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Conserved domains on  [gi|445945212|ref|WP_000023067|]
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MULTISPECIES: type I pantothenate kinase [Salmonella]

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 ...
 27-316 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: 594.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   27 VPMTLTEDEIAQLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  107 VLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPEG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTDPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 445945212  267 KEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRLRK 316
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 ...
 27-316 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: 594.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   27 VPMTLTEDEIAQLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  107 VLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPEG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTDPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 445945212  267 KEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 4-316 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: 531.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   4 KEQSLMTPYLQFDRSQWAALRDSVPMTLTEDEIAQLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 83
Cdd:COG1072    2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  84 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDL 163
Cdd:COG1072   82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 164 KSGVPNVTAPVYSHLIYDVIPEGDKTVAQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEELLQTWYINR 243
Cdd:COG1072  162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445945212 244 FLKFREGAFTDPDSYFHNYAKLSKEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRLRK 316
Cdd:COG1072  237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 1.57e-137

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: 388.21  E-value: 1.57e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 170 VTAPVYSHLIYDVIPEGDKTVAQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445945212 250 GAFTDPDSYFHNYAKLSKEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 89-251 1.25e-20

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 88.45  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  89 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 168
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 169 NVTAPVYSHLIYDVIPEGDKTVAQPDILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEELLQTWYINRFLKF- 247
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLAGg 186


                 ....*.
gi 445945212 248 --REGA 251
Cdd:PRK09270 187 lsPEAA 192
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 3.47e-13

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: 67.04  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNHVLKERGlMKKKGF----PESYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  162 DLKSGVpNVTAPVYSHLIYDVIPEGDKtVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEELLQTWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 445945212  242 NRFLKFR 248
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 ...
 27-316 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: 594.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   27 VPMTLTEDEIAQLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTAR 106
Cdd:TIGR00554   1 VPLKLSEDDIAPLKGFNEDLSLDEVAEIYLPLSRLINFYIDENLHRQAVLEQFLGRNGAKIPYIISIAGSVAVGKSTSAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  107 VLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPEG 186
Cdd:TIGR00554  81 ILQALLSHWPEERKVDLITTDGFLHPLNKLKEDGLLKKKGFPESYDMHKLIKFLADLKSGKPNVTAPIYSHLIYDIIPDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  187 DKTVAQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFREGAFTDPDSYFHNYAKLS 266
Cdd:TIGR00554 161 DDTVDKPDILILEGLNVLQSGMDKPHDPDHTFVSDFVDFSIYVDAEEDLLKEWYIKRFLKFREGAFNDPDSYFHHYAKLS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 445945212  267 KEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRLRK 316
Cdd:TIGR00554 241 KEEAIATAMKIWDEINGLNLKQNILPTRERANLILKKGANHAVEEIKLRK 290
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 4-316 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: 531.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   4 KEQSLMTPYLQFDRSQWAALRDSVPMTLTEDEIAQLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTN 83
Cdd:COG1072    2 SDTDELSPYVEFSREEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIYLPLSRLLNLYVAATQRLHRATSAFLGQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  84 GQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDL 163
Cdd:COG1072   82 DKKTPFIIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVLERRGLMDRKGFPESYDRRGLLRFLARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 164 KSGVPNVTAPVYSHLIYDVIPEGDKTVAQPDILILEGLNVLQSGMdyphdPHHVFVSDFVDFSIYVDAPEELLQTWYINR 243
Cdd:COG1072  162 KSGDPEVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEP-----NPWLFVSDFFDFSIYVDADEEDLREWYVER 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445945212 244 FLKFREGAFTDPDSYFHNYAKLSKEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRLRK 316
Cdd:COG1072  237 FLKLRETAFRDPDSYFHRYAGLSEEEARAWAEEIWREINLPNLAENILPTRSRADLILRKGADHSVERVRLRK 309
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 90-314 1.57e-137

