYKEGDG 523
                         330
                  ....*....|....*...
gi 1063729094 319 LTY-TGIVGGQITSLFLD 335
Cdd:cd00684   524 FTHpEGEIKDHITSLLFE 541
 
Name Accession Description Interval E-value
Terpene_cyclase_plant_C1 cd00684
Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene ...
3-335 2.95e-131

Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene cyclases (Tspa-Tspf) that convert the acyclic isoprenoid diphosphates, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) into cyclic monoterpenes, diterpenes, or sesquiterpenes, respectively; a few form acyclic species. Terpnoid cyclases are soluble enzymes localized to the cytosol (sesquiterpene synthases) or plastids (mono- and diterpene synthases). All monoterpene and diterpene synthases have restrict substrate specificity, however, some sesquiterpene synthases can accept both FPP and GPP. 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 diphosphates, via bridging Mg2+ ions (K+ preferred by gymnosperm cyclases), inducing conformational changes such that an N-terminal region forms a cap over the catalytic core. Loss of diphosphate from the enzyme-bound substrate (GPP, FPP, or GGPP) results in an allylic carbocation that electrophilically attacks a double bond further down the terpene chain to effect the first ring closure. Unlike monoterpene, sesquiterene, and macrocyclic diterpenes synthases, which undergo substrate ionization by diphosphate ester scission, Tpsc-like diterpene synthases catalyze cyclization reactions by an initial protonation step producing a copalyl diphosphate intermediate. These enzymes lack the aspartate-rich sequences mentioned above. Most diterpene synthases have an N-terminal, internal element (approx 210 aa) whose function is unknown.


Pssm-ID: 173832 [Multi-domain]  Cd Length: 542  Bit Score: 385.01  E-value: 2.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094   3 REYIQFYEQETHHDETLLKFAKINFKFMQLHYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVAR 82
Cdd:cd00684   205 RWYIEFYEQEDDHNETLLELAKLDFNILQALHQEELKILSRWWKDLDLASKLP-FARDRLVECYFWAAGTYFEPQYSLAR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  83 IILSKSLVLWTIIDDLYDAYCTLPEAIAFTENMERWETDAIDM-PDHMKVLLRSLIDLMEDFKGEVRSEGRLYSVEYGID 161
Cdd:cd00684   284 IALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAIDQlPEYMKIVFKALLNTVNEIEEELLKEGGSYVVPYLKE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 162 EWKRLFRADLTISKWARTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDV 240
Cdd:cd00684   364 AWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDiLTEEAFEWLESRPKLVRASSTIGRLMNDI 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 241 ATYKDEMARGEIATGINCYMKQYKVTEEEAFLEFHRRIKHTSKLVNEEYFK--TTVPLKLVRIAFNVGRVIDTNYKHGDG 318
Cdd:cd00684   444 ATYEDEMKRGDVASSIECYMKEYGVSEEEAREEIKKMIEDAWKELNEEFLKpsSDVPRPIKQRFLNLARVIDVFYKEGDG 523
                         330
                  ....*....|....*...
gi 1063729094 319 LTY-TGIVGGQITSLFLD 335
Cdd:cd00684   524 FTHpEGEIKDHITSLLFE 541
Terpene_synth_C pfam03936
Terpene synthase family, metal binding domain; It has been suggested that this gene family be ...
20-283 2.35e-113

Terpene synthase family, metal binding domain; It has been suggested that this gene family be designated tps (for terpene synthase). It has been split into six subgroups on the basis of phylogeny, called tpsa-tpsf. tpsa includes vetispiridiene synthase, 5-epi- aristolochene synthase, and (+)-delta-cadinene synthase. tpsb includes (-)-limonene synthase. tpsc includes kaurene synthase A. tpsd includes taxadiene synthase, pinene synthase, and myrcene synthase. tpse includes kaurene synthase B. tpsf includes linalool synthase.


