NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500639189|ref|WP_011962485|]
View 

geranylgeranylglycerol-phosphate geranylgeranyltransferase [Flavobacterium psychrophilum]

Protein Classification

geranylgeranylglycerol-phosphate geranylgeranyltransferase( domain architecture ID 10195482)

geranylgeranylglycerol-phosphate (DGGGP) geranylgeranyltransferase is a prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP) to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 15-289 5.51e-63

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: 200.04  E-value: 5.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  15 SLFSVVRGYNIPVVVLAQYLSSIFILSPekraLDVILDWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQ 94
Cdd:cd13961    1 AYLELIRPPNLLMAALAQYLGALFALGP----LLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRINKPDRPIPSGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  95 VSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIF 174
Cdd:cd13961   77 ISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLLIIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 175 AHAMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIekYDVGYMDIYFYIS-LII 253
Cdd:cd13961  157 LLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPY--LLGGLGILYLILIiIAD 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500639189 254 LILFLLKLWKSETQAEYVQLHVVLKILIVAGVFCIV 289
Cdd:cd13961  235 LLFLYSAIRLAKSPKDYSKLSKLLKLAMLLGLLAFL 270
 
Name Accession Description Interval E-value
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 15-289 5.51e-63

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: 200.04  E-value: 5.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  15 SLFSVVRGYNIPVVVLAQYLSSIFILSPekraLDVILDWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQ 94
Cdd:cd13961    1 AYLELIRPPNLLMAALAQYLGALFALGP----LLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRINKPDRPIPSGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  95 VSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIF 174
Cdd:cd13961   77 ISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLLIIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 175 AHAMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIekYDVGYMDIYFYIS-LII 253
Cdd:cd13961  157 LLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPY--LLGGLGILYLILIiIAD 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500639189 254 LILFLLKLWKSETQAEYVQLHVVLKILIVAGVFCIV 289
Cdd:cd13961  235 LLFLYSAIRLAKSPKDYSKLSKLLKLAMLLGLLAFL 270
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 21-291 1.17e-40

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: 142.68  E-value: 1.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  21 RGYNIPVVVLAQYLSSIFilspekrALDVILDWRLFLLVFVST-LTISSGYIINNFYDSEKDLIN--RPNKTRLDRQVSQ 97
Cdd:COG0382   11 RPIGILLLLWPTLWALFL-------AAGGLPDLLLLLLAVLGTvLMRSAGYVINDYFDREIDRINerKPNRPLASGRISL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  98 TTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFF-GILLYFKNFYHVIFAH 176
Cdd:COG0382   84 REALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTLLGNLVLGLLFGLGILmGFAAVTGSLPLSAWLL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 177 AMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIEKYDVGYMdIYFYISLIILIL 256
Cdd:COG0382  164 ALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLGLL-YLLGLLAALLLL 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500639189 257 FLLKLWK-SETQAEYVQLHVVLKILIVAGVFCIVLI 291
Cdd:COG0382  243 YLSQLWLlRPRKKDPARALKLFKLNMLLGLLLFLGI 278
ubiA PRK12872
prenyltransferase; Reviewed
 33-292 4.65e-20

prenyltransferase; Reviewed


Pssm-ID: 237241  Cd Length: 285  Bit Score: 87.69  E-value: 4.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  33 YLSSIFILSPEKRALDVIL---DWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTrldrQVSQTTKLQVYFVLNF 109
Cdd:PRK12872  13 YGNLLIAALGQSLVYMASLllgLPISWLLLLITFLIAAAVYIINYLTDLEEDIINKPERV----VFSETKAYGLFLLLNV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 110 LATALSLIIS-----FRAALFFATYIFLIWFYS----HKLKKYPIVGNLTASLL--AVLPFFGILLYFKNFYHVIFAHAM 178
Cdd:PRK12872  89 LGLYLGAYLLaviggPKFALIFIIPLILGILYSvffkRRLKRIPLFKNLVVSLLwaLSPLILGVYYYQLTIFSLLLLYAV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 179 FLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIEKYDVGYMDIYFYISLIILILFL 258
Cdd:PRK12872 169 FIFLKSFIREIVFDIKDIEGDRKSGLKTLPIVLGKERTLKFLLILNLLFLILLILGVYTGLLPLLLLVLLLLLAYVLYYI 248

