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Conserved domains on  [gi|402797847|gb|AFQ99308|]
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homogentisate phytyl transferase [Chloroplast transformation vector pSyHPT]

Protein Classification

homogentisate phytyltransferase( domain architecture ID 10014104)

homogentisate phytyltransferase (HPT) catalyzes the condensation of homogentisate and phytyl diphosphate to form dimethylphytylhydrquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
1-300 2.88e-163

tocopherol phytyltransferase; Reviewed


:

Pssm-ID: 183813  Cd Length: 308  Bit Score: 456.35  E-value: 2.88e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNL 80
Cdd:PRK12887  10 TSWLYALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIAL-ANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  81 PLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFL 160
Cdd:PRK12887  89 PLAAGEFSRRQGQRIVIITGILALILAALLGPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLW 240
Cdd:PRK12887 169 HFQWLLGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLL 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 241 AAMPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPLALWL 300
Cdd:PRK12887 249 SLPTVNPAFLIVSHLILLALLWWRSQRVDLQDKQAIAQFYQFIWKLFFLEYLLFPIACLL 308
 
Name Accession Description Interval E-value
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
1-300 2.88e-163

tocopherol phytyltransferase; Reviewed


Pssm-ID: 183813  Cd Length: 308  Bit Score: 456.35  E-value: 2.88e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNL 80
Cdd:PRK12887  10 TSWLYALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIAL-ANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  81 PLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFL 160
Cdd:PRK12887  89 PLAAGEFSRRQGQRIVIITGILALILAALLGPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLW 240
Cdd:PRK12887 169 HFQWLLGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLL 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 241 AAMPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPLALWL 300
Cdd:PRK12887 249 SLPTVNPAFLIVSHLILLALLWWRSQRVDLQDKQAIAQFYQFIWKLFFLEYLLFPIACLL 308
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
7-295 1.73e-133

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: 380.37  E-value: 1.73e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   7 FWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGD 86
Cdd:cd13960    1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLL-FLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  87 FSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGI-SLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIG 165
Cdd:cd13960   80 LSVRTAWAIVASCGILGLALGALLGSPLLLTLLLlSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 166 LGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPL 245
Cdd:cd13960  160 LGLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALF 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 402797847 246 NTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYP 295
Cdd:cd13960  240 SKIFMVVGHAVLAAVLWYRSKRVDLESKESIYSFYMFIWKLFYAEYLLLP 289
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-266 1.00e-33

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: 124.57  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   5 QAFWRFSRPHTIIGTTLSVWAVYLLTILgdgnSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRIN--KPNLPL 82
Cdd:COG0382    1 RAYLRLLRLDRPIGILLLLWPTLWALFL----AAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINerKPNRPL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  83 ANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYsvpPVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:COG0382   77 ASGRISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAY---SLFLKRFTLLGNLVLGLLFGLGILMGFAAVT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 163 RiglgyppTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAa 242
Cdd:COG0382  154 G-------SLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLA- 225
                        250       260
                 ....*....|....*....|....
gi 402797847 243 mPLNTAFLIVshLCLLALLWWRSR 266
Cdd:COG0382  226 -GLGLLYLLG--LLAALLLLYLSQ 246
UbiA pfam01040
UbiA prenyltransferase family;
37-286 6.90e-30

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 113.48  E-value: 6.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   37 SVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRI--NKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWL 114
Cdd:pfam01040  12 AAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAImpRTPNRPLPSGRISPREALIFALVLLALGLLLLLLLNPLT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  115 GLTVGISLIIGTAYSVppvRLKRFSLLAALCILTVRGIVVNLGLFLFFriglgypPTLITPIWVLTLFILVFTVAIAIFK 194
Cdd:pfam01040  92 ALLGLAALLLYVLYTL---RLKRRTLLGQLVGGLAFGLPPLLGWAAVT-------GSLSPLALLLALALFLWTWAIALAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  195 DVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLntaFLIVSHLCLLALLWWRSRDVHLESKT 274
Cdd:pfam01040 162 DLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL---YLLLALLLAALALLYAARLLRLRDPK 238
                         250
                  ....*....|..
gi 402797847  275 EIASFYQFIWKL 286
Cdd:pfam01040 239 KDAKAFFFLSSL 250
 
