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Conserved domains on  [gi|2314083693|ref|WP_262605388|]
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hydroxyethylthiazole kinase [Staphylococcus sp. IVB6240]

Protein Classification

hydroxyethylthiazole kinase( domain architecture ID 10793194)

hydroxyethylthiazole kinase catalyzes the phosphorylation of the hydroxylgroup of 4-methyl-5-beta-hydroxyethylthiazole

CATH:  3.40.1190.20
EC:  2.7.1.50
PubMed:  8382990|19348578
SCOP:  4000759

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
1-263 3.99e-119

hydroxyethylthiazole kinase; Validated


:

Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 341.01  E-value: 3.99e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   1 MSDYLTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEAN 80
Cdd:PRK09355    2 IAEALEKVREKNPLVHNITNDVVMNFTANGLLALGASPAMAHAPEEAEEMAKIAGALVINIGTLTEERIEAMLAAGKIAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  81 RQNVPIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDST-IEDVPVEAARKAHLKYGAAIV 159
Cdd:PRK09355   82 EAGKPVVLDPVGVGATSYRTEFALELLAEVKPAVIRGNASEIAALAGEAAETKGVDSTdGSADAVEIAKAAAKKYGTVVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 160 MTGKTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAgADLPGTFS 239
Cdd:PRK09355  162 VTGEVDYITDGERVVSVHNGHPLMTKVTGTGCLLSAVVAAFAAVEKDY-LEAAAAACAVYGIAGELAAERS-EKGPGSFQ 239
                         250       260
                  ....*....|....*....|....
gi 2314083693 240 VAFLDALNQTATVAFQQEIKKREV 263
Cdd:PRK09355  240 PAFLDALYQLTEEDIAERAKVEEV 263
 
Name Accession Description Interval E-value
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
1-263 3.99e-119

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 341.01  E-value: 3.99e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   1 MSDYLTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEAN 80
Cdd:PRK09355    2 IAEALEKVREKNPLVHNITNDVVMNFTANGLLALGASPAMAHAPEEAEEMAKIAGALVINIGTLTEERIEAMLAAGKIAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  81 RQNVPIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDST-IEDVPVEAARKAHLKYGAAIV 159
Cdd:PRK09355   82 EAGKPVVLDPVGVGATSYRTEFALELLAEVKPAVIRGNASEIAALAGEAAETKGVDSTdGSADAVEIAKAAAKKYGTVVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 160 MTGKTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAgADLPGTFS 239
Cdd:PRK09355  162 VTGEVDYITDGERVVSVHNGHPLMTKVTGTGCLLSAVVAAFAAVEKDY-LEAAAAACAVYGIAGELAAERS-EKGPGSFQ 239
                         250       260
                  ....*....|....*....|....
gi 2314083693 240 VAFLDALNQTATVAFQQEIKKREV 263
Cdd:PRK09355  240 PAFLDALYQLTEEDIAERAKVEEV 263
ThiM COG2145
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; ...
1-263 1.73e-114

Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; Hydroxyethylthiazole kinase, sugar kinase family is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441748 [Multi-domain]  Cd Length: 264  Bit Score: 329.37  E-value: 1.73e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   1 MSDYLTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEAN 80
Cdd:COG2145     4 IAEALEAVREKKPLVHCITNYVVMNDTANVLLAIGASPAMADAPEEVAEMAAIASALVINIGTLTPEQVEAMLLAGKAAN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  81 RQNVPIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDST-IEDVPVEAARKAHLKYGAAIV 159
Cdd:COG2145    84 EAGKPVVLDPVGVGATPYRTETARRLLKELKPTVIRGNASEIAALAGEGGGGKGVDSTdSSDDALEAAKALARKYGTVVA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 160 MTGKTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEvrAGADLPGTFS 239
Cdd:COG2145   164 VTGETDYVTDGERVYRVSNGHPLMTKVTGTGCMLGALIAAFLAVEEDP-LEAAVAALAVMGIAGELAA--EKAQGPGSFR 240
                         250       260
                  ....*....|....*....|....
gi 2314083693 240 VAFLDALNQTATVAFQQEIKKREV 263
Cdd:COG2145   241 VALLDALYLLTPEDLAERARIEEV 264
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
5-246 9.35e-109