Pssm-ID: 461096 [Multi-domain]  Cd Length: 266  Bit Score: 329.48  E-value: 2.35e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  20 LKFAKINFKFMQLHYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVARIILSKSLVLWTIIDDLY 99
Cdd:pfam03936   1 LELAKLDFNLLQSLHQKELKELTRWWKELGLASKLP-FARDRLVECYFWALGVYFEPQYSRARIILAKVIVLITIIDDTY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 100 DAYCTLPEAIAFTENMERWETDAID-MPDHMKVLLRSLIDLMEDFKGEVRSeGRLYSVE-YGIDEWKRLFRADLTISKWA 177
Cdd:pfam03936  80 DVYGTLEELELLTEAVERWDESAIEqLPEYMKICFKALLNTFNEIEEELSK-GKGYNVIpYLKEAWKDLVKAYLQEAKWR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 178 RTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDVATYKDEMARGEIATGI 256
Cdd:pfam03936 159 HEGYVPTFEEYLENGVVSSGYPLLLLHSFVGMGDlITKEAFEWLKSYPKIVRASSTIGRLLNDIATYEDEQERGGVASSV 238
                         250       260
                  ....*....|....*....|....*..
gi 1063729094 257 NCYMKQYKVTEEEAFLEFHRRIKHTSK 283
Cdd:pfam03936 239 ECYMKEHGVSEEEAREEIRKLIEDAWK 265
PLN02279 PLN02279
ent-kaur-16-ene synthase
19-320 1.51e-16

ent-kaur-16-ene synthase


Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 80.70  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  19 LLKFAKINFKFMQLHYVQELQTIVKWWKELDLESKipNYYRVRAVECLYWAMAVYMEPQYSVARIILSKSLVLWTIIDDL 98
Cdd:PLN02279  455 FLKLAVEDFNFCQSIHREELKQLERWIVENRLDKL--KFARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDF 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  99 YDAYCTLPEAIAFTENMERWETDAID--MPDHMKVLLRSLIDLMEDFkGEVRSEGRLYSVEYG-IDEWKRLFRADLTISK 175
Cdd:PLN02279  533 FDVGGSEEELENLIQLVEKWDVNGSPdfCSEQVEIIFSALRSTISEI-GDKAFTWQGRNVTSHiIKIWLDLLKSMLTEAQ 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 176 WARTGYIPNYDEYMEVGIVTG--GVDVTVAFAFIGMGEAGKEAFDwirsrPKFIQTIDLKS---RLRDDVATYKDEMARG 250
Cdd:PLN02279  612 WSSNKSTPTLDEYMTNAYVSFalGPIVLPALYLVGPKLSEEVVDS-----PELHKLYKLMStcgRLLNDIRGFKRESKEG 686
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063729094 251 EiATGINCYMKQYK--VTEEEAFLEF----HRRIKHTSKLVNEEYfKTTVPLKLVRIAFNVGRVIDTNYKHGDGLT 320
Cdd:PLN02279  687 K-LNAVSLHMIHGNgnSTEEEAIESMkgliESQRRELLRLVLQEK-GSNVPRECKDLFWKMSKVLHLFYRKDDGFT 760
 
Name Accession Description Interval E-value
Terpene_cyclase_plant_C1 cd00684
Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene ...
3-335 2.95e-131

Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene cyclases (Tspa-Tspf) that convert the acyclic isoprenoid diphosphates, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) into cyclic monoterpenes, diterpenes, or sesquiterpenes, respectively; a few form acyclic species. Terpnoid cyclases are soluble enzymes localized to the cytosol (sesquiterpene synthases) or plastids (mono- and diterpene synthases). All monoterpene and diterpene synthases have restrict substrate specificity, however, some sesquiterpene synthases can accept both FPP and GPP. 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 diphosphates, via bridging Mg2+ ions (K+ preferred by gymnosperm cyclases), inducing conformational changes such that an N-terminal region forms a cap over the catalytic core. Loss of diphosphate from the enzyme-bound substrate (GPP, FPP, or GGPP) results in an allylic carbocation that electrophilically attacks a double bond further down the terpene chain to effect the first ring closure. Unlike monoterpene, sesquiterene, and macrocyclic diterpenes synthases, which undergo substrate ionization by diphosphate ester scission, Tpsc-like diterpene synthases catalyze cyclization reactions by an initial protonation step producing a copalyl diphosphate intermediate. These enzymes lack the aspartate-rich sequences mentioned above. Most diterpene synthases have an N-terminal, internal element (approx 210 aa) whose function is unknown.


