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Conserved domains on  [gi|148847320|gb|EDL61654|]
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hypothetical protein PM8797T_05115 [Gimesia maris DSM 8797]

Protein Classification

UbiA family prenyltransferase( domain architecture ID 10195487)

UbiA family prenyltransferase catalyzes the Mg2+-dependent transfer of a hydrophobic polyprenyl chain onto a variety of acceptor molecules and is involved in the synthesis of molecules that mediate electron transport, including Vitamin K and Coenzyme Q

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 7-295 5.32e-87

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: 261.75  E-value: 5.32e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQKAA 86
Cdd:cd13964    1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  87 TLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFLAPLMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964   81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 167 ALGLFIVGLTWFARMEAKDSHRGHLI--GGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964  158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148847320 245 PVPQNVQIAVKTMLMSYVMLNAILVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964  232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
 
Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 7-295 5.32e-87

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: 261.75  E-value: 5.32e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQKAA 86
Cdd:cd13964    1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  87 TLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFLAPLMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964   81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 167 ALGLFIVGLTWFARMEAKDSHRGHLI--GGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964  158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148847320 245 PVPQNVQIAVKTMLMSYVMLNAILVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964  232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 7.84e-55

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 179.66  E-value: 7.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   6 AYFQLMRLPAVFTAMSDIILGF------LLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGR 79
Cdd:NF035940   1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  80 ISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAvareinlwV 158
Cdd:NF035940  81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKhHAIFGPLNMGLCRGGNLLLGMSV--------V 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 159 KPQLRIAAALGL----FIVGLTWFARMEAKDSHRGHLIGGLLVINSGLGALaWMLATYPWpreTNLSMVLAALGVVALTI 234
Cdd:NF035940 153 PEALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLYALVIASL-LGLAFLQN---GNLLIALPFVLLFAILI 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148847320 235 NRRLVQAILNPVPQNVQIAVKTMLMSYVMLNAILVFVWtANPQYAILTAALLLPTILLSRWMAVT 299
Cdd:NF035940 229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
ubiA PRK12884
prenyltransferase; Reviewed
 4-152 3.12e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 71.14  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   4 LLAYFQLMRLPAVFTAMSDIILGFLLTHGsFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQ 83
Cdd:PRK12884   4 MKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRISRR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  84 KAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNT-FLAPLMMGICRFLNVMLGASAVAR 152
Cdd:PRK12884  83 EALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 5-158 6.15e-14

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: 70.26  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   5 LAYFQLMRLPA---VFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDA--AERPSRPIPSGR 79
Cdd:COG0382    1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  80 ISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAVAREINLWV 158
Cdd:COG0382   81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKrFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
UbiA pfam01040
UbiA prenyltransferase family;
23-178 1.69e-12

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 65.71  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   23 IILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAER--PSRPIPSGRISTQKAATLGGLLMLAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPrtPNRPLPSGRISPREALIFALVLLALGLLLL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148847320  101 QTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAVAREINLWVkpqLRIAAALGLFIVGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKrRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
 56-138 4.99e-07

bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130541  Cd Length: 283  Bit Score: 50.16  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   56 VFNDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLL-VVAILGYDM----LLKNTFL 130
Cdd:TIGR01476  56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppikLKRNGWL 135


                  ....*...
gi 148847320  131 APLMMGIC 138
Cdd:TIGR01476 136 GPPAVGLS 143
 
Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 7-295 5.32e-87

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: 261.75  E-value: 5.32e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQKAA 86
Cdd:cd13964    1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  87 TLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFLAPLMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964   81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 167 ALGLFIVGLTWFARMEAKDSHRGHLI--GGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964  158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148847320 245 PVPQNVQIAVKTMLMSYVMLNAILVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964  232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 7.84e-55

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 179.66  E-value: 7.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   6 AYFQLMRLPAVFTAMSDIILGF------LLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGR 79
Cdd:NF035940   1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  80 ISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAvareinlwV 158
Cdd:NF035940  81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKhHAIFGPLNMGLCRGGNLLLGMSV--------V 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 159 KPQLRIAAALGL----FIVGLTWFARMEAKDSHRGHLIGGLLVINSGLGALaWMLATYPWpreTNLSMVLAALGVVALTI 234
Cdd:NF035940 153 PEALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLYALVIASL-LGLAFLQN---GNLLIALPFVLLFAILI 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148847320 235 NRRLVQAILNPVPQNVQIAVKTMLMSYVMLNAILVFVWtANPQYAILTAALLLPTILLSRWMAVT 299
Cdd:NF035940 229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
ubiA PRK12884
prenyltransferase; Reviewed
 4-152 3.12e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 71.14  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   4 LLAYFQLMRLPAVFTAMSDIILGFLLTHGsFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQ 83
Cdd:PRK12884   4 MKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRISRR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  84 KAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNT-FLAPLMMGICRFLNVMLGASAVAR 152
Cdd:PRK12884  83 EALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 5-158 6.15e-14

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: 70.26  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   5 LAYFQLMRLPA---VFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDA--AERPSRPIPSGR 79
Cdd:COG0382    1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  80 ISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAVAREINLWV 158
Cdd:COG0382   81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKrFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 6-130 8.64e-14

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: 69.84  E-value: 8.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   6 AYFQLMRLP-AVFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYL-SGMVFNDVFDRKVDAAERPSRPIPSGRISTQ 83
Cdd:cd13961    1 AYLELIRPPnLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAaAGYIINDYFDVEIDRINKPDRPIPSGRISRR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148847320  84 KAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFL 130
Cdd:cd13961   81 EALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPL 127
ubiA PRK12882
prenyltransferase; Reviewed
 1-128 6.67e-13

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 67.31  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   1 MKTLLAYFQLMRLPAVFTAMSDIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRI 80
Cdd:PRK12882   1 GMTVRGYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148847320  81 STQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNT 128
Cdd:PRK12882  81 SPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGT 128
UbiA pfam01040
UbiA prenyltransferase family;
23-178 1.69e-12

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 65.71  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   23 IILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAER--PSRPIPSGRISTQKAATLGGLLMLAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPrtPNRPLPSGRISPREALIFALVLLALGLLLL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148847320  101 QTVGTQSLIVASLLVVAILGYDMLLK-NTFLAPLMMGICRFLNVMLGASAVAREINLWVkpqLRIAAALGLFIVGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKrRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 8-178 7.00e-11

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: 61.60  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   8 FQLMRLPAVFTAMSDIILGFLL-THGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAAERPSRPIPSGRISTQKAA 86
Cdd:cd13956    1 LRLMRPYTLLYVLAPALAGAALaGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  87 TLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFLA-PLMMGICRFLNVMLGASAVAREINLWvkPQLRIA 165
Cdd:cd13956   81 AFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGgWGVLGYATGLALLPGLGAVAAGGLVP--LALLLA 158

                        170
                 ....*....|...
gi 148847320 166 AALGLFIVGLTWF 178
Cdd:cd13956  159 LVFLLLGLGINLY 171
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
 4-128 1.24e-10

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 60.74  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   4 LLAYFQLMRLPAVFTAMSDIILGFLLTHGS--FSPPISFALLLIASASLYlsGMVFNDVFDRKVDAAERPSRPIPSGRIS 81
Cdd:PRK09573   3 IKAYFELIRPKNCIGASIGAIIGYLIASNFkiDLKGIILAALVVFLVCAG--GNVINDIYDIEIDKINKPERPIPSGRIS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148847320  82 TQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNT 128
Cdd:PRK09573  81 LKEAKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKT 127
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 24-177 1.63e-10

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: 60.56  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  24 ILGFLLTHGSFSPPISFALLLIASASLYLS--GMVFNDVFDRKVDAA-ERP-SRPIPSGRISTQKAATLGGLLMLAGVGA 99
Cdd:cd13959   17 LWGLLLAAGGLPLPLLKLLLLFLLGAFLMRsaGCTINDIADRDIDAKvPRTkNRPLASGAISVKEALLFLAVQLLLGLAL 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148847320 100 AQTVGTQSLIVASLLVVAILGYDMLLKNTFLAPLMMGICRFLNVMLGASAVAREINLwvkpqlriaAALGLFIVGLTW 177
Cdd:cd13959   97 LLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPL---------PALLLYLAVIFW 165
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
1-127 2.67e-07

