NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2452684595|ref|NP_001404660|]
View 

ribokinase isoform 4 [Mus musculus]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 23-211 7.65e-80

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).


The actual alignment was detected with superfamily member TIGR02152:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 293  Bit Score: 240.97  E-value: 7.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNE-------------------------------------------------------VKTLFNPAPA 127
Cdd:TIGR02152  81 KDTPTGTAFITVDDTgenrivvvaganaeltpedidaaealiaesdivllqleipletvleaakiakkhgVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 128 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 207
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 2452684595 208 VDTT 211
Cdd:TIGR02152 239 VDTT 242
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 23-211 7.65e-80

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 240.97  E-value: 7.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNE-------------------------------------------------------VKTLFNPAPA 127
Cdd:TIGR02152  81 KDTPTGTAFITVDDTgenrivvvaganaeltpedidaaealiaesdivllqleipletvleaakiakkhgVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 128 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 207
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 2452684595 208 VDTT 211
Cdd:TIGR02152 239 VDTT 242
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 23-211 1.35e-71

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 220.11  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01174     6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVN-------------------------------------------------------NEVKTLFNPAPA 127
Cdd:cd01174    86 VGAPTGTAVITVDesgenrivvvpgangeltpadvdaaleliaaadvlllqleipletvlaalraarrAGVTVILNPAPA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 128 MADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSqaEPVPKHIPTEAVKA 207
Cdd:cd01174   166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242


                  ....
gi 2452684595 208 VDTT 211
Cdd:cd01174   243 VDTT 246
PTZ00292 PTZ00292
ribokinase; Provisional
 23-211 7.16e-58

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 186.10  E-value: 7.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292   22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIV-----NNE----------------------------------------------------VKTLFNPA 125
Cdd:PTZ00292  102 ENSSTGLAMIFVdtktgNNEiviipgannaltpqmvdaqtdniqnickylicqneiplettldalkeakergCYTVFNPA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 126 PAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQaEPVPKHIP 201
Cdd:PTZ00292  182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-ENEPVHVP 260

                         250
                  ....*....|
gi 2452684595 202 TEAVKAVDTT 211
Cdd:PTZ00292  261 GKRVKAVDTT 270
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 23-211 2.58e-43

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: 147.72  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:COG0524     6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNE----------------------------------------------------------VKTLFNP 124
Cdd:COG0524    86 PGAPTGLAFILVDPDgertivfyrganaeltpedldeallagadilhlggitlaseppreallaaleaaraagVPVSLDP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 125 A------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpk 198
Cdd:COG0524   166 NyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV-- 238

                         250
                  ....*....|...
gi 2452684595 199 HIPTEAVKAVDTT 211
Cdd:COG0524   239 HVPAFPVEVVDTT 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 23-211 2.29e-34

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 124.38  E-value: 2.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPktGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:pfam00294   6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNEVKTLFN----------------------------------------------------------- 123
Cdd:pfam00294  84 EDTRTGTALIEVDGDGERTIVfnrgaaadltpeeleenedllenadllyisgslplglpeatleelieaaknggtfdpnl 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 124 --PAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHIP 201
Cdd:pfam00294 164 ldPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVPA 242

                         250
                  ....*....|
gi 2452684595 202 TEAVKAVDTT 211
Cdd:pfam00294 243 VPKVKVVDTT 252
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 23-211 7.65e-80

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 240.97  E-value: 7.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNE-------------------------------------------------------VKTLFNPAPA 127
Cdd:TIGR02152  81 KDTPTGTAFITVDDTgenrivvvaganaeltpedidaaealiaesdivllqleipletvleaakiakkhgVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 128 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 207
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 2452684595 208 VDTT 211
Cdd:TIGR02152 239 VDTT 242
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 23-211 1.35e-71

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 220.11  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01174     6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVN-------------------------------------------------------NEVKTLFNPAPA 127
Cdd:cd01174    86 VGAPTGTAVITVDesgenrivvvpgangeltpadvdaaleliaaadvlllqleipletvlaalraarrAGVTVILNPAPA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 128 MADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSqaEPVPKHIPTEAVKA 207
Cdd:cd01174   166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242


                  ....
gi 2452684595 208 VDTT 211
Cdd:cd01174   243 VDTT 246
PTZ00292 PTZ00292
ribokinase; Provisional
 23-211 7.16e-58