Name Accession Description Interval E-value
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
1-300 2.88e-163

tocopherol phytyltransferase; Reviewed


Pssm-ID: 183813  Cd Length: 308  Bit Score: 456.35  E-value: 2.88e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNL 80
Cdd:PRK12887  10 TSWLYALWKFSRPHTIIGTSLSVLGLYLIAIAASSNTIAL-ANLGLLLGAWIACLCGNVYIVGLNQLTDIEIDRINKPHL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  81 PLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFL 160
Cdd:PRK12887  89 PLAAGEFSRRQGQRIVIITGILALILAALLGPWLLITVGISLLIGTAYSLPPIRLKRFPLLAALCIFTVRGVIVNLGLFL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLW 240
Cdd:PRK12887 169 HFQWLLGGSVLIPPTVWLLTLFVLVFTFAIAIFKDIPDMEGDRQYQITTFTLRLGKQAVFKLSCWVLTACYLGMIAVGLL 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 241 AAMPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPLALWL 300
Cdd:PRK12887 249 SLPTVNPAFLIVSHLILLALLWWRSQRVDLQDKQAIAQFYQFIWKLFFLEYLLFPIACLL 308
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
7-295 1.73e-133

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: 380.37  E-value: 1.73e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   7 FWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSpASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGD 86
Cdd:cd13960    1 FWKFSRPHTIIGTILSVTSLSLLALESNSDLLLL-FLLPGALQALVALLLGNVYIVGLNQIYDVEIDKINKPYLPLASGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  87 FSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGI-SLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIG 165
Cdd:cd13960   80 LSVRTAWAIVASCGILGLALGALLGSPLLLTLLLlSLLLGTAYSVPPPRLKRFPLLAALCILTVRGFLVNLGFYLHFQAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 166 LGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPL 245
Cdd:cd13960  160 LGLPFAWPPSLWFLTAFMTVFAIVIALFKDIPDVEGDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVGLTSPALF 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 402797847 246 NTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYP 295
Cdd:cd13960  240 SKIFMVVGHAVLAAVLWYRSKRVDLESKESIYSFYMFIWKLFYAEYLLLP 289
PLN02878 PLN02878
homogentisate phytyltransferase
21-296 2.42e-70

homogentisate phytyltransferase


Pssm-ID: 178466  Cd Length: 280  Bit Score: 219.57  E-value: 2.42e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  21 LSVWAVYLLTIlgDGNSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCG 100
Cdd:PLN02878   1 LGITSVSLLAV--ESLSDFSPLFFTGLLEALVPALLMNIYIVGLNQLYDIEIDKVNKPYLPLASGEFSVATGVAIVTSFA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 101 VASLAIAWGLGLW-LGLTVGISLIIGTAYSV--PPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIG-LGYPPTLITPI 176
Cdd:PLN02878  79 IMSFGMGWIVGSWpLFWALFVSFVLGTAYSInlPLLRWKRSAVAAASCILAVRAVVVQLAFFLHMQTHvLGRPAVFTRPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 177 WVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLC 256
Cdd:PLN02878 159 IFATAFMCFFSVVIALFKDIPDVEGDRIFGIRSFSVRLGQKRVFWLCVNLLEMAYAAAILVGASSSFLWSKIITVLGHGI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 402797847 257 LLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPL 296
Cdd:PLN02878 239 LASILWQRAQSVDLSSKAAITSFYMFIWKLFYAEYFLIPL 278
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-266 1.00e-33

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: 124.57  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   5 QAFWRFSRPHTIIGTTLSVWAVYLLTILgdgnSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRIN--KPNLPL 82
Cdd:COG0382    1 RAYLRLLRLDRPIGILLLLWPTLWALFL----AAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINerKPNRPL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  83 ANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYsvpPVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:COG0382   77 ASGRISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAY---SLFLKRFTLLGNLVLGLLFGLGILMGFAAVT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 163 RiglgyppTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAa 242
Cdd:COG0382  154 G-------SLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLA- 225
                        250       260
                 ....*....|....*....|....
gi 402797847 243 mPLNTAFLIVshLCLLALLWWRSR 266
Cdd:COG0382  226 -GLGLLYLLG--LLAALLLLYLSQ 246
UbiA pfam01040
UbiA prenyltransferase family;
37-286 6.90e-30