4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 314.09  E-value: 9.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:cd01170     1 LEKLREKKPLVHCITNYVVMNFVANVLLAIGASPIMSDAPEEVEELAKIAGALVINIGTLTSEQIEAMLKAGKAANQLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTIEDV--PVEAARKAHLKYGAAIVMTG 162
Cdd:cd01170    81 PVVLDPVGVGATSFRTEVAKELLAEGQPTVIRGNASEIAALAGLTGLGKGVDSSSSDEedALELAKALARKYGAVVVVTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 163 KTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGAdlPGTFSVAF 242
Cdd:cd01170   161 EVDYITDGERVVVVKNGHPLLTKITGTGCLLGAVIAAFLAVGDDP-LEAAVSAVLVYGIAGELAAERAKG--PGSFRVAL 237

                  ....
gi 2314083693 243 LDAL 246
Cdd:cd01170   238 LDEL 241
HK pfam02110
Hydroxyethylthiazole kinase family;
5-248 1.63e-83

Hydroxyethylthiazole kinase family;


Pssm-ID: 396609 [Multi-domain]  Cd Length: 247  Bit Score: 250.37  E-value: 1.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:pfam02110   1 LSKLREFSPLVHHITNYVAQNFSANGLLALGASPIMSEAYEEVADLAKIAGALLINIGTLTNYRIEAMIAAVKSANELGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTI-EDVPVEAARKAHLKYGAAIVMTGK 163
Cdd:pfam02110  81 PVTLDPVGVGATELRRETALELLNEGGFAAIRGNAGEILSLAGETGLMKGVDSGSgATAAIRAAQRVAQKYGCVVVMTGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 164 TDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGADLpGTFSVAFL 243
Cdd:pfam02110 161 VDYVSDGTSVYVIHNGTELLGKITASGCLLGSVVAAFCAVPKDP-LFAAAEACLLYKVAGELAAARSEGSL-GSFIPELL 238

                  ....*
gi 2314083693 244 DALNQ 248
Cdd:pfam02110 239 DALSQ 243
thiM TIGR00694
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a ...
5-248 1.21e-81

hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria, and C-terminal domains of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC 2.5.1.3), ThiE. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 188074 [Multi-domain]  Cd Length: 249  Bit Score: 245.73  E-value: 1.21e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:TIGR00694   1 LKRVREHRPLVHNITNYVAMNFTANGLLALGASPVMSEAEEEVAELAKIAGALVINIGTLDKESIEAMIAAGKSANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTIEDV-PVEAARKAHLKYGAAIVMTGK 163
Cdd:TIGR00694  81 PVVLDPVGVGATKFRTETSLELLSEGRVAAIKGNAGEIAALAGEEGKMRGVDSGEGAEdAIRAAQQAAREYGTVVVVTGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 164 TDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGAdlPGTFSVAFL 243
Cdd:TIGR00694 161 VDYVSDGRRVYTIHNGTELLGKVTGSGCLLGSVVAAFCAVEEDP-LDAAISACLLYKIAGELAAERSKG--PGSFHVELL 237

                  ....*
gi 2314083693 244 DALNQ 248
Cdd:TIGR00694 238 DALSQ 242
 
Name Accession Description Interval E-value
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
1-263 3.99e-119