                        250       260       270
                 ....*....|....*....|....*....|....
gi 500639189 259 LKLWKSETQAEYVQLHVVLKILIVAGVFCIVLIN 292
Cdd:PRK12872 249 IKLFAADDKKDLLYLSLLDKEHMLLGLISMLLGL 282
UbiA pfam01040
UbiA prenyltransferase family;
46-234 5.26e-19

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 84.20  E-value: 5.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189   46 ALDVILDWRLFLLVFVST-LTISSGYIINNFYDSEKDLINRPNKTR--LDRQVSQTTKLQVYFVLNFLATALSLIISFRA 122
Cdd:pfam01040  12 AAGGVPDLLLLLLALLGTvLARAAANALNDYYDRDIDAIMPRTPNRplPSGRISPREALIFALVLLALGLLLLLLLNPLT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  123 ALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIFA-HAMFLFLLLFIREMIKDLENIKGDIA 201
Cdd:pfam01040  92 ALLGLAALLLYVLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALlLALALFLWTWAIALANDLRDREDDRK 171

                         170       180       190
                  ....*....|....*....|....*....|...
gi 500639189  202 NNYQTIPVRFGERVSKQIITFLTISTIIPVYIL 234
Cdd:pfam01040 172 AGIKTLPVVLGRKAARILLALLLAVALLLLLLL 204
 
Name Accession Description Interval E-value
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 15-289 5.51e-63

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: 200.04  E-value: 5.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  15 SLFSVVRGYNIPVVVLAQYLSSIFILSPekraLDVILDWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQ 94
Cdd:cd13961    1 AYLELIRPPNLLMAALAQYLGALFALGP----LLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRINKPDRPIPSGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  95 VSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIF 174
Cdd:cd13961   77 ISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLLIIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 175 AHAMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIekYDVGYMDIYFYIS-LII 253
Cdd:cd13961  157 LLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPY--LLGGLGILYLILIiIAD 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500639189 254 LILFLLKLWKSETQAEYVQLHVVLKILIVAGVFCIV 289
Cdd:cd13961  235 LLFLYSAIRLAKSPKDYSKLSKLLKLAMLLGLLAFL 270
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 21-291 1.17e-40

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: 142.68  E-value: 1.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  21 RGYNIPVVVLAQYLSSIFilspekrALDVILDWRLFLLVFVST-LTISSGYIINNFYDSEKDLIN--RPNKTRLDRQVSQ 97
Cdd:COG0382   11 RPIGILLLLWPTLWALFL-------AAGGLPDLLLLLLAVLGTvLMRSAGYVINDYFDREIDRINerKPNRPLASGRISL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  98 TTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFF-GILLYFKNFYHVIFAH 176
Cdd:COG0382   84 REALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTLLGNLVLGLLFGLGILmGFAAVTGSLPLSAWLL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 177 AMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIEKYDVGYMdIYFYISLIILIL 256
Cdd:COG0382  164 ALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLGLL-YLLGLLAALLLL 242

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500639189 257 FLLKLWK-SETQAEYVQLHVVLKILIVAGVFCIVLI 291
Cdd:COG0382  243 YLSQLWLlRPRKKDPARALKLFKLNMLLGLLLFLGI 278
ubiA PRK12872
prenyltransferase; Reviewed
 33-292 4.65e-20

prenyltransferase; Reviewed


Pssm-ID: 237241  Cd Length: 285  Bit Score: 87.69  E-value: 4.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  33 YLSSIFILSPEKRALDVIL---DWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTrldrQVSQTTKLQVYFVLNF 109
Cdd:PRK12872  13 YGNLLIAALGQSLVYMASLllgLPISWLLLLITFLIAAAVYIINYLTDLEEDIINKPERV----VFSETKAYGLFLLLNV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 110 LATALSLIIS-----FRAALFFATYIFLIWFYS----HKLKKYPIVGNLTASLL--AVLPFFGILLYFKNFYHVIFAHAM 178
Cdd:PRK12872  89 LGLYLGAYLLaviggPKFALIFIIPLILGILYSvffkRRLKRIPLFKNLVVSLLwaLSPLILGVYYYQLTIFSLLLLYAV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 179 FLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILIEKYDVGYMDIYFYISLIILILFL 258
Cdd:PRK12872 169 FIFLKSFIREIVFDIKDIEGDRKSGLKTLPIVLGKERTLKFLLILNLLFLILLILGVYTGLLPLLLLVLLLLLAYVLYYI 248