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 113.48  E-value: 6.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   37 SVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRI--NKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWL 114
Cdd:pfam01040  12 AAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAImpRTPNRPLPSGRISPREALIFALVLLALGLLLLLLLNPLT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  115 GLTVGISLIIGTAYSVppvRLKRFSLLAALCILTVRGIVVNLGLFLFFriglgypPTLITPIWVLTLFILVFTVAIAIFK 194
Cdd:pfam01040  92 ALLGLAALLLYVLYTL---RLKRRTLLGQLVGGLAFGLPPLLGWAAVT-------GSLSPLALLLALALFLWTWAIALAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  195 DVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLntaFLIVSHLCLLALLWWRSRDVHLESKT 274
Cdd:pfam01040 162 DLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL---YLLLALLLAALALLYAARLLRLRDPK 238
                         250
                  ....*....|..
gi 402797847  275 EIASFYQFIWKL 286
Cdd:pfam01040 239 KDAKAFFFLSSL 250
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
8-270 9.14e-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: 89.71  E-value: 9.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   8 WRFSRPHTIIGTTLSVWAVYLLTILGDgnsvnsPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDF 87
Cdd:cd13956    1 LRLMRPYTLLYVLAPALAGAALAGAFA------GPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  88 SIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLaalciltVRGIVVnlGLFLFFRIGLG 167
Cdd:cd13956   75 SPRQALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGWG-------VLGYAT--GLALLPGLGAV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 168 YPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKqnvfRGTLILLTGCYLAMAIWGLWAAMPLNT 247
Cdd:cd13956  146 AAGGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGP----RRARRLAAGLLLAALILVVLLAVAGLL 221
                        250       260
                 ....*....|....*....|...
gi 402797847 248 AFLIVSHLCLLALLWWRSRDVHL 270
Cdd:cd13956  222 GPLALLALLAVALLALRARFARA 244
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
6-286 2.12e-17

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: 80.24  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   6 AFWRFSRPHTIIGTTLSVWAVYLLtILGDGNSVNSPASLDLVFGAWLACLLGNVyivgLNQLWDVDIDRINKPNLPLANG 85
Cdd:cd13961    1 AYLELIRPPNLLMAALAQYLGALF-ALGPLLSLNDLELLLLFLSVFLIAAAGYI----INDYFDVEIDRINKPDRPIPSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  86 DFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALciltvrgIVVNLGLFLFFRIG 165
Cdd:cd13961   76 RISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYS---HKLKRTPLIGNL-------LVALLTGLPFLFGG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 166 LGYPPTLITpIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNvfrgTLILLTGCYLAMAIWGLWAAM-- 243
Cdd:cd13961  146 LAAGNLLLI-ILLLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKK----AKKIAALLLLLAILLSPLPYLlg 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 402797847 244 PLNTAFLIVSHLCLLALLWWRSRdvhLESKTEIASFYQFIWKL 286
Cdd:cd13961  221 GLGILYLILIIIADLLFLYSAIR---LAKSPKDYSKLSKLLKL 260
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
23-250 2.32e-15

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: 74.57  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  23 VWAVyLLTILGDGNSV-NSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGV 101
Cdd:cd13958   14 MWAF-LCGAAASGAFQwSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 102 ASLAIAWGL-GLWLGLTVGISLIIGTAYSVPPVRLKRFSLL-AALCILTVRGIVVNLGLFLFfriglgyPPTLITPIWVL 179
Cdd:cd13958   93 LSLLVALFLdGPWVFAAAVVGLVLAYIYSAPPLKLKQNGWWgNAAVGLSYEGLPWWAGAAAF-------AGLLTWESLAL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402797847 180 TLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFL 250
Cdd:cd13958  166 ALLYSIGAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIACGVIDVPQLAVAALLLAWGETWYAAVV 236
ubiA PRK12882
prenyltransferase; Reviewed
1-240 5.32e-15

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 73.47  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSRPHTIIgttlsvwAVYLLTILG---DGNSVNSPASLDLVFGA-WLACLLGNVyivgLNQLWDVDIDRIN 76
Cdd:PRK12882   1 GMTVRGYLELTRPVNAV-------VAGVAAFIGafiAGGILSSPSLTGLAFAAvFLATGAGNA----INDYFDREIDRIN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  77 KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVvnl 156
Cdd:PRK12882  70 RPDRPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYA---ETLKGTPGLGNASVAYLTGST--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 157 glFLFFRIGLGypptLITPIWVLTLFILVF--TVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLA- 233
Cdd:PRK12882 144 --FLFGGAAVG----TEGLLALLVLFALAAlaTLAREIIKDVEDIEGDRAEGARTLPILIGVRKALYVAAAFLLVAVAAs 217
                        250
                 ....*....|..
gi 402797847 234 -----MAIWGLW 240
Cdd:PRK12882 218 plpylLSTFGLW 229
PRK07566 PRK07566
chlorophyll synthase ChlG;
64-252 1.52e-14

