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Conserved domains on  [gi|1063723030|ref|NP_001329376|]
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terpene synthase 03 [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 ...
26-340 4.42e-138

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: 403.88  E-value: 4.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  26 RRSANYQPSLWQHEYLLSLGNTYVKEDN-VERVTLLKQEVSKMLNETEG---LLEQLELIDTLQRLGVSYHFEQEIKKTL 101
Cdd:cd00684     1 RPSANFPPSLWGDDHFLSLSSDYSEEDElEEEIEELKEEVRKMLEDSEYpvdLFERLWLIDRLQRLGISYHFEDEIKEIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 102 TNVHVKNVRAHKNRIDrnrwgDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLD-----DKDIKGILSLYEASYLSTRID 176
Cdd:cd00684    81 DYIYRYWTERGESNED-----DLYTTALGFRLLRQHGYNVSSDVFKKFKDEDGKfkeslTQDVKGMLSLYEASHLSFPGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 177 TKLKESIYYTTKRLRKFVEVNKNETKSytLRRMVIHALEMPYHRRVGRLEARWYIEVYGERHDMNPILLELAKLDFNFVQ 256
Cdd:cd00684   156 DILDEALSFTTKHLEEKLESNWIIDPD--LSGEIEYALEIPLHASLPRLEARWYIEFYEQEDDHNETLLELAKLDFNILQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 257 AIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFT 336
Cdd:cd00684   234 ALHQEELKILSRWWKDLDLASKLPFARDRLVECYFWAAGTYFEPQYSLARIALAKTIALITVIDDTYDVYGTLEELELFT 313

                  ....
gi 1063723030 337 TIVE 340
Cdd:cd00684   314 EAVE 317
 
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 ...
26-340 4.42e-138

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: 403.88  E-value: 4.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  26 RRSANYQPSLWQHEYLLSLGNTYVKEDN-VERVTLLKQEVSKMLNETEG---LLEQLELIDTLQRLGVSYHFEQEIKKTL 101
Cdd:cd00684     1 RPSANFPPSLWGDDHFLSLSSDYSEEDElEEEIEELKEEVRKMLEDSEYpvdLFERLWLIDRLQRLGISYHFEDEIKEIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 102 TNVHVKNVRAHKNRIDrnrwgDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLD-----DKDIKGILSLYEASYLSTRID 176
Cdd:cd00684    81 DYIYRYWTERGESNED-----DLYTTALGFRLLRQHGYNVSSDVFKKFKDEDGKfkeslTQDVKGMLSLYEASHLSFPGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 177 TKLKESIYYTTKRLRKFVEVNKNETKSytLRRMVIHALEMPYHRRVGRLEARWYIEVYGERHDMNPILLELAKLDFNFVQ 256
Cdd:cd00684   156 DILDEALSFTTKHLEEKLESNWIIDPD--LSGEIEYALEIPLHASLPRLEARWYIEFYEQEDDHNETLLELAKLDFNILQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 257 AIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFT 336
Cdd:cd00684   234 ALHQEELKILSRWWKDLDLASKLPFARDRLVECYFWAAGTYFEPQYSLARIALAKTIALITVIDDTYDVYGTLEELELFT 313

                  ....
gi 1063723030 337 TIVE 340
Cdd:cd00684   314 EAVE 317
Terpene_synth pfam01397
Terpene synthase, N-terminal domain; It has been suggested that this gene family be designated ...
35-214 2.24e-54

Terpene synthase, N-terminal 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: 460194 [Multi-domain]  Cd Length: 190  Bit Score: 177.40  E-value: 2.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  35 LWQHEYLLSLGNTYVK-----EDNVERVTLLKQEVSKMLNETEG-----LLEQLELIDTLQRLGVSYHFEQEIKKTLTNV 104
Cdd:pfam01397   1 DWGDHFLLSLSNGSLFnsptaEALMREAEDLKEEVRKMLKAVPTvypvdLKEKLELIDTLQRLGISYHFEKEIEEILDQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 105 HvknvRAHKNRIDRNRWGDLYATALEFRLLRQHGFSIAQDVF------DGNIGVDLDDkDIKGILSLYEASYLSTRIDTK 178
Cdd:pfam01397  81 Y----RNWEDDGIEDDDLDLYTTALAFRLLRQHGYDVSSDVFnkfkdeDGNFKECLSE-DVKGLLSLYEASHLSTPGEDI 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063723030 179 LKESIYYTTKRLRKFVeVNKNETKSYTLRRMVIHAL 214
Cdd:pfam01397 156 LDEALSFTRSHLKESL-AGNLGLISPHLAEEVEHAL 190
PLN02592 PLN02592
ent-copalyl diphosphate synthase
74-324 7.76e-30