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: 388.21  E-value: 1.57e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  90 IISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPN 169
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKELIERGLMDRKGFPESYDMEALLKFLKDIKSGKKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 170 VTAPVYSHLIYDVIPEGDKTVAQPDILILEGLNVLQSGMDYphdphHVFVSDFVDFSIYVDAPEELLQTWYINRFLKFRE 249
Cdd:cd02025   81 VKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNP-----RLFVSDFFDFSIYVDADEDDIEKWYIKRFLKLRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445945212 250 GAFTDPDSYFHNYAKLSKEEAVNTAASLWKEINWLNLKQNILPTRERASLIMTKSANHAVEQVRL 314
Cdd:cd02025  156 TAFSDPDSYFHRYAKMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLILEKGADHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 89-251 1.25e-20

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 88.45  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  89 YIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELiTTDGFLHPNHVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 168
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRAGDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 169 NVTAPVYSHLIYDVIPEGDKTVAQPDILILEGlNVLQSGmDYPHDPhhvfVSDFVDFSIYVDAPEELLQTWYINRFLKF- 247
Cdd:PRK09270 113 EVYWPVFDRSLEDPVADAIVVPPTARLVIVEG-NYLLLD-EEPWRR----LAGLFDFTIFLDAPAEVLRERLVARKLAGg 186


                 ....*.
gi 445945212 248 --REGA 251
Cdd:PRK09270 187 lsPEAA 192
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 88-300 4.07e-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: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  88 PYIISIAGSVAVGKSTTARVLQALLSRwpehRRVELITTDGFLHP--NHVLKERGlmkKKGF--PESYDMHRLVKFVSDL 163
Cdd:COG0572    7 PRIIGIAGPSGSGKTTFARRLAEQLGA----DKVVVISLDDYYKDreHLPLDERG---KPNFdhPEAFDLDLLNEHLEPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 164 KSGVPnVTAPVYSHLIYDVIPEgDKTVAQPDILILEGLNVLqsgmdypHDPhhvFVSDFVDFSIYVDAPEELLQTWYINR 243
Cdd:COG0572   80 KAGES-VELPVYDFATGTRSGE-TVKVEPADVIIVEGIHAL-------NDE---LLRDLLDLKIYVDADTDVRLIRRIVR 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445945212 244 flkfregaftdpDSYFHNYaklskeeavnTAASLWKEInWLNLK----QNILPTRERASLI 300
Cdd:COG0572  148 ------------DGEERGR----------TAESVIEQY-WATVRpgheQYIEPTKEYADIV 185
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 90-248 3.47e-13

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: 67.04  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212   90 IISIAGSVAVGKSTTARVLQALLSRWPEHRR----VELITTDGFLHPNHVLKERGlMKKKGF----PESYDMHRLVKFVS 161
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVgiegDSFHSTDRFYMDLHPEDRKR-AGNNGYsfdgPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  162 DLKSGVpNVTAPVYSHLIYDVIPEGDKtVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAPEELLQTWYI 241
Cdd:pfam00485  80 ELKEGG-SVDKPIYNHVTHERDPTPEL-IEGADVLVIEGL----------HALYDERVAQLLDLKIYVDPDIDLELARKI 147


                  ....*..
gi 445945212  242 NRFLKFR 248
Cdd:pfam00485 148 QRDMAER 154
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 90-235 9.61e-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: 9.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITTDGFLHPN-HVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVP 168
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLsHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445945212 169 nVTAPVYSHLIYDVIPEGdKTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEEL 235
Cdd:cd02023   77 -VEIPVYDFKTHSRLKET-VTVYPADVIILEGILAL-------YDKE---LRDLMDLKIFVDTDADV 131
PRK07429 PRK07429
phosphoribulokinase; Provisional
 88-243 2.52e-10

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 60.41  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  88 PYIISIAGSVAVGKSTTARVLQALLSrwPEhrRVELITTDGFlhpnHVL--KERglmKKKGF----PESYDMHRLVKFVS 161
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLG--EE--LVTVICTDDY----HSYdrKQR---KELGItaldPRANNLDIMYEHLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 162 DLKSGVPnVTAPVYSH---LIydVIPEgdkTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEELLQT 238
Cdd:PRK07429  77 ALKTGQP-ILKPIYNHetgTF--DPPE---YIEPNKIVVVEGLHPL-------YDER---VRELYDFKVYLDPPEEVKIA 140


