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Conserved domains on  [gi|1014403471|gb|KYU98954|]
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type I 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 ...
 29-318 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 1014403471  29 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 108
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 109 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 188
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 189 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 268
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1014403471 269 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 318
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 ...
 29-318 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 1014403471  29 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 108
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 109 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 188
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 189 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 268
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1014403471 269 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 318
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 6-318 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: 531.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471   6 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 85
Cdd:COG1072     2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  86 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 165
Cdd:COG1072    82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 166 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 245
Cdd:COG1072   162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014403471 246 FLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 318
Cdd:COG1072   237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 92-316 4.60e-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: 392.06  E-value: 4.60e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 171
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 172 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 251
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014403471 252 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 316
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 91-253 2.40e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 90.38  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  91 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 170
Cdd:PRK09270   34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 171 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 248
Cdd:PRK09270  113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                  ....*...
gi 1014403471 249 F---REGA 253
Cdd:PRK09270  185 GglsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 92-250 5.29e-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: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 163
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 164 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 243
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1014403471 244 NRFLKFR 250
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 ...
 29-318 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 1014403471  29 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 108
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 109 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 188
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 189 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 268
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1014403471 269 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 318
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 6-318 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: 531.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471   6 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 85
Cdd:COG1072     2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  86 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 165
Cdd:COG1072    82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 166 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 245
Cdd:COG1072   162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1014403471 246 FLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 318
Cdd:COG1072   237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 92-316 4.60e-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: 392.06  E-value: 4.60e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 171
Cdd:cd02025     1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 172 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 251
Cdd:cd02025    81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1014403471 252 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 316
Cdd:cd02025   156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 91-253 2.40e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 90.38  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  91 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 170
Cdd:PRK09270   34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 171 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 248
Cdd:PRK09270  113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                  ....*...
gi 1014403471 249 F---REGA 253
Cdd:PRK09270  185 GglsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 90-316 3.00e-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: 84.12  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  90 PYIISIAGSVAVGKSTTARVLQALLSRwpehRRVELITTDGFLHP--NQVLKERGlmkKKGF--PESYDMHRLVKFVSDL 165
Cdd:COG0572     7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 166 KSGVPnVTAPVYSHLIYDviPDGDKTVVQP-DILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEDLLQTWYIN 244
Cdd:COG0572    80 KAGES-VELPVYDFATGT--RSGETVKVEPaDVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1014403471 245 RflkfregaftdpDSYFHNYaklTKEEAIKTAMTLWKEinwlNLKQNILPTRERASLILTKSANHAVEEVRL 316
Cdd:COG0572   147 R------------DGEERGR---TAESVIEQYWATVRP----GHEQYIEPTKEYADIVIPNGGPLNPVALDL 199
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 92-250 5.29e-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: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 163
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 164 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 243
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 1014403471 244 NRFLKFR 250
Cdd:pfam00485 148 QRDMAER 154
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 92-237 9.03e-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: 9.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITTDGFLHPN-QVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 170
Cdd:cd02023     1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1014403471 171 nVTAPVYSHLIYDVIPDGdKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 237
Cdd:cd02023    77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 90-245 4.46e-09

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 56.56  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  90 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrRVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDL 165
Cdd:PRK07429    8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDYHSYDR--KQR---KELGItaldPRANNLDIMYEHLKAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 166 KSGVPnVTAPVYSH---LIydvipDGDKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDLLQTWY 242
Cdd:PRK07429   79 KTGQP-ILKPIYNHetgTF-----DPPEYIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIAWK 142


                  ...
gi 1014403471 243 INR 245
Cdd:PRK07429  143 IKR 145
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 92-250 5.41e-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: 56.19  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLSrwPEHrrVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDLKS 167
Cdd:cd02026     1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDYHSLDR--KGR---KETGItaldPRANNFDLMYEQLKALKE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 168 GVPnVTAPVYSHLIYdvIPDGDKTVVQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEDLLQTWYINRFL 247
Cdd:cd02026    72 GQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                  ...
gi 1014403471 248 KFR 250
Cdd:cd02026   139 AER 141
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 90-237 1.82e-08

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 53.62  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  90 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrRVELITTDGFLHPNQVL--KERglmKKKGF--PESYDMHRLVKFVSDL 165
Cdd:PRK05480    6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQSHLsfEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1014403471 166 KSGVPnVTAPVYSHLIYDVIpdgDKTV-VQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 237
Cdd:PRK05480   79 KAGKA-IEIPVYDYTEHTRS---KETIrVEPkDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 90-245 5.18e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 47.53  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  90 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRRVELITTDGFLHPNQVLKERGlMKKKGF----PESYDMH 156
Cdd:PLN02348   49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTVICLDDYHSLDRTG-RKEKGVtaldPRANNFD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 157 RLVKFVSDLKSGVPnVTAPVYSHLiyDVIPDGDKTVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPED 236
Cdd:PLN02348  128 LMYEQVKALKEGKA-VEKPIYNHV--TGLLDPPELIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLDISDD 194


                  ....*....
gi 1014403471 237 LLQTWYINR 245
Cdd:PLN02348  195 VKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 76-236 2.27e-04

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 41.89  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471  76 AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRRVELITTDGFLHPNQVLKERGLMKKKGFPE-SYD 154
Cdd:PRK06696    9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1014403471 155 MHRLVKFVsdLKSGVPN-----VTApVYSHLiyDVIPDGDKTVVQPD--ILILEGLnvlqsgmdYPHDPHhvfVSDFVDF 227
Cdd:PRK06696   86 YTALRRLL--LDPLGPNgdrqyRTA-SHDLK--TDIPVHNPPLLAAPnaVLIVDGT--------FLLRPE---LRDLWDY 149


                  ....*....
gi 1014403471 228 SIYVDAPED 236
Cdd:PRK06696  150 KIFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 92-128 2.81e-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: 2.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1014403471  92 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITT 128
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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