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Conserved domains on  [gi|446347915|ref|WP_000425770|]
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MULTISPECIES: 1,4-dihydroxy-2-naphthoate polyprenyltransferase [Bacillus]

Protein Classification

prenyltransferase( domain architecture ID 10792743)

prenyltransferase transfers an isoprenyl group to an aromatic substrate acceptor; may be involved in the biosynthesis of menaquinone or phylloquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
22-315 9.23e-134

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


:

Pssm-ID: 235695  Cd Length: 293  Bit Score: 381.41  E-value: 9.23e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  22 WRIWWSLLRPHTLTAAFVPVFIGTAYSMQVGginQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAI 101
Cdd:PRK06080   3 FKAWLELARPKTLPAAFAPVLVGTALAYWLG---SFHPLLALLALLAALLLQIATNLANDYGDYVKGTDTEDRVGPLRAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 102 VRDGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISF 181
Cdd:PRK06080  80 GRGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 182 FIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSP 261
Cdd:PRK06080 160 YLQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCIVLLALLGLASP 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446347915 262 WMLIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:PRK06080 240 WGLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLSQ 293
 
Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
22-315 9.23e-134

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


Pssm-ID: 235695  Cd Length: 293  Bit Score: 381.41  E-value: 9.23e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  22 WRIWWSLLRPHTLTAAFVPVFIGTAYSMQVGginQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAI 101
Cdd:PRK06080   3 FKAWLELARPKTLPAAFAPVLVGTALAYWLG---SFHPLLALLALLAALLLQIATNLANDYGDYVKGTDTEDRVGPLRAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 102 VRDGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISF 181
Cdd:PRK06080  80 GRGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 182 FIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSP 261
Cdd:PRK06080 160 YLQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCIVLLALLGLASP 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446347915 262 WMLIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:PRK06080 240 WGLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLSQ 293
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
24-315 4.70e-110

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 321.32  E-value: 4.70e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  24 IWWSLLRPHTLTAAFVPVFIGTAYSMQVGGinQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVR 103
Cdd:COG1575    1 AWLEAARPRTLPAAVAPVLLGTALAYYETG--SFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEERVGPSRVIVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 104 DGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFI 183
Cdd:COG1575   79 GLLSPKQVLRAALLLLALALLLGLYLVLLSGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGTYYV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 184 QTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWM 263
Cdd:COG1575  159 QTGTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLLVLLGLLPPWA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446347915 264 LIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:COG1575  239 LLALLSLPLALKLVRRVLRGAKPEALIPALKNTALLNLLFGLLLALGLLLGR 290
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
26-310 8.69e-92

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: 274.39  E-value: 8.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  26 WSLLRPHTLTAAFVPVFIGTAYSMQVGGinQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDG 105
Cdd:cd13962    1 LLAARPRTLPASLAPVLLGTALAYYLGG--FFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEPRSGPSRVLVSGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFIQT 185
Cdd:cd13962   79 LSPRQVLRAALVLLLLAALLGLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYYVQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 186 GTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWMLI 265
Cdd:cd13962  159 GSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLLGLLPLWSLL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 446347915 266 VFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIG 310
Cdd:cd13962  239 ALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLALG 283
menA TIGR00751
1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1, ...
30-310 3.29e-33