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 341.01  E-value: 3.99e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   1 MSDYLTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEAN 80
Cdd:PRK09355    2 IAEALEKVREKNPLVHNITNDVVMNFTANGLLALGASPAMAHAPEEAEEMAKIAGALVINIGTLTEERIEAMLAAGKIAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  81 RQNVPIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDST-IEDVPVEAARKAHLKYGAAIV 159
Cdd:PRK09355   82 EAGKPVVLDPVGVGATSYRTEFALELLAEVKPAVIRGNASEIAALAGEAAETKGVDSTdGSADAVEIAKAAAKKYGTVVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 160 MTGKTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAgADLPGTFS 239
Cdd:PRK09355  162 VTGEVDYITDGERVVSVHNGHPLMTKVTGTGCLLSAVVAAFAAVEKDY-LEAAAAACAVYGIAGELAAERS-EKGPGSFQ 239
                         250       260
                  ....*....|....*....|....
gi 2314083693 240 VAFLDALNQTATVAFQQEIKKREV 263
Cdd:PRK09355  240 PAFLDALYQLTEEDIAERAKVEEV 263
ThiM COG2145
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; ...
1-263 1.73e-114

Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; Hydroxyethylthiazole kinase, sugar kinase family is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441748 [Multi-domain]  Cd Length: 264  Bit Score: 329.37  E-value: 1.73e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   1 MSDYLTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEAN 80
Cdd:COG2145     4 IAEALEAVREKKPLVHCITNYVVMNDTANVLLAIGASPAMADAPEEVAEMAAIASALVINIGTLTPEQVEAMLLAGKAAN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  81 RQNVPIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDST-IEDVPVEAARKAHLKYGAAIV 159
Cdd:COG2145    84 EAGKPVVLDPVGVGATPYRTETARRLLKELKPTVIRGNASEIAALAGEGGGGKGVDSTdSSDDALEAAKALARKYGTVVA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 160 MTGKTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEvrAGADLPGTFS 239
Cdd:COG2145   164 VTGETDYVTDGERVYRVSNGHPLMTKVTGTGCMLGALIAAFLAVEEDP-LEAAVAALAVMGIAGELAA--EKAQGPGSFR 240
                         250       260
                  ....*....|....*....|....
gi 2314083693 240 VAFLDALNQTATVAFQQEIKKREV 263
Cdd:COG2145   241 VALLDALYLLTPEDLAERARIEEV 264
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
5-246 9.35e-109

4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 314.09  E-value: 9.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:cd01170     1 LEKLREKKPLVHCITNYVVMNFVANVLLAIGASPIMSDAPEEVEELAKIAGALVINIGTLTSEQIEAMLKAGKAANQLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTIEDV--PVEAARKAHLKYGAAIVMTG 162
Cdd:cd01170    81 PVVLDPVGVGATSFRTEVAKELLAEGQPTVIRGNASEIAALAGLTGLGKGVDSSSSDEedALELAKALARKYGAVVVVTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 163 KTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGAdlPGTFSVAF 242
Cdd:cd01170   161 EVDYITDGERVVVVKNGHPLLTKITGTGCLLGAVIAAFLAVGDDP-LEAAVSAVLVYGIAGELAAERAKG--PGSFRVAL 237

                  ....
gi 2314083693 243 LDAL 246
Cdd:cd01170   238 LDEL 241
HK pfam02110
Hydroxyethylthiazole kinase family;
5-248 1.63e-83

Hydroxyethylthiazole kinase family;


Pssm-ID: 396609 [Multi-domain]  Cd Length: 247  Bit Score: 250.37  E-value: 1.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:pfam02110   1 LSKLREFSPLVHHITNYVAQNFSANGLLALGASPIMSEAYEEVADLAKIAGALLINIGTLTNYRIEAMIAAVKSANELGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTI-EDVPVEAARKAHLKYGAAIVMTGK 163
Cdd:pfam02110  81 PVTLDPVGVGATELRRETALELLNEGGFAAIRGNAGEILSLAGETGLMKGVDSGSgATAAIRAAQRVAQKYGCVVVMTGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 164 TDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGADLpGTFSVAFL 243
Cdd:pfam02110 161 VDYVSDGTSVYVIHNGTELLGKITASGCLLGSVVAAFCAVPKDP-LFAAAEACLLYKVAGELAAARSEGSL-GSFIPELL 238

