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Conserved domains on  [gi|238479737|ref|NP_001154609|]
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homogentisate prenyltransferase [Arabidopsis thaliana]

Protein Classification

UbiA prenyltransferase family protein( domain architecture ID 10195480)

UbiA prenyltransferase family protein such as tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1) or tocopherol phytyltransferase, that catalyzes the first step in the biosynthesis of tocopherol forms of vitamin E; this involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
 101-391 9.98e-146

Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


:

Pssm-ID: 260123  Cd Length: 289  Bit Score: 414.65  E-value: 9.98e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 101 CWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDL 180
Cdd:cd13960    1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLLFLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 181 SVQSAWLLVIFFAIAGLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAAL 260
Cdd:cd13960   81 SVRTAWAIVASCGILGLALGALLGSPLLLTLLLLSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 261 GLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFR 340
Cdd:cd13960  161 GLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALFS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238479737 341 GSLMIPAHVILASGLIFQTWVLEKANYtkEAISGYYRFIWNLFYAEYLLFP 391
Cdd:cd13960  241 KIFMVVGHAVLAAVLWYRSKRVDLESK--ESIYSFYMFIWKLFYAEYLLLP 289
 
Name Accession Description Interval E-value
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
 101-391 9.98e-146

Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260123  Cd Length: 289  Bit Score: 414.65  E-value: 9.98e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 101 CWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDL 180
Cdd:cd13960    1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLLFLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 181 SVQSAWLLVIFFAIAGLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAAL 260
Cdd:cd13960   81 SVRTAWAIVASCGILGLALGALLGSPLLLTLLLLSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 261 GLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFR 340
Cdd:cd13960  161 GLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALFS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238479737 341 GSLMIPAHVILASGLIFQTWVLEKANYtkEAISGYYRFIWNLFYAEYLLFP 391
Cdd:cd13960  241 KIFMVVGHAVLAAVLWYRSKRVDLESK--ESIYSFYMFIWKLFYAEYLLLP 289
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
 100-391 1.36e-76

tocopherol phytyltransferase; Reviewed


Pssm-ID: 183813  Cd Length: 308  Bit Score: 239.49  E-value: 1.36e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 100 ACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGD 179
Cdd:PRK12887  15 ALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIALANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHLPLAAGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 180 LSVQSAWLLVIFFAIAGLLVVGFNfGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAA 259
Cdd:PRK12887  95 FSRRQGQRIVIITGILALILAALL-GPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFLHFQWL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 260 LGLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVF 339
Cdd:PRK12887 174 LGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLLSLPTV 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 238479737 340 RGSLMIPAHVILasgLIFQTWVLEKANY-TKEAISGYYRFIWNLFYAEYLLFP 391
Cdd:PRK12887 254 NPAFLIVSHLIL---LALLWWRSQRVDLqDKQAIAQFYQFIWKLFFLEYLLFP 303
UbiA pfam01040
UbiA prenyltransferase family;
140-382 7.28e-25

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 101.92  E-value: 7.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  140 ALSGLLALICGNGYIVGINQIYDIGIDKV--NKPYLPIAAGDLSVQSAWLLVIFFAIAGLLVvGFNFGPFITSLYSLGLF 217
Cdd:pfam01040  22 LLLALLGTVLARAAANALNDYYDRDIDAImpRTPNRPLPSGRISPREALIFALVLLALGLLL-LLLLNPLTALLGLAALL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  218 LGTIYSvppLRMKRFPVAAFLIIATVRGFLLNFGVYHATRaalglpfQWSAPVAFITSFVTLFALVIAITKDLPDVEGDR 297
Cdd:pfam01040 101 LYVLYT---LRLKRRTLLGQLVGGLAFGLPPLLGWAAVTG-------SLSPLALLLALALFLWTWAIALANDLRDREDDR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  298 KFQISTLATKLGVRNIAFLGSGLLlvnYVSAISLAFYMPQVFRGSLMIPAHVILASGLIFQTWVLEKANYTKEAISgyYR 377
Cdd:pfam01040 171 KAGIKTLPVVLGRKAARILLALLL---AVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPKKDAKA--FF 245