Pssm-ID: 173832 [Multi-domain]  Cd Length: 542  Bit Score: 385.01  E-value: 2.95e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094   3 REYIQFYEQETHHDETLLKFAKINFKFMQLHYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVAR 82
Cdd:cd00684   205 RWYIEFYEQEDDHNETLLELAKLDFNILQALHQEELKILSRWWKDLDLASKLP-FARDRLVECYFWAAGTYFEPQYSLAR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  83 IILSKSLVLWTIIDDLYDAYCTLPEAIAFTENMERWETDAIDM-PDHMKVLLRSLIDLMEDFKGEVRSEGRLYSVEYGID 161
Cdd:cd00684   284 IALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAIDQlPEYMKIVFKALLNTVNEIEEELLKEGGSYVVPYLKE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 162 EWKRLFRADLTISKWARTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDV 240
Cdd:cd00684   364 AWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDiLTEEAFEWLESRPKLVRASSTIGRLMNDI 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 241 ATYKDEMARGEIATGINCYMKQYKVTEEEAFLEFHRRIKHTSKLVNEEYFK--TTVPLKLVRIAFNVGRVIDTNYKHGDG 318
Cdd:cd00684   444 ATYEDEMKRGDVASSIECYMKEYGVSEEEAREEIKKMIEDAWKELNEEFLKpsSDVPRPIKQRFLNLARVIDVFYKEGDG 523
                         330
                  ....*....|....*...
gi 1063729094 319 LTY-TGIVGGQITSLFLD 335
Cdd:cd00684   524 FTHpEGEIKDHITSLLFE 541
Terpene_synth_C pfam03936
Terpene synthase family, metal binding domain; It has been suggested that this gene family be ...
20-283 2.35e-113

Terpene synthase family, metal binding domain; It has been suggested that this gene family be designated tps (for terpene synthase). It has been split into six subgroups on the basis of phylogeny, called tpsa-tpsf. tpsa includes vetispiridiene synthase, 5-epi- aristolochene synthase, and (+)-delta-cadinene synthase. tpsb includes (-)-limonene synthase. tpsc includes kaurene synthase A. tpsd includes taxadiene synthase, pinene synthase, and myrcene synthase. tpse includes kaurene synthase B. tpsf includes linalool synthase.


Pssm-ID: 461096 [Multi-domain]  Cd Length: 266  Bit Score: 329.48  E-value: 2.35e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  20 LKFAKINFKFMQLHYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVARIILSKSLVLWTIIDDLY 99
Cdd:pfam03936   1 LELAKLDFNLLQSLHQKELKELTRWWKELGLASKLP-FARDRLVECYFWALGVYFEPQYSRARIILAKVIVLITIIDDTY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 100 DAYCTLPEAIAFTENMERWETDAID-MPDHMKVLLRSLIDLMEDFKGEVRSeGRLYSVE-YGIDEWKRLFRADLTISKWA 177
Cdd:pfam03936  80 DVYGTLEELELLTEAVERWDESAIEqLPEYMKICFKALLNTFNEIEEELSK-GKGYNVIpYLKEAWKDLVKAYLQEAKWR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 178 RTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDVATYKDEMARGEIATGI 256
Cdd:pfam03936 159 HEGYVPTFEEYLENGVVSSGYPLLLLHSFVGMGDlITKEAFEWLKSYPKIVRASSTIGRLLNDIATYEDEQERGGVASSV 238
                         250       260
                  ....*....|....*....|....*..
gi 1063729094 257 NCYMKQYKVTEEEAFLEFHRRIKHTSK 283
Cdd:pfam03936 239 ECYMKEHGVSEEEAREEIRKLIEDAWK 265
Terpene_cyclase_C1 cd00868
Terpene cyclases, Class 1; Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid ...
33-313 1.27e-89

Terpene cyclases, Class 1; Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid biosynthesis enzymes, which share the 'isoprenoid synthase fold' and convert linear, all-trans, isoprenoids, geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate into numerous cyclic forms of monoterpenes, diterpenes, and sesquiterpenes. Also included in this CD are the cis-trans terpene cyclases such as trichodiene synthase. 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. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD. Taxonomic distribution includes bacteria, fungi and plants.