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 72.65  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  64 LNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLA- 142
Cdd:PRK07566  84 LNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLFLAWIYSAPPLRLKQNGWLGn 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 143 ALCILTVRGIVVNLGLFLFfriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRG 222
Cdd:PRK07566 164 YAVGLSYEGLPWWAGAAAF------GAGLPSWPIVILALLYSLGAHGIMTLNDFKSVEGDRQLGLRSLPVVFGEKNAARI 237
                        170       180       190
                 ....*....|....*....|....*....|
gi 402797847 223 TLILLTGCYLAMAIWGLWAAMPLNTAFLIV 252
Cdd:PRK07566 238 ACVVIDLFQLAVIALLLAWGQPLYAAIVGL 267
ubiA PRK12884
prenyltransferase; Reviewed
1-217 4.26e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 71.14  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSRP-HTIIgttlSVWAVYLLTILGDGNSVNSPASLDLVfGAWLACLLGNVyivgLNQLWDVDIDRINKPN 79
Cdd:PRK12884   1 RTKMKAYLELLRPeHGLM----AGIAVVLGAIIALGGLPLDEALLGFL-TAFFASGSANA----LNDYFDYEVDRINRPD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  80 LPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVvnlglF 159
Cdd:PRK12884  72 RPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYN---WKLKEYGLIGNLYVAFLTGMT-----F 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 402797847 160 LFFRIGLGYPPTLitpIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQ 217
Cdd:PRK12884 144 IFGGIAVGELNEA---VILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEK 198
PRK12392 PRK12392
bacteriochlorophyll c synthase; Provisional
56-252 1.43e-09

bacteriochlorophyll c synthase; Provisional


Pssm-ID: 171463  Cd Length: 331  Bit Score: 58.16  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  56 LGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRW---IVGLcgvaslaIAWGLGLWLGLTVG------------I 120
Cdd:PRK12392  61 LGTGFSQSVNDYFDLELDRVNEPTRPIPSGRLSEKEALWnsiIVLL-------LAIGLGVWLGLHIGgergmviissilA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 121 SLIIGTAYSVPPVRLKRFSLLAAlciltvRGIVVNLGLFLFFRIGLGYPPTLITPIWVLTLFILVfTVAIAIFKDVPDME 200
Cdd:PRK12392 134 GLFVAYIYSAPPLKLKKNILTSA------PAVGFSYGFITFLSANALFSDIRPEVVWLAGLNFFM-AIALIIMNDFKSVE 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 402797847 201 GDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAI----WGLWAAMPLNTAFLIV 252
Cdd:PRK12392 207 GDKEGGLKSLTVMIGAKNTFLVSFIIIDLVFAVFAWlawsWGFTVLMYFILVGLVL 262
PT_UbiA_4 cd13966
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
8-299 4.62e-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: 56.12  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   8 WRFSRPHTIIGTTLSVWAVYLLTilGDGNSVNSPAsldLVFGAWLaCLLGNVYIVGLNQLWDVDIDRINK-------PNL 80
Cdd:cd13966    2 LKVSRPRFWINTAGPFAVGYLLA--GSGFDDLLRL---ILGLLYF-LFPANLLIYGVNDVFDYESDARNPrkggiegALL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  81 PLANGDFSIaqgRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALciltvrgivvNLGLFL 160
Cdd:cd13966   76 DPAEHRPLL---WAVAVSNVPFLLYLVLVGPPAALLLLALFLFLVVAYSAPPLRFKERPFLDSL----------SNGLYF 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 161 FFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKqnvfRGTLILLTGCYLAMAIWGLW 240
Cdd:cd13966  143 LPPALVGLLASGTLPPWLALAAFFLWGMAMHAFGAIQDIEADREAGIRTTATVLGA----RGTLRLALALWLLAAVLVLP 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 402797847 241 AAMPLNTAFLivshlcLLALLWWRSRDVHLESKTEIASFYqFIWKLFFLEYLLYPLALW 299
Cdd:cd13966  219 LSLPLPLSYL------ALVYPAISLADALAGRTNPRGYWR-FPWINTVVGFVLTVLLIW 270
PLN00012 PLN00012
chlorophyll synthetase; Provisional
54-215 1.46e-08