                  ....*
gi 238479737  378 FIWNL 382
Cdd:pfam01040 246 FLSSL 250
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 100-385 3.01e-24

4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440151  Cd Length: 280  Bit Score: 100.69  E-value: 3.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 100 ACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALsglLALICGNGYIVGINQIYDIGIDKVN--KPYLPIAA 177
Cdd:COG0382    2 AYLRLLRLDRPIGILLLLWPTLWALFLAAGGLPDLLLLLLAV---LGTVLMRSAGYVINDYFDREIDRINerKPNRPLAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 178 GDLSVQSAWLLVIFFAIAGLLVVGFnFGPFITSLYSLGLFLGTIYsvpPLRMKRFPVAAFLIIATVRGFLLNFGVYHATR 257
Cdd:COG0382   79 GRISLREALLLAIVLLLLALALALL-LNPLTFLLALAALALAWAY---SLFLKRFTLLGNLVLGLLFGLGILMGFAAVTG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 258 AAlglpfqwSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVnyvsAISLAFYMPQ 337
Cdd:COG0382  155 SL-------PLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYAL----AVLLLLLLGL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 238479737 338 VFRGSLMIPAHVILASGLIFQTWVLEKANYTKEAISGYYRFIWNLFYA 385
Cdd:COG0382  224 LAGLGLLYLLGLLAALLLLYLSQLWLLRPRKKDPARALKLFKLNMLLG 271
 
Name Accession Description Interval E-value
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
 101-391 9.98e-146

Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260123  Cd Length: 289  Bit Score: 414.65  E-value: 9.98e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 101 CWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDL 180
Cdd:cd13960    1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLLFLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 181 SVQSAWLLVIFFAIAGLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAAL 260
Cdd:cd13960   81 SVRTAWAIVASCGILGLALGALLGSPLLLTLLLLSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 261 GLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFR 340
Cdd:cd13960  161 GLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALFS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238479737 341 GSLMIPAHVILASGLIFQTWVLEKANYtkEAISGYYRFIWNLFYAEYLLFP 391
Cdd:cd13960  241 KIFMVVGHAVLAAVLWYRSKRVDLESK--ESIYSFYMFIWKLFYAEYLLLP 289
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
 100-391 1.36e-76

tocopherol phytyltransferase; Reviewed


Pssm-ID: 183813  Cd Length: 308  Bit Score: 239.49  E-value: 1.36e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 100 ACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGD 179
Cdd:PRK12887  15 ALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIALANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHLPLAAGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 180 LSVQSAWLLVIFFAIAGLLVVGFNfGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATRAA 259
Cdd:PRK12887  95 FSRRQGQRIVIITGILALILAALL-GPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFLHFQWL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 260 LGLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVF 339
Cdd:PRK12887 174 LGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLLSLPTV 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 238479737 340 RGSLMIPAHVILasgLIFQTWVLEKANY-TKEAISGYYRFIWNLFYAEYLLFP 391
Cdd:PRK12887 254 NPAFLIVSHLIL---LALLWWRSQRVDLqDKQAIAQFYQFIWKLFFLEYLLFP 303
PLN02878 PLN02878
homogentisate phytyltransferase
 141-393 2.06e-55

homogentisate phytyltransferase


Pssm-ID: 178466  Cd Length: 280  Bit Score: 183.75  E-value: 2.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 141 LSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSAWLLVIFFAIAGLLvVGFNFG--PFITSLYsLGLFL 218
Cdd:PLN02878  26 LEALVPALLMNIYIVGLNQLYDIEIDKVNKPYLPLASGEFSVATGVAIVTSFAIMSFG-MGWIVGswPLFWALF-VSFVL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 219 GTIYSV--PPLRMKRFPVAAFLIIATVRGFLLNFGVY-HATRAALGLPFQWSAPVAFITSFVTLFALVIAITKDLPDVEG 295
Cdd:PLN02878 104 GTAYSInlPLLRWKRSAVAAASCILAVRAVVVQLAFFlHMQTHVLGRPAVFTRPLIFATAFMCFFSVVIALFKDIPDVEG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 296 DRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFRGSLMIPAHVILASGLIFQTWVLEKANytKEAISGY 375
Cdd:PLN02878 184 DRIFGIRSFSVRLGQKRVFWLCVNLLEMAYAAAILVGASSSFLWSKIITVLGHGILASILWQRAQSVDLSS--KAAITSF 261

