|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
73-358 |
1.29e-155 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 439.90 E-value: 1.29e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 73 LVSAAKPYAQLMRIDRPIGTYLLFWPCAWSIALSADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRL 152
Cdd:PLN02809 2 LPPSLRPYAKLARLDKPIGTWLLAWPCMWSIALAAPPGSLPDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 153 RPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQG 232
Cdd:PLN02809 82 RPIASGALTPFQGVGFLGAQLLLGLGILLQLNNYSRILGASSLLLVFTYPLMKRFTFWPQAFLGLTFNWGALLGWAAVKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 233 SVNLAACLPLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTVPYYAA 312
Cdd:PLN02809 162 SLDPAVVLPLYASGVCWTLVYDTIYAHQDKEDDLKVGVKSTALRFGDDTKLWLTGFGAASIGGLALSGYNAGLGWPYYAG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 257681406 313 VGVVGAHLVQQIYSLNIDNPSDCAKKFISNHQVGLILFLGIVLGTL 358
Cdd:PLN02809 242 LAAAAGHLAWQIQTVDLSSRADCNRKFVSNKWFGAIVFAGIVLGKL 287
|
|
| ubiA_proteo |
TIGR01474 |
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of ... |
79-358 |
3.36e-136 |
|
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of integral membrane proteins that condenses para-hydroxybenzoate with any of several polyprenyldiphosphates. Heterologous expression studies suggest that for, many but not all members, the activity seen (e.g. octaprenyltransferase in E. coli) reflects available host isoprenyl pools rather than enzyme specificity. A fairly deep split by both clustering (UPGMA) and phylogenetics (NJ tree) separates this group (mostly Proteobacterial and mitochondrial), with several characterized members, from another group (mostly archaeal and Gram-positive bacterial) lacking characterized members. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 130539 Cd Length: 281 Bit Score: 390.14 E-value: 3.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 79 PYAQLMRIDRPIGTYLLFWPCAWSIALSADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASG 158
Cdd:TIGR01474 3 PYAKLMRADKPIGTLLLLWPCLWSLLLAAQAGGIPPLYLLGLFTVGAILMRGAGCVINDIWDRDFDPQVERTKSRPLASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 159 QISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLAA 238
Cdd:TIGR01474 83 AVSVRQAILFLLVQLLVALGVLLQLNPLTILLGVASLALVATYPFMKRITYWPQLVLGLAFGWGALMGWAAVTGDLSTAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 239 CLpLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTVPYYAAVGVVGA 318
Cdd:TIGR01474 163 WV-LYLANILWTLGYDTIYAMQDKEDDIKIGVKSTALRFGDNTKPWLGGLYALMILLLALAGLIAGLGPVYYLGLAAAAL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 257681406 319 HLVQQIYSLNIDNPSDCAKKFISNHQVGLILFLGIVLGTL 358
Cdd:TIGR01474 242 LLIRQIATLDIRDPENCLKLFKANNYVGLLLFAGIALGWL 281
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
84-356 |
8.34e-127 |
|
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: 366.02 E-value: 8.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 84 MRIDRPIGTYLLFWPCAWSIALSADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASGQISQF 163
Cdd:cd13959 1 MRLDKPIGTLLLLPPALWGLLLAAGGLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 164 DAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLaACLPLY 243
Cdd:cd13959 81 EALLFLAVQLLLGLALLLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPL-PALLLY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 244 LSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTVPYYAAVGVVgAHLVQQ 323
Cdd:cd13959 160 LAVIFWTAGYDTIYAHQDREDDRKIGVKSTAVLFGDRTKLILALLLHLFVALLLLAGGLAGLGWPYYLGLGAA-AHLLWQ 238
|
250 260 270
....*....|....*....|....*....|....