                  ....*
gi 2314083693 244 DALNQ 248
Cdd:pfam02110 239 DALSQ 243
thiM TIGR00694
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a ...
5-248 1.21e-81

hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria, and C-terminal domains of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC 2.5.1.3), ThiE. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 188074 [Multi-domain]  Cd Length: 249  Bit Score: 245.73  E-value: 1.21e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693   5 LTSVREAQPLVICYTNDVVKNFTANGLLSLDASPAMSEAPEEAADFFKVAQALLINIGTLTQQSGEDMLKIAKEANRQNV 84
Cdd:TIGR00694   1 LKRVREHRPLVHNITNYVAMNFTANGLLALGASPVMSEAEEEVAELAKIAGALVINIGTLDKESIEAMIAAGKSANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  85 PIVLDPVAVGASQFRKDFCRKFLEEIQVTVIKGNASEILSLVDASATMKGTDSTIEDV-PVEAARKAHLKYGAAIVMTGK 163
Cdd:TIGR00694  81 PVVLDPVGVGATKFRTETSLELLSEGRVAAIKGNAGEIAALAGEEGKMRGVDSGEGAEdAIRAAQQAAREYGTVVVVTGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 164 TDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKETHPsIEKLSEAVSYYTISAERAEVRAGAdlPGTFSVAFL 243
Cdd:TIGR00694 161 VDYVSDGRRVYTIHNGTELLGKVTGSGCLLGSVVAAFCAVEEDP-LDAAISACLLYKIAGELAAERSKG--PGSFHVELL 237

                  ....*
gi 2314083693 244 DALNQ 248
Cdd:TIGR00694 238 DALSQ 242
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
61-216 3.77e-08

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 52.87  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  61 IGTLTqqSGEDMLKIAKEANRQNVPIVLDPVAV---GASQFRKDFCRKFLEEI--QVTVIKGNASEilslvdASATMKGT 135
Cdd:pfam08543  66 TGMLG--SAEIIEAVAEKLDKYGVPVVLDPVMVaksGDSLLDDEAIEALKEELlpLATLITPNLPE------AEALTGRK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 136 DSTIEDVpVEAARKAHlKYGA-AIVMTG---------KTDIIVQDGRVFALDNGTPLLVKVTGTGCLLGAVIASFLMKEt 205
Cdd:pfam08543 138 IKTLEDM-KEAAKKLL-ALGAkAVLIKGghlegeeavVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKG- 214
                         170
                  ....*....|.
gi 2314083693 206 hpsiEKLSEAV 216
Cdd:pfam08543 215 ----LSLPEAV 221
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
26-201 2.17e-07

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 50.17  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  26 FTANGLLSLDASPAmseapeeaadfFKVAQALLINIGTLtqqSGEDMLKIAKEANRQNVPIVLDPVAVGASQFRKDFCRK 105
Cdd:cd00287    41 NVAVALARLGVSVT-----------LVGADAVVISGLSP---APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 106 FleeIQVTVIKGNASEILSLVdasatmkGTDSTIEDVPVEAARKAHLKYGAAIVMTG--KTDIIV-QDGRVFALDNGTPL 182
Cdd:cd00287   107 L---PGVDILTPNEEEAEALT-------GRRDLEVKEAAEAAALLLSKGPKVVIVTLgeKGAIVAtRGGTEVHVPAFPVK 176
                         170       180
                  ....*....|....*....|
gi 2314083693 183 LVKVTGTG-CLLGAVIASFL 201
Cdd:cd00287   177 VVDTTGAGdAFLAALAAGLA 196
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
69-241 2.24e-06