                        250
                 ....*....|....*...
gi 238479737 376 YRFIWNLFYAEYLLFPFL 393
Cdd:PLN02878 262 YMFIWKLFYAEYFLIPLV 279
UbiA pfam01040
UbiA prenyltransferase family;
140-382 7.28e-25

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 101.92  E-value: 7.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  140 ALSGLLALICGNGYIVGINQIYDIGIDKV--NKPYLPIAAGDLSVQSAWLLVIFFAIAGLLVvGFNFGPFITSLYSLGLF 217
Cdd:pfam01040  22 LLLALLGTVLARAAANALNDYYDRDIDAImpRTPNRPLPSGRISPREALIFALVLLALGLLL-LLLLNPLTALLGLAALL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  218 LGTIYSvppLRMKRFPVAAFLIIATVRGFLLNFGVYHATRaalglpfQWSAPVAFITSFVTLFALVIAITKDLPDVEGDR 297
Cdd:pfam01040 101 LYVLYT---LRLKRRTLLGQLVGGLAFGLPPLLGWAAVTG-------SLSPLALLLALALFLWTWAIALANDLRDREDDR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  298 KFQISTLATKLGVRNIAFLGSGLLlvnYVSAISLAFYMPQVFRGSLMIPAHVILASGLIFQTWVLEKANYTKEAISgyYR 377
Cdd:pfam01040 171 KAGIKTLPVVLGRKAARILLALLL---AVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPKKDAKA--FF 245


                  ....*
gi 238479737  378 FIWNL 382
Cdd:pfam01040 246 FLSSL 250
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 100-385 3.01e-24

4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440151  Cd Length: 280  Bit Score: 100.69  E-value: 3.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 100 ACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALsglLALICGNGYIVGINQIYDIGIDKVN--KPYLPIAA 177
Cdd:COG0382    2 AYLRLLRLDRPIGILLLLWPTLWALFLAAGGLPDLLLLLLAV---LGTVLMRSAGYVINDYFDREIDRINerKPNRPLAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 178 GDLSVQSAWLLVIFFAIAGLLVVGFnFGPFITSLYSLGLFLGTIYsvpPLRMKRFPVAAFLIIATVRGFLLNFGVYHATR 257
Cdd:COG0382   79 GRISLREALLLAIVLLLLALALALL-LNPLTFLLALAALALAWAY---SLFLKRFTLLGNLVLGLLFGLGILMGFAAVTG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 258 AAlglpfqwSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVnyvsAISLAFYMPQ 337
Cdd:COG0382  155 SL-------PLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYAL----AVLLLLLLGL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 238479737 338 VFRGSLMIPAHVILASGLIFQTWVLEKANYTKEAISGYYRFIWNLFYA 385
Cdd:COG0382  224 LAGLGLLYLLGLLAALLLLYLSQLWLLRPRKKDPARALKLFKLNMLLG 271
PRK07566 PRK07566
chlorophyll synthase ChlG;
134-334 8.34e-21

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 91.91  E-value: 8.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 134 WSLVLKALSG-LLA--LICGngYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSAWLLVIFFAIAGLLVvGFNFGPFITS 210
Cdd:PRK07566  60 LENVLKLLAGmLLAgpLLCG--TSQTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAV-AYLLGPWVFL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 211 LYSLGLFLGTIYSVPPLRMKRfpvaafliiatvRGFLLNFGV---YHA----TRAALGLPFQWSAPVAFITSFVTLFALV 283
Cdd:PRK07566 137 AALLGLFLAWIYSAPPLRLKQ------------NGWLGNYAVglsYEGlpwwAGAAAFGAGLPSWPIVILALLYSLGAHG 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 238479737 284 IAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFY 334
Cdd:PRK07566 205 IMTLNDFKSVEGDRQLGLRSLPVVFGEKNAARIACVVIDLFQLAVIALLLA 255
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 140-360 9.29e-21

UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 90.87  E-value: 9.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 140 ALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSAWLLVIFFAIAGLLvVGFNFGPFITSLYSLGLFLG 219
Cdd:cd13956   34 LLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQALAFAAALLLVGLA-LALALGPLALLLLLAGLLLG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 220 TIYSVPPLRMKRFPVAafliiatVRGFLLNFGVYHATRAALGLPFQWSAPVAFItsFVTLFALVIAITKDLPDVEGDRKF 299
Cdd:cd13956  113 LAYSLGLKRLKLGGWG-------VLGYATGLALLPGLGAVAAGGLVPLALLLAL--VFLLLGLGINLYNDLPDVEGDRAA 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238479737 300 QISTLATKLGVRNIAFLGSGLLLVnyVSAISLAFYMPQVFRGSLMIPAHVILASGLIFQTW 360
Cdd:cd13956  184 GIRTLPVRLGPRRARRLAAGLLLA--ALILVVLLAVAGLLGPLALLALLAVALLALRARFA 242
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 100-357 1.42e-20

Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260124  Cd Length: 270  Bit Score: 90.26  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 100 ACWRFLRPHTIRGTALGSTALVTRALIENTHLIKWSLVLKALSGllALICGNGYIvgINQIYDIGIDKVNKPYLPIAAGD 179
Cdd:cd13961    1 AYLELIRPPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSV--FLIAAAGYI--INDYFDVEIDRINKPDRPIPSGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 180 LSVQSAWLLVIFFAIAGLLvVGFNFGPFITSLYSLGLFLGTIYSvppLRMKRFPVAAFLIIATVRGFLLNFGVYHAtraa 259
Cdd:cd13961   77 ISRREALILSILLNALGLI-LAFLLSPLALLIALLNSLLLWLYS---HKLKRTPLIGNLLVALLTGLPFLFGGLAA---- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 260 lglpFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVnyvsAISLAFYMPQVF 339
Cdd:cd13961  149 ----GNLLLIILLLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLL----AILLSPLPYLLG 220

                        250
                 ....*....|....*...
gi 238479737 340 RGSLMIPAHVILASGLIF 357
Cdd:cd13961  221 GLGILYLILIIIADLLFL 238
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
 128-334 3.00e-17

Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of chlorophyll (Chl) biosynthesis, the addition of the tetraprenyl (phytyl or geranylgeranyl) side chain. In plant chloroplast, the chlorophyll synthase is located in thylakoid membrane and has been shown to also have a regulatory or channeling function. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260121  Cd Length: 277  Bit Score: 81.12  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 128 NTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSAWLLVIFFAIAGLLVVGFNFGPF 207
Cdd:cd13958   26 AFQWSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLDGPW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 208 ITSLYSLGLFLGTIYSVPPLRMKRfpvaafliiatvRGFLLNFGV--------YHATRAALGLPFQWsaPVAFITSFVTL 279
Cdd:cd13958  106 VFAAAVVGLVLAYIYSAPPLKLKQ------------NGWWGNAAVglsyeglpWWAGAAAFAGLLTW--ESLALALLYSI 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238479737 280 FALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFY 334
Cdd:cd13958  172 GAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIACGVIDVPQLAVAALLLA 226
ubiA PRK12884
prenyltransferase; Reviewed
 99-335 4.18e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 71.91  E-value: 4.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737  99 NACWRFLRPhtirGTALGS-TALVTRALIENTHLIKWSLVLKALSGLLALICGNGyivgINQIYDIGIDKVNKPYLPIAA 177
Cdd:PRK12884   5 KAYLELLRP----EHGLMAgIAVVLGAIIALGGLPLDEALLGFLTAFFASGSANA----LNDYFDYEVDRINRPDRPIPS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 178 GDLSVQSAWLLVIFFAIAGlLVVGFNFGPFITSLYSLGLFLGTIYSvppLRMKRFPVAAFLIIATVRGFLLNFGVYHATR 257
Cdd:PRK12884  77 GRISRREALLLAILLFILG-LIAAYLISPLAFLVVILVSVLGILYN---WKLKEYGLIGNLYVAFLTGMTFIFGGIAVGE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238479737 258 aalglpfqWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGvRNIAFLGSGLLLVNYVSAISLAFYM 335
Cdd:PRK12884 153 --------LNEAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYG-EKIAGRIAAALFILAVLLSPLPYLF 221
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
 105-323 1.60e-13

(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed


Pssm-ID: 181963  Cd Length: 279  Bit Score: 70.37  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 105 LRPHTIRGTALGStalVTRALIENTHLIKWSLVLKALSgLLALICGNGYIvgINQIYDIGIDKVNKPYLPIAAGDLSVQS 184
Cdd:PRK09573  10 IRPKNCIGASIGA---IIGYLIASNFKIDLKGIILAAL-VVFLVCAGGNV--INDIYDIEIDKINKPERPIPSGRISLKE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 185 AWLL-VIFFAIAGLLVVGFNFGPFITSLY-SLGLFLgtiYSvppLRMKRFPVAAFLIIATVRGFLLNFGvyhatraalGL 262
Cdd:PRK09573  84 AKIFsITLFIVGLILSIFINIYAFLIALLnSILLYL---YA---KDLKKTGLIGNLIVAYLTGLSFIFG---------GL 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238479737 263 PFQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLV 323
Cdd:PRK09573 149 AVFNVLRIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIKKSWYIAKILLIL 209
PLN00012 PLN00012
chlorophyll synthetase; Provisional
 149-339 9.33e-13

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 69.12  E-value: 9.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 149 CGNGYIVGINQIYDIGIDKVNKPYLPIAAGDLS-----VQSAWLLVIFFAIAGLLVV--GFNFgPFITSLYSLGLFLGTI 221
Cdd:PLN00012 134 FLTGYTQTINDWYDREIDAINEPYRPIPSGAISeneviTQIWVLLLGGLGLAYTLDVwaGHDF-PIVFYLALGGSLLSYI 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 222 YSVPPLRMKRfpvaafliiatvRGFLLNFGV--------YHATRAALGlpfQWSAPVAFITSFVTLFALVIAITKDLPDV 293
Cdd:PLN00012 213 YSAPPLKLKQ------------NGWIGNYALgasyislpWWAGQALFG---TLTPDVVVLTLLYSIAGLGIAIVNDFKSI 277

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 294 EGDRKFQISTLATKLGVRNIAFLGSGLLLVN--------------YVSAISLAFYMPQVF 339
Cdd:PLN00012 278 EGDRALGLQSLPVAFGVETAKWICVGSIDITqlsvagyllaigkpYYALALLGLIIPQIF 337
PRK12392 PRK12392
bacteriochlorophyll c synthase; Provisional
 150-353 1.47e-11

bacteriochlorophyll c synthase; Provisional


Pssm-ID: 171463  Cd Length: 331  Bit Score: 65.10  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 150 GNGYIVGINQIYDIGIDKVNKPYLPIAAGDLSVQSA---WLLVIFFAIAGLLVVGFNFGP----FITSLYSLGLFLGTIY 222
Cdd:PRK12392  62 GTGFSQSVNDYFDLELDRVNEPTRPIPSGRLSEKEAlwnSIIVLLLAIGLGVWLGLHIGGergmVIISSILAGLFVAYIY 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 223 SVPPLRMKRfpvaAFLIIATVRGFLLNFGVYHATRAALG---LPFQWSAPVAFitsfvtLFALVIAITKDLPDVEGDRKF 299
Cdd:PRK12392 142 SAPPLKLKK----NILTSAPAVGFSYGFITFLSANALFSdirPEVVWLAGLNF------FMAIALIIMNDFKSVEGDKEG 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 238479737 300 QISTLATKLGVRNiAFLGSgLLLVNYVSAIsLAFYMpqvFRGSLMIPAHVILAS 353
Cdd:PRK12392 212 GLKSLTVMIGAKN-TFLVS-FIIIDLVFAV-FAWLA---WSWGFTVLMYFILVG 259
ubiA PRK12872
prenyltransferase; Reviewed
 152-334 4.22e-10