                        250       260       270
                 ....*....|....*....|....*....|....
gi 500639189 259 LKLWKSETQAEYVQLHVVLKILIVAGVFCIVLIN 292
Cdd:PRK12872 249 IKLFAADDKKDLLYLSLLDKEHMLLGLISMLLGL 282
UbiA pfam01040
UbiA prenyltransferase family;
46-234 5.26e-19

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 84.20  E-value: 5.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189   46 ALDVILDWRLFLLVFVST-LTISSGYIINNFYDSEKDLINRPNKTR--LDRQVSQTTKLQVYFVLNFLATALSLIISFRA 122
Cdd:pfam01040  12 AAGGVPDLLLLLLALLGTvLARAAANALNDYYDRDIDAIMPRTPNRplPSGRISPREALIFALVLLALGLLLLLLLNPLT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  123 ALFFATYIFLIWFYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIFA-HAMFLFLLLFIREMIKDLENIKGDIA 201
Cdd:pfam01040  92 ALLGLAALLLYVLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALlLALALFLWTWAIALANDLRDREDDRK 171

                         170       180       190
                  ....*....|....*....|....*....|...
gi 500639189  202 NNYQTIPVRFGERVSKQIITFLTISTIIPVYIL 234
Cdd:pfam01040 172 AGIKTLPVVLGRKAARILLALLLAVALLLLLLL 204
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
 46-229 2.11e-18

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 83.24  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  46 ALDVILDWRLFLLVF-VSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAAL 124
Cdd:PRK12883  29 ALGGIPPIKTLILIFlVVYLGCSGGNTINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAYLINIEAFL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 125 FFATYIFLIWFYSHKLKKYPIVGNLT-ASLLAVLPFFGILlyfkNFYHVIFAH--AMFLFLLLFIREMIKDLENIKGDIA 201
Cdd:PRK12883 109 FALGAYVLMFLYAWKLKPLPFIGNVVvALLTGATPIYGAI----AVGRIGLAGylAICAFLVNVAREIMKDIEDIEGDKA 184

                        170       180
                 ....*....|....*....|....*...
gi 500639189 202 NNYQTIPVRFGERVSKQIITFLTISTII 229
Cdd:PRK12883 185 KGAKTLPIIIGKKRAAYIGAIFGVLTVI 212
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
 55-229 4.02e-18

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 82.31  E-value: 4.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  55 LFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIW 134
Cdd:PRK09573  39 IILAALVVFLVCAGGNVINDIYDIEIDKINKPERPIPSGRISLKEAKIFSITLFIVGLILSIFINIYAFLIALLNSILLY 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 135 FYSHKLKKYPIVGNLTASLLAVLPFFGILLYFKNFYHVIFAHAMFLFLLLfIREMIKDLENIKGDIANNYQTIPVRFGER 214
Cdd:PRK09573 119 LYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVFNVLRIIILFLCAFFSTW-SREIVKDIEDIEGDLKENVITLPIKYGIK 197

                        170
                 ....*....|....*
gi 500639189 215 VSKQIITFLTISTII 229
Cdd:PRK09573 198 KSWYIAKILLILAIV 212
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 46-232 9.73e-16

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: 75.46  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  46 ALDVILDWRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALF 125
Cdd:cd13956   25 AFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQALAFAAALLLVGLALALALGPLALLL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 126 FATYIFLIWFYSHKLK--KYPIVGNLTASLLAVLPFFGILLYFKNFYHVIFAHAMFLFLLLFIREMIKDLENIKGDIANN 203
Cdd:cd13956  105 LLAGLLLGLAYSLGLKrlKLGGWGVLGYATGLALLPGLGAVAAGGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAG 184

                        170       180       190
                 ....*....|....*....|....*....|
gi 500639189 204 YQTIPVRFGERVSKQII-TFLTISTIIPVY 232
Cdd:cd13956  185 IRTLPVRLGPRRARRLAaGLLLAALILVVL 214
ubiA PRK12884
prenyltransferase; Reviewed
 57-243 2.28e-15