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 55.26  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  54 CLLGnvYIVGLNQLWDVDIDRINKPNLPLANGDFS----IAQgRWIVGLCGvasLAIAWGLGLWLG--------LTVGIS 121
Cdd:PLN00012 134 FLTG--YTQTINDWYDREIDAINEPYRPIPSGAISenevITQ-IWVLLLGG---LGLAYTLDVWAGhdfpivfyLALGGS 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 122 LiIGTAYSVPPVRLKRfsllaalciltvRGIVVNLGL-----FLFFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDV 196
Cdd:PLN00012 208 L-LSYIYSAPPLKLKQ------------NGWIGNYALgasyiSLPWWAGQALFGTLTPDVVVLTLLYSIAGLGIAIVNDF 274
                        170
                 ....*....|....*....
gi 402797847 197 PDMEGDRQFKIQTLTLQIG 215
Cdd:PLN00012 275 KSIEGDRALGLQSLPVAFG 293
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
59-146 1.67e-08

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: 54.40  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  59 VYIvgLNQLWDVDIDRIN--KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLK 136
Cdd:cd13963   49 VYI--LNDLLDLEADRLHptKRNRPIASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYS---LKLK 123
                         90
                 ....*....|
gi 402797847 137 RFSLLAALCI 146
Cdd:cd13963  124 RIPLLDVFVI 133
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
4-227 1.85e-08

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 54.58  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   4 IQAFWRFSRPHTIIGTTLSVWAVYLLTIlgdGNSVNSPASLDLVFGAWLACLLGNVyivgLNQLWDVDIDRINKPNLPLA 83
Cdd:PRK09573   3 IKAYFELIRPKNCIGASIGAIIGYLIAS---NFKIDLKGIILAALVVFLVCAGGNV----INDIYDIEIDKINKPERPIP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  84 NGDFSIAQGRWIvglcGVASLAIAWGLGLWLGL-TVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:PRK09573  76 SGRISLKEAKIF----SITLFIVGLILSIFINIyAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVF 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402797847 163 RIGlgypptlitPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILL 227
Cdd:PRK09573 152 NVL---------RIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIKKSWYIAKILL 207
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
4-217 2.63e-08

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 53.96  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   4 IQAFWRFSRPHTIIGTTLsvwaVYLLTILGDGNSVNSPASLDLVF-GAWLACLLGNVyivgLNQLWDVDIDRINKPNLPL 82
Cdd:PRK12883   3 LKAFIEITRPHNCILAGI----VGILGSLVALGGIPPIKTLILIFlVVYLGCSGGNT----INDYFDYEIDKINRPNRPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  83 ANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSvppVRLKRFSLLAALCILTVRGIVVNLGLFLFF 162
Cdd:PRK12883  75 PRGAMSRKAALYYSLLLFAVGLALAYLINIEAFLFALGAYVLMFLYA---WKLKPLPFIGNVVVALLTGATPIYGAIAVG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 402797847 163 RIGL-GYpptlitpiwvLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQ 217
Cdd:PRK12883 152 RIGLaGY----------LAICAFLVNVAREIMKDIEDIEGDKAKGAKTLPIIIGKK 197
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
8-288 4.92e-08

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: 53.29  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   8 WRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSPASLdlvfgAWLACLLGNVYIVGLNQLWD----VDIDRINKPNLPLA 83
Cdd:cd13962    1 LLAARPRTLPASLAPVLLGTALAYYLGGFFNWLLFLL-----ALLAALLLQIGVNLANDYFDykkgTDTEPRSGPSRVLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  84 NGDFSIAQGRWIVGLCGVAS----LAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLF 159
Cdd:cd13962   76 SGLLSPRQVLRAALVLLLLAallgLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 160 LffriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGL 239
Cdd:cd13962  156 V-------QTGSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 402797847 240 WAAMPLNTAFLIVShLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFF 288
Cdd:cd13962  229 LGLLPLWSLLALLS-LPLAIKLLRRLLRKADKPLLLIALKLTALLTLLF 276
ubiA PRK12875
prenyltransferase; Reviewed
57-251 7.37e-08