prenyltransferase; Reviewed


Pssm-ID: 237241  Cd Length: 285  Bit Score: 59.96  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 152 GYIvgINQIYDIGIDKVNKPylpiAAGDLSVQSAWLLVIFFAIAGL----LVVGFNFGPFITSLYSLGLFLGTIYSVPPL 227
Cdd:PRK12872  52 VYI--INYLTDLEEDIINKP----ERVVFSETKAYGLFLLLNVLGLylgaYLLAVIGGPKFALIFIIPLILGILYSVFFK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 228 -RMKRFPVAAFLIIATVRGFLLNF-GVYHATRAalglpfqWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLA 305
Cdd:PRK12872 126 rRLKRIPLFKNLVVSLLWALSPLIlGVYYYQLT-------IFSLLLLYAVFIFLKSFIREIVFDIKDIEGDRKSGLKTLP 198

                        170       180
                 ....*....|....*....|....*....
gi 238479737 306 TKLGVRNIAFLgsgLLLVNYVSAISLAFY 334
Cdd:PRK12872 199 IVLGKERTLKF---LLILNLLFLILLILG 224
PT_UbiA_4 cd13966
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 134-380 4.43e-09

UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.


Pssm-ID: 260129  Cd Length: 272  Bit Score: 56.89  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 134 WSLVLKALSGLLA-LICGNGYIVGINQIYDIGIDKVN---KPYLPIAAGDLSVQSAWLLVIFFAIAGLLVVGFNFGPFIT 209
Cdd:cd13966   28 FDDLLRLILGLLYfLFPANLLIYGVNDVFDYESDARNprkGGIEGALLDPAEHRPLLWAVAVSNVPFLLYLVLVGPPAAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 210 SLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATvrgFLLNFGVYHAtrAALGLPFQWSAPVAFItsfvtLFALVIAITKD 289
Cdd:cd13966  108 LLLALFLFLVVAYSAPPLRFKERPFLDSLSNGL---YFLPPALVGL--LASGTLPPWLALAAFF-----LWGMAMHAFGA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 290 LPDVEGDRKFQISTLATKLGVRNIAflgsGLLLVNYVSAISLAFYMPQVfrgslmipaHVILASGLIFQTWVLEKANYTK 369
Cdd:cd13966  178 IQDIEADREAGIRTTATVLGARGTL----RLALALWLLAAVLVLPLSLP---------LPLSYLALVYPAISLADALAGR 244

                        250
                 ....*....|.
gi 238479737 370 EAISGYYRFIW 380
Cdd:cd13966  245 TNPRGYWRFPW 255
ubiA PRK12882
prenyltransferase; Reviewed
 146-323 1.18e-08

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 55.75  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 146 ALICGNGYivGINQIYDIGIDKVNKPYLPIAAGDLSVQSA-WLLVIFFAIAGLLVVGFNFGPFITSLYSLGLFLgtIYSV 224
Cdd:PRK12882  48 FLATGAGN--AINDYFDREIDRINRPDRPIPSGAVSPRGAlAFSILLFAAGVALAFLLPPLCLAIALFNSLLLV--LYAE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 225 pplRMKRFPVAAFLIIATVRGFLLNFGVyhatrAALGLPFQWSAPVAFITSFVTLFALviAITKDLPDVEGDRKFQISTL 304
Cdd:PRK12882 124 ---TLKGTPGLGNASVAYLTGSTFLFGG-----AAVGTEGLLALLVLFALAALATLAR--EIIKDVEDIEGDRAEGARTL 193

                        170
                 ....*....|....*....
gi 238479737 305 ATKLGVRNIAFLGSGLLLV 323
Cdd:PRK12882 194 PILIGVRKALYVAAAFLLV 212
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
 102-333 4.11e-07