                 ....*
gi 445945212 239 WYINR 243
Cdd:PRK07429 141 WKIKR 145
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 90-248 2.10e-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: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  90 IISIAGSVAVGKSTTARVLQALLSrwPEHrrVELITTDGFlhpnHVL--KERglmKKKGF----PESYDMHRLVKFVSDL 163
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFG--SDL--VTVICLDDY----HSLdrKGR---KETGItaldPRANNFDLMYEQLKAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 164 KSGVPnVTAPVYSHLIYdvIPEGDKTVAQPDILILEGLNVLqsgmdYPHDphhvfVSDFVDFSIYVDAPEELLQTWYINR 243
Cdd:cd02026   70 KEGQA-IEKPIYNHVTG--LIDPPELIKPTKIVVIEGLHPL-----YDER-----VRELLDFSVYLDISDEVKFAWKIQR 136


                 ....*
gi 445945212 244 FLKFR 248
Cdd:cd02026  137 DMAER 141
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 88-235 3.53e-08

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 52.85  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  88 PYIISIAGSVAVGKSTTARVLQALLsrwPEHrRVELITTDGFLHPN-HV-LKERglmKKKGF--PESYDMHRLVKFVSDL 163
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEEL---GDE-SIAVIPQDSYYKDQsHLsFEER---VKTNYdhPDAFDHDLLIEHLKAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445945212 164 KSGVPnVTAPVYSHLIYDVIPEgDKTVAQPDILILEGLNVLqsgmdypHDPHhvfVSDFVDFSIYVDAPEEL 235
Cdd:PRK05480  79 KAGKA-IEIPVYDYTEHTRSKE-TIRVEPKDVIILEGILLL-------EDER---LRDLMDIKIFVDTPLDI 138
PLN02348 PLN02348
phosphoribulokinase
 88-243 3.23e-07

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 51.38  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  88 PYIISIAGSVAVGKSTTARVLQALLS---------RWPEHRRVELITTDGFLHPNHVLKERGlMKKKGF----PESYDMH 154
Cdd:PLN02348  49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggNPDSNTLISDTTTVICLDDYHSLDRTG-RKEKGVtaldPRANNFD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 155 RLVKFVSDLKSGVPnVTAPVYSHL--IYDViPEgdkTVAQPDILILEGLnvlqsgmdypHDPHHVFVSDFVDFSIYVDAP 232
Cdd:PLN02348 128 LMYEQVKALKEGKA-VEKPIYNHVtgLLDP-PE---LIEPPKILVIEGL----------HPMYDERVRDLLDFSIYLDIS 192

                        170
                 ....*....|.
gi 445945212 233 EELLQTWYINR 243
Cdd:PLN02348 193 DDVKFAWKIQR 203
PRK06696 PRK06696
uridine kinase; Validated
 74-234 1.23e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 45.74  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212  74 AVLEQFLGTNGQRiPYIISIAGSVAVGKSTTARVLQALLSRWpeHRRVELITTDGFLHPNHVLKERGLMKKKGFPE-SYD 152
Cdd:PRK06696   9 ELAEHILTLNLTR-PLRVAIDGITASGKTTFADELAEEIKKR--GRPVIRASIDDFHNPRVIRYRRGRESAEGYYEdAYD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445945212 153 MHRLVKFVsdLKSGVPN-----VTApVYSHLiyDVIPEGDKTV-AQPD-ILILEGLnvlqsgmdYPHDPHhvfVSDFVDF 225
Cdd:PRK06696  86 YTALRRLL--LDPLGPNgdrqyRTA-SHDLK--TDIPVHNPPLlAAPNaVLIVDGT--------FLLRPE---LRDLWDY 149


                 ....*....
gi 445945212 226 SIYVDAPEE 234
Cdd:PRK06696 150 KIFLDTDFE 158
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 90-126 2.32e-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: 2.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 445945212  90 IISIAGSVAVGKSTTARVLQALLsrwpEHRRVELITT 126
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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