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Conserved domains on  [gi|734879535|ref|WP_034127102|]
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MULTISPECIES: heme o synthase [Pseudomonas]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10195468)

protoheme IX farnesyltransferase acts in step 1 of the conversion protoheme IX to heme O in heme O biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 25-284 3.83e-87

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: 261.61  E-value: 3.83e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHgLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:cd13957    1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLL-LLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:cd13957   80 ALIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLLSL----AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:cd13957  160 FLILFLWQPPHFWALAILYRDDYARAGIPMLPVvkgeRRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFL 239

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPTgWARRIFGFSI 284
Cdd:cd13957  240 YLAIKLYRSPDDK-WARKLFFASL 262
 
Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 25-284 3.83e-87

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: 261.61  E-value: 3.83e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHgLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:cd13957    1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLL-LLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:cd13957   80 ALIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLLSL----AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:cd13957  160 FLILFLWQPPHFWALAILYRDDYARAGIPMLPVvkgeRRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFL 239

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPTgWARRIFGFSI 284
Cdd:cd13957  240 YLAIKLYRSPDDK-WARKLFFASL 262
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 25-284 2.69e-86

Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 439879  Cd Length: 299  Bit Score: 260.45  E-value: 2.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:COG0109   20 LALTKPRIILLLLFTALAGMLLAAGGLP-DLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:COG0109   99 ALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLL----SLAQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:COG0109  179 FLIIFLWTPPHFWALALKRRDDYARAGVPMLpvvkGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFL 258

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPtGWARRIFGFSI 284
Cdd:COG0109  259 YLAVRLYRRPDR-KWARKLFKFSI 281
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 25-284 1.72e-85

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 258.15  E-value: 1.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:PRK04375  14 LALTKPRVISLNLFTALGGMLLAPPGVP-PLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPRE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:PRK04375  93 ALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEALIL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLL----SLAQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:PRK04375 173 FLIIFLWTPPHFWALAIFRKDDYAAAGIPMLpvvkGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLLGAWFL 252

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPTgWARRIFGFSI 284
Cdd:PRK04375 253 YYAWRLYRKDDRK-WARKLFRYSI 275
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 25-284 1.64e-75

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: 232.14  E-value: 1.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535   25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:TIGR01473   4 LQLTKPRIISLLLITAFAGMWLAPGGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:TIGR01473  84 ALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLLSLAQ----AHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:TIGR01473 164 FAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKgeriTKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGALFL 243

                         250       260
                  ....*....|....*....|....
gi 734879535  261 TLAASGTRLADPTGWARRIFGFSI 284
Cdd:TIGR01473 244 YLAFKFYRDPTDRKKARKLFKFSL 267
UbiA pfam01040
UbiA prenyltransferase family;
37-280 4.95e-42

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 145.06  E-value: 4.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535   37 LASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCG 116
Cdd:pfam01040   2 LIPALAGLALAAGGVP-DLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  117 FGLLWAGsNALACGLAMVGLVIYAgVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLLIVVFCCWQMPHS 196
Cdd:pfam01040  81 LLLLLLL-NPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  197 HAINVMRREDFRAAGLPLLSL---AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWLTLAASGTRLADPT 273
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVvlgRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPK 238


                  ....*..
gi 734879535  274 GWARRIF 280
Cdd:pfam01040 239 KDAKAFF 245
 
Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 25-284 3.83e-87

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: 261.61  E-value: 3.83e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHgLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:cd13957    1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLL-LLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:cd13957   80 ALIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLLSL----AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:cd13957  160 FLILFLWQPPHFWALAILYRDDYARAGIPMLPVvkgeRRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFL 239

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPTgWARRIFGFSI 284
Cdd:cd13957  240 YLAIKLYRSPDDK-WARKLFFASL 262
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 25-284 2.69e-86

Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 439879  Cd Length: 299  Bit Score: 260.45  E-value: 2.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:COG0109   20 LALTKPRIILLLLFTALAGMLLAAGGLP-DLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:COG0109   99 ALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLL----SLAQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:COG0109  179 FLIIFLWTPPHFWALALKRRDDYARAGVPMLpvvkGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFL 258

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPtGWARRIFGFSI 284
Cdd:COG0109  259 YLAVRLYRRPDR-KWARKLFKFSI 281
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 25-284 1.72e-85

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 258.15  E-value: 1.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:PRK04375  14 LALTKPRVISLNLFTALGGMLLAPPGVP-PLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPRE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:PRK04375  93 ALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEALIL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLL----SLAQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:PRK04375 173 FLIIFLWTPPHFWALAIFRKDDYAAAGIPMLpvvkGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLLGAWFL 252

                        250       260
                 ....*....|....*....|....
gi 734879535 261 TLAASGTRLADPTgWARRIFGFSI 284
Cdd:PRK04375 253 YYAWRLYRKDDRK-WARKLFRYSI 275
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 25-284 1.64e-75

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: 232.14  E-value: 1.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535   25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVST 104
Cdd:TIGR01473   4 LQLTKPRIISLLLITAFAGMWLAPGGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  105 AAGYGIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:TIGR01473  84 ALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  185 IVVFCCWQMPHSHAINVMRREDFRAAGLPLLSLAQ----AHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:TIGR01473 164 FAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKgeriTKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGALFL 243

                         250       260
                  ....*....|....*....|....
gi 734879535  261 TLAASGTRLADPTGWARRIFGFSI 284
Cdd:TIGR01473 244 YLAFKFYRDPTDRKKARKLFKFSL 267
UbiA pfam01040
UbiA prenyltransferase family;
37-280 4.95e-42

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 145.06  E-value: 4.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535   37 LASVLGGYLLAASGHVaSVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCG 116
Cdd:pfam01040   2 LIPALAGLALAAGGVP-DLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  117 FGLLWAGsNALACGLAMVGLVIYAgVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLLIVVFCCWQMPHS 196
Cdd:pfam01040  81 LLLLLLL-NPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  197 HAINVMRREDFRAAGLPLLSL---AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWLTLAASGTRLADPT 273
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVvlgRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPK 238


                  ....*..
gi 734879535  274 GWARRIF 280
Cdd:pfam01040 239 KDAKAFF 245
PLN02776 PLN02776
prenyltransferase
 43-280 2.67e-36

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 132.56  E-value: 2.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  43 GYLLAaSGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLWA 122
Cdd:PLN02776  17 GFVLG-SGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 123 GSNALACGLAMVGLVIYAGVYTYwLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLLIVVFCCWQMPHSHAINVM 202
Cdd:PLN02776  96 KTNMLTAGLGAGNILLYAFVYTP-LKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 203 RREDFRAAGLPLLSLAQAH-RQIQAYMLAFLASALVLGAVAQMAAL----YFVVMLGLGSYWLTLAASGTRlaDPT-GWA 276
Cdd:PLN02776 175 CRDDYAAGGYRMLSLADATgRRTALVALRNCLYLAPLGFLAYDWGVtsspFALEAALLTAYLAASAASFYR--EPTnANA 252


                 ....
gi 734879535 277 RRIF 280
Cdd:PLN02776 253 RKMF 256
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 25-256 7.57e-22

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: 92.60  E-value: 7.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGY--LLAASGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISV 102
Cdd:COG0382    4 LRLLRLDRPIGILLLLWPTLwaLFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 103 STAAGYGIVLGTCGFGLLWA-GSNALACGLAMVGLVIyagVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTA 181
Cdd:COG0382   84 REALLLAIVLLLLALALALLlNPLTFLLALAALALAW---AYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 182 LLLIVVFCCWqmphSHAINVM----RREDFRAAGLPLLSL----AQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVML 253
Cdd:COG0382  161 WLLALAAFLW----TLAYDTIydleDREGDRKIGIKTLAIlfgvRDALIIAGVLYALAVLLLLLLGLLAGLGLLYLLGLL 236