1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1,4-dihydroxy-2-naphthoic acid (DHNA) to demethylmenaquinone, a step in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 129834  Cd Length: 284  Bit Score: 123.84  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   30 RPHTLTAAFVPVFIGTAYSMQVGGINQIhlpLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDGIQPK 109
Cdd:TIGR00751   1 RPKTLPLAIAPIVAGTALAAWLHAFVWL---VALLALATAVLLQILSNYANDYGDGIKGSDTDDRIGPLRGVQKGLITPR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  110 TV-----LNLAFGFF-GIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFI 183
Cdd:TIGR00751  78 EVktaliTSVALGALsGLVLALLAAPNLSDLFWFIALGALCIAAAITYTVGSKPYGYAGLGDISVLVFFGPLAVLGTQYL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  184 QTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWM 263
Cdd:TIGR00751 158 QAHRVDWVGILPAVATGLLACAVLNINNLRDIPTDARAGKNTLAVRLGDARTRMYHQGLLAVAGVCTFVFMLATPISWWC 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 446347915  264 LIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIG 310
Cdd:TIGR00751 238 VLFLLAAPLLLKAAGPVRSGRGPRELRPVLRDTGLAMLLWNLLFALG 284
UbiA pfam01040
UbiA prenyltransferase family;
41-274 3.61e-25

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 101.15  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   41 VFIGTAYSMQVGGINQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGigGAIVRDGIQPKTVLNLAFGFFG 120
Cdd:pfam01040   1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPN--RPLPSGRISPREALIFALVLLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  121 IAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTggpLPIAY-TPFGELTAGLFMGVIIIgISFFIQTGTVTSEVILLSIPS 199
Cdd:pfam01040  79 LGLLLLLLL----NPLTALLGLAALLLYVLYT---LRLKRrTLLGQLVGGLAFGLPPL-LGWAAVTGSLSPLALLLALAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446347915  200 SILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWMLIVFLSAPKAF 274
Cdd:pfam01040 151 FLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALAL 225
 
Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
22-315 9.23e-134

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


Pssm-ID: 235695  Cd Length: 293  Bit Score: 381.41  E-value: 9.23e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  22 WRIWWSLLRPHTLTAAFVPVFIGTAYSMQVGginQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAI 101
Cdd:PRK06080   3 FKAWLELARPKTLPAAFAPVLVGTALAYWLG---SFHPLLALLALLAALLLQIATNLANDYGDYVKGTDTEDRVGPLRAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 102 VRDGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISF 181
Cdd:PRK06080  80 GRGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 182 FIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSP 261
Cdd:PRK06080 160 YLQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCIVLLALLGLASP 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446347915 262 WMLIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:PRK06080 240 WGLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLSQ 293
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
24-315 4.70e-110

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 321.32  E-value: 4.70e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  24 IWWSLLRPHTLTAAFVPVFIGTAYSMQVGGinQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVR 103
Cdd:COG1575    1 AWLEAARPRTLPAAVAPVLLGTALAYYETG--SFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEERVGPSRVIVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 104 DGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFI 183
Cdd:COG1575   79 GLLSPKQVLRAALLLLALALLLGLYLVLLSGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGTYYV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 184 QTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWM 263
Cdd:COG1575  159 QTGTLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAYLLILLLVLLGLLPPWA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446347915 264 LIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:COG1575  239 LLALLSLPLALKLVRRVLRGAKPEALIPALKNTALLNLLFGLLLALGLLLGR 290
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
26-310 8.69e-92

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: 274.39  E-value: 8.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  26 WSLLRPHTLTAAFVPVFIGTAYSMQVGGinQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDG 105
Cdd:cd13962    1 LLAARPRTLPASLAPVLLGTALAYYLGG--FFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTEPRSGPSRVLVSGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFIQT 185
Cdd:cd13962   79 LSPRQVLRAALVLLLLAALLGLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYYVQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 186 GTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWMLI 265
Cdd:cd13962  159 GSLSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLLGLLPLWSLL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 446347915 266 VFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIG 310
Cdd:cd13962  239 ALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLALG 283
PRK13387 PRK13387
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Provisional
26-315 1.30e-75