gi 257681406 324 IYSLNIDNP-SDCAKKFISNHQVGLILFLGIVLG 356
Cdd:cd13959 239 EHRLDLPDPlRSCLAFFLSNGWVGLLLFAGLLLD 272
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
78-355 |
2.35e-83 |
|
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: 255.54 E-value: 2.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 78 KPYAQLMRIDRPIGTYLLFWPCAWSIALSADAgcWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLAS 157
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPTLWALFLAAGG--LPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 158 GQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPL-MKRVTYWPQLVLGMAFNWGALLGWCATQGSVNL 236
Cdd:COG0382 79 GRISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLfLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 237 AAcLPLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSG-FTAAMLTGLSAAGWACDQTVPYYAAVGV 315
Cdd:COG0382 159 SA-WLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGvLYALAVLLLLLLGLLAGLGLLYLLGLLA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 257681406 316 VGAHLVQ-QIYSLNID--NPSDCAKKFISNHQVGLILFLGIVL 355
Cdd:COG0382 238 ALLLLYLsQLWLLRPRkkDPARALKLFKLNMLLGLLLFLGIAL 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
95-339 |
4.98e-56 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 184.35 E-value: 4.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 95 LFWPCAWSIALSADAgcWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLS 174
Cdd:pfam01040 1 LLIPALAGLALAAGG--VPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 175 LGLLVLVQLNWQSILLGASSLGLVITYPL-MKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLAAcLPLYLSGVCWTIVY 253
Cdd:pfam01040 79 LGLLLLLLLNPLTALLGLAALLLYVLYTLrLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA-LLLALALFLWTWAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 254 DTIYAHQDKLDDLQIGVKSTALRFGENTKVWLS-GFTAAMLTGLSAAGWACDQTVPYYAAVGVVGAHLVQQIYSLNIDNP 332
Cdd:pfam01040 158 ALANDLRDREDDRKAGIKTLPVVLGRKAARILLaLLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDP 237
|
....*..
gi 257681406 333 SDCAKKF 339
Cdd:pfam01040 238 KKDAKAF 244
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
78-359 |
1.03e-46 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 161.37 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 78 KPYAQLMRIDRPIGTYLLFWPCAWSIALSADAGcwPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLAS 157
Cdd:PRK12873 8 SPWFELLRWNKPTGRLILLIPAGWSLWLTPSAP--PSLLLLLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 158 GQISQFDAIVFLSAQLSLGLLVLVQL----NWQSILLGASSLGLVITYPLMKRVTYWPQLVLgmAFNWG--ALLGWCATQ 231
Cdd:PRK12873 86 GKISLKTAYSLLIVLLLLSLFVVLSLpqpsRNLCLSLAFLALPPILIYPSAKRWFAYPQAIL--ALCWGfaVLIPWAAAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 232 GSVN----LAAClplYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTV 307
Cdd:PRK12873 164 GSLNggwpLLFC---WLATLLWTFGFDTVYAMADRRDDAKIGLNSSALSLGSNALKTVQICYFLTSIFLALAAFIAQVGF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 257681406 308 PYYAAVGVVGAHLVQQIYSLnidNPSDCAKKFISNH-----QVGLILFLGIVLGTLL 359
Cdd:PRK12873 241 IFWPFWLIASIGMQRDILKL---FPEKQSIKTIGNHfsnqvILGSLLLLGLILARGG 294
|
|
| ubiA_other |
TIGR01475 |
putative 4-hydroxybenzoate polyprenyltransferase; A fairly deep split separates this ... |
78-359 |
1.18e-27 |
|
putative 4-hydroxybenzoate polyprenyltransferase; A fairly deep split separates this polyprenyltransferase subfamily from the set of mitochondrial and proteobacterial 4-hydroxybenzoate polyprenyltransferases, described in TIGR01474. Protoheme IX farnesyltransferase (heme O synthase) (TIGR01473) is more distantly related. Because no species appears to have both this protein and a member of TIGR01474, it is likely that this model represents 4-hydroxybenzoate polyprenyltransferase, a critical enzyme of ubiquinone biosynthesis, in the Archaea, Gram-positive bacteria, Aquifex aeolicus, the Chlamydias, etc. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273646 Cd Length: 282 Bit Score: 110.13 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 78 KPYAQLMRIDrpigtYLLF-WPCAWSIALSAdAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLA 156
