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Conserved domains on  [gi|300845606|gb|EFK73366|]
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pantothenate kinase [Escherichia coli MS 78-1]

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

 Zoom to residue level

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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 ...
 34-323 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: 610.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606   34 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 113
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  114 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 193
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  194 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 273
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 300845606  274 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 323
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 ...
 34-323 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: 610.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606   34 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 113
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  114 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 193
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  194 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 273
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 300845606  274 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 323
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 11-323 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 300845606  11 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 90
Cdd:COG1072    2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  91 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 170
Cdd:COG1072   82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 171 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 250
Cdd:COG1072  162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300845606 251 FLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 323
Cdd:COG1072  237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 97-321 3.15e-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: 392.83  E-value: 3.15e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  97 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 176
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 177 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 256
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300845606 257 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 321
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 96-258 2.77e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 90.38  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  96 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 175
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 176 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 253
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                 ....*...
gi 300845606 254 F---REGA 258
Cdd:PRK09270 185 GglsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 97-255 5.35e-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: 63.96  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606   97 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 168
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  169 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 248
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 300845606  249 NRFLKFR 255
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 ...
 34-323 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: 610.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606   34 VPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 113
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  114 VLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDG 193
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  194 DKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLT 273
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 300845606  274 KEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 323
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 11-323 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 300845606  11 KEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 90
Cdd:COG1072    2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  91 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDL 170
Cdd:COG1072   82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 171 KSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEDLLQTWYINR 250
Cdd:COG1072  162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300845606 251 FLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK 323
Cdd:COG1072  237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 97-321 3.15e-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: 392.83  E-value: 3.15e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  97 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 176
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 177 VTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFRE 256
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300845606 257 GAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRL 321
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 96-258 2.77e-21

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 90.38  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  96 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 175
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 176 NVTAPVYSHLIYDVIPDGdkTVVQPD--ILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEDLLQTWYINRFLK 253
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADA--IVVPPTarLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLA 184


                 ....*...
gi 300845606 254 F---REGA 258
Cdd:PRK09270 185 GglsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 95-321 2.73e-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: 84.51  E-value: 2.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  95 PYIISIAGSVAVGKSTTARVLQALLSRwpehRRVELITTDGFLHP--NQVLKERGlmkKKGF--PESYDMHRLVKFVSDL 170
Cdd:COG0572    7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 171 KSGVPnVTAPVYSHLIYDviPDGDKTVVQP-DILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEDLLQTWYIN 249
Cdd:COG0572   80 KAGES-VELPVYDFATGT--RSGETVKVEPaDVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIV 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300845606 250 RflkfregaftdpDSYFHNYaklTKEEAIKTAMTLWKEinwlNLKQNILPTRERASLILTKSANHAVEEVRL 321
Cdd:COG0572  147 R------------DGEERGR---TAESVIEQYWATVRP----GHEQYIEPTKEYADIVIPNGGPLNPVALDL 199
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 97-255 5.35e-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: 63.96  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606   97 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNQVLKERGlMKKKGF----PESYDMHRLVKFVS 168
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  169 DLKSGVpNVTAPVYSHLIYDVIPDGDKtVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEDLLQTWYI 248
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 300845606  249 NRFLKFR 255
Cdd:pfam00485 148 QRDMAER 154
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 97-242 8.66e-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: 8.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  97 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITTDGFLHPN-QVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 175
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300845606 176 nVTAPVYSHLIYDVIPDGdKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 242
Cdd:cd02023   77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 95-250 4.08e-09

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 56.94  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  95 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrRVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDL 170
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDYHSYDR--KQR---KELGItaldPRANNLDIMYEHLKAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 171 KSGVPnVTAPVYSH---LIydvipDGDKTVVQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDLLQTWY 247
Cdd:PRK07429  79 KTGQP-ILKPIYNHetgTF-----DPPEYIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIAWK 142


                 ...
gi 300845606 248 INR 250
Cdd:PRK07429 143 IKR 145
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 97-255 5.35e-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: 5.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  97 IISIAGSVAVGKSTTARVLQALLSrwPEHrrVELITTDGFLHPNQvlKERglmKKKGF----PESYDMHRLVKFVSDLKS 172
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDYHSLDR--KGR---KETGItaldPRANNFDLMYEQLKALKE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 173 GVPnVTAPVYSHLIYdvIPDGDKTVVQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEDLLQTWYINRFL 252
Cdd:cd02026   72 GQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQRDM 138


                 ...
gi 300845606 253 KFR 255
Cdd:cd02026  139 AER 141
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 95-242 1.74e-08

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 54.01  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  95 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrRVELITTDGFLHPNQVL--KERglmKKKGF--PESYDMHRLVKFVSDL 170
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQSHLsfEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300845606 171 KSGVPnVTAPVYSHLIYDVIpdgDKTV-VQP-DILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEDL 242
Cdd:PRK05480  79 KAGKA-IEIPVYDYTEHTRS---KETIrVEPkDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 95-250 5.35e-06

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 47.53  E-value: 5.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  95 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRRVELITTDGFLHPNQVLKERGlMKKKGF----PESYDMH 161
Cdd:PLN02348  49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTVICLDDYHSLDRTG-RKEKGVtaldPRANNFD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 162 RLVKFVSDLKSGVPnVTAPVYSHLiyDVIPDGDKTVVQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPED 241
Cdd:PLN02348 128 LMYEQVKALKEGKA-VEKPIYNHV--TGLLDPPELIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLDISDD 194


                 ....*....
gi 300845606 242 LLQTWYINR 250
Cdd:PLN02348 195 VKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 81-241 2.24e-04

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 41.89  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606  81 AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRRVELITTDGFLHPNQVLKERGLMKKKGFPE-SYD 159
Cdd:PRK06696   9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300845606 160 MHRLVKFVsdLKSGVPN-----VTApVYSHLiyDVIPDGDKTVVQPD--ILILEGLnvlqsgmdYPHDPHhvfVSDFVDF 232
Cdd:PRK06696  86 YTALRRLL--LDPLGPNgdrqyRTA-SHDLK--TDIPVHNPPLLAAPnaVLIVDGT--------FLLRPE---LRDLWDY 149


                 ....*....
gi 300845606 233 SIYVDAPED 241
Cdd:PRK06696 150 KIFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 97-133 2.37e-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: 38.86  E-value: 2.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 300845606  97 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITT 133
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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