|
Name |
Accession |
Description |
Interval |
E-value |
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
7-295 |
5.93e-89 |
|
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: 266.75 E-value: 5.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 7 YFQLMRLPAVFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQHAA 86
Cdd:cd13964 1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 87 VLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRTILGPLAMGLCRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964 81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 167 ILGMYVVGLTWFARMEAKNSHRGHL--LGGTLVINAGLAALVWMIATYPWPrelnltMLLTALGVVVLTINRRLIQAILN 244
Cdd:cd13964 158 ALGVYIAGVTYIARGEVHGGPRRLLplALLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1712560517 245 PVPQNVQIAVKTMLYSYVMLNAIIVFVWtTNPQYAILTAALLIPTIVLSRW 295
Cdd:cd13964 232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
|
|
| prenyl_rel_EboC |
NF035940 |
UbiA-like protein EboC; |
6-299 |
2.18e-57 |
|
UbiA-like protein EboC;
Pssm-ID: 468273 Cd Length: 292 Bit Score: 186.21 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLPAVFTAMSDILLGY------LLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940 1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 80 ISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILK-RTILGPLAMGLCRFLNVMLGASAV-AREINLW 157
Cdd:NF035940 81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKhHAIFGPLNMGLCRGGNLLLGMSVVpEALSEYW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 158 VkpqlrIAAILGMYVVGLTWFARMEAKNSHRGHLLGGtLVINAGLAALVWMIATYPWPrelNLTMLLTALGVVVLTINRR 237
Cdd:NF035940 161 F-----LALIPIVYIAAITMISRGEVHGGKKSTLIIA-LLLYALVIASLLGLAFLQNG---NLLIALPFVLLFAILIFPP 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712560517 238 LIQAILNPVPQNVQIAVKTMLYSYVMLNAIIVFVWTTNPqYAILTAALLIPTIVLSRWMSVT 299
Cdd:NF035940 232 LIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGFGGWP-YGLLVLLLLPLSLLLAKIFAVT 292
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
5-158 |
1.45e-15 |
|
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: 74.88 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 5 LAYFQLMRLPA---VFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382 1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 80 ISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLWV 158
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRfTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
6-128 |
2.79e-14 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 71.54 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLPAVFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQHA 85
Cdd:PRK12882 6 GYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAVSPRGA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712560517 86 AVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT 128
Cdd:PRK12882 86 LAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGT 128
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
23-178 |
3.45e-13 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 23 ILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQHAAVLGGLLMLAGVGAA 100
Cdd:pfam01040 5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712560517 101 QAVGKQSLIVASLLVVAILSYDSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLWVkpqLRIAAILGMYVVGLTWF 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 |
8.18e-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: 49.39 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 56 VFNDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLL-VVAILSYDS---ILKRTI-L 130
Cdd:TIGR01476 56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppiKLKRNGwL 135
|
....*...
gi 1712560517 131 GPLAMGLC 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 |
5.93e-89 |
|
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: 266.75 E-value: 5.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 7 YFQLMRLPAVFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQHAA 86
Cdd:cd13964 1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 87 VLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRTILGPLAMGLCRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964 81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 167 ILGMYVVGLTWFARMEAKNSHRGHL--LGGTLVINAGLAALVWMIATYPWPrelnltMLLTALGVVVLTINRRLIQAILN 244
Cdd:cd13964 158 ALGVYIAGVTYIARGEVHGGPRRLLplALLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1712560517 245 PVPQNVQIAVKTMLYSYVMLNAIIVFVWtTNPQYAILTAALLIPTIVLSRW 295
Cdd:cd13964 232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
|
|
| prenyl_rel_EboC |
NF035940 |
UbiA-like protein EboC; |
6-299 |
2.18e-57 |
|
UbiA-like protein EboC;
Pssm-ID: 468273 Cd Length: 292 Bit Score: 186.21 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLPAVFTAMSDILLGY------LLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940 1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 80 ISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILK-RTILGPLAMGLCRFLNVMLGASAV-AREINLW 157
Cdd:NF035940 81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKhHAIFGPLNMGLCRGGNLLLGMSVVpEALSEYW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 158 VkpqlrIAAILGMYVVGLTWFARMEAKNSHRGHLLGGtLVINAGLAALVWMIATYPWPrelNLTMLLTALGVVVLTINRR 237