Pssm-ID: 173837 [Multi-domain]  Cd Length: 284  Bit Score: 270.01  E-value: 1.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  33 HYVQELQTIVKWWKELDLESKIPnYYRVRAVECLYWAMAVYMEPQYSVARIILSKSLVLWTIIDDLYDAYCTLPEAIAFT 112
Cdd:cd00868     1 LHQEELKELSRWWKELGLQEKLP-FARDRLVECYFWAAGSYFEPQYSEARIALAKTIALLTVIDDTYDDYGTLEELELFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 113 ENMERWETDAID-MPDHMKVLLRSLIDLMEDFKGEVRSEGRLYSVEYGIDEWKRLFRADLTISKWARTGYIPNYDEYMEV 191
Cdd:cd00868    80 EAVERWDISAIDeLPEYMKPVFKALYDLVNEIEEELAKEGGSESLPYLKEAWKDLLRAYLVEAKWANEGYVPSFEEYLEN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 192 GIVTGGVDVTVAFAFIGMGE-AGKEAFDWIRSRPKFIQTIDLKSRLRDDVATYKDEMARGEIATGINCYMKQYKVTEEEA 270
Cdd:cd00868   160 RRVSIGYPPLLALSFLGMGDiLPEEAFEWLPSYPKLVRASSTIGRLLNDIASYEKEIARGEVANSVECYMKEYGVSEEEA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1063729094 271 FLEFHRRIKHTSKLVNEEYFKTT--VPLKLVRIAFNVGRVIDTNY 313
Cdd:cd00868   240 LEELRKMIEEAWKELNEEVLKLSsdVPRAVLETLLNLARGIYVWY 284
Terpene_syn_C_2 pfam19086
Terpene synthase family 2, C-terminal metal binding;
87-281 1.18e-43

Terpene synthase family 2, C-terminal metal binding;


Pssm-ID: 465972 [Multi-domain]  Cd Length: 199  Bit Score: 148.90  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  87 KSLVLWTIIDDLYDA-YCTLPEAIAFTENMERW----ETDAIDMPDHMKVLLRSLIDLMEdfkgEVRSEGRLYSVEYGID 161
Cdd:pfam19086   1 KWLAWLFILDDIYDEvYGTLEELELFTEAIERWdallPLDGPELPEYMKPLYRALADLWE----RLAKEASPDWRRRFKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 162 EWKRLFRADLTISKWARTGYIPNYDEYMEVGIVTGGVDVTVAFAFIGMG-EAGKEAFDWIRSRPKFIQTIDLkSRLRDDV 240
Cdd:pfam19086  77 AWKDYLDAYLWEAKWRASGYVPTLEEYLELRRVTSGVPPLLALIEFGLGiELPDEVFEHPVVRRLVRAASDI-VRLVNDL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063729094 241 ATYKDEMARGEIATGINCYMKQYKVTEEEAFLEFHRRIKHT 281
Cdd:pfam19086 156 FSYKKEQARGDVHNLVLVLMKEYGVSLQEAVDEVGELIEEA 196
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
67-307 1.55e-26

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: 105.27  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  67 YWAMAVYMEPQYSVARIILSKSLVLWTIIDDLYDAYCTLPEAIAFTENMERWetdaiDMPDHMKVLLRSLIDLMEdfkgE 146
Cdd:cd00385     1 FRPLAVLLEPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAID-----GLPEAILAGDLLLADAFE----E 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 147 VRSEGRLYSVEYGIDEWKRLFRADLTISKWARTgYIPNYDEYMEVGIVTGGVdVTVAFAFIGMGEAGKEaFDWIRSRPKF 226
Cdd:cd00385    72 LAREGSPEALEILAEALLDLLEGQLLDLKWRRE-YVPTLEEYLEYCRYKTAG-LVGALCLLGAGLSGGE-AELLEALRKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 227 IQTIDLKSRLRDDVATYKDEMARGE-IATGINCYMKQYKV------------TEEEAFLEFHRRIKHTSKLVNEEYFK-T 292
Cdd:cd00385   149 GRALGLAFQLTNDLLDYEGDAERGEgKCTLPVLYALEYGVpaedlllveksgSLEEALEELAKLAEEALKELNELILSlP 228
                         250
                  ....*....|....*
gi 1063729094 293 TVPLKLVRIAFNVGR 307
Cdd:cd00385   229 DVPRALLALALNLYR 243
PLN02279 PLN02279
ent-kaur-16-ene synthase
19-320 1.51e-16