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 74.61  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  57 LLVFVSTLTIS-SGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWF 135
Cdd:PRK12884  40 LLGFLTAFFASgSANALNDYFDYEVDRINRPDRPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGIL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 136 YSHKLKKYPIVGNLTASLLAVLPF-FGILLyFKNFYHVIFAHAMFLFLLLFIREMIKDLENIKGDIANNYQTIPVRFGER 214
Cdd:PRK12884 120 YNWKLKEYGLIGNLYVAFLTGMTFiFGGIA-VGELNEAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEK 198

                        170       180       190
                 ....*....|....*....|....*....|.
gi 500639189 215 VSKQI--ITFLTISTIIPVYILIEKYDVGYM 243
Cdd:PRK12884 199 IAGRIaaALFILAVLLSPLPYLFGIFNILYL 229
ubiA PRK12882
prenyltransferase; Reviewed
 57-214 1.56e-12

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 66.53  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  57 LLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFLIWFY 136
Cdd:PRK12882  42 LAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLY 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 137 SHKLKKYPIVGNLTASLLAVLPF------FGILLYFKNFyhVIFAHAmflFLLLFIREMIKDLENIKGDIANNYQTIPVR 210
Cdd:PRK12882 122 AETLKGTPGLGNASVAYLTGSTFlfggaaVGTEGLLALL--VLFALA---ALATLAREIIKDVEDIEGDRAEGARTLPIL 196


                 ....
gi 500639189 211 FGER 214
Cdd:PRK12882 197 IGVR 200
PT_UbiA_5 cd13967
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 57-235 2.50e-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: 260130  Cd Length: 277  Bit Score: 47.99  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  57 LLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQvsqttKLQVYFVLNFLATALSLIISFRAALFFATYIFLI--- 133
Cdd:cd13967   36 PALLIAGLVVYSVYTLNRLTDSEEDAYNDPERAAFYEK-----YKKLLLALAIAAGLLALALAFILGLLAFAILLLPlll 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 134 -WFYSHKLKK----------YPIVGNLTASLL-AVLPFFGILLYFKNFYHVIFAHAMFLFLLLFIREMIKDLENIKGDIA 201
Cdd:cd13967  111 gLLYSLPIKPgklrlrrrkdIPGSKNLVVALAwAVVIALLPALYGQPSTPSVLVVFLFFFLKVFVNTAIFDIRDVEGDRI 190

                        170       180       190
                 ....*....|....*....|....*....|....
gi 500639189 202 NNYQTIPVRFGERVSKQIITFLTISTIIPVYILI 235
Cdd:cd13967  191 VGIETLPVLLGEERTRLLLLVLNILLALLLVAGV 224
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
 51-235 4.16e-04

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: 41.34  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  51 LDWRLFLLVFVSTLTI-SSGYIINNFYDSEKDLINRPNK--TRL--DRQVSQTTKLQVYFVLNFLATALSLIISFRAALF 125
Cdd:cd13962   30 FNWLLFLLALLAALLLqIGVNLANDYFDYKKGTDTEPRSgpSRVlvSGLLSPRQVLRAALVLLLLAALLGLYLVALGGWL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 126 F----ATYIFLIWFYSHKLKKYpivGNLTASLLAVLPFFGILL----YF---KNFYHVIFAHAMFLFLLLFIREMIKDLE 194
Cdd:cd13962  110 LlllgLLGILAGYFYTGGPFPL---SYRGLGELFVFLFFGLLAvlgtYYvqtGSLSWEVLLAALPLGLLIAAILLANNIR 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500639189 195 NIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILI 235
Cdd:cd13962  187 DIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLV 227
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
57-146 1.23e-03

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 39.85  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  57 LLVFVS-TLTISSGYIINNFYDSEKDLiNRPNKTRldR-----QVSQTTKLQVYFVLNFLATALSLIISFRAALFFATYI 130
Cdd:PRK12324  49 LLAFVLfCLASSAVYLVNDIRDVEADR-LHPTKRN--RpiasgVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYL 125

                         90
                 ....*....|....*.
gi 500639189 131 FLIWFYSHKLKKYPIV 146
Cdd:PRK12324 126 VLNLAYSFKLKHQPVL 141
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
 47-225 1.55e-03