1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260125  Cd Length: 283  Bit Score: 50.97  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 102 WRFLRPHT----IRGTALGSTAlvtrALIENTHLIKWSLVLKALSGLLALICGNG------YIVGINQIYDIGIDKVnkp 171
Cdd:cd13962    1 LLAARPRTlpasLAPVLLGTAL----AYYLGGFFNWLLFLLALLAALLLQIGVNLandyfdYKKGTDTEPRSGPSRV--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 172 ylpIAAGDLSVQSA-WLLVIFFAIAGL--LVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVAAFLIIATVRGFLL 248
Cdd:cd13962   74 ---LVSGLLSPRQVlRAALVLLLLAALlgLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 249 NFGVYHATRAALGLPFQWSAPVAFITSfvtlfalVIAITKDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSA 328
Cdd:cd13962  151 LGTYYVQTGSLSWEVLLAALPLGLLIA-------AILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLL 223


                 ....*
gi 238479737 329 ISLAF 333
Cdd:cd13962  224 LLLVL 228
PT_UbiA_3 cd13965
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 101-298 9.71e-06

UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.


Pssm-ID: 260128  Cd Length: 273  Bit Score: 46.87  E-value: 9.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 101 CWRFLRpHTIRGTALGSTALVTRALIENTHLikwsLVLKALSGLLALICGNGYIVGI---NQIYDIGIDKVNKPYLPIAA 177
Cdd:cd13965    1 LWLFTK-SDIKTIVLPITIFALAAAPSGSLL----TAELALPLLLGFLWIWLHLYQFdnqNQPESVEEDRINKPWRPIPS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 178 GDLSVQSA-WLLVIFFAIAglLVVGFNFGPFITSLysLGLFLGTIYSVPPLR---MKRFPVAAFLIIATVRGfllnfgvy 253
Cdd:cd13965   76 GRITPRQArRLRWLLVPLC--LALSAYLGVLEESL--LLIVLTWLYNELGLAdhwLTRNLLNALGYAAFLAG-------- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 238479737 254 hATRAALGLPFQWSAPvafITSFVTLFALVIAIT---KDLPDVEGDRK 298
Cdd:cd13965  144 -ATRIAGGGPHPLDPT---AWAWILLSAAIILTTihaQDFRDVEGDRA 187
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
 144-333 2.37e-05

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 45.52  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 144 LLALICGNGYIVGINQI-----YDIGIDKVNK--PYLPIAAGDLSVQSA-WLLVIFFAIAGLLVVGFNF--GPFITSLYS 213
Cdd:COG1575   38 LLALLAALLLQIGVNLAndyfdYKKGTDTEERvgPSRVIVSGLLSPKQVlRAALLLLALALLLGLYLVLlsGWPLLLLGL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 214 LGLFLGTIYSVPPLRMKRFP---VAAFL---IIATVRGFLLNFGVYHATRAALGLPfqwsapvafitsfVTLFALVIAIT 287
Cdd:COG1575  118 LGILAAIFYTGGPFPLGYRGlgeLFVFLffgLVAVLGTYYVQTGTLSWAALLASLP-------------VGLLSAAVLLA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 238479737 288 KDLPDVEGDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAF 333
Cdd:COG1575  185 NNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLLVL 230
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
 157-318 6.69e-05

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 44.33  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 157 INQIYDIGIDKVNKPYLPIAAGDLSVQSA-WLLVIFFAIAGLLVVGFNFGPFITSLysLGLFLGTIYSvppLRMKRFPVA 235
Cdd:PRK12883  56 INDYFDYEIDKINRPNRPLPRGAMSRKAAlYYSLLLFAVGLALAYLINIEAFLFAL--GAYVLMFLYA---WKLKPLPFI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 236 AFLIIATVRGFLLNFGVYHATRAALGlpfQWSAPVAFitsfvtLFALVIAITKDLPDVEGDRKFQISTLATKLGVRNIAF 315
Cdd:PRK12883 131 GNVVVALLTGATPIYGAIAVGRIGLA---GYLAICAF------LVNVAREIMKDIEDIEGDKAKGAKTLPIIIGKKRAAY 201