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 186.10  E-value: 7.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292   22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIV-----NNE----------------------------------------------------VKTLFNPA 125
Cdd:PTZ00292  102 ENSSTGLAMIFVdtktgNNEiviipgannaltpqmvdaqtdniqnickylicqneiplettldalkeakergCYTVFNPA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 126 PAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQaEPVPKHIP 201
Cdd:PTZ00292  182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-ENEPVHVP 260

                         250
                  ....*....|
gi 2452684595 202 TEAVKAVDTT 211
Cdd:PTZ00292  261 GKRVKAVDTT 270
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 23-211 2.58e-43

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: 147.72  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:COG0524     6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNE----------------------------------------------------------VKTLFNP 124
Cdd:COG0524    86 PGAPTGLAFILVDPDgertivfyrganaeltpedldeallagadilhlggitlaseppreallaaleaaraagVPVSLDP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 125 A------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpk 198
Cdd:COG0524   166 NyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV-- 238

                         250
                  ....*....|...
gi 2452684595 199 HIPTEAVKAVDTT 211
Cdd:COG0524   239 HVPAFPVEVVDTT 251
PRK11142 PRK11142
ribokinase; Provisional
 36-211 3.89e-40

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 139.62  E-value: 3.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  36 LPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVN 115
Cdd:PRK11142   22 FPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 116 NE-------------------------------------------------------VKTLFNPAPAMAdLDPQFYTLSS 140
Cdd:PRK11142  102 DEgensigihaganaaltpalveahrelianadallmqletpletvlaaakiakqhgTKVILNPAPARE-LPDELLALVD 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2452684595 141 IFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPvPKHIPTEAVKAVDTT 211
Cdd:PRK11142  181 IITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSENGE-GQRVPGFRVQAVDTI 249
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 23-211 2.29e-34

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 124.38  E-value: 2.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPktGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:pfam00294   6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVNNEVKTLFN----------------------------------------------------------- 123
Cdd:pfam00294  84 EDTRTGTALIEVDGDGERTIVfnrgaaadltpeeleenedllenadllyisgslplglpeatleelieaaknggtfdpnl 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 124 --PAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHIP 201
Cdd:pfam00294 164 ldPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVPA 242

                         250
                  ....*....|
gi 2452684595 202 TEAVKAVDTT 211
Cdd:pfam00294 243 VPKVKVVDTT 252
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 23-211 2.95e-17

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: 76.75  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIV----CKVGNDSFGNDYIENLkqnhistef 98
Cdd:cd00287     6 GSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVgadaVVISGLSPAPEAVLDA--------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  99 tyqTRDAATGTASIIVNNEVKTLFNPAPAMADLDPQFytlsSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVV 178
Cdd:cd00287    77 ---LEEARRRGVPVVLDPGPRAVRLDGEELEKLLPGV----DILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVV 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2452684595 179 VITLGASGCVILSQAEPVpKHIPTEAVKAVDTT 211
Cdd:cd00287   150 IVTLGEKGAIVATRGGTE-VHVPAFPVKVVDTT 181
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 23-211 1.14e-15

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 74.15  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVsltsrlPKTGETIHGHEFF-IGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQ 101
Cdd:cd01166     6 GEVMVDLS------PPGGGRLEQADSFrKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 102 TRDAATGT-------------------------------------ASIIV------------------------NNEVKT 120
Cdd:cd01166    80 DPGRPTGLyfleigaggerrvlyyragsaasrltpedldeaalagADHLHlsgitlalsesareallealeaakARGVTV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 121 LF--NPAPAMADLD------PQFYTLSSIFCCNESEAEILTGHAvSDPTTAGKAAMilLERGCQVVVITLGASGCVILSQ 192
Cdd:cd01166   160 SFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDE-DPTDAAERALA--LALGVKAVVVKLGAEGALVYTG 236

                         250
                  ....*....|....*....
gi 2452684595 193 AEPVpkHIPTEAVKAVDTT 211
Cdd:cd01166   237 GGRV--FVPAYPVEVVDTT 253
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 53-211 3.06e-15

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 73.03  E-value: 3.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTrDAATGTASIIVNNE--------------- 117
Cdd:cd01168    55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVTPDaertmctylgaanel 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 118 ---------VKT---------LFNPAPAMADLDPQF---------YTLSSIFC-------------------CNESEAEI 151
Cdd:cd01168   134 spddldwslLAKakylylegyLLTVPPEAILLAAEHakengvkiaLNLSAPFIvqrfkeallellpyvdilfGNEEEAEA 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2452684595 152 LTGHAVSDPTTAGKAamiLLERGCQVVVITLGASGCVILSQAE--PVPkhiPTEAVKAVDTT 211
Cdd:cd01168   214 LAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEvyPVP---AIPVEKIVDTN 269
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 23-211 7.21e-15

Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238917 [Multi-domain]  Cd Length: 279  Bit Score: 71.57  E-value: 7.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01942     6 GHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIV---NNEVkTLFNPAPA----MADLDPQFYTLSSIFCCNESEAEILT------GHAVS-DPTTA----- 163
Cdd:cd01942    86 DEDSTGVAFILTdgdDNQI-AYFYPGAMdelePNDEADPDGLADIVHLSSGPGLIELArelaagGITVSfDPGQElprls 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2452684595 164 --------GKA---------AMILLER----------GCQVVVITLGASGCVILSQAEPVpKHIPTEAVKAVDTT 211
Cdd:cd01942   165 geeleeilERAdilfvndyeAELLKERtglseaelasGVRVVVVTLGPKGAIVFEDGEEV-EVPAVPAVKVVDTT 238
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 53-211 1.87e-14

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 70.74  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTA------------SIIVNNEVKT 120
Cdd:cd01167    28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAfvtldadgersfEFYRGPAADL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 121 LFNPA---------------------PAMAD-----------------LDP------------------QFYTLSSIFCC 144
Cdd:cd01167   108 LLDTElnpdllseadilhfgsialasEPSRSallelleaakkagvlisFDPnlrpplwrdeeeareriaELLELADIVKL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2452684595 145 NESEAEILTGHavSDPTtagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTT 211
Cdd:cd01167   188 SDEELELLFGE--EDPE---EIAALLLLFGLKLVLVTRGADGALLYTKGGVG--EVPGIPVEVVDTT 247
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 23-211 1.48e-12

Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .


Pssm-ID: 238920 [Multi-domain]  Cd Length: 284  Bit Score: 65.39  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01945     6 GLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 103 RDAATGTASIIVN--NEVKTLFNPA------------------------------------------PAMADLDPQF--- 135
Cdd:cd01945    86 PGARSPISSITDItgDRATISITAIdtqaapdslpdailggadavlvdgrqpeaalhlaqearargiPIPLDLDGGGlrv 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 136 ----YTLSSIFCCNESEAEILTGhaVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHIPTEAVKAVDTT 211
Cdd:cd01945   166 leelLPLADHAICSENFLRPNTG--SADD----EALELLASLGIPFVAVTLGEAGCLWLERDGEL-FHVPAFPVEVVDTT 238
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 54-211 1.15e-10

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 59.88  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEF--------TYQTR---------------------- 103
Cdd:cd01172    40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGivdegrptTTKTRviarnqqllrvdreddsplsae 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 104 ----------DAATGTASIIVNNEVKTLFNP---------APAMADL---DPQ-----FYTLSSIFCCNESEAEILTGHA 156
Cdd:cd01172   120 eeqrlieriaERLPEADVVILSDYGKGVLTPrviealiaaARELGIPvlvDPKgrdysKYRGATLLTPNEKEAREALGDE 199

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2452684595 157 VSDPTTAGKAAMILLER-GCQVVVITLGASGCVILSQAEPvPKHIPTEAVKAVDTT 211
Cdd:cd01172   200 INDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGE-VQHIPALAKEVYDVT 254
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
145-213 7.30e-07

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 48.98  E-value: 7.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2452684595 145 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDtTVG 213
Cdd:COG1105   184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVS-TVG 249
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 28-211 3.54e-06

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 46.64  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  28 DLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHIstEFTYQTRDAAT 107
Cdd:cd01947    11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KHTVAWRDKPT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 108 G-TASIIVNNEVKTLFNP---------APAMADLDPQFYTLS-----SIFCCNESEAEIL--TGHAVS------------ 158
Cdd:cd01947    89 RkTLSFIDPNGERTITVPgerleddlkWPILDEGDGVFITAAavdkeAIRKCRETKLVILqvTPRVRVdelnqalipldi 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2452684595 159 ------DPTTAGKAAMILLeRGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKAVDTT 211
Cdd:cd01947   169 ligsrlDPGELVVAEKIAG-PFPRYLIVTEGELGAILYPGGR--YNHVPAKKAKVPDST 224
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 121-210 7.17e-06

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 45.88  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 121 LFNPAPAMADLDPQFYT----LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGcqvVVITLGASGCVILSQAEPv 196
Cdd:cd01944   160 VFDPGPRISDIPDTILQalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAP---VVVRLGSNGAWIRLPDGN- 235

                          90
                  ....*....|....
gi 2452684595 197 PKHIPTEAVKAVDT 210
Cdd:cd01944   236 THIIPGFKVKAVDT 249
PLN02323 PLN02323
probable fructokinase
 53-97 9.27e-06

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 45.77  E-value: 9.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2452684595  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTE 97
Cdd:PLN02323   43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNE 87
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 53-115 1.57e-05

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 44.93  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2452684595  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQtrDAATGTASIIVN 115
Cdd:PRK09434   28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVD 88
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 53-211 4.46e-05

Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.