ent-kaur-16-ene synthase


Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 80.70  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  19 LLKFAKINFKFMQLHYVQELQTIVKWWKELDLESKipNYYRVRAVECLYWAMAVYMEPQYSVARIILSKSLVLWTIIDDL 98
Cdd:PLN02279  455 FLKLAVEDFNFCQSIHREELKQLERWIVENRLDKL--KFARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDF 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  99 YDAYCTLPEAIAFTENMERWETDAID--MPDHMKVLLRSLIDLMEDFkGEVRSEGRLYSVEYG-IDEWKRLFRADLTISK 175
Cdd:PLN02279  533 FDVGGSEEELENLIQLVEKWDVNGSPdfCSEQVEIIFSALRSTISEI-GDKAFTWQGRNVTSHiIKIWLDLLKSMLTEAQ 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 176 WARTGYIPNYDEYMEVGIVTG--GVDVTVAFAFIGMGEAGKEAFDwirsrPKFIQTIDLKS---RLRDDVATYKDEMARG 250
Cdd:PLN02279  612 WSSNKSTPTLDEYMTNAYVSFalGPIVLPALYLVGPKLSEEVVDS-----PELHKLYKLMStcgRLLNDIRGFKRESKEG 686
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063729094 251 EiATGINCYMKQYK--VTEEEAFLEF----HRRIKHTSKLVNEEYfKTTVPLKLVRIAFNVGRVIDTNYKHGDGLT 320
Cdd:PLN02279  687 K-LNAVSLHMIHGNgnSTEEEAIESMkgliESQRRELLRLVLQEK-GSNVPRECKDLFWKMSKVLHLFYRKDDGFT 760
PLN02150 PLN02150
terpene synthase/cyclase family protein
247-334 1.63e-14

terpene synthase/cyclase family protein


Pssm-ID: 177811 [Multi-domain]  Cd Length: 96  Bit Score: 68.34  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 247 MARGEIATGINCYMKQYKVTEEEAFLEFHRRIKHTSKLVNEEYFKTT-VPLKLVRIAFNVGRVIDT-NYKHGDGLTYT-G 323
Cdd:PLN02150    1 MRRGEVANGVNCYMKQHGVTKEEAVSELKKMIRDNYKIVMEEFLTIKdVPRPVLVRCLNLARLIDVyCYNEGDGFTYPhG 80
                          90
                  ....*....|.
gi 1063729094 324 IVGGQITSLFL 334
Cdd:PLN02150   81 KLKDLITSLFF 91
Terpene_cyclase_nonplant_C1 cd00687
Non-plant Terpene Cyclases, Class 1; This CD includes terpenoid cyclases such as pentalenene ...
45-273 2.46e-07

Non-plant Terpene Cyclases, Class 1; This CD includes terpenoid cyclases such as pentalenene synthase and aristolochene synthase which, using an all-trans pathway, catalyze the ionization of farnesyl diphosphate, followed by the formation of a macrocyclic intermediate by bond formation between C1 with either C10 (aristolochene synthase) or C11 (pentalenene synthase), resulting in production of tricyclic hydrocarbon pentalenene or bicyclic hydrocarbon aristolochene. As with other enzymes with the 'terpenoid synthase fold', they have two conserved metal binding motifs, proposed to coordinate Mg2+ ion-bridged binding of the diphosphate moiety of FPP to the enzymes. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function in the monomeric form and are found in fungi, bacteria and Dictyostelium.


Pssm-ID: 173835 [Multi-domain]  Cd Length: 303  Bit Score: 51.60  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094  45 WKELDLESKIPNYyrvravECLYWamavymePQYSVARIILSKSLVLW-TIIDDLYD-AYCTLPEAIAFTENMER-WETD 121
Cdd:cd00687    34 AEKRFLSADFGDL------AALFY-------PDADDERLMLAADLMAWlFVFDDLLDrDQKSPEDGEAGVTRLLDiLRGD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729094 122 AIDMPDHMKVLLRSLIDLMEDFKGEVRSEGRLYSVEYgideWKRLFRADLTISKWARTGYIPNYDEYMEVGIVTGGVDVT 201
Cdd:cd00687   101 GLDSPDDATPLEFGLADLWRRTLARMSAEWFNRFAHY----TEDYFDAYIWEGKNRLNGHVPDVAEYLEMRRFNIGADPC 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063729094 202 VAFAFIGMgeaGKEAFDWIRSRPKFIQTIDLKSR---LRDDVATY-KDEMARGEIATGINCYMKQYKVTEEEAFLE 273
Cdd:cd00687   177 LGLSEFIG---GPEVPAAVRLDPVMRALEALASDaiaLVNDIYSYeKEIKANGEVHNLVKVLAEEHGLSLEEAISV 249
 
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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