ent-copalyl diphosphate synthase


Pssm-ID: 215321 [Multi-domain]  Cd Length: 800  Bit Score: 121.13  E-value: 7.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  74 LLEQLELIDTLQRLGVSYHFEQEIKKTLTNVH----------VKNVRAHknridrnrwgDLYATALEFRLLRQHGFSIAQ 143
Cdd:PLN02592  310 LFEHIWAVDRLQRLGISRYFEPEIKECIDYVHrywtengicwARNSHVH----------DIDDTAMGFRLLRLHGHQVSA 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 144 DVF-----DGNIG--VDLDDKDIKGILSLYEASYLSTRIDTKLKESIYYTTKRLRKFVEVNKNETKSYTLRRM---VIHA 213
Cdd:PLN02592  380 DVFkhfekGGEFFcfAGQSTQAVTGMFNLYRASQVLFPGEKILENAKEFSSKFLREKQEANELLDKWIIMKDLpgeVGFA 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 214 LEMPYHRRVGRLEARWYIEVYGERHDM-------------NPILLELAKLDFNFVQAIHQDELKSLSSWWSKTGLtKHLD 280
Cdd:PLN02592  460 LEIPWYASLPRVETRFYIEQYGGEDDVwigktlyrmpyvnNNEYLELAKLDYNNCQALHQLEWDNFQKWYEECNL-GEFG 538
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1063723030 281 FVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYD 324
Cdd:PLN02592  539 VSRSELLLAYFLAAASIFEPERSHERLAWAKTTVLVEAISSYFN 582
 
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 ...
26-340 4.42e-138

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: 403.88  E-value: 4.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  26 RRSANYQPSLWQHEYLLSLGNTYVKEDN-VERVTLLKQEVSKMLNETEG---LLEQLELIDTLQRLGVSYHFEQEIKKTL 101
Cdd:cd00684     1 RPSANFPPSLWGDDHFLSLSSDYSEEDElEEEIEELKEEVRKMLEDSEYpvdLFERLWLIDRLQRLGISYHFEDEIKEIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 102 TNVHVKNVRAHKNRIDrnrwgDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLD-----DKDIKGILSLYEASYLSTRID 176
Cdd:cd00684    81 DYIYRYWTERGESNED-----DLYTTALGFRLLRQHGYNVSSDVFKKFKDEDGKfkeslTQDVKGMLSLYEASHLSFPGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 177 TKLKESIYYTTKRLRKFVEVNKNETKSytLRRMVIHALEMPYHRRVGRLEARWYIEVYGERHDMNPILLELAKLDFNFVQ 256
Cdd:cd00684   156 DILDEALSFTTKHLEEKLESNWIIDPD--LSGEIEYALEIPLHASLPRLEARWYIEFYEQEDDHNETLLELAKLDFNILQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 257 AIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFT 336
Cdd:cd00684   234 ALHQEELKILSRWWKDLDLASKLPFARDRLVECYFWAAGTYFEPQYSLARIALAKTIALITVIDDTYDVYGTLEELELFT 313

                  ....
gi 1063723030 337 TIVE 340
Cdd:cd00684   314 EAVE 317
Terpene_synth pfam01397
Terpene synthase, N-terminal domain; It has been suggested that this gene family be designated ...
35-214 2.24e-54

Terpene synthase, N-terminal 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: 460194 [Multi-domain]  Cd Length: 190  Bit Score: 177.40  E-value: 2.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  35 LWQHEYLLSLGNTYVK-----EDNVERVTLLKQEVSKMLNETEG-----LLEQLELIDTLQRLGVSYHFEQEIKKTLTNV 104
Cdd:pfam01397   1 DWGDHFLLSLSNGSLFnsptaEALMREAEDLKEEVRKMLKAVPTvypvdLKEKLELIDTLQRLGISYHFEKEIEEILDQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 105 HvknvRAHKNRIDRNRWGDLYATALEFRLLRQHGFSIAQDVF------DGNIGVDLDDkDIKGILSLYEASYLSTRIDTK 178
Cdd:pfam01397  81 Y----RNWEDDGIEDDDLDLYTTALAFRLLRQHGYDVSSDVFnkfkdeDGNFKECLSE-DVKGLLSLYEASHLSTPGEDI 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063723030 179 LKESIYYTTKRLRKFVeVNKNETKSYTLRRMVIHAL 214
Cdd:pfam01397 156 LDEALSFTRSHLKESL-AGNLGLISPHLAEEVEHAL 190
Terpene_synth_C pfam03936
Terpene synthase family, metal binding domain; It has been suggested that this gene family be ...
245-341 3.00e-49