                 ...
gi 238479737 316 LGS 318
Cdd:PRK12883 202 IGA 204
ubiA PRK12875
prenyltransferase; Reviewed
 147-312 7.95e-05

prenyltransferase; Reviewed


Pssm-ID: 237243  Cd Length: 282  Bit Score: 43.87  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 147 LICGNGYIVGINQIYDIGIDKVNkpylPIAAGD--LSVQSAWLLVIFFAIAGLLVVGFNFG-PFITSLYSLG-LFLGTIY 222
Cdd:PRK12875  54 LFPANVFLYGVNDVFDADTDELN----PKKDREreVRYRGDRRVLVAVALSGALALAFLLVlPPAAWPALLAfLVLSVEY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 223 SVPPLRMKRFPVAAFL-----IIATVRGFLLNFGVYHATRAALGlpfQWsapvafitsfvtLFALVIAITKDLPDVEGDR 297
Cdd:PRK12875 130 SAPPLRFKTTPVLDSLsnglyILPGVAAYALVSGSLPPLLAVAG---GW------------LWAMGMHTFSAIPDIEPDR 194

                        170
                 ....*....|....*
gi 238479737 298 KFQISTLATKLGVRN 312
Cdd:PRK12875 195 AAGIRTTATVLGERR 209
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 130-248 5.11e-04

UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.


Pssm-ID: 260126  Cd Length: 278  Bit Score: 41.31  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 130 HLIKWSLVLKALSGLLA--LICGNGYIvgINQIYDIGIDKVN--KPYLPIAAGDLSVQSAWLLVIFFAIAGlLVVGFNFG 205
Cdd:cd13963   25 QLFDPDLLLAALLAFVAfcLAASAVYI--LNDLLDLEADRLHptKRNRPIASGRLSIPAALALAVVLLLAG-LALALLLS 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 238479737 206 PFITSLYSLGLFLGTIYSvppLRMKRFPVAAFLIIATvrGFLL 248
Cdd:cd13963  102 PAFLLVLLAYLVLNLAYS---LKLKRIPLLDVFVIAA--GFVL 139
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 157-335 2.14e-03

4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known as Coq2, catalyzes the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group, an important step in ubiquinone (CoQ) biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260122 [Multi-domain]  Cd Length: 272  Bit Score: 39.37  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 157 INQIYDIGIDKVNK--PYLPIAAGDLSVQSAWLLVIFFAIAGLLVVGF-NFGPFITSLYSLGLFLgtIYsvpPLrMKRFp 233
Cdd:cd13959   52 INDIADRDIDAKVPrtKNRPLASGAISVKEALLFLAVQLLLGLALLLQlNPLTILLSPIALLLVL--IY---PL-MKRF- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 234 vaafliiatvrgfllnfgvYHATRAALGLPFQWSAPVAFI----TSFVTLFALVIA-----ITKD----LPDVEGDRKFQ 300
Cdd:cd13959  125 -------------------TYWPQLVLGLAFGWGPLMGWAavtgSLPLPALLLYLAvifwtAGYDtiyaHQDREDDRKIG 185

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 238479737 301 ISTLATKLGVRNIAFLgsGLLLVNYVSAISLAFYM 335
Cdd:cd13959  186 VKSTAVLFGDRTKLIL--ALLLHLFVALLLLAGGL 218
PT_UbiA_5 cd13967
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 180-335 6.72e-03

UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.


Pssm-ID: 260130  Cd Length: 277  Bit Score: 37.98  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 180 LSVQSAWLLVIFFAIAGLLVVGFNFGPFIT-SLYSLGLFLGTIysVPPLRMKRFPVAAFLIIATVRGFLLNFGVYHATra 258
Cdd:cd13967   81 LAIAAGLLALALAFILGLLAFAILLLPLLLgLLYSLPIKPGKL--RLRRRKDIPGSKNLVVALAWAVVIALLPALYGQ-- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479737 259 alglpfQWSAPVAFITSFVTLFALVIAITKDLPDVEGDRKFQISTLATKLGVRN--------IAFLGSGLLLVNYVSAIS 330
Cdd:cd13967  157 ------PSTPSVLVVFLFFFLKVFVNTAIFDIRDVEGDRIVGIETLPVLLGEERtrllllvlNILLALLLVAGVLLGLLA 230


                 ....*
gi 238479737 331 LAFYM 335
Cdd:cd13967  231 SEFLV 235
 
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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