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Conserved domains on  [gi|567316250|ref|NP_001274509|]
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ribokinase isoform 2 [Homo sapiens]

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

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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 ...
 1-251 3.92e-118

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: 339.19  E-value: 3.92e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250    1 MTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAK 80
Cdd:TIGR02152  47 EVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   81 VMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:TIGR02152 127 IVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  161 GCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:TIGR02152 207 GVKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGA 282

                         250
                  ....*....|.
gi 567316250  241 QSSYPYKKDLP 251
Cdd:TIGR02152 283 QSSIPYLEEVE 293
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 1-251 3.92e-118

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: 339.19  E-value: 3.92e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250    1 MTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAK 80
Cdd:TIGR02152  47 EVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   81 VMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:TIGR02152 127 IVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  161 GCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:TIGR02152 207 GVKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGA 282

                         250
                  ....*....|.
gi 567316250  241 QSSYPYKKDLP 251
Cdd:TIGR02152 283 QSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 2-246 1.09e-102

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: 300.24  E-value: 1.09e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:cd01174   53 VAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPqFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRG 161
Cdd:cd01174  133 LLLQLEIPLETVLAALRAARRAGVTVILNPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 162 CQVVIITLGAEGCVVLSqtEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:cd01174  212 VKNVIVTLGAKGALLAS--GGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQ 287


                 ....*
gi 567316250 242 SSYPY 246
Cdd:cd01174  288 PSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
 2-251 3.67e-84

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 254.28  E-value: 3.67e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNE-GQNIIVIVAGANLLLNTEDLRAAANVI-SRA 79
Cdd:PTZ00292  69 VAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNIC 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  80 KVMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQ----FYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:PTZ00292 149 KYLICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASK 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 VLLKRGCQVVIITLGAEGCVvLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSV 235
Cdd:PTZ00292 229 ELQQLGVENVIITLGANGCL-IVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISV 305

                        250
                 ....*....|....*.
gi 567316250 236 QAAGTQSSYPYKKDLP 251
Cdd:PTZ00292 306 TRHGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 2-250 2.25e-61

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: 195.10  E-value: 2.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAAnvISRAKV 81
Cdd:COG0524   53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQL-----EITPATSLEALTMARRSGVKTLFNPAPAIADLDP------QFYTLSDVFCCNESEAEILTGLTvgsaaDA 150
Cdd:COG0524  131 LHLGGitlasEPPREALLAALEAARAAGVPVSLDPNYRPALWEParellrELLALVDILFPNEEEAELLTGET-----DP 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 151 GEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFI 230
Cdd:COG0524  206 EEAAAALLARGVKLVVVTLGAEGALLYTGGEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAA 281

                        250       260
                 ....*....|....*....|
gi 567316250 231 AAVSVQAAGTQSSYPYKKDL 250
Cdd:COG0524  282 AALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 2-242 2.64e-46

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 155.96  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250    2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:pfam00294  51 VAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   82 MV----CQLEITPATSLEALTMARRSG--VKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:pfam00294 131 LYisgsLPLGLPEATLEELIEAAKNGGtfDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  156 VLLKRGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEDMLNRSNFIAAVS 234
Cdd:pfam00294 211 KLLAKGIKTVIVTLGADGALVVEGDG-EVHVPAVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALV 286


                  ....*...
gi 567316250  235 VQAAGTQS 242
Cdd:pfam00294 287 VQKSGAQT 294
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 1-251 3.92e-118

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: 339.19  E-value: 3.92e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250    1 MTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAK 80
Cdd:TIGR02152  47 EVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   81 VMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:TIGR02152 127 IVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  161 GCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:TIGR02152 207 GVKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGA 282

                         250
                  ....*....|.
gi 567316250  241 QSSYPYKKDLP 251
Cdd:TIGR02152 283 QSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 2-246 1.09e-102

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: 300.24  E-value: 1.09e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:cd01174   53 VAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPqFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRG 161
Cdd:cd01174  133 LLLQLEIPLETVLAALRAARRAGVTVILNPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 162 CQVVIITLGAEGCVVLSqtEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:cd01174  212 VKNVIVTLGAKGALLAS--GGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQ 287


                 ....*
gi 567316250 242 SSYPY 246
Cdd:cd01174  288 PSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
 2-251 3.67e-84

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 254.28  E-value: 3.67e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNE-GQNIIVIVAGANLLLNTEDLRAAANVI-SRA 79
Cdd:PTZ00292  69 VAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNIC 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  80 KVMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQ----FYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:PTZ00292 149 KYLICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASK 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 VLLKRGCQVVIITLGAEGCVvLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSV 235
Cdd:PTZ00292 229 ELQQLGVENVIITLGANGCL-IVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISV 305

                        250
                 ....*....|....*.
gi 567316250 236 QAAGTQSSYPYKKDLP 251
Cdd:PTZ00292 306 TRHGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 2-250 2.25e-61