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Provisional


Pssm-ID: 237373  Cd Length: 317  Bit Score: 234.68  E-value: 1.30e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  26 WSLLRPHTLTAAFVPVFIGTAYSMQVGGINQIhlPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDG 105
Cdd:PRK13387   7 LKLVEIHTKIASFFPVILGTLFSLYVAKIFDW--LLFLAFMVAMLAFDIATTAINNYMDFKKALDTADYVGIGNGIGQHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFIQT 185
Cdd:PRK13387  85 LKPRNVLTVILLMYVVAAILGVYLCMNTSWLLLVIGLICFAIGILYTGGPLPLSRMPLGEIFSGLTMGFGIFLLAVYINT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 186 GTVTSE--------------------VILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIV 245
Cdd:PRK13387 165 NTITIEsllfqgemftiqgnliaiiaIGVISLPIIFTIANIMLANNLRDLDEDIKNHRYTLVYYIGREKGVVLFAILFYA 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446347915 246 SYIWTIALIIVGIVSPWMLIVFLSAPKAFKATKGFI-GKSIPMEMVPAMIATAKTNTIFGFLMGIGLLLGY 315
Cdd:PRK13387 245 SYLAIAVIVLMGYISPWALLSFLTLRKPISNLQSFQkEAKDPKYFVIAIRNTVLTNTTFGFLLSASLLIQY 315
menA TIGR00751
1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1, ...
30-310 3.29e-33

1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1,4-dihydroxy-2-naphthoic acid (DHNA) to demethylmenaquinone, a step in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 129834  Cd Length: 284  Bit Score: 123.84  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   30 RPHTLTAAFVPVFIGTAYSMQVGGINQIhlpLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDGIQPK 109
Cdd:TIGR00751   1 RPKTLPLAIAPIVAGTALAAWLHAFVWL---VALLALATAVLLQILSNYANDYGDGIKGSDTDDRIGPLRGVQKGLITPR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  110 TV-----LNLAFGFF-GIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFI 183
Cdd:TIGR00751  78 EVktaliTSVALGALsGLVLALLAAPNLSDLFWFIALGALCIAAAITYTVGSKPYGYAGLGDISVLVFFGPLAVLGTQYL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  184 QTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWM 263
Cdd:TIGR00751 158 QAHRVDWVGILPAVATGLLACAVLNINNLRDIPTDARAGKNTLAVRLGDARTRMYHQGLLAVAGVCTFVFMLATPISWWC 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 446347915  264 LIVFLSAPKAFKATKGFIGKSIPMEMVPAMIATAKTNTIFGFLMGIG 310
Cdd:TIGR00751 238 VLFLLAAPLLLKAAGPVRSGRGPRELRPVLRDTGLAMLLWNLLFALG 284
ubiA PRK05951
prenyltransferase; Reviewed
33-314 8.27e-27

prenyltransferase; Reviewed


Pssm-ID: 180323  Cd Length: 296  Bit Score: 106.79  E-value: 8.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  33 TLTAAFVPVFIGTAYSMQVGGI--NQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGIGGAIVRDGI-QPK 109
Cdd:PRK05951  11 TRPWSFVMTAIVAFFSIAYGYYlfRSFDPLLGALMLLGYFLLHASLNVFNDYKDYVLDCDHHETTGYRQHPIQAGImTLG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 110 TVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIIIGISFFIQTGTVT 189
Cdd:PRK05951  91 HLRVLGIALGAIALQLGWSLVLDRGIGAVTLALLGVFLWTCYMGPPFFLKYRWLGEHLVFYAWSHMLVMGLIYVWLGNLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 190 SEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFiVSYIWTIALIIVGIVSPWMLIVFLS 269
Cdd:PRK05951 171 SPNLLAGVPLGLLMALVLLSNNLRDIEDDERKGIPTLAVIFGRRGAALYIFALL-SPYVILQILLIAILTPLISLWALLS 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 446347915 270 APKAFKATKGFIGKSIPmemvPAMIATAKTNTIFGFLMGIGLLLG 314
Cdd:PRK05951 250 LLVAYALCLWQLRKFPP----DPDEATVQLFMLFGYLYILATLLS 290
UbiA pfam01040
UbiA prenyltransferase family;
41-274 3.61e-25

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 101.15  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   41 VFIGTAYSMQVGGINQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSVGigGAIVRDGIQPKTVLNLAFGFFG 120
Cdd:pfam01040   1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPN--RPLPSGRISPREALIFALVLLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  121 IAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTggpLPIAY-TPFGELTAGLFMGVIIIgISFFIQTGTVTSEVILLSIPS 199
Cdd:pfam01040  79 LGLLLLLLL----NPLTALLGLAALLLYVLYT---LRLKRrTLLGQLVGGLAFGLPPL-LGWAAVTGSLSPLALLLALAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446347915  200 SILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWMLIVFLSAPKAF 274
Cdd:pfam01040 151 FLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALAL 225
PRK07419 PRK07419
2-carboxy-1,4-naphthoquinone phytyltransferase;
7-317 3.67e-23

2-carboxy-1,4-naphthoquinone phytyltransferase;


Pssm-ID: 236015  Cd Length: 304  Bit Score: 96.90  E-value: 3.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   7 TNSSPTAPKpskqtgwRIWWSLLRPHTLTAAFVPVFIGTAYSMQVGGInqIHLPLFLMMLLACLLIQAATNMFNEYFDYK 86
Cdd:PRK07419   4 TTSMSPSRR-------KLWLAAIKPPMYSVAIMPILVGTAWALGETGV--FRLDQFITFLLAAILILAWENLSNDVFDAD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  87 RGLD----HegsvgiggAIVRDGIQPKTVLNLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTP 162
Cdd:PRK07419  75 TGIDknkfH--------SVVNLTGNKSLVFWLANLFLLLGLLGILAIALQSDWTVLGLVLLCCFLGYLYQGPPFRLGYQG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 163 FGELTAGLFMGVIIIGISFFIQTGTvtseVILLSIPSSILIGA----ILLANNIRDLDGDKENGRKTLAILVGRERAVGV 238
Cdd:PRK07419 147 LGEPLCFLAFGPLAVAAALYSQTPS----WSLIPLAASIILGLatslILFCSHFHQVEDDLAAGKRSPIVRLGTKRGAQL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 239 LASMFIVSYIWTIALIIVGIVSPWMLIVFLSAPKAFKATKgFIGKSipmEMVPAMIATAK-----TNTIFGFLMGIGLLL 313
Cdd:PRK07419 223 LPWIVGLIYALELLPVLLGFWPWTTLLSLLSLPFAIKLIR-LVREN---HDQPEKVSNSKfiavrFHFWSGLLLSLGLIL 298

                 ....
gi 446347915 314 GYFL 317
Cdd:PRK07419 299 AYLL 302
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
26-268 1.39e-18

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: 83.55  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  26 WSLLRPHTLTAAFVPVFIGTAYSMQVGGINqihLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDhegsVGIGGAIVRDG 105
Cdd:cd13956    1 LRLMRPYTLLYVLAPALAGAALAGAFAGPL---PALLLLALLAVFLGAGAGYALNDYTDRELDAI----NKPDRPLPSGR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTGGPLPIayTPFGELTAGLFMGVIIIGISFFIQT 185
Cdd:cd13956   74 LSPRQALAFAAALLLVGLALALAL----GPLALLLLLAGLLLGLAYSLGLKRL--KLGGWGVLGYATGLALLPGLGAVAA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 186 GTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWMLI 265
Cdd:cd13956  148 GGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAAGLLLAALILVVLLAVAGLLGPLALL 227

                 ...
gi 446347915 266 VFL 268
Cdd:cd13956  228 ALL 230
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
23-271 2.53e-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: 74.50  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  23 RIWWSLLR---PHTLTAAFVPVFIGTAYSMQvggiNQIHLPLFLMMLLACLLIQAATNMFNEYFDYKrgLDHEGSVGIGG 99
Cdd:COG0382    1 RAYLRLLRldrPIGILLLLWPTLWALFLAAG----GLPDLLLLLLAVLGTVLMRSAGYVINDYFDRE--IDRINERKPNR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 100 AIVRDGIQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYtggplPIA---YTPFGELTAGLFMGVII 176
Cdd:COG0382   75 PLASGRISLREALLLAIVLLLLALALALLL----NPLTFLLALAALALAWAY-----SLFlkrFTLLGNLVLGLLFGLGI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 177 IgISFFIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIV 256
Cdd:COG0382  146 L-MGFAAVTGSLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLL 224
                        250
                 ....*....|....*
gi 446347915 257 GIVSPWMLIVFLSAP 271
Cdd:COG0382  225 AGLGLLYLLGLLAAL 239
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
25-271 1.71e-13

Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260124  Cd Length: 270  Bit Score: 69.07  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  25 WWSLLRPHTLTAAFVPVFIGTAYSMqvGGINQIHLPLFLMMLLACLLIQAATNMFNEYFDYK--------Rgldhegsvg 96
Cdd:cd13961    2 YLELIRPPNLLMAALAQYLGALFAL--GPLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEidrinkpdR--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  97 iggAIVRDGIQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTggpLPIAYTPF-GELTAGLFMGVI 175
Cdd:cd13961   71 ---PIPSGRISRREALILSILLNALGLILAFLL----SPLALLIALLNSLLLWLYS---HKLKRTPLiGNLLVALLTGLP 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 176 IIGISFFIqtGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALII 255
Cdd:cd13961  141 FLFGGLAA--GNLLLIILLLALFAFLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYL 218
                        250
                 ....*....|....*.
gi 446347915 256 VGIVSPWMLIVFLSAP 271
Cdd:cd13961  219 LGGLGILYLILIIIAD 234
ubiA PRK12872
prenyltransferase; Reviewed
59-271 1.50e-10

prenyltransferase; Reviewed


Pssm-ID: 237241  Cd Length: 285  Bit Score: 60.73  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  59 LPLFLMMLLACLLIQAATNMFNEYFDYKRGldhegsvgIGGAIVRDGIQPKTVLNLAFGFFGIAILLGVYI-CMNSSWWL 137
Cdd:PRK12872  35 LPISWLLLLITFLIAAAVYIINYLTDLEED--------IINKPERVVFSETKAYGLFLLLNVLGLYLGAYLlAVIGGPKF 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 138 AAIGLVCMAVAYLYTGGPLPIA-YTP-FGELTAGLFMGVIIIGISFFIQTGTVTSEVILLSIPSSILIGAILLANNIRDL 215
Cdd:PRK12872 107 ALIFIIPLILGILYSVFFKRRLkRIPlFKNLVVSLLWALSPLILGVYYYQLTIFSLLLLYAVFIFLKSFIREIVFDIKDI 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446347915 216 DGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVS-PWMLIVFLSAP 271
Cdd:PRK12872 187 EGDRKSGLKTLPIVLGKERTLKFLLILNLLFLILLILGVYTGLLPlLLLVLLLLLAY 243
ubiA PRK12884
prenyltransferase; Reviewed
26-270 2.42e-09

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 57.27  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  26 WSLLRPHTLTAAFVPVFIGTAYSMQVGGINQIhlplfLMMLLACLLIQAATNMFNEYFDYKRGLDHEgsvgIGGAIVRDG 105
Cdd:PRK12884   8 LELLRPEHGLMAGIAVVLGAIIALGGLPLDEA-----LLGFLTAFFASGSANALNDYFDYEVDRINR----PDRPIPSGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTggpLPIAYTPF-GELTAGLFMG--VIIIGISFf 182
Cdd:PRK12884  79 ISRREALLLAILLFILGLIAAYLI----SPLAFLVVILVSVLGILYN---WKLKEYGLiGNLYVAFLTGmtFIFGGIAV- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 183 iqtGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPW 262
Cdd:PRK12884 151 ---GELNEAVILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFILAVLLSPLPYLFGIFNIL 227

                 ....*...
gi 446347915 263 MLIVFLSA 270
Cdd:PRK12884 228 YLAPVLVA 235
PLN02922 PLN02922
prenyltransferase
24-313 4.84e-08

prenyltransferase


Pssm-ID: 215499  Cd Length: 315  Bit Score: 53.59  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  24 IWWSLLRPHTLTAAFVPVFIGTAYS-MQVGGINQIHLplFLMMLLACLLIqAATNMFNEYFDYKRGLDH---EGSVGIGG 99
Cdd:PLN02922  17 LWWRAIKLPMYSVALVPLTVGAAAAyLQTGLFDARRY--GTLLLSSVLVI-TWLNLSNDAYDADTGVDKnkkESVVNLVG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 100 AivRDGIQPKTVLNLAFGFFGIaillgVYICMNSSWWLAAIGLVC-MAVAYLYTGGPLPIAYTPFGE-LTAGLFMGVIII 177
Cdd:PLN02922  94 S--RRGVLAAAIGCLALGAAGL-----VWASLVAGNIRVILLLAAaILCGYVYQCPPFRLSYKGLGEpLCFAAFGPLATT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 178 GISFFIQTGTVTSEVILLSIP-----SSILIG----AILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYI 248
Cdd:PLN02922 167 AFYLALASGAGGSEMAILPLTptvlsASVLVGltttLILFCSHFHQIDGDRAVGKMSPLVRLGTEKGSRVVRWAVLLLYS 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446347915 249 WTIALIIVGIV-SPWMLIVFLSAPKAfKATKGFIGKSipmEMVPAMIATAK-----TNTIFGFLMGIGLLL 313
Cdd:PLN02922 247 LLAALGLLKALpLPCALLCFLTLPLG-KLVVDFVEKN---HKDNAKIFMAKyycvrLHALFGAALALGLVL 313
PT_UbiA_5 cd13967
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
113-270 3.84e-07

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


Pssm-ID: 260130  Cd Length: 277  Bit Score: 50.69  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 113 NLAFGFFGIAILLGVYICMNSSWWLAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVII-----IGISFFIqtGT 187
Cdd:cd13967   76 KLLLALAIAAGLLALALAFILGLLAFAILLLPLLLGLLYSLPIKPGKLRLRRRKDIPGSKNLVValawaVVIALLP--AL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 188 VTSEVILLSIPSSILIGAILLAN----NIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIVSPWM 263
Cdd:cd13967  154 YGQPSTPSVLVVFLFFFLKVFVNtaifDIRDVEGDRIVGIETLPVLLGEERTRLLLLVLNILLALLLVAGVLLGLLASEF 233

                 ....*..
gi 446347915 264 LIVFLSA 270
Cdd:cd13967  234 LVLLLSL 240
PT_UbiA_3 cd13965
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
135-268 8.96e-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: 260128  Cd Length: 273  Bit Score: 43.40  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 135 WWLAAIgLVCMAVAYLYTGGPLPIAYTPF------GELTAGLFMGVIIIGISFFIQT-------GTVTSEVILLSIPSSI 201
Cdd:cd13965   86 LRWLLV-PLCLALSAYLGVLEESLLLIVLtwlyneLGLADHWLTRNLLNALGYAAFLagatriaGGGPHPLDPTAWAWIL 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446347915 202 LIGAILL----ANNIRDLDGDKENGRKTLAILVGrERAVGVLASMFIVSyiWTIALIIVGIVSPWMLIVFL 268
Cdd:cd13965  165 LSAAIILttihAQDFRDVEGDRARGRRTLPLVFG-DAAARWLIAAGVVA--WSVVLPYFWGLPPLLAALLV 232
ubiA PRK12882
prenyltransferase; Reviewed
27-279 1.14e-04

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 43.04  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  27 SLLRPHTLTAAFVPVFIGTAysmqVGGINQIHLPLFLMMLLACLLIQAATNMFNEYFDYK--------Rgldhegsvgig 98
Cdd:PRK12882   9 ELTRPVNAVVAGVAAFIGAF----IAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREidrinrpdR----------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  99 gAIVRDGIQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYT----GGPLpiaytpFGELTAGLFMGV 174
Cdd:PRK12882  74 -PIPSGAVSPRGALAFSILLFAAGVALAFLL----PPLCLAIALFNSLLLVLYAetlkGTPG------LGNASVAYLTGS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 175 IIIGISFFIQTGTVTSEVILLSIpSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERA---------VGVLASM--F 243
Cdd:PRK12882 143 TFLFGGAAVGTEGLLALLVLFAL-AALATLAREIIKDVEDIEGDRAEGARTLPILIGVRKAlyvaaafllVAVAASPlpY 221
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446347915 244 IVSYIWTIALIIVGIVSPWMLIVFLSAPKAFKATKG 279
Cdd:PRK12882 222 LLSTFGLWYLVLVAPADLVMLAAAYRSLKKTDPTAS 257
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
28-279 8.15e-04

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 40.48  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  28 LLRPHTLTAAFVPVFIGTAYSMqvGGINQIH--LPLFLMMLLAClliqAATNMFNEYFDYKRGLDHEGSvgigGAIVRDG 105
Cdd:PRK12883   9 ITRPHNCILAGIVGILGSLVAL--GGIPPIKtlILIFLVVYLGC----SGGNTINDYFDYEIDKINRPN----RPLPRGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 106 IQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYLYTGGPLPIaytPF-GELTAGLFMGVI----IIGIS 180
Cdd:PRK12883  79 MSRKAALYYSLLLFAVGLALAYLI----NIEAFLFALGAYVLMFLYAWKLKPL---PFiGNVVVALLTGATpiygAIAVG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 181 FFIQTGTVTSEVILLSIPSSILigaillaNNIRDLDGDKENGRKTLAILVGRERAvGVLASMFIVSYIWT---------- 250
Cdd:PRK12883 152 RIGLAGYLAICAFLVNVAREIM-------KDIEDIEGDKAKGAKTLPIIIGKKRA-AYIGAIFGVLTVIAsflpvkagig 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 446347915 251 ---IALIIVGIVSPWMLIVFLSAPKAFKATKG 279
Cdd:PRK12883 224 lgyLPIIIVDAIILYAAYLVLRNPDRETAHKG 255
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
25-261 1.21e-03

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 39.94  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  25 WWSLLRPHTLTAAFVPVFIGTAYSMQVgginQIHLPLFLMMLLACLLIQAATNMFNEYFDYKRGLDHEGSvgigGAIVRD 104
Cdd:PRK09573   6 YFELIRPKNCIGASIGAIIGYLIASNF----KIDLKGIILAALVVFLVCAGGNVINDIYDIEIDKINKPE----RPIPSG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 105 GIQPKTVLNLAFGFFGIAILLGVYICMnsswwlAAIGLVCMAVAYLYTGGPLPIAYTPFGELTAGLFMGVIII--GISFF 182
Cdd:PRK09573  78 RISLKEAKIFSITLFIVGLILSIFINI------YAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIfgGLAVF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 183 iqtgTVTSEVIL-LSIPSSILIGAILlaNNIRDLDGDKENGRKTLAILVGRERAVgvlasmfivsYIWTIALIIVGIVSP 261
Cdd:PRK09573 152 ----NVLRIIILfLCAFFSTWSREIV--KDIEDIEGDLKENVITLPIKYGIKKSW----------YIAKILLILAIVLSP 215
PRK07566 PRK07566
chlorophyll synthase ChlG;
1-274 3.10e-03

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 38.75  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915   1 MEMNVKTNSSPTAPKPSKQTGWRIWWS----LLRPHT---LTAAFVPvfiGTAYSMQVGGINQIHLPLFLMMLLACLLIQ 73
Cdd:PRK07566   2 SEALENTSKPRQLLGPKGASPTTSIWKarlqLMKPITwfpPMWAFLC---GAVSSGAFGWTLENVLKLLAGMLLAGPLLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  74 AATNMFNEYFDykRGLD--HEGSVGI-GGAivrdgIQPKTVLNLAFGFFGIAILLGVYIcmnsSWWLAAIGLVCMAVAYL 150
Cdd:PRK07566  79 GTSQTLNDYFD--REVDaiNEPYRPIpSGA-----ISLRWVLYLIAVLTVLGLAVAYLL----GPWVFLAALLGLFLAWI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 151 YTGGPLpiaytpfgELTAGLFMGVIIIGIS----------FFIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKE 220
Cdd:PRK07566 148 YSAPPL--------RLKQNGWLGNYAVGLSyeglpwwagaAAFGAGLPSWPIVILALLYSLGAHGIMTLNDFKSVEGDRQ 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446347915 221 NGRKTLAILVGRERAVGV------LASMFIVSYI-----WTIALIIVGIVSP--WMLIVFLSAPKAF 274
Cdd:PRK07566 220 LGLRSLPVVFGEKNAARIacvvidLFQLAVIALLlawgqPLYAAIVGLLLIPqiTLQDRLLRDPLER 286
ubiA PRK13591
prenyltransferase; Provisional
121-267 4.29e-03

prenyltransferase; Provisional


Pssm-ID: 184169  Cd Length: 307  Bit Score: 38.15  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 121 IAILLGVYICMNSSWWLAAigLVCMAVAYLYTGGplpIAYTPFG-ELTAGLFMGVIIIGISFfiqtGTVTSEVILLSIPS 199
Cdd:PRK13591 107 LAFLLGTYILAMDGMLLLA--FLPFITGYLYSKG---IKIGKFAlKLKGGLGVKNIVVGITW----GGFIAGIAGSYCGS 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 200 SILIGAILL-----------ANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIALIIVGIV-SPWMLIVF 267
Cdd:PRK13591 178 LIPVGLIFLffgvklfinscVYDFKDVKGDTLAGIKTLPVSLGEQKTRNLLLGIHLFSHLVLGIALIFGVIaFEPIILLY 257
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
28-253 9.06e-03

Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of chlorophyll (Chl) biosynthesis, the addition of the tetraprenyl (phytyl or geranylgeranyl) side chain. In plant chloroplast, the chlorophyll synthase is located in thylakoid membrane and has been shown to also have a regulatory or channeling function. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260121  Cd Length: 277  Bit Score: 37.21  E-value: 9.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915  28 LLRPHTLTAAFVPVFIGTAYSMQVGGINQIHLPLFLMMLLACLLIQAATNMFNEYFDykRGLD--HEGSVGI-GGAI-VR 103
Cdd:cd13958    4 LLKPVTWFPPMWAFLCGAAASGAFQWSNWDVWLLLLGMLLAGPLLTGTSQTINDYYD--REVDaiNEPYRPIpSGRIsER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347915 104 DGIQPKTVLNLafGFFGIAILLGvyicmnsSWWLAAIGLVCMAVAYLYTGGPLpiaytpfgELTAGLFMGVIIIGISF-- 181
Cdd:cd13958   82 EALWNIWVLLL--LSLLVALFLD-------GPWVFAAAVVGLVLAYIYSAPPL--------KLKQNGWWGNAAVGLSYeg 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446347915 182 -------FIQTGTVTSEVILLSIPSSILIGAILLANNIRDLDGDKENGRKTLAILVGRERAVGVLASMFIVSYIWTIAL 253
Cdd:cd13958  145 lpwwagaAAFAGLLTWESLALALLYSIGAHGIMTLNDFKSIEGDRQLGLRSLPVALGVDTAAWIACGVIDVPQLAVAAL 223
 
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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