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: 166.54  E-value: 3.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 245 LELAKLDFNFVQAIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYD 324
Cdd:pfam03936   1 LELAKLDFNLLQSLHQKELKELTRWWKELGLASKLPFARDRLVECYFWALGVYFEPQYSRARIILAKVIVLITIIDDTYD 80
                          90
                  ....*....|....*..
gi 1063723030 325 IYGTLEELQLFTTIVEK 341
Cdd:pfam03936  81 VYGTLEELELLTEAVER 97
PLN02592 PLN02592
ent-copalyl diphosphate synthase
74-324 7.76e-30

ent-copalyl diphosphate synthase


Pssm-ID: 215321 [Multi-domain]  Cd Length: 800  Bit Score: 121.13  E-value: 7.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  74 LLEQLELIDTLQRLGVSYHFEQEIKKTLTNVH----------VKNVRAHknridrnrwgDLYATALEFRLLRQHGFSIAQ 143
Cdd:PLN02592  310 LFEHIWAVDRLQRLGISRYFEPEIKECIDYVHrywtengicwARNSHVH----------DIDDTAMGFRLLRLHGHQVSA 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 144 DVF-----DGNIG--VDLDDKDIKGILSLYEASYLSTRIDTKLKESIYYTTKRLRKFVEVNKNETKSYTLRRM---VIHA 213
Cdd:PLN02592  380 DVFkhfekGGEFFcfAGQSTQAVTGMFNLYRASQVLFPGEKILENAKEFSSKFLREKQEANELLDKWIIMKDLpgeVGFA 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 214 LEMPYHRRVGRLEARWYIEVYGERHDM-------------NPILLELAKLDFNFVQAIHQDELKSLSSWWSKTGLtKHLD 280
Cdd:PLN02592  460 LEIPWYASLPRVETRFYIEQYGGEDDVwigktlyrmpyvnNNEYLELAKLDYNNCQALHQLEWDNFQKWYEECNL-GEFG 538
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1063723030 281 FVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYD 324
Cdd:PLN02592  539 VSRSELLLAYFLAAASIFEPERSHERLAWAKTTVLVEAISSYFN 582
Terpene_cyclase_C1 cd00868
Terpene cyclases, Class 1; Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid ...
258-341 2.87e-28

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: 111.69  E-value: 2.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 258 IHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFTT 337
Cdd:cd00868     1 LHQEELKELSRWWKELGLQEKLPFARDRLVECYFWAAGSYFEPQYSEARIALAKTIALLTVIDDTYDDYGTLEELELFTE 80

                  ....
gi 1063723030 338 IVEK 341
Cdd:cd00868    81 AVER 84
PLN02279 PLN02279
ent-kaur-16-ene synthase
77-341 2.94e-28

ent-kaur-16-ene synthase


Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 116.53  E-value: 2.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030  77 QLELIDTLQRLGVSYHFEQEIKKTLTNVHVKNVRAhknriDRNRWGDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLDD 156
Cdd:PLN02279  273 RLSMVDTLERLGIDRHFRKEIKSVLDETYRYWLQG-----EEEIFLDLATCALAFRILRLNGYDVSSDPLKQFAEDHFSD 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 157 ------KDIKGILSLYEASYLSTRIDTKLKESIYYTTKRLRKfvEVNKNETKSYTLRRMVIH----ALEMPYHRRVGRLE 226
Cdd:PLN02279  348 slggylKDTGAVLELFRASQISYPDESLLEKQNSWTSHFLEQ--GLSNWSKTADRLRKYIKKevedALNFPYYANLERLA 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723030 227 ARWYIE------------VYGERHDMNPILLELAKLDFNFVQAIHQDELKSLSSWWSKTGLTKhLDFVRDRITEGYFSSV 294
Cdd:PLN02279  426 NRRSIEnyavddtrilktSYRCSNICNQDFLKLAVEDFNFCQSIHREELKQLERWIVENRLDK-LKFARQKLAYCYFSAA 504
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1063723030 295 GVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFTTIVEK 341
Cdd:PLN02279  505 ATLFSPELSDARLSWAKNGVLTTVVDDFFDVGGSEEELENLIQLVEK 551
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
291-340 6.54e-06

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: 47.10  E-value: 6.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063723030 291 FSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFTTIVE 340
Cdd:cd00385     1 FRPLAVLLEPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVA 50
Terpene_syn_C_2 pfam19086
Terpene synthase family 2, C-terminal metal binding;
311-342 5.19e-05

Terpene synthase family 2, C-terminal metal binding;


Pssm-ID: 465972 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 5.19e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063723030 311 KVFMLITTIDDIYD-IYGTLEELQLFTTIVEKL 342
Cdd:pfam19086   1 KWLAWLFILDDIYDeVYGTLEELELFTEAIERW 33
 
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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