Pssm-ID: 238915 [Multi-domain]  Cd Length: 264  Bit Score: 43.50  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTyQTRDAATGTASI-IVNNEVKTLFNPAPAMAD- 130
Cdd:cd01940    22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVeLVDGDRIFGLSNKGGVARe 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 131 --LDPQFYTLSS---IFC-CNESEAEIL--------TGHAVS----------------------------DPTTAGKAAM 168
Cdd:cd01940   101 hpFEADLEYLSQfdlVHTgIYSHEGHLEkalqalvgAGALISfdfsdrwdddylqlvcpyvdfaffsasdLSDEEVKAKL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2452684595 169 I-LLERGCQVVVITLGASGCVILSQAEPVPKHIptEAVKAVDTT 211
Cdd:cd01940   181 KeAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAP--RPVEVVDTL 222
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 145-225 8.85e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 42.86  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 145 NESEA-EILTGHAVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIP-TEAVKAVDTTVGFKL--SQFL 220
Cdd:PLN02379  239 NEDEArELLRGEQESDP----EAALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPaIGETNAVDATGAGDLfaSGFL 312


                  ....*
gi 2452684595 221 SHLIQ 225
Cdd:PLN02379  313 YGLIK 317
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 145-186 2.56e-04

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 40.98  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2452684595 145 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASG 186
Cdd:cd01164   184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADG 225
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 68-213 3.95e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 40.97  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  68 AKAAI-VCKVgndSFGNDYIenlkQNHISTEFTYQTRDAATGTASIIvnnevktLFNPAP---AMADLDP-------QFY 136
Cdd:PLN02341  218 AKMAIrQSKA---LFCNGYV----FDELSPSAIASAVDYAIDVGTAV-------FFDPGPrgkSLLVGTPderraleHLL 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2452684595 137 TLSSIFCCNESEAEILTGhaVSDPTTAGKAamiLLERGC--QVVVITLGASGCVILSQAEPVPKhiPTEAVKAVDtTVG 213
Cdd:PLN02341  284 RMSDVLLLTSEEAEALTG--IRNPILAGQE---LLRPGIrtKWVVVKMGSKGSILVTRSSVSCA--PAFKVNVVD-TVG 354
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 125-208 5.75e-04

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 39.99  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 125 APAMADLDPQFYTLSsifcCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV-PKHIPTE 203
Cdd:cd01941   167 LKKLFYLLHAIDLLT----PNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVeTKLFPAP 242


                  ....*
gi 2452684595 204 AVKAV 208
Cdd:cd01941   243 QPETV 247
PLN02543 PLN02543
pfkB-type carbohydrate kinase family protein
 47-110 5.84e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215299  Cd Length: 496  Bit Score: 40.28  E-value: 5.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2452684595  47 EFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTA 110
Cdd:PLN02543  166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACS 229
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 77-181 7.88e-04

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 39.68  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595  77 GNDSFGNDYI---ENLKQNHISTEFTY------QTRDAATGTASI---IVNNEVKTLFNPAPAMADlDPQFYT------- 137
Cdd:PTZ00344   54 GHRLDLNELItlmDGLRANNLLSDYTYvltgyiNSADILREVLATvkeIKELRPKLIFLCDPVMGD-DGKLYVkeevvda 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2452684595 138 ------LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 181
Cdd:PTZ00344  133 yrelipYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 145-181 8.31e-04

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: 39.64  E-value: 8.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2452684595 145 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 181
Cdd:COG0351   133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVK 169
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 126-181 1.09e-03

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 39.36  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2452684595 126 PAMADLDPQFYTLSSIFCC--------------NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 181
Cdd:COG2240   112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT 181
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 144-181 3.13e-03

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 37.56  E-value: 3.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2452684595 144 CNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 181
Cdd:cd01173   142 PNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT 179
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 148-181 3.39e-03

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: 37.46  E-value: 3.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2452684595 148 EAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 181
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH