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Conserved domains on  [gi|1619715150|dbj|GCP28850|]
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pantothenate kinase [Escherichia coli]

Protein Classification

type I pantothenate kinase( domain architecture ID 10794612)

type I pantothenate kinase catalyzes the phosphorylation of (R)-pantothenate to form (R)-4'-phosphopantothenate, the first of five steps in coenzyme A biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 19-308 0e+00

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


:

Pssm-ID: 273134  Cd Length: 290  Bit Score: 609.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  19 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 98
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  99 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 178
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 179 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 258
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619715150 259 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 308
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
 
Name Accession Description Interval E-value
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 19-308 0e+00

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 609.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  19 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 98
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  99 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 178
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 179 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 258
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619715150 259 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 308
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 2-308 0e+00

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 529.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150   2 TPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPY 81
Cdd:COG1072     8 SPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 161
Cdd:COG1072    88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKSGDPE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 162 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 241
Cdd:COG1072   168 VRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1619715150 242 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 308
Cdd:COG1072   243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 82-306 4.27e-139

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 391.68  E-value: 4.27e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 161
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 162 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 241
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1619715150 242 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 306
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 81-243 3.13e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 89.99  E-value: 3.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  81 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 160
Cdd:PRK09270   34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 161 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 238
Cdd:PRK09270  113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                  ....*...
gi 1619715150 239 F---REGA 243
Cdd:PRK09270  185 GglsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 82-240 6.59e-12

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 63.57  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 153
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 154 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 233
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1619715150 234 NRFLKFR 240
Cdd:pfam00485 148 QRDMAER 154
 
Name Accession Description Interval E-value
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 19-308 0e+00

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 609.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  19 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 98
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  99 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 178
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 179 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 258
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619715150 259 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 308
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 2-308 0e+00

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 529.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150   2 TPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPY 81
Cdd:COG1072     8 SPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 161
Cdd:COG1072    88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARVKSGDPE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 162 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 241
Cdd:COG1072   168 VRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLRE 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1619715150 242 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 308
Cdd:COG1072   243 TAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 82-306 4.27e-139

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 391.68  E-value: 4.27e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 161
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 162 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 241
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1619715150 242 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 306
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 81-243 3.13e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 89.99  E-value: 3.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  81 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 160
Cdd:PRK09270   34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 161 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 238
Cdd:PRK09270  113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                  ....*...
gi 1619715150 239 F---REGA 243
Cdd:PRK09270  185 GglsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 80-306 3.65e-19

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 83.74  E-value: 3.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  80 PYIISIAGSVAVGKSTTARVLQALLSRwpehRRVELITTDGFLHP--NQVLKERGlmkKKGF--PESYDMHRLVKFVSDL 155
Cdd:COG0572     7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 156 KSGVPnVTAPVYSHLIYDviPDGDKTVVQP-DILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEDLLQTWYIN 234
Cdd:COG0572    80 KAGES-VELPVYDFATGT--RSGETVKVEPaDVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1619715150 235 RflkfregaftdpDSYFHNYaklTKEEAIKTAMTLWKEinwlNLKQNILPTRERASLILTKSANHAVEEVRL 306
Cdd:COG0572   147 R------------DGEERGR---TAESVIEQYWATVRP----GHEQYIEPTKEYADIVIPNGGPLNPVALDL 199
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 82-240 6.59e-12

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 63.57  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 153
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 154 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 233
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1619715150 234 NRFLKFR 240
Cdd:pfam00485 148 QRDMAER 154
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 82-227 8.96e-11

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 60.26  E-value: 8.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITTDGFLHPN-QVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 160
Cdd:cd02023     1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1619715150 161 nVTAPVYSHLIYDVIPDGdKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 227
Cdd:cd02023    77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 80-235 4.38e-09

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 56.56  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  80 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrRVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDL 155
Cdd:PRK07429    8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDYHSYDR--KQR---KELGItaldPRANNLDIMYEHLKAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 156 KSGVPnVTAPVYSH---LIydvipDGDKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDLLQTWY 232
Cdd:PRK07429   79 KTGQP-ILKPIYNHetgTF-----DPPEYIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIAWK 142


                  ...
gi 1619715150 233 INR 235
Cdd:PRK07429  143 IKR 145
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 82-240 6.40e-09

Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.


Pssm-ID: 238984 [Multi-domain]  Cd Length: 273  Bit Score: 55.81  E-value: 6.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLSrwPEHrrVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDLKS 157
Cdd:cd02026     1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDYHSLDR--KGR---KETGItaldPRANNFDLMYEQLKALKE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 158 GVPnVTAPVYSHLIYdvIPDGDKTVVQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEDLLQTWYINRFL 237
Cdd:cd02026    72 GQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                  ...
gi 1619715150 238 KFR 240
Cdd:cd02026   139 AER 141
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 80-227 1.42e-08

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 54.01  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  80 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrRVELITTDGFLHPNQVL--KERglmKKKGF--PESYDMHRLVKFVSDL 155
Cdd:PRK05480    6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQSHLsfEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1619715150 156 KSGVPnVTAPVYSHLIYDVIpdgDKTV-VQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 227
Cdd:PRK05480   79 KAGKA-IEIPVYDYTEHTRS---KETIrVEPkDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 80-235 4.84e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 47.53  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  80 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRRVELITTDGFLHPNQVLKERGlMKKKGF----PESYDMH 146
Cdd:PLN02348   49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTVICLDDYHSLDRTG-RKEKGVtaldPRANNFD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 147 RLVKFVSDLKSGVPnVTAPVYSHLiyDVIPDGDKTVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPED 226
Cdd:PLN02348  128 LMYEQVKALKEGKA-VEKPIYNHV--TGLLDPPELIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLDISDD 194


                  ....*....
gi 1619715150 227 LLQTWYINR 235
Cdd:PLN02348  195 VKFAWKIQR 203
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 82-118 2.88e-04

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 38.47  E-value: 2.88e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1619715150  82 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITT 118
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQL----GGRSVVVLDE 33
PRK06696 PRK06696
uridine kinase; Validated
 66-226 3.15e-04

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 41.12  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150  66 AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRRVELITTDGFLHPNQVLKERGLMKKKGFPE-SYD 144
Cdd:PRK06696    9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619715150 145 MHRLVKFVsdLKSGVPN-----VTApVYSHLiyDVIPDGDKTVVQPD--ILILEGLnvlqsgmdYPHDPHhvfVSDFVDF 217
Cdd:PRK06696   86 YTALRRLL--LDPLGPNgdrqyRTA-SHDLK--TDIPVHNPPLLAAPnaVLIVDGT--------FLLRPE---LRDLWDY 149


                  ....*....
gi 1619715150 218 SIYVDAPED 226
Cdd:PRK06696  150 KIFLDTDFE 158
 
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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