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 47.61  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  69 GEDMLKIAKEANRQNVPIVLDpvaVGASQFRKDFCRKFLEEIQVtVIKGNASEILSLVDASatmkgtDSTIEDVPVEAAR 148
Cdd:cd01171    90 DEEAAEILEKALAKDKPLVLD---ADALNLLADEPSLIKRYGPV-VLTPHPGEFARLLGAL------VEEIQADRLAAAR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 149 KAHLKYGAAIVMTGKTDIIVQ-DGRVFALDNGTPLLvKVTGTGCLLGAVIASFLMKEtHPSIEKLSEAVSYYTISAERAE 227
Cdd:cd01171   160 EAAAKLGATVVLKGAVTVIADpDGRVYVNPTGNPGL-ATGGSGDVLAGIIAALLAQG-LSPLEAAALAVYLHGLAGDLAA 237
                         170
                  ....*....|....
gi 2314083693 228 VRAGADLPGTFSVA 241
Cdd:cd01171   238 KKKGAGLTAADLVA 251
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
79-201 3.15e-05

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 44.26  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  79 ANRQNVPIVLDPVAV---GASQFRKDFCRKFLEEI--QVTVIKGNASEILSLVDASATmkgtdsTIEDVpVEAARKAHLK 153
Cdd:COG0351    89 ADYPLVPVVLDPVMVaksGDRLLDEDAVEALRELLlpLATVVTPNLPEAEALLGIEIT------TLDDM-REAAKALLEL 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2314083693 154 YGAAIVMTGK-------TDIIVQDGRVFALDnGTPLLVKVT-GTGCLLGAVIASFL 201
Cdd:COG0351   162 GAKAVLVKGGhlpgdeaVDVLYDGDGVREFS-APRIDTGNThGTGCTLSSAIAALL 216
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
135-201 2.51e-04

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 41.65  E-value: 2.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2314083693 135 TDSTIEDV---PVEAARKAHLKYGAAIVMTGKTDIIVQ-DGRVFALDNGTPLLvKVTGTGCLLGAVIASFL 201
Cdd:COG0063   161 LGCSVAEIqadRLEAAREAAKRYGAVVVLKGAGTVIAApDGRVYINPTGNPGL-ATAGSGDVLAGIIAGLL 230
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
26-207 5.66e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 37.35  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  26 FTANGLLSLDASPAMSEAPEEAADFFKVAQALL--------------INIGTLTQQsgeDMLKIAKE--ANRQNVPIVLD 89
Cdd:PRK12413   27 YTRNGLHGFVAVTCLTAMTEKGFEVFPVDKEIFqqqldslkdvpfsaIKIGLLPNV---EIAEQALDfiKGHPGIPVVLD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  90 PVAV-------GASQFRKDFcRKFLEeiQVTVIKGNaseilsLVDASATMKGTDSTIEDVpVEAARKAHlKYGA-AIVMT 161
Cdd:PRK12413  104 PVLVckethdvEVSELRQEL-IQFFP--YVTVITPN------LVEAELLSGKEIKTLEDM-KEAAKKLY-DLGAkAVVIK 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2314083693 162 GKTDI-------IVQDGRVFA-LDNgtPLLVKV-TGTGCLLGAVIASFLMKETHP 207
Cdd:PRK12413  173 GGNRLsqkkaidLFYDGKEFViLES--PVLEKNnIGAGCTFASSIASQLVKGKSP 225
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
39-201 9.99e-03

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 36.79  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693  39 AMSEAPEEAADFFKVAQALLINIGTLTQQS---GEDMLKIAKEANRQNVPIVLDPvavGASQFRKDFCRKFLEEI--QVT 113
Cdd:COG0524   111 ANAELTPEDLDEALLAGADILHLGGITLASeppREALLAALEAARAAGVPVSLDP---NYRPALWEPARELLRELlaLVD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314083693 114 VIKGNASEILSLVdasatmkGTDStiedvPVEAARKAHLKYGAAIVMT-GKtdiivqDGrVFALDNGT-----PLLVKV- 186
Cdd:COG0524   188 ILFPNEEEAELLT-------GETD-----PEEAAAALLARGVKLVVVTlGA------EG-ALLYTGGEvvhvpAFPVEVv 248
                         170
                  ....*....|....*...
gi 2314083693 187 --TGTG-CLLGAVIASFL 201
Cdd:COG0524   249 dtTGAGdAFAAGFLAGLL 266
 
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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