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: 195.10  E-value: 2.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAAnvISRAKV 81
Cdd:COG0524   53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQL-----EITPATSLEALTMARRSGVKTLFNPAPAIADLDP------QFYTLSDVFCCNESEAEILTGLTvgsaaDA 150
Cdd:COG0524  131 LHLGGitlasEPPREALLAALEAARAAGVPVSLDPNYRPALWEParellrELLALVDILFPNEEEAELLTGET-----DP 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 151 GEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFI 230
Cdd:COG0524  206 EEAAAALLARGVKLVVVTLGAEGALLYTGGEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAA 281

                        250       260
                 ....*....|....*....|
gi 567316250 231 AAVSVQAAGTQSSYPYKKDL 250
Cdd:COG0524  282 AALVVTRPGAQPALPTREEV 301
PRK11142 PRK11142
ribokinase; Provisional
 2-251 1.34e-58

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 188.15  E-value: 1.34e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:PRK11142  56 IAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQLEiTPATS-LEALTMARRSGVKTLFNPAPAiADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:PRK11142 136 LLMQLE-TPLETvLAAAKIAKQHGTKVILNPAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQK 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 161 GCQVVIITLGAEGcVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAfyLAYYPNLSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:PRK11142 214 GIETVLITLGSRG-VWLSENG-EGQRVPGFRVQAVDTIAAGDTFNGALV--TALLEGKPLPEAIRFAHAAAAIAVTRKGA 289

                        250
                 ....*....|.
gi 567316250 241 QSSYPYKKDLP 251
Cdd:PRK11142 290 QPSIPWREEID 300
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 2-242 2.64e-46

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 155.96  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250    2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:pfam00294  51 VAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   82 MV----CQLEITPATSLEALTMARRSG--VKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:pfam00294 131 LYisgsLPLGLPEATLEELIEAAKNGGtfDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  156 VLLKRGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEDMLNRSNFIAAVS 234
Cdd:pfam00294 211 KLLAKGIKTVIVTLGADGALVVEGDG-EVHVPAVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALV 286


                  ....*...
gi 567316250  235 VQAAGTQS 242
Cdd:pfam00294 287 VQKSGAQT 294
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 2-240 1.57e-30

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: 115.40  E-value: 1.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDIstEFTYQT-KDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAAnvISRAK 80
Cdd:cd01168   72 AAFIGRVGDDKLGDFLLKDLRAAGV--DTRYQVqPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAK 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  81 VMVC---QLEITPATSLEALTMARRSGVKTLFN-PAPAIAD-----LDPQFYTLSDVFCcNESEAEILTGLTVGSAAdag 151
Cdd:cd01168  148 YLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFIVQrfkeaLLELLPYVDILFG-NEEEAEALAEAETTDDL--- 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 152 EAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEK-VKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFI 230
Cdd:cd01168  224 EAALKLLALRCRIVVITQGAKGAVVVEGGEVY--PVPAIPvEKIVDTNGAGDAFAG--GFLYGLVQGEPLEECIRLGSYA 299

                        250
                 ....*....|
gi 567316250 231 AAVSVQAAGT 240
Cdd:cd01168  300 AAEVIQQLGP 309
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 2-239 8.35e-28

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: 107.66  E-value: 8.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIV--NNEGQNIIVIVAGANLLLNTEDLRAAAnvISRA 79
Cdd:cd01166   48 VALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIgaGGERRVLYYRAGSAASRLTPEDLDEAA--LAGA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  80 KvMVCQLEITPATS-------LEALTMARRSGVKTLF--NPAPAIADLD------PQFYTLSDVFCCNESEAEILTGLTV 144
Cdd:cd01166  126 D-HLHLSGITLALSesarealLEALEAAKARGVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDED 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 145 GSAAdagEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEDM 223
Cdd:cd01166  205 PTDA---AERALALALGVKAVVVKLGAEGALVYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLE---GWDLEEA 276

                        250
                 ....*....|....*.
gi 567316250 224 LNRSNFIAAVSVQAAG 239
Cdd:cd01166  277 LRFANAAAALVVTRPG 292
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 2-239 1.22e-27

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: 107.34  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAG--ANLLLNTEDLraaANVISRA 79
Cdd:cd01167   45 AAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADLLLDTELN---PDLLSEA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  80 K-VMVCQL----EITPATSLEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVFCCNESEAEILTGLTvg 145
Cdd:cd01167  122 DiLHFGSIalasEPSRSALLELLEAAKKAGVLISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGEE-- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 146 saaDAGEAALVLLKRGCQVVIITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLS-----L 220
Cdd:cd01167  200 ---DPEEIAALLLLFGLKLVLVTRGADGALLY--TKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedeL 274

                        250
                 ....*....|....*....
gi 567316250 221 EDMLNRSNFIAAVSVQAAG 239
Cdd:cd01167  275 AEALRFANAVGALTCTKAG 293
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 5-241 9.71e-27