Cdd:TIGR01475 3 KDILELIKFE-----HTVFaLPFAYAGALLA-AKGLPGLKTLILILIAAVSARTAAMAFNRIIDRAIDARNPRTKNRPLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 157 SGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQG--SV 234
Cdd:TIGR01475 77 SGLISKKEARTMIILSLALFLSASYFLNPLAFILSPLVLLVLIIYPYTKRFTFLCHYVLGSTYGLAPLAGWVAVIGtiSF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 235 NLAACLpLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSaagWACDQTVP----YY 310
Cdd:TIGR01475 157 FLVAWL-LGIGVGFWIAGFDLIYAIQDYEFDRKNGLHSIPARFGIKAALKIASLSHVITFILL---LLVGFYVGngyiAL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 257681406 311 AAVGVVGAHLVQQIYSLNIDNPSDCAKKFIS-NHQVGLILFLGIVLGTLL 359
Cdd:TIGR01475 233 LALILIGLILAYEHYIVDPGDQSKIQRAFFYaNGFLSITFLIGVIIDVLL 282
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
85-356 |
1.55e-26 |
|
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: 107.05 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 85 RIDRPIGTYLLFWPCAWSIALsADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAkvERTRLRPLASGQISQFD 164
Cdd:cd13956 2 RLMRPYTLLYVLAPALAGAAL-AGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 165 AIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQ-LVLGMAFNWGALLGWCATQGSVNLAACLPLY 243
Cdd:cd13956 79 ALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGwGVLGYATGLALLPGLGAVAAGGLVPLALLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 244 LSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLS-GFTAAMLTGLSAAGWACDQTVPYYAAVGVVGAhLVQ 322
Cdd:cd13956 159 LVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAaGLLLAALILVVLLAVAGLLGPLALLALLAVAL-LAL 237
|
250 260 270
....*....|....*....|....*....|....
gi 257681406 323 QIYSLNIDNPSDCAKKFISNHQVGLILFLGIVLG 356
Cdd:cd13956 238 RARFARADRLPALPRGFLLLAVYRLLLFAALLLA 271
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
98-359 |
3.33e-20 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 89.78 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 98 PCAWSIALSA--DAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSL 175
Cdd:PRK12888 19 PFAYIAALTAmfASDGSVHWADLLLVTVAMVGARTFAMAANRIIDREIDARNPRTAGRELVTGAVSVRTAWTGALVALAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 176 GLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLAACLpLYLSGVCWTIVYDT 255
Cdd:PRK12888 99 FLGAAALLNPLCLALAPLAVAPLVVYPYAKRFTNFPHAILGLAQAVGPVGAWIAVTGTWSWPAVL-LGLAVGLWIGGFDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 256 IYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAA-GWACDQTVPYYAAVGVVGAHLVqqiYSLNIDNPSD 334
Cdd:PRK12888 178 IYACQDAEVDRRIGVRSVPARFGVRAALWASRVAHVVTFALFVWfGLAVGFGALWWIGLAITAGAFA---YEHAIVSPTD 254
|
250 260
....*....|....*....|....*....
gi 257681406 335 CAKK----FISNHQVGLILFlGIVLGTLL 359
Cdd:PRK12888 255 LSRVnrafFTANGFVGIALF-GFALLDLL 282
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
112-351 |
1.05e-19 |
|
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: 87.88 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 112 WPDLTMLGLFGTgALIMrGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVL-VQLNWQSILL 190
Cdd:cd13957 29 DLLLLLLTLLGT-ALVS-ASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALIFGLVLGILGLALLaLFVNPLTALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 191 GASSLGL-VITYPLMKRVTYWPQLVLGmAFNwGA---LLGWCATQGSVNLAACLpLYLSGVCWT--------IVYDTIYA 258
Cdd:cd13957 107 GLLGIFLyVFVYTPLKKRTTPLNTVIG-GIA-GAippLIGWAAATGSLDLGAWL-LFLILFLWQpphfwalaILYRDDYA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 259 hqdklddlQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTVPYYAAVGVV-GAHLVQQIYSLNIDNPSDCAK 337
Cdd:cd13957 184 --------RAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLlGLYFLYLAIKLYRSPDDKWAR 255
|
250
....*....|....*.
gi 257681406 338 K--FISNHQVGLILFL 351
Cdd:cd13957 256 KlfFASLIYLPLLFLL 271
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
113-251 |
2.01e-18 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 84.80 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 113 PDLTMLGLFGTGALImrGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVL-VQLNWQSILLG 191
Cdd:COG0109 49 LLLLLLTLLGGALAA--GAANALNNYIDRDIDALMKRTKNRPLPTGRISPREALIFGLVLGVLGLALLaLFVNPLAALLG 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257681406 192 ASSLGL-VITY-PLMKRVTYWPQLVLGMAfnwGA---LLGWCATQGSVNLAAclpLYLSGV--CWTI 251
Cdd:COG0109 127 LLGIFFyVVVYtLWLKRRTPQNIVIGGAA---GAmppLIGWAAVTGSLSLEA---LLLFLIifLWTP 187
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
115-250 |
1.74e-17 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 82.11 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 115 LTMLGlfgtGALIMrGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQL-NWQSILLGAS 193
Cdd:PRK04375 48 LTLLG----IALVA-GAAGALNNYIDRDIDAKMERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFvNPLAAWLTLA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257681406 194 SL-GLVITYPL-MKRVTywPQ-LVLGMAFnwGA---LLGWCATQGSVNLAACLpLYLSGVCWT 250
Cdd:PRK04375 123 GIfFYVVVYTLwLKRRT--PQnIVIGGAA--GAmppLIGWAAVTGSLSWEALI-LFLIIFLWT 180
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
129-355 |
2.19e-17 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 81.66 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 129 RGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVT 208
Cdd:PRK12886 55 RTAAMGFNRLIDAEIDARNPRTAGRAIPAGLISKGSAILFIVLSSLLMLFAAWFLNPLCLYLSPPALFFLLLYSYCKRFT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 209 YWPQLVLGMAFNWGALLGWCATQGSVNLAACLpLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLS-G 287
Cdd:PRK12886 135 ALAHVVLGFCLALAPLGAWIAIRGTIELPAIL-LGLAVLFWVAGFDILYALQDLEFDRKEGLHSIPAKLGVNGSLWIArV 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257681406 288 FTAAMLTGLSAAGWACDQTVPYYAAVGVVGAHLVQQIYSL-NIDNPSDCAKKFISNHQVGLILFLGIVL 355
Cdd:PRK12886 214 FHLLMIGFLFALGISAGLGPWFLAGLAVTGILLLYEHWLLrGGDLTRLDAAFFNMNGYISVTLFAATLF 282
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
75-359 |
8.06e-17 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 80.16 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 75 SAAKPYAqLMRIDRpIGTYLLFWPCAWSIALSADAGCwPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRP 154
Cdd:PRK13106 11 TRSKFYI-ILRFLR-IEQTFFSLPMAYLGAFVAIKGI-PPISTLILIFLALFFLRTAGMTNDNLADLEIDAKNPRTKNRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 155 LASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQL----VLGMAFNWGAL--LGWC 228
Cdd:PRK13106 88 LVTGAIKISEAKALITAGLILFFASAYLVNRWALLLSPIVALIAMSYPYMKRYTAFANYhlasIQGLAVFSGAVavLGLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 229 ATQGSVNLAACLPLYLSGVC-WTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTV 307
Cdd:PRK13106 168 ANSLIQVLLRVPWLFVIGTIlWAAGFDLYNHIPDAEFDREMGLHSFAVVLGKWALTFAGLNQLFSVVLDLLGDLYYGLGP 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 257681406 308 PYYAAVGVVGAHLVQQIYSLNIDNpsDCAKKFISNHQVGLILFLGIVLGTLL 359
Cdd:PRK13106 248 IAIAATILHGLIMAYAYYLASKKG--DFGRAFYYNIYSSIVLGLGIIIDVLL 297
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
115-354 |
6.69e-16 |
|
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also called heme O synthase, an enzyme that creates an intermediate in the biosynthesis of heme A. Prior to the description of its enzymatic function, this protein was often called a cytochrome o ubiquinol oxidase assembly factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273645 Cd Length: 280 Bit Score: 77.29 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 115 LTMLGlfgtGALIMrGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVL-VQLNWQSILLGAS 193
Cdd:TIGR01473 39 LTLLG----TTLAA-ASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREALAFGLLLGVLGVAILaAFVNPLAALLGLF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 194 SL---GLVITYPLmKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLAACLpLYLSGVCWTIVYDTIYAHQDKLDDLQIGV 270
Cdd:TIGR01473 114 GIffyVIVYTIWL-KRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWL-LFAIIFLWQPPHFWALALKYKDDYRAAGI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 271 KSTALRFGE---NTKVWLS----GFTAAMLTGLSAAGWacdqtvPYYAAVGVVGAHLVQQIYSL--NIDNPSDCAKKFI- 340
Cdd:TIGR01473 192 PMLPVVKGEritKRQIALYtaalLPVSLLLAFLGGTGW------LYLIVATLLGALFLYLAFKFyrDPTDRKKARKLFKf 265
|
250
....*....|....