Cdd:NF035940 161 F-----LALIPIVYIAAITMISRGEVHGGKKSTLIIA-LLLYALVIASLLGLAFLQNG---NLLIALPFVLLFAILIFPP 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712560517 238 LIQAILNPVPQNVQIAVKTMLYSYVMLNAIIVFVWTTNPqYAILTAALLIPTIVLSRWMSVT 299
Cdd:NF035940 232 LIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGFGGWP-YGLLVLLLLPLSLLLAKIFAVT 292
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
6-150 |
4.78e-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: 79.08 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLP-AVFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYL-SGMVFNDVFDRKVDAEERPSRPIPSGRISTQ 83
Cdd:cd13961 1 AYLELIRPPnLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAaAGYIINDYFDVEIDRINKPDRPIPSGRISRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712560517 84 HAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT-ILGPLAMGLCRFLNVMLGASAV 150
Cdd:cd13961 81 EALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTpLIGNLLVALLTGLPFLFGGLAA 148
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
5-158 |
1.45e-15 |
|
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: 74.88 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 5 LAYFQLMRLPA---VFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382 1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 80 ISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLWV 158
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRfTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
6-128 |
2.79e-14 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 71.54 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLPAVFTAMSDILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQHA 85
Cdd:PRK12882 6 GYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAVSPRGA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712560517 86 AVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT 128
Cdd:PRK12882 86 LAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGT 128
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
1-152 |
4.38e-14 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 70.76 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 1 MKKWLAYFQLMRLPAVFTAMSDILLGYLLTHnSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRI 80
Cdd:PRK12884 1 RTKMKAYLELLRPEHGLMAGIAVVLGAIIAL-GGLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRI 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712560517 81 STQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT-ILGPLAMGLCRFLNVMLGASAVAR 152
Cdd:PRK12884 80 SRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
23-178 |
3.45e-13 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 23 ILLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQHAAVLGGLLMLAGVGAA 100
Cdd:pfam01040 5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712560517 101 QAVGKQSLIVASLLVVAILSYDSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLWVkpqLRIAAILGMYVVGLTWF 178
Cdd:pfam01040 85 LLLNPLTALLGLAALLLYVLYTLRLKRrTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
6-128 |
4.43e-12 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 64.98 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 6 AYFQLMRLPAVFTAMSDILLGYLLTHNsFELPIQFALLIVASTSLYLS-GMVFNDVFDRKVDAEERPSRPIPSGRISTQH 84
Cdd:PRK09573 5 AYFELIRPKNCIGASIGAIIGYLIASN-FKIDLKGIILAALVVFLVCAgGNVINDIYDIEIDKINKPERPIPSGRISLKE 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1712560517 85 AAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT 128
Cdd:PRK09573 84 AKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKT 127
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
8-178 |
1.13e-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: 63.91 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 8 FQLMRLPAVFTAMSDILLGYLLTHNSF-ELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQHAA 86
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAgPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 87 VLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKRT-ILGPLAMGLCRFLNVMLGASAVAREINLWvkPQLRIA 165
Cdd:cd13956 81 AFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLkLGGWGVLGYATGLALLPGLGAVAAGGLVP--LALLLA 158
|
170
....*....|...
gi 1712560517 166 AILGMYVVGLTWF 178
Cdd:cd13956 159 LVFLLLGLGINLY 171
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
24-158 |
1.11e-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: 60.94 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 24 LLGYLLTHNSFELPI--QFALLIVASTSLYLSGMVFNDVFDRKVDAE-ERP-SRPIPSGRISTQHAAVLGGLLMLAGVGA 99
Cdd:cd13959 17 LWGLLLAAGGLPLPLlkLLLLFLLGAFLMRSAGCTINDIADRDIDAKvPRTkNRPLASGAISVKEALLFLAVQLLLGLAL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 100 AQAVGKQSLIVASLLVVAILSYdSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLWV 158
Cdd:cd13959 97 LLQLNPLTILLSPIALLLVLIY-PLMKRfTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPA 155
|
|
| PRK07566 |
PRK07566 |
chlorophyll synthase ChlG; |
52-138 |
5.27e-07 |
|
chlorophyll synthase ChlG;
Pssm-ID: 236052 Cd Length: 314 Bit Score: 50.31 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 52 LSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDS---ILK 126
Cdd:PRK07566 77 LCGTsqTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLFLAWIYSApplRLK 156
|
90
....*....|...
gi 1712560517 127 RTI-LGPLAMGLC 138
Cdd:PRK07566 157 QNGwLGNYAVGLS 169
|
|
| chlor_syn_BchG |
TIGR01476 |
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ... |
56-138 |
8.18e-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: 49.39 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 56 VFNDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLL-VVAILSYDS---ILKRTI-L 130
Cdd:TIGR01476 56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppiKLKRNGwL 135
|
....*...
gi 1712560517 131 GPLAMGLC 138
Cdd:TIGR01476 136 GPPAVGLS 143
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
16-121 |
9.82e-07 |
|
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: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 16 VFTAMSdillGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAE-ERPS-RPIPSGRISTQHAAVLGGLLM 93
Cdd:cd13957 13 LLTALA----GYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKmKRTRnRPLPSGRISPKHALIFGLVLG 88
|
90 100
....*....|....*....|....*...
gi 1712560517 94 LAGVGAAQAvgKQSLIVASLLVVAILSY 121
Cdd:cd13957 89 ILGLALLAL--FVNPLTALLGLLGIFLY 114
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
1-126 |
2.82e-06 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 47.93 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 1 MKKWLAYFQLMR----LPAVFtamsdILLGYLLTHNSFELP------IQFALLIVASTSLYLsgmvFNDVFDRKVDAE-- 68
Cdd:PRK12324 8 KNLLAGYLKLLRpkqwIKNLF-----VFAAPIFAGNLLNPGallkvlLAFVLFCLASSAVYL----VNDIRDVEADRLhp 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712560517 69 ERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILK 126
Cdd:PRK12324 79 TKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYLVLNLAYSFKLK 136
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
40-130 |
2.10e-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: 260126 Cd Length: 278 Bit Score: 45.16 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 40 FALLIVASTSLYlsgmVFNDVFDRKVDAE--ERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVA 117
Cdd:cd13963 39 FVAFCLAASAVY----ILNDLLDLEADRLhpTKRNRPIASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVL 114
|
90
....*....|...
gi 1712560517 118 ILSYDSILKRTIL 130
Cdd:cd13963 115 NLAYSLKLKRIPL 127
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
3-128 |
2.51e-05 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 45.13 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 3 KWLAYFQL-----MRLpAVFTAmsdiLLGYLLTHNSFELPIQFALLIVASTSLYLSGMVFNDVFDRKVDAE-ERPS-RPI 75
Cdd:PRK04375 9 TLKDYLALtkprvISL-NLFTA----LGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKmERTKnRPL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712560517 76 PSGRISTQHAAVLGGLLMLAGVGA-AQAVgkqSLIVASLLVVAILSYDSI----LKRT 128
Cdd:PRK04375 84 VTGRISPREALIFGLVLGVLGFLLlGLFV---NPLAAWLTLAGIFFYVVVytlwLKRR 138
|
|
| PLN00012 |
PLN00012 |
chlorophyll synthetase; Provisional |
58-100 |
7.04e-05 |
|
chlorophyll synthetase; Provisional
Pssm-ID: 215028 Cd Length: 375 Bit Score: 43.70 E-value: 7.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1712560517 58 NDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAA 100
Cdd:PLN00012 143 NDWYDREIDAINEPYRPIPSGAISENEVITQIWVLLLGGLGLA 185
|
|
| PRK12392 |
PRK12392 |
bacteriochlorophyll c synthase; Provisional |
58-121 |
7.16e-05 |
|
bacteriochlorophyll c synthase; Provisional
Pssm-ID: 171463 Cd Length: 331 Bit Score: 43.91 E-value: 7.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 58 NDVFDRKVDAEERPSRPIPSGRISTQHAA----VLGGLLMLAGVGAAQAVGKQS--LIVASLLVVAILSY 121
Cdd:PRK12392 70 NDYFDLELDRVNEPTRPIPSGRLSEKEALwnsiIVLLLAIGLGVWLGLHIGGERgmVIISSILAGLFVAY 139
|
|
| PT_UbiA_chlorophyll |
cd13958 |
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ... |
31-295 |
2.13e-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: 42.22 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 31 HNSFELPIQFALLIVASTSLyLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGkqSL 108
Cdd:cd13958 28 QWSNWDVWLLLLGMLLAGPL-LTGTsqTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLD--GP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 109 IVASLLVVAIlsydsilkrtilgplamglcrFLNVMLGASAVAREINLWVKPqlriaAILGMYVVGLTWFArmeaknshr 188
Cdd:cd13958 105 WVFAAAVVGL---------------------VLAYIYSAPPLKLKQNGWWGN-----AAVGLSYEGLPWWA--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 189 GHLLggtlvinaglaalvwmIATYPWPRELNLTMLLTALGVVVLTIN--------RRL-IQAIlnPVPQNVQ----IAVK 255
Cdd:cd13958 150 GAAA----------------FAGLLTWESLALALLYSIGAHGIMTLNdfksiegdRQLgLRSL--PVALGVDtaawIACG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1712560517 256 TMLYSYVMlnAIIVFVWTTNPQYAILTAALLIPTIVLSRW 295
Cdd:cd13958 212 VIDVPQLA--VAALLLAWGETWYAAVVGALLLAQIPLQFK 249
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
56-157 |
5.36e-04 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 41.40 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 56 VFNDVFDRKVDaEERPS---RPIPSGRISTQHAAVLGGLLMLAGVGAAQAVGKQSLIVASLLVVAILSYDSILKR-TILG 131
Cdd:PRK08238 244 ILNDLLDLEAD-RAHPRkrrRPFASGALPIPFGLAAAPLLLLAGLALALALGPAFLLVLLAYLALTLAYSLRLKRkVLVD 322
|
90 100
....*....|....*....|....*.
gi 1712560517 132 PLAMGLCRFLNVMLGASAVAREINLW 157
Cdd:PRK08238 323 VLTLAALYTLRIIAGAAAIGVALSFW 348
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
24-152 |
1.88e-03 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 39.33 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 24 LLGYLLTHNSFElPIQFALLIVASTSLYLS-GMVFNDVFDRKVDAEERPSRPIPSGRISTQHAAVLGGLLMLAGVGAAQA 102
Cdd:PRK12883 23 ILGSLVALGGIP-PIKTLILIFLVVYLGCSgGNTINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAYL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1712560517 103 VGKQSLIVASLLVVAILSYDSILK-RTILGPLAMGLCRFLNVMLGASAVAR 152
Cdd:PRK12883 102 INIEAFLFALGAYVLMFLYAWKLKpLPFIGNVVVALLTGATPIYGAIAVGR 152
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
31-157 |
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 1712560517 31 HNSFELPIQFALLIVASTSLYLSG---------------------MVFNDVFDRKVDAE--ERPSRPIPSGRISTQHAAV 87
Cdd:PRK12874 19 HSIFSLPFIFIAMIVASKQKNDTGwfgfkllilgilaavsarnfaMAFNRLVDRDIDKDnpRTANRPSVDGRISVKSMVL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712560517 88 LGGLLMLAGVGAAQAVGKQSLIVaSLLVVAILSYDSILKR-TILGPLAMGLCRFLNVMLGASAVAREINLW 157
Cdd:PRK12874 99 FIVLNALIFIGVSYFINPLAFKL-SFPFLIVLGGYSYFKRfSSLAHLVLGLSLGLAPIAGVVAVLGEIPLW 168
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
8-119 |
2.69e-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: 38.65 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712560517 8 FQLMRLPAVFTAMSDILLGYLLT--HNSFELPIQFALLIVASTSLYLSGMVFNDVFD--RKVDAEER--PSRPIPSGRIS 81
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALAyyLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRsgPSRVLVSGLLS 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1712560517 82 TQHAAVLGGLLMLAGVGAAQA-VGKQSLIVASLLVVAIL 119
Cdd:cd13962 81 PRQVLRAALVLLLLAALLGLYlVALGGWLLLLLGLLGIL 119
|
|
|