                 ...
gi 734879535 254 GLG 256
Cdd:COG0382  237 AAL 239
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 43-257 2.56e-19

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: 85.21  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  43 GYLLAASGHVASVTHGLAT-LLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLW 121
Cdd:cd13959   19 GLLLAAGGLPLPLLKLLLLfLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQLLLGLALLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 122 AGsNALACGLAMVGLVIyAGVYTYwLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLLIVVFCCWQMphshAINV 201
Cdd:cd13959   99 QL-NPLTILLSPIALLL-VLIYPL-MKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFWTA----GYDT 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 734879535 202 ----MRREDFRAAGL---PLLSLAQAHRQIQAYMLAFLASALVLGAVAQMAALYFVVMLGLGS 257
Cdd:cd13959  172 iyahQDREDDRKIGVkstAVLFGDRTKLILALLLHLFVALLLLAGGLAGLGWPYYLGLGAAAH 234
ubiA_proteo TIGR01474
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of ...
 45-270 9.31e-14

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: 70.04  E-value: 9.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535   45 LLAASGHVASVTHGLAT-LLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLWAg 123
Cdd:TIGR01474  28 LLAAQAGGIPPLYLLGLfTVGAILMRGAGCVINDIWDRDFDPQVERTKSRPLASGAVSVRQAILFLLVQLLVALGVLLQ- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  124 SNALACGLAMVGLVIyagVYTY-WLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALLLIVVFCCWQMPHSHAINVM 202
Cdd:TIGR01474 107 LNPLTILLGVASLAL---VATYpFMKRITYWPQLVLGLAFGWGALMGWAAVTGDLSTAAWVLYLANILWTLGYDTIYAMQ 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 734879535  203 RREDFRAAGLPLLSLAQAhRQIQAYMLAFLASALVLGAVAQMaalyfvvMLGLGS-YWLTLAASGTRLA 270
Cdd:TIGR01474 184 DKEDDIKIGVKSTALRFG-DNTKPWLGGLYALMILLLALAGL-------IAGLGPvYYLGLAAAALLLI 244
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 25-280 8.22e-13

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: 66.99  E-value: 8.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRrmVRTCHRPLALRTISVST 104
Cdd:cd13956    1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWAGS-NALACGLAMVGLVIyagVYTYWLKRRSHWATLIGSVSGAMPPVIGY-CAVTGRFDLTAL 182
Cdd:cd13956   79 ALAFAAALLLVGLALALALGpLALLLLLAGLLLGL---AYSLGLKRLKLGGWGVLGYATGLALLPGLgAVAAGGLVPLAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 183 LLIVVFCCWQMPHSHAINVMRREDFRAAGLPLLSLAQAHRQI--QAYMLAFLASALVLGAVAQMAALYFVVMLGLGSYWL 260
Cdd:cd13956  156 LLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRArrLAAGLLLAALILVVLLAVAGLLGPLALLALLAVALL 235

                        250       260
                 ....*....|....*....|
gi 734879535 261 TLAASGTRLADPTGWARRIF 280
Cdd:cd13956  236 ALRARFARADRLPALPRGFL 255
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 25-189 2.48e-08

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: 54.05  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPG-IIIGNLASVLGGYLLAASGHVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRrmVRTCHRPLALRTISVS 103
Cdd:cd13961    3 LELIRPPnLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDR--INKPDRPIPSGRISRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 104 TAAGYGIVLGTCGFGLLWAGSnaLACGLAMVGLVIYAGVYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALL 183
Cdd:cd13961   81 EALILSILLNALGLILAFLLS--PLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLLIILLL 158


                 ....*.
gi 734879535 184 LIVVFC 189
Cdd:cd13961  159 ALFAFL 164
ubiA PRK12873
4-hydroxybenzoate polyprenyltransferase;
62-138 6.24e-07

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 171787 [Multi-domain]  Cd Length: 294  Bit Score: 50.05  E-value: 6.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  62 LLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGL---LWAGSNALACGLAMVGLVI 138
Cdd:PRK12873  50 ILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAYSLLIVLLLLSLFVvlsLPQPSRNLCLSLAFLALPP 129
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
46-148 4.53e-06

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 47.16  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  46 LAASG---HVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLWA 122
Cdd:PRK12324  33 PIFAGnllNPGALLKVLLAFVLFCLASSAVYLVNDIRDVEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYL 112

                         90       100
                 ....*....|....*....|....*....
gi 734879535 123 GSNALAcglamVGLVIYAGV---YTYWLK 148
Cdd:PRK12324 113 LSPKLA-----LVLLVYLVLnlaYSFKLK 136
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 74-149 8.47e-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: 46.31  E-value: 8.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 734879535  74 VVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLWAGSnaLACGLAMVGLVIYAGVYTYWLKR 149
Cdd:cd13963   51 ILNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLALALLLS--PAFLLVLLAYLVLNLAYSLKLKR 124
PRK08238 PRK08238
UbiA family prenyltransferase;
74-150 1.19e-05

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 46.41  E-value: 1.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 734879535  74 VVNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYGIVLGTCGFGLLWAGSnaLACGLAMVGLVIYAGVYTYWLKRR 150
Cdd:PRK08238 244 ILNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAPLLLLAGLALALALG--PAFLLVLLAYLALTLAYSLRLKRK 318
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
75-184 3.04e-05

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 44.61  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  75 VNNCIDRDIDRRMVRTCHRPLALRTISVSTAAGYgIVLGTCGFGLLWAGSNALACGLAMVGLVIYAGvYTYwLKRRSHWA 154
Cdd:PRK12874  66 FNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLF-IVLNALIFIGVSYFINPLAFKLSFPFLIVLGG-YSY-FKRFSSLA 142

                         90       100       110
                 ....*....|....*....|....*....|
gi 734879535 155 TLIGSVSGAMPPVIGYCAVTGRFDLTALLL 184
Cdd:PRK12874 143 HLVLGLSLGLAPIAGVVAVLGEIPLWSVFL 172
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 64-168 1.34e-04

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 42.76  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  64 GTALVIGCGCVVNNCIDRDIDRRMVRTCHRPLALRTISVSTA---------AGYGIVLGTCGFGLLWAGSNalacgLAMV 134
Cdd:PLN02809  53 GALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPFQGvgflgaqllLGLGILLQLNNYSRILGASS-----LLLV 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 734879535 135 GLVIYAGVYTYW----LKRRSHWATLIG--SVSGAMPPVI 168
Cdd:PLN02809 128 FTYPLMKRFTFWpqafLGLTFNWGALLGwaAVKGSLDPAV 167
ubiA PRK12887
tocopherol phytyltransferase; Reviewed
 25-162 1.81e-04

tocopherol phytyltransferase; Reviewed


Pssm-ID: 183813  Cd Length: 308  Bit Score: 42.26  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGHVASVTH-GLATLLGTALVIGCGCV----VNNCIDRDIDRrmVRTCHRPLALRT 99
Cdd:PRK12887  17 WKFSRPHTIIGTSLSVLGLYLIAIAASSNTIALaNLGLLLGAWIACLCGNVyivgLNQLTDIEIDR--INKPHLPLAAGE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 734879535 100 ISVSTAAGYGIVLGTCGFGLLWAGSNALacgLAMVGLVIYAG-VYTY---WLKRRSHWATL-IGSVSG 162
Cdd:PRK12887  95 FSRRQGQRIVIITGILALILAALLGPWL---LITVGISLLIGtAYSLppiRLKRFPLLAALcIFTVRG 159
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 37-149 2.25e-03

UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.


Pssm-ID: 260127  Cd Length: 282  Bit Score: 39.10  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  37 LASVLGGYLLAASGhVASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRRMVRtcHRPLALRTISVSTAAGYGIVLGTCG 116
Cdd:cd13964   14 PADVLAGAALAGGG-LGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERP--ERPIPSGRVSRGAALALGAGLLAAG 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 734879535 117 FGLLWAGS-NALACGLAMVGLVIyagVYTYWLKR 149
Cdd:cd13964   91 VALAALVGrLSGLVALLLAAAIL---LYDAWLKH 121
PT_UbiA_HPT1 cd13960
Tocopherol phytyltransferase; Tocopherol polyprenyltransferase (TPT1), also known as ...
 26-164 4.80e-03

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: 37.93  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  26 ELTKPGIIIGNLASVLGGYLLAASGHVASV-THGLATLLGTALVIGCGCV----VNNCIDRDIDRrmVRTCHRPLALRTI 100
Cdd:cd13960    3 KFSRPHTIIGTILSVTSLSLLALESNSDLLlLFLLPGALQALVALLLGNVyivgLNQIYDVEIDK--INKPYLPLASGEL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 734879535 101 SVSTAAGYGIVLGTCGFGL-LWAGSNALACgLAMVGLVIyAGVYT---YWLKRRSHWATL-IGSVSGAM 164
Cdd:cd13960   81 SVRTAWAIVASCGILGLALgALLGSPLLLT-LLLLSLLL-GTAYSvppPRLKRFPLLAALcILTVRGFL 147
ubiA PRK12871
prenyltransferase; Reviewed
 62-260 5.01e-03

prenyltransferase; Reviewed


Pssm-ID: 106000  Cd Length: 297  Bit Score: 37.87  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  62 LLGTALVIG-----CGCVVNNCIDRDIDRRMVRTCH----RPLALRTI---SVSTAAGYGIvlgtcgFGLLWAGSNALAC 129
Cdd:PRK12871  42 LTIKAALIGlfgfeAGFVLNDYVDRKRDRLDVENTLtrywRPFKERPIpsgKLSSKNAFAL------FILLAAVTSALIL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 130 GLA--------MVGLVIYAGVYTYWLKRRSH---WATLIGSVSGAMPPVIGYCaVTGRFDLTALLLIVVFCCWQMPHSHA 198
Cdd:PRK12871 116 TLPypnslyvfVIMLYSYGIEAFYQVKKRNQkypVAQLLGRTDFTLFPAAGYL-CYGQPDMTALLYMVFFYPWTMAHLGL 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 199 INVMRREDFRAAGLPLLSLAQAHRQIQAYMLAFLA----SALV----LGAVAQMAALYFVVMLGLGSYWL 260
Cdd:PRK12871 195 NDFIDLENDRARGMKSIAVLYGMKGTMYWVTGFTAlhflAAIFflreLGPIALYGFLAGFVLLAGANLYL 264
ubiA PRK12884
prenyltransferase; Reviewed
 25-188 9.04e-03

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 37.24  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535  25 IELTKPGIIIGNLASVLGGYLLAASGhvASVTHGLATLLGTALVIGCGCVVNNCIDRDIDRrmVRTCHRPLALRTISVST 104
Cdd:PRK12884   8 LELLRPEHGLMAGIAVVLGAIIALGG--LPLDEALLGFLTAFFASGSANALNDYFDYEVDR--INRPDRPIPSGRISRRE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 734879535 105 AAGYGIVLGTCGFGLLWA-GSNALACGLAMVGLVIYagvYTYWLKRRSHWATLIGSVSGAMPPVIGYCAVTGRFDLTALL 183
Cdd:PRK12884  84 ALLLAILLFILGLIAAYLiSPLAFLVVILVSVLGIL---YNWKLKEYGLIGNLYVAFLTGMTFIFGGIAVGELNEAVILL 160


                 ....*
gi 734879535 184 LIVVF 188
Cdd:PRK12884 161 AAMAF 165
 
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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