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 51.02  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   1 MKTLLAYFQLMR----LPAVFTAMSDIILGFLLTHGSFSP-PISFALLLIASASLYLsgmvFNDVFDRKVDAA--ERPSR 73
Cdd:PRK12324   8 KNLLAGYLKLLRpkqwIKNLFVFAAPIFAGNLLNPGALLKvLLAFVLFCLASSAVYL----VNDIRDVEADRLhpTKRNR 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148847320  74 PIPSGRISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKN 127
Cdd:PRK12324  84 PIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYLVLNLAYSFKLKH 137
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
 56-138 4.99e-07

bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130541  Cd Length: 283  Bit Score: 50.16  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   56 VFNDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLL-VVAILGYDM----LLKNTFL 130
Cdd:TIGR01476  56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppikLKRNGWL 135


                  ....*...
gi 148847320  131 APLMMGIC 138
Cdd:TIGR01476 136 GPPAVGLS 143
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 16-121 1.02e-06

Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O synthase, heme A:farnesyltransferase, cytochrome c oxidase subunit X [Cox10]) converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of the heme B porphyrin ring with a hydroxyethyl farnesyl side group. It is localized at the mitochondrial inner membrane. Eukaryotic Cox10 is important for the maturation of the heme A prosthetic group of cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, that catalyzes the electron transfer from reduced cytochrome c to oxygen. 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: 260120  Cd Length: 271  Bit Score: 48.97  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  16 VFTAMSdiilGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAA-ERPS-RPIPSGRISTQKAATLGGLLM 93
Cdd:cd13957   13 LLTALA----GYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKmKRTRnRPLPSGRISPKHALIFGLVLG 88

                         90       100
                 ....*....|....*....|....*...
gi 148847320  94 LAGVGAAQTvgTQSLIVASLLVVAILGY 121
Cdd:cd13957   89 ILGLALLAL--FVNPLTALLGLLGIFLY 114
PRK07566 PRK07566
chlorophyll synthase ChlG;
52-138 2.34e-06

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 48.38  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  52 LSGM--VFNDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDM----LL 125
Cdd:PRK07566  77 LCGTsqTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLFLAWIYSApplrLK 156

                         90
                 ....*....|...
gi 148847320 126 KNTFLAPLMMGIC 138
Cdd:PRK07566 157 QNGWLGNYAVGLS 169
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 23-127 6.31e-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: 260126  Cd Length: 278  Bit Score: 46.70  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  23 IILGFLLTHGSFSPPISFALL---LIASASlYlsgmVFNDVFDRKVDAA--ERPSRPIPSGRISTQKAATLGGLLMLAGV 97
Cdd:cd13963   20 LLFAGQLFDPDLLLAALLAFVafcLAASAV-Y----ILNDLLDLEADRLhpTKRNRPIASGRLSIPAALALAVVLLLAGL 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 148847320  98 GAAQTVGTQSLIVASLLVVAILGYDMLLKN 127
Cdd:cd13963   95 ALALLLSPAFLLVLLAYLVLNLAYSLKLKR 124
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 3-126 8.37e-06

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 46.29  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   3 TLLAYFQL-----MRLpAVFTAmsdiILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDAA-ERPS-RPI 75
Cdd:PRK04375   9 TLKDYLALtkprvISL-NLFTA----LGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKmERTKnRPL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148847320  76 PSGRISTQKAATLGGLLMLAGV---GAAQTVGTQSLIVASLLVVAILgYDMLLK 126
Cdd:PRK04375  84 VTGRISPREALIFGLVLGVLGFlllGLFVNPLAAWLTLAGIFFYVVV-YTLWLK 136
PRK12392 PRK12392
bacteriochlorophyll c synthase; Provisional
 58-172 9.60e-06

bacteriochlorophyll c synthase; Provisional


Pssm-ID: 171463  Cd Length: 331  Bit Score: 46.22  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  58 NDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTVGTQS------LIVASLLVVAILGYDM------LL 125
Cdd:PRK12392  70 NDYFDLELDRVNEPTRPIPSGRLSEKEALWNSIIVLLLAIGLGVWLGLHIggergmVIISSILAGLFVAYIYsapplkLK 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148847320 126 KNTFLAPLMMGICRFLNVMLGASAVAREInlwvKPQLRIAAALGLFI 172
Cdd:PRK12392 150 KNILTSAPAVGFSYGFITFLSANALFSDI----RPEVVWLAGLNFFM 192
PLN00012 PLN00012
chlorophyll synthetase; Provisional
 58-103 2.28e-05

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 45.24  E-value: 2.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148847320  58 NDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTV 103
Cdd:PLN00012 143 NDWYDREIDAINEPYRPIPSGAISENEVITQIWVLLLGGLGLAYTL 188
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
 24-126 1.72e-04

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 42.41  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  24 ILGFLLTHGSFsPPISFALLLIASASLYLS-GMVFNDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQT 102
Cdd:PRK12883  23 ILGSLVALGGI-PPIKTLILIFLVVYLGCSgGNTINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAYL 101

                         90       100
                 ....*....|....*....|....
gi 148847320 103 VGTQSLIVASLLVVAILGYDMLLK 126
Cdd:PRK12883 102 INIEAFLFALGAYVLMFLYAWKLK 125
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
 32-295 2.46e-04

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: 41.83  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  32 GSFSPPISFALLLIASASLYLSGM--VFNDVFDRKVDAAERPSRPIPSGRISTQKAATLGGLLMLAGVGAAQTVGtqSLI 109
Cdd:cd13958   28 QWSNWDVWLLLLGMLLAGPLLTGTsqTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLD--GPW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 110 VASLLVVAIlgydmllkntflaplmmgicrFLNVMLGASAVAREINLWVKPqlriaAALGLFIVGLTWFARMEAKDSHRG 189
Cdd:cd13958  106 VFAAAVVGL---------------------VLAYIYSAPPLKLKQNGWWGN-----AAVGLSYEGLPWWAGAAAFAGLLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320 190 HLIGGLLVINSgLGALAWMLATYPWPRETNLSMVLAALgVVALTINRRLVqailnpvpqnvqIAVKTMLMSYVMLNAILV 269
Cdd:cd13958  160 WESLALALLYS-IGAHGIMTLNDFKSIEGDRQLGLRSL-PVALGVDTAAW------------IACGVIDVPQLAVAALLL 225

                        250       260
                 ....*....|....*....|....*.
gi 148847320 270 fvWTANPQYAILTAALLLPTILLSRW 295
Cdd:cd13958  226 --AWGETWYAAVVGALLLAQIPLQFK 249
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
 8-121 1.12e-03

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: 39.80  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   8 FQLMRLPAVFTAMSDIILGFLLT--HGSFSPPISFALLLIASASLYLSGMVFNDVFD--RKVDAAER--PSRPIPSGRIS 81
Cdd:cd13962    1 LLAARPRTLPASLAPVLLGTALAyyLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRsgPSRVLVSGLLS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148847320  82 TQKAATLGGLLMLAGVGAAQTVGTQSLIVasLLVVAILGY 121
Cdd:cd13962   81 PRQVLRAALVLLLLAALLGLYLVALGGWL--LLLLGLLGI 118
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
13-157 1.97e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 39.22  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  13 LPAVFTAMsdIILGFLLTHGSFSPPISFALLLIASASLYLSGMVFNDVFDRKVDA-----AERPSrpiPSGRISTQKAAT 87
Cdd:PRK12874  24 LPFIFIAM--IVASKQKNDTGWFGFKLLILGILAAVSARNFAMAFNRLVDRDIDKdnprtANRPS---VDGRISVKSMVL 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320  88 LGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLKNTFLAPLMMGICRFLNVMLGASAVAREINLW 157
Cdd:PRK12874  99 FIVLNALIFIGVSYFINPLAFKLSFPFLIVLGGYSYFKRFSSLAHLVLGLSLGLAPIAGVVAVLGEIPLW 168
PRK08238 PRK08238
UbiA family prenyltransferase;
4-126 4.01e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 38.70  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148847320   4 LLAYFQLMRLPAVFTAmsdiILGFLlthgSFSppisfallLIASASlYlsgmVFNDVFDRKVDAAErPS---RPIPSGRI 80
Cdd:PRK08238 213 LLAAHQFGDLQALLAA----LLAFL----AFS--------LCASAV-Y----ILNDLLDLEADRAH-PRkrrRPFASGAL 270

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148847320  81 STQKAATLGGLLMLAGVGAAQTVGTQSLIVASLLVVAILGYDMLLK 126
Cdd:PRK08238 271 PIPFGLAAAPLLLLAGLALALALGPAFLLVLLAYLALTLAYSLRLK 316
 
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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