gi 257681406 341 SNHQVGLILFLGIV 354
Cdd:TIGR01473 266 SLIYLALLFVALLI 279
|
|
| ubiA |
PRK12876 |
prenyltransferase; Reviewed |
122-279 |
2.55e-11 |
|
prenyltransferase; Reviewed
Pssm-ID: 237244 Cd Length: 300 Bit Score: 64.00 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 122 GTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASGQISqFDAIVFLSAQLSLGLLVLVQ-LNWQSILLGASSLGLVIT 200
Cdd:PRK12876 53 GSAFFCARTVGIIVNQIIDCAIDKKNPRTSSRVLPAKLLS-INFSMLLLTLCSFLFLSLCWlLNPLCFSLAVLSTLLMII 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 201 YPLMKRVTYWPQLVLGMAFNWGALLGWCA-TQGSVNLAACLPLYLSGVCWTIVY---DTIYAHQDKLDDLQIGVKSTALR 276
Cdd:PRK12876 132 YPYTKRVTFLCHWILGLVYYLAILMNFFAiIETPLSFSLFCMASLWGISFGMIIaanDIIYAIQDLEFDRKEGLFSIPAR 211
|
...
gi 257681406 277 FGE 279
Cdd:PRK12876 212 FGE 214
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
135-360 |
2.81e-09 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 57.71 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 135 INDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLV 214
Cdd:PRK12874 66 FNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIVLNALIFIGVSYFINPLAFKLSFPFLIVLGGYSYFKRFSSLAHLV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 215 LGMAfnwgalLGWCATQGSVNLAACLPLY---LS-GVC-WTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLS--- 286
Cdd:PRK12874 146 LGLS------LGLAPIAGVVAVLGEIPLWsvfLAlGVMfWVAGFDLLYSLQDMEFDKKRGLHSIPSKFGEKATLFISrlf 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257681406 287 -----GFTAAMLTGLSAAGWAcdqtvpyYAAVGVVGAHLVQQIYSLNIDNPSDCAKKFISNHQVGLILFLGIVLGTLLK 360
Cdd:PRK12874 220 hllavLFWLLFVWCAHLGLFA-------YLGVIVSALILLYEHYLVRKDFKKIDKAFFTLNGYLGIVFFIFIVLDVLFK 291
|
|
| ubiA |
PRK12895 |
prenyltransferase; Reviewed |
129-356 |
2.58e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 237251 Cd Length: 286 Bit Score: 54.82 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 129 RGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVT 208
Cdd:PRK12895 50 RTSAMSINRIEGLRYDMINPRKKDWALVSGRIKMREAIAFTIIFIAIFEICTFLLNRLVFILSPIVIFLFIIDPFLKRYT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 209 YWPQLVLGMAFNWGALLGWCATQGSV--NLAACLpLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLS 286
Cdd:PRK12895 130 AWRHIYMGSIIGLGVLAGYLAVIPAFpyNLLIYI-IFISSSLWIAGFDIIYVIPDIEYDKINGLKTIMNTYGIKNGLYIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257681406 287 G-FTAAMLTGLSAAGWACdQTVPYYAAVGVVGAHLVQQIYSLNIDNPSDCAKKFI-SNHQVGLILFLGIVLG 356
Cdd:PRK12895 209 DiFHISSLILFWISGIYI-RTLWYLAALIIIYTLVIYQHLIIDPRNPINKRMSFFnANSFIGFVFLIGIILS 279
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
77-359 |
1.10e-07 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 52.65 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 77 AKPYAQLMRIDRPIGTYLlfwpCAWSIALSADAGCWPDLTMLGlFGTGALIMrGAGCTINDLWDKDIDaKVERTRlRPLA 156
Cdd:PRK12884 4 MKAYLELLRPEHGLMAGI----AVVLGAIIALGGLPLDEALLG-FLTAFFAS-GSANALNDYFDYEVD-RINRPD-RPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 157 SGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLM-KRVTYWPQLVL----GMAFNWGALLGWCATQ 231
Cdd:PRK12884 76 SGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKlKEYGLIGNLYVafltGMTFIFGGIAVGELNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 232 GSVNLAAClpLYLSGVCWTIVYDTiyahQDKLDDLQIGVKSTALRFGENTKVWLSG--FTAAMLTGLS--AAGWacdQTV 307
Cdd:PRK12884 156 AVILLAAM--AFLMTLGREIMKDI----EDVEGDRLRGARTLAILYGEKIAGRIAAalFILAVLLSPLpyLFGI---FNI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 257681406 308 PYYAAVGVVGAHLVQQIYSLNIDNPSDCAKKFISNHQVG-LILFLGIVLGTLL 359
Cdd:PRK12884 227 LYLAPVLVADLIFLYSAYSLLRSQDRETIRKVRKITLTAmLLALVAFALGAIT 279
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
103-353 |
1.16e-07 |
|
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260125 Cd Length: 283 Bit Score: 52.52 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 103 IALSADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWD--KDIDAKVERTRLRPLASGQISQFD----AIVFLSAQLSLG 176
Cdd:cd13962 20 TALAYYLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLSPRQvlraALVLLLLAALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 177 LLVLVQLNWQSILLGASSLGLVITYplmkrvTYWP---------QLVLGMAFNWGALLG-WCATQGSVNLAAclpLYLSG 246
Cdd:cd13962 100 LYLVALGGWLLLLLGLLGILAGYFY------TGGPfplsyrglgELFVFLFFGLLAVLGtYYVQTGSLSWEV---LLAAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 247 VCWTIVYDTIYAHQ--DKLDDLQIGVKSTALRFG-ENTKVWLSGFTAAMLtgLSAAGWACDQTVPYYAAVGVVGA----H 319
Cdd:cd13962 171 PLGLLIAAILLANNirDIEADRAAGKRTLAVRLGrKRARRLYAALLLLAY--LLLLLLVLLGLLPLWSLLALLSLplaiK 248
|
250 260 270
....*....|....*....|....*....|....
gi 257681406 320 LVQQIYSLNIDNPSDCAKKFISNHQVGLILFLGI 353
Cdd:cd13962 249 LLRRLLRKADKPLLLIALKLTALLTLLFGLLLAL 282
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
119-238 |
1.25e-06 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 49.74 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 119 GLFGTGALIMRGAGC--TINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVL-VQLNWQSILLGASSL 195
Cdd:PLN02776 30 GLGWTCAGTMLCAASanTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLaYKTNMLTAGLGAGNI 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 257681406 196 GL-VITYPLMKRVTYWPQLVlgmafnwGA-------LLGWCATQGSVNLAA 238
Cdd:PLN02776 110 LLyAFVYTPLKQIHPANTWV-------GAvvgaippLMGWAAASGQLDAGA 153
|
|
| PT_UbiA_HPT1 |
cd13960 |
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ... |
88-321 |
1.69e-06 |
|
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as homogentisate phytyltransferase 1 (HPT1), tocopherol phytyltransferase, or VTE2, catalyzes the first step in the biosynthesis of the tocopherol forms of vitamin E, which involves the prenylation of homogentisate using phytyl diphosphate (PDP) as the prenyl donor. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260123 Cd Length: 289 Bit Score: 49.10 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 88 RP---IGTYLlfwpCAWS---IALSADAGCWPDLTMLGLFGT--GALIMRGAGCTINDLWDKDIDaKVERTRLrPLASGQ 159
Cdd:cd13960 6 RPhtiIGTIL----SVTSlslLALESNSDLLLLFLLPGALQAlvALLLGNVYIVGLNQIYDVEID-KINKPYL-PLASGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 160 ISQFDA--IVFLSAQLSLGlLVLVQLNWQSILLGASSLGLVITY----PLMKRVTYWPQL----VLGMAFNWGALLgwcA 229
Cdd:cd13960 80 LSVRTAwaIVASCGILGLA-LGALLGSPLLLTLLLLSLLLGTAYsvppPRLKRFPLLAALciltVRGFLVNLGFYL---H 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 230 TQGSVNLAACLPLylsGVCWTIVYDTIYA-----HQDKLD---DLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGW 301
Cdd:cd13960 156 FQAALGLPFAWPP---SLWFLTAFMTVFAivialFKDIPDvegDRKFGIRTFSVRLGVKRVFWLCVGLLLMNYAGAILVG 232
|
250 260
....*....|....*....|.
gi 257681406 302 AcdqTVPYYAAVGV-VGAHLV 321
Cdd:cd13960 233 L---TSPALFSKIFmVVGHAV 250
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
130-321 |
5.37e-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: 260127 Cd Length: 282 Bit Score: 47.58 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 130 GAGCTINDLWDKDIDAkVERtRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPL-MKRVT 208
Cdd:cd13964 46 AAGMVLNDVFDAELDA-RER-PERPIPSGRVSRGAALALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAwLKHTP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 209 YWPqLVLGMAFNWGALLGWCATQGSVN-----LAACLPLYLSGVcwtivydTIYAHQDKLddlqigvkstalrfGENTKV 283
Cdd:cd13964 124 LGP-LLMGLCRGLNLLLGASAAAAGGLgpallAALALGVYIAGV-------TYIARGEVH--------------GGPRRL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 257681406 284 WLSGFTAAMLTGLSAAGWACDQTVPYYAAVGVVGAHLV 321
Cdd:cd13964 182 LPLALLAVLLVIGLALALAAPRGGRVLLALLFLALFAA 219
|
|
| PT_UbiA_chlorophyll |
cd13958 |
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ... |
104-325 |
1.25e-05 |
|
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: 46.45 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 104 ALSADAGCWPDLTM----LGLFGTGALiMRGAGCTINDLWDKDIDAKVERTRlrPLASGQISQFDAIVFLSAQLSLGLLV 179
Cdd:cd13958 21 AAASGAFQWSNWDVwlllLGMLLAGPL-LTGTSQTINDYYDREVDAINEPYR--PIPSGRISEREALWNIWVLLLLSLLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 180 LVQLNWQSIlLGASSLGLVITY-----PL-MKRVTYWPQLVLGMAFnwgALLGWcatqgsvnLAACLpLYLSGVCWTIVY 253
Cdd:cd13958 98 ALFLDGPWV-FAAAVVGLVLAYiysapPLkLKQNGWWGNAAVGLSY---EGLPW--------WAGAA-AFAGLLTWESLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 254 DT----IYAH--------QDKLDDLQIGVKSTALRFGENTKVWLSgFTAAMLTGLSAAGWACDQTVPYYAAvgVVGAHLV 321
Cdd:cd13958 165 LAllysIGAHgimtlndfKSIEGDRQLGLRSLPVALGVDTAAWIA-CGVIDVPQLAVAALLLAWGETWYAA--VVGALLL 241
|
....
gi 257681406 322 QQIY 325
Cdd:cd13958 242 AQIP 245
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
135-230 |
7.98e-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: 44.00 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 135 INDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPL-MKRVTYWPQL 213
Cdd:cd13963 52 LNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYSLkLKRIPLLDVF 131
|
90
....*....|....*..
gi 257681406 214 VLGMAFNWGALLGWCAT 230
Cdd:cd13963 132 VIAAGFVLRVLAGAVAI 148
|
|
| PT_UbiA_4 |
cd13966 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
83-299 |
1.25e-04 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260129 Cd Length: 272 Bit Score: 43.40 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 83 LMRIDRPIGTYLLFWPCAWSIALSADAgcwPDLTMLGLFGTGA------LIMRGagctINDLWDKDIDAKVER-----TR 151
Cdd:cd13966 1 LLKVSRPRFWINTAGPFAVGYLLAGSG---FDDLLRLILGLLYflfpanLLIYG----VNDVFDYESDARNPRkggieGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 152 LRPLASGQisqFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITY---PL-MKRVTYWPQLVLGMAFnWGALLGW 227
Cdd:cd13966 74 LLDPAEHR---PLLWAVAVSNVPFLLYLVLVGPPAALLLLALFLFLVVAYsapPLrFKERPFLDSLSNGLYF-LPPALVG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257681406 228 CATQGSVNLAACLplyLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAA 299
Cdd:cd13966 150 LLASGTLPPWLAL---AAFFLWGMAMHAFGAIQDIEADREAGIRTTATVLGARGTLRLALALWLLAAVLVLP 218
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
79-201 |
1.39e-04 |
|
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: 43.26 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 79 PYAQLMRIDRPIGTYLLFWPCAwsIALSADAGCWPDLTMLGLFGTGALIMrGAGCTINDLWDKDIDA--KVErtrlRPLA 156
Cdd:cd13961 1 AYLELIRPPNLLMAALAQYLGA--LFALGPLLSLNDLELLLLFLSVFLIA-AAGYIINDYFDVEIDRinKPD----RPIP 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 257681406 157 SGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITY 201
Cdd:cd13961 74 SGRISRREALILSILLNALGLILAFLLSPLALLIALLNSLLLWLY 118
|
|
| PLN00012 |
PLN00012 |
chlorophyll synthetase; Provisional |
134-325 |
2.08e-04 |
|
chlorophyll synthetase; Provisional
Pssm-ID: 215028 Cd Length: 375 Bit Score: 42.93 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 134 TINDLWDKDIDAKVErtRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLN-W----QSILLGASSLGLVITY-----PL 203
Cdd:PLN00012 141 TINDWYDREIDAINE--PYRPIPSGAISENEVITQIWVLLLGGLGLAYTLDvWaghdFPIVFYLALGGSLLSYiysapPL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 204 MKRVTYWP-QLVLGMAFNwgALLGWC--ATQGSVNL-AACLPLYLS--GVCWTIVYDTIYAHQDKlddlQIGVKSTALRF 277
Cdd:PLN00012 219 KLKQNGWIgNYALGASYI--SLPWWAgqALFGTLTPdVVVLTLLYSiaGLGIAIVNDFKSIEGDR----ALGLQSLPVAF 292
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 257681406 278 GENTKVWLSgFTAAMLTGLSAAGWACDQTVPYYAAVGVvgAHLVQQIY 325
Cdd:PLN00012 293 GVETAKWIC-VGSIDITQLSVAGYLLAIGKPYYALALL--GLIIPQIF 337
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
130-339 |
2.17e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 42.65 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 130 GAGCTINDLWDKDIDaKVERTRlRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYP-LMKRVT 208
Cdd:PRK12882 52 GAGNAINDYFDREID-RINRPD-RPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAeTLKGTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 209 YWPQLVL----GMAFNWGAllgwcATQGSVNLAACLPLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVW 284
Cdd:PRK12882 130 GLGNASVayltGSTFLFGG-----AAVGTEGLLALLVLFALAALATLAREIIKDVEDIEGDRAEGARTLPILIGVRKALY 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257681406 285 LSGFTAAMLTGLSAA-------GWAcdqtvpYYAAVGVVGAHLVQQIY-SLNIDNPSDCAKKF 339
Cdd:PRK12882 205 VAAAFLLVAVAASPLpyllstfGLW------YLVLVAPADLVMLAAAYrSLKKTDPTASQKLL 261
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
135-201 |
2.43e-04 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 42.54 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257681406 135 INDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITY 201
Cdd:PRK12324 65 VNDIRDVEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYLVLNLAY 131
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
135-219 |
1.16e-03 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 41.01 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257681406 135 INDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPL-MKRVTYWPQL 213
Cdd:PRK08238 245 LNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAPLLLLAGLALALALGPAFLLVLLAYLALTLAYSLrLKRKVLVDVL 324
|
....*.
gi 257681406 214 VLGMAF 219
Cdd:PRK08238 325 TLAALY 330
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
131-204 |
4.85e-03 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 38.56 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257681406 131 AGCTINDLWDKDIDaKVERTRlRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGasslglVITYPLM 204
Cdd:PRK12883 52 GGNTINDYFDYEID-KINRPN-RPLPRGAMSRKAALYYSLLLFAVGLALAYLINIEAFLFA------LGAYVLM 117
|
|
| |