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: 39.52  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  47 LDVILDWRLFLLVFVS-TLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALF 125
Cdd:cd13958   29 WSNWDVWLLLLGMLLAgPLLTGTSQTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLDGPWVFA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 126 FATY-IFLIWFYSH---KLKKYPIVGNLTASLLAV-LPFF-GILLYFKNFYHVIFAHAmFLFLLLFIREMI-KDLENIKG 198
Cdd:cd13958  109 AAVVgLVLAYIYSApplKLKQNGWWGNAAVGLSYEgLPWWaGAAAFAGLLTWESLALA-LLYSIGAHGIMTlNDFKSIEG 187

                        170       180
                 ....*....|....*....|....*..
gi 500639189 199 DIANNYQTIPVRFGERVSKqIITFLTI 225
Cdd:cd13958  188 DRQLGLRSLPVALGVDTAA-WIACGVI 213
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 53-165 3.66e-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: 260127  Cd Length: 282  Bit Score: 38.33  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  53 WRLFLLVFVSTLTISSGYIINNFYDSEKDLINRPNKTRLDRQVSQTTKLQVYFVLNFLATALSLIISFRAALFFATYIFL 132
Cdd:cd13964   32 LRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAALALGAGLLAAGVALAALVGRLSGLVALLLAAA 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 500639189 133 IWFYSHKLKKYPI---------VGN--LTASLLAVLPFFGILLY 165
Cdd:cd13964  112 ILLYDAWLKHTPLgpllmglcrGLNllLGASAAAAGGLGPALLA 155
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 32-146 3.86e-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: 260126  Cd Length: 278  Bit Score: 38.22  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  32 QYLSSIFILSP---EKRALDVILDWRLFLLVFVSTLTISSGYIINNFYDSEKDlinRPNKTRLDR-----QVSQTTKLQV 103
Cdd:cd13963    9 QWVKNLLVFAPllfAGQLFDPDLLLAALLAFVAFCLAASAVYILNDLLDLEAD---RLHPTKRNRpiasgRLSIPAALAL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 500639189 104 YFVLNFLATALSLIISFRAALFFATYIFLIWFYSHKLKKYPIV 146
Cdd:cd13963   86 AVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYSLKLKRIPLL 128
PRK08238 PRK08238
UbiA family prenyltransferase;
57-184 7.32e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 37.93  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  57 LLVFVS-TLTISSGYIINNFYDSEKDlinR--PNKTRldR-----QVSQTTKLQVYFVLNFLATALSLIISFRAALFFAT 128
Cdd:PRK08238 229 LLAFLAfSLCASAVYILNDLLDLEAD---RahPRKRR--RpfasgALPIPFGLAAAPLLLLAGLALALALGPAFLLVLLA 303

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500639189 129 YIFLIWFYSHKLKKYPIVGNLTASLL--------AVLpfFGILLYFknfyhVIFAHAMFLFLLL 184
Cdd:PRK08238 304 YLALTLAYSLRLKRKVLVDVLTLAALytlriiagAAA--IGVALSF-----WLLAFSMFFFLSL 360
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
 51-235 7.76e-03

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: 37.43  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189  51 LDWRLFLLVFVSTLTISSG-YIINNFYDSEK--DLINRPNKTRL--DRQVSQTTKLQVYFVLNFLATALSLIISFRA--- 122
Cdd:COG1575   32 FNWLLFLLALLAALLLQIGvNLANDYFDYKKgtDTEERVGPSRVivSGLLSPKQVLRAALLLLALALLLGLYLVLLSgwp 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500639189 123 -ALFFATYIFLIWFYShkLKKYPIvGNLTASLLAVLPFFGILL----YF---KNFYHVIFAHAMFLFLLLFIREMIKDLE 194
Cdd:COG1575  112 lLLLGLLGILAAIFYT--GGPFPL-GYRGLGELFVFLFFGLVAvlgtYYvqtGTLSWAALLASLPVGLLSAAVLLANNLR 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500639189 195 NIKGDIANNYQTIPVRFGERVSKQIITFLTISTIIPVYILI 235
Cdd:COG1575  189 DIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLLV 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH