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Conserved domains on  [gi|1619414233|dbj|GDB89489|]
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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 ...
 135-424 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: 618.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 135 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 214
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 215 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 294
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 295 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 374
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619414233 375 KEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 424
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 ...
 135-424 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: 618.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 135 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 214
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 215 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 294
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 295 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 374
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619414233 375 KEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 424
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 112-424 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: 541.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 112 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 191
Cdd:COG1072     2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 192 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 271
Cdd:COG1072    82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 272 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 351
Cdd:COG1072   162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1619414233 352 FLKFREGAFTDPDSYFHNYAKLTKEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 424
Cdd:COG1072   237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 198-422 2.54e-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: 397.07  E-value: 2.54e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 277
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 278 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 357
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1619414233 358 GAFTDPDSYFHNYAKLTKEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 422
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 178-359 1.35e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 92.69  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 178 LRRQAVLEQflgTNGQRipYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPE 257
Cdd:PRK09270   20 LRRLAALQA---EPQRR--TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 258 SYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSI 335
Cdd:PRK09270   94 TFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTI 165

                         170       180
                  ....*....|....*....|....*..
gi 1619414233 336 YVDAPEDLLQTWYINRFLKF---REGA 359
Cdd:PRK09270  166 FLDAPAEVLRERLVARKLAGglsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 198-356 3.78e-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: 64.73  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 269
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 270 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 349
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1619414233 350 NRFLKFR 356
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 ...
 135-424 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: 618.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 135 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 214
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 215 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 294
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 295 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 374
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1619414233 375 KEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 424
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 112-424 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: 541.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 112 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 191
Cdd:COG1072     2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 192 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 271
Cdd:COG1072    82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 272 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 351
Cdd:COG1072   162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1619414233 352 FLKFREGAFTDPDSYFHNYAKLTKEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 424
Cdd:COG1072   237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 198-422 2.54e-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: 397.07  E-value: 2.54e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 277
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 278 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 357
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1619414233 358 GAFTDPDSYFHNYAKLTKEEAINTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 422
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 178-359 1.35e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 92.69  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 178 LRRQAVLEQflgTNGQRipYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPE 257
Cdd:PRK09270   20 LRRLAALQA---EPQRR--TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 258 SYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSI 335
Cdd:PRK09270   94 TFDVAGLAALLRRLRAGDDEVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTI 165

                         170       180
                  ....*....|....*....|....*..
gi 1619414233 336 YVDAPEDLLQTWYINRFLKF---REGA 359
Cdd:PRK09270  166 FLDAPAEVLRERLVARKLAGglsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 196-422 5.14e-20

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: 87.59  E-value: 5.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 196 PYIISIAGSVAVGKSTTARVLQALLSRwpehRRVELITTDGFLHP--NQVLKERGlmkKKGF--PESYDMHRLVKFVSDL 271
Cdd:COG0572     7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 272 KSGVPnVTAPVYSHLIYDviPDGDKTVVQP-DILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEDLLQTWYIN 350
Cdd:COG0572    80 KAGES-VELPVYDFATGT--RSGETVKVEPaDVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1619414233 351 RflkfregaftdpDSYFHNYaklTKEEAIntamtlwkEINWLNLK----QNILPTRERASLILTKSANHAVEEVRL 422
Cdd:COG0572   147 R------------DGEERGR---TAESVI--------EQYWATVRpgheQYIEPTKEYADIVIPNGGPLNPVALDL 199
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 198-356 3.78e-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: 64.73  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 269
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 270 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 349
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1619414233 350 NRFLKFR 356
Cdd:pfam00485 148 QRDMAER 154
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 198-343 6.46e-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: 61.42  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITTDGFLHPN-QVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 276
Cdd:cd02023     1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1619414233 277 nVTAPVYSHLIYDVIPDGdKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 343
Cdd:cd02023    77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 196-351 1.90e-09

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 58.87  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 196 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrRVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDL 271
Cdd:PRK07429    8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDYHSYDR--KQR---KELGItaldPRANNLDIMYEHLKAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 272 KSGVPnVTAPVYSH---LIydvipDGDKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDLLQTWY 348
Cdd:PRK07429   79 KTGQP-ILKPIYNHetgTF-----DPPEYIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIAWK 142


                  ...
gi 1619414233 349 INR 351
Cdd:PRK07429  143 IKR 145
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 198-356 3.31e-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: 57.35  E-value: 3.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLSrwPEHrrVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDLKS 273
Cdd:cd02026     1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDYHSLDR--KGR---KETGItaldPRANNFDLMYEQLKALKE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 274 GVPnVTAPVYSHLIYdvIPDGDKTVVQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEDLLQTWYINRFL 353
Cdd:cd02026    72 GQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                  ...
gi 1619414233 354 KFR 356
Cdd:cd02026   139 AER 141
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 196-343 1.06e-08

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 55.16  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 196 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrRVELITTDGFLHPNQVL--KERglmKKKGF--PESYDMHRLVKFVSDL 271
Cdd:PRK05480    6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQSHLsfEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1619414233 272 KSGVPnVTAPVYSHLIYDVIpdgDKTV-VQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 343
Cdd:PRK05480   79 KAGKA-IEIPVYDYTEHTRS---KETIrVEPkDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 196-351 8.86e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 47.53  E-value: 8.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 196 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRRVELITTDGFLHPNQVLKERGlMKKKGF----PESYDMH 262
Cdd:PLN02348   49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTVICLDDYHSLDRTG-RKEKGVtaldPRANNFD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 263 RLVKFVSDLKSGVPnVTAPVYSHLiyDVIPDGDKTVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPED 342
Cdd:PLN02348  128 LMYEQVKALKEGKA-VEKPIYNHV--TGLLDPPELIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLDISDD 194


                  ....*....
gi 1619414233 343 LLQTWYINR 351
Cdd:PLN02348  195 VKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 177-342 1.12e-04

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 43.43  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 177 NLRRQ---AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRRVELITTDGFLHPNQVLKERGLMKKK 253
Cdd:PRK06696    1 MSRKQlikELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619414233 254 GFPE-SYDMHRLVKFVsdLKSGVPN-----VTApVYSHLiyDVIPDGDKTVVQPD--ILILEGLnvlqsgmdYPHDPHhv 325
Cdd:PRK06696   78 GYYEdAYDYTALRRLL--LDPLGPNgdrqyRTA-SHDLK--TDIPVHNPPLLAAPnaVLIVDGT--------FLLRPE-- 142

                         170
                  ....*....|....*..
gi 1619414233 326 fVSDFVDFSIYVDAPED 342
Cdd:PRK06696  143 -LRDLWDYKIFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 198-234 2.36e-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: 39.24  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1619414233 198 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITT 234
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQL----GGRSVVVLDE 33
 
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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