prenyltransferase; Reviewed


Pssm-ID: 237243  Cd Length: 282  Bit Score: 52.73  E-value: 7.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  57 GNVYIVGLNQLWDVDIDRINKPNlplANGDFSIAQGRW----IVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPP 132
Cdd:PRK12875  57 ANVFLYGVNDVFDADTDELNPKK---DREREVRYRGDRrvlvAVALSGALALAFLLVLPPAAWPALLAFLVLSVEYSAPP 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 133 VRLKRFSLLAALCiltvRGIVVNLGLFLFFRIGLGYPPTLITPIWVLtlfilvFTVAIAIFKDVPDMEGDRQFKIQTLTL 212
Cdd:PRK12875 134 LRFKTTPVLDSLS----NGLYILPGVAAYALVSGSLPPLLAVAGGWL------WAMGMHTFSAIPDIEPDRAAGIRTTAT 203
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 402797847 213 QIGKqnvfRGTLILLTGCYLAMAIWGLWAAMPLNTAFLI 251
Cdd:PRK12875 204 VLGE----RRTYAYCAACWLLAAAAFAAVDLRLGALLLV 238
PRK08238 PRK08238
UbiA family prenyltransferase;
49-146 9.81e-07

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 49.87  E-value: 9.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  49 GAWLACLLG---------NVYIvgLNQLWDVDIDRIN--KPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLT 117
Cdd:PRK08238 223 QALLAALLAflafslcasAVYI--LNDLLDLEADRAHprKRRRPFASGALPIPFGLAAAPLLLLAGLALALALGPAFLLV 300
                         90       100
                 ....*....|....*....|....*....
gi 402797847 118 VGISLIIGTAYSvppVRLKRFSLLAALCI 146
Cdd:PRK08238 301 LLAYLALTLAYS---LRLKRKVLVDVLTL 326
ubiA PRK12872
prenyltransferase; Reviewed
1-261 1.25e-06

prenyltransferase; Reviewed


Pssm-ID: 237241  Cd Length: 285  Bit Score: 48.79  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847   1 MATIQAFWRFSR--PHTIIGTTLSVwaVYLLTILgdgnsVNSPASLDLVFGAWLACLLGNVYivglNQLWDVDIDRINKP 78
Cdd:PRK12872   1 RKLLFAFLKLFRygNLLIAALGQSL--VYMASLL-----LGLPISWLLLLITFLIAAAVYII----NYLTDLEEDIINKP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  79 -----NLPLANGDFSIAqgrwIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPV-RLKRFSLLAALCILTVRGI 152
Cdd:PRK12872  70 ervvfSETKAYGLFLLL----NVLGLYLGAYLLAVIGGPKFALIFIIPLILGILYSVFFKrRLKRIPLFKNLVVSLLWAL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 153 VVnlgLFLFFrigLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNvfrgTLILLTGCYL 232
Cdd:PRK12872 146 SP---LILGV---YYYQLTIFSLLLLYAVFIFLKSFIREIVFDIKDIEGDRKSGLKTLPIVLGKER----TLKFLLILNL 215
                        250       260
                 ....*....|....*....|....*....
gi 402797847 233 AMAIWglwaaMPLNTAFLIVSHLCLLALL 261
Cdd:PRK12872 216 LFLIL-----LILGVYTGLLPLLLLVLLL 239
PT_UbiA_3 cd13965
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
65-265 7.23e-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: 46.48  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  65 NQLWDVDIDRINKPNLPLANGDFSIAQGRWIVglcgVASLAIAWGLGLWLG-LTVGISLIIGTAYsvppvrlkrFSLLAA 143
Cdd:cd13965   56 NQPESVEEDRINKPWRPIPSGRITPRQARRLR----WLLVPLCLALSAYLGvLEESLLLIVLTWL---------YNELGL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 144 LCILTVRGIVVNLGLFLFFR------IGLGYPPTLITPIWVLTLFILVFTVAIAifKDVPDMEGDRQFKIQTLTLQIGkq 217
Cdd:cd13965  123 ADHWLTRNLLNALGYAAFLAgatriaGGGPHPLDPTAWAWILLSAAIILTTIHA--QDFRDVEGDRARGRRTLPLVFG-- 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 402797847 218 NVFRGTLILLTGCYLAMAIWGLWAAMPLNTA-FLIVSHLCLLALLWWRS 265
Cdd:cd13965  199 DAAARWLIAAGVVAWSVVLPYFWGLPPLLAAlLVALGAVVAVRFLLLRS 247
PT_UbiA_5 cd13967
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
51-273 3.84e-05

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: 44.52  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  51 WLACLLGNVYIV---GLNQLWDVDIDRINKPN---LPLANGDFSIAqgrwiVGLC-GVASLAIAWGLGLWLGLTVGISLI 123
Cdd:cd13967   35 LPALLIAGLVVYsvyTLNRLTDSEEDAYNDPEraaFYEKYKKLLLA-----LAIAaGLLALALAFILGLLAFAILLLPLL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 124 IGTAYSVPpVRLKRFSLLAALCILTVRGIVVNL--GLFLFFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFkDVPDMEG 201
Cdd:cd13967  110 LGLLYSLP-IKPGKLRLRRRKDIPGSKNLVVALawAVVIALLPALYGQPSTPSVLVVFLFFFLKVFVNTAIF-DIRDVEG 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402797847 202 DRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLCLLALLWWRSRDVHLESK 273
Cdd:cd13967  188 DRIVGIETLPVLLGEERTRLLLLVLNILLALLLVAGVLLGLLASEFLVLLLSLIYGLIYIIFFSRDENEEGL 259
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
82-253 3.07e-04

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: 41.67  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  82 LANGDFSIAQGRWIVGLCGVASLAIAWGL----GLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLG 157
Cdd:COG1575   76 IVSGLLSPKQVLRAALLLLALALLLGLYLvllsGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGT 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 158 LFLffriglgYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIW 237
Cdd:COG1575  156 YYV-------QTGTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLL 228
                        170
                 ....*....|....*.
gi 402797847 238 GLWAAMPLNTAFLIVS 253
Cdd:COG1575  229 VLLGLLPPWALLALLS 244
ubiA PRK13595
prenyltransferase; Provisional
58-266 8.12e-04

prenyltransferase; Provisional


Pssm-ID: 172161  Cd Length: 292  Bit Score: 40.61  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  58 NVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWL----GLTVGISLIIGTAYSVPPV 133
Cdd:PRK13595  60 NLLIYGLNDLADRETDAASPRKGGWQGARLSPGEVRPLLRAVLLLNAPFLLYLALLLppaaTLLLLLYAALFVGYSLPPL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 134 RLKRFSLLAALCILTvrgivvnlglflfFRIGLGYPPTLI--TPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLT 211
Cdd:PRK13595 140 RFKARPFLDGLSNAA-------------YALPLALPALALgaPVPWPPLLALMAWSVGKHAFDAAQDIPADRAAGTRTVA 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 402797847 212 LQIGkqnvFRGTlILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLCLLALLWWRSR 266
Cdd:PRK13595 207 TTLG----VRGT-ALYALAWFLLAGALLWPVSRLTALALWLICGGMALALWRRPT 256
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
11-284 1.88e-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: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  11 SRPHTIIGTTLSVWAVYLLTILGDGNSVNSPASLDLVF--GAWLACLLGNVYivglNQLWDVDIDRINK--PNLPLANGD 86
Cdd:cd13959    1 MRLDKPIGTLLLLPPALWGLLLAAGGLPLPLLKLLLLFllGAFLMRSAGCTI----NDIADRDIDAKVPrtKNRPLASGA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847  87 FSIAQGRWIVGLCGVASLAIAWGLG---LWLGLtvgISLIIGTAYSVppvrLKRFSLLAALciltVRGIVVNLGLFLFFR 163
Cdd:cd13959   77 ISVKEALLFLAVQLLLGLALLLQLNpltILLSP---IALLLVLIYPL----MKRFTYWPQL----VLGLAFGWGPLMGWA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402797847 164 IGLGyppTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQnvfrgTLILLTGCYLAMAIWGLWAA- 242
Cdd:cd13959  146 AVTG---SLPLPALLLYLAVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDR-----TKLILALLLHLFVALLLLAGg 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 402797847 243 -MPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIW 284
Cdd:cd13959  218 lAGLGWPYYLGLGAAAHLLWQEHRLDLPDPLRSCLAFFLSNGW 260
 
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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