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: 104.70  E-value: 9.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   5 VCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLnteDLRAAANVISRAKVmvc 84
Cdd:cd01942   56 VAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDEL---EPNDEADPDGLADI--- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  85 qLEITPATSLEALTMARRSGVKTL-FNPAPAIADLD----PQFYTLSDVFCCNESEAEILTGLTVGSAADageaalvlLK 159
Cdd:cd01942  130 -VHLSSGPGLIELARELAAGGITVsFDPGQELPRLSgeelEEILERADILFVNDYEAELLKERTGLSEAE--------LA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFvgALAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:cd01942  201 SGVRVVVVTLGPKGAIVFEDGE-EVEVPAVPAVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277


                 ..
gi 567316250 240 TQ 241
Cdd:cd01942  278 AQ 279
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 8-236 4.88e-23

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: 94.69  E-value: 4.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   8 VGKDSFGNDYIENLKQNDISTEFTyQTKDAATGTASIIVNNEGqNIIVIVAGANL--LLNTEDLRAAANVISRAKVMVCQ 85
Cdd:cd01941   58 VGDDSEGESILEESEKAGLNVRGI-VFEGRSTASYTAILDKDG-DLVVALADMDIyeLLTPDFLRKIREALKEAKPIVVD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  86 LEITPATSLEALTMARRSGVKTLFNPA-----PAIADLDPQFYTLSdvfcCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:cd01941  136 ANLPEEALEYLLALAAKHGVPVAFEPTsapklKKLFYLLHAIDLLT----PNRAELEALAGALIENNEDENKAAKILLLP 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567316250 161 GCQVVIITLGAEGcVVLSQTEP--EPKHIPTEKV-KAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSVQ 236
Cdd:cd01941  212 GIKNVIVTLGAKG-VLLSSREGgvETKLFPAPQPeTVVNVTGAGDAFVAGLVAGLLE--GMSLDDSLRFAQAAAALTLE 287
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 8-245 2.75e-22

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: 93.01  E-value: 2.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   8 VGKDSFGNDYIENLKQNDISTEFTYQtKDAATGTASIIVNnEGQNIIVIVAGANLLLNTED----LRAAANVISRAKVMV 83
Cdd:cd01172   62 VGDDEAGDLLRKLLEKEGIDTDGIVD-EGRPTTTKTRVIA-RNQQLLRVDREDDSPLSAEEeqrlIERIAERLPEADVVI 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  84 cqLE------ITPATSLEALTMARRSGVKTLFNPAPaiadLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVL 157
Cdd:cd01172  140 --LSdygkgvLTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 158 LKR-GCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQ 236
Cdd:cd01172  214 LELlNLEALLVTLGEEGMTLFERDG-EVQHIPALAKEVYDVTGAGDTVIATLALALA--AGADLEEAAFLANAAAGVVVG 290


                 ....*....
gi 567316250 237 AAGTQSSYP 245
Cdd:cd01172  291 KVGTAPVTP 299
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 2-246 1.20e-21

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: 91.20  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAG----ANLLLNTEDLRAAANVI- 76
Cdd:cd01945   53 ARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGGADAVLv 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  77 -SRAkvmvcqleitPATSLEALTMARRSGVktlfnpaPAIADLDPQF-------YTLSDVFCCNESEAEILTGLtvgsaa 148
Cdd:cd01945  133 dGRQ----------PEAALHLAQEARARGI-------PIPLDLDGGGlrvleelLPLADHAICSENFLRPNTGS------ 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 149 dAGEAALVLLK-RGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRS 227
Cdd:cd01945  190 -ADDEALELLAsLGIPFVAVTLGEAGCLWLERDG-ELFHVPAFPVEVVDTTGAGDVFHGAFAHALA--EGMPLREALRFA 265

                        250
                 ....*....|....*....
gi 567316250 228 NFIAAVSVQAAGTQSSYPY 246
Cdd:cd01945  266 SAAAALKCRGLGGRAGLPT 284
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 8-240 1.62e-21

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 91.41  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   8 VGKDSFGNDYIENLKQNDISTEFTYQTKDAATgTASIIVNNEGQNIIVIVAGANLLLNTED----LRAAANVISRAKVMV 83
Cdd:COG2870   78 VGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT-TTKTRVIAGGQQLLRLDFEDRFPLSAELearlLAALEAALPEVDAVI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  84 cqLE------ITPATSLEALTMARRSGVKTLFNPAPAiadlDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVL 157
Cdd:COG2870  157 --LSdygkgvLTPELIQALIALARAAGKPVLVDPKGR----DFSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAAAEL 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 158 LKR-GCQVVIITLGAEGCVVLSQTEPePKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSVQ 236
Cdd:COG2870  231 LERlGLEALLVTRGEEGMTLFDADGP-PHHLPAQAREVFDVTGAGDTVIATLALALAA--GASLEEAAELANLAAGIVVG 307


                 ....
gi 567316250 237 AAGT 240
Cdd:COG2870  308 KLGT 311
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 89-213 2.92e-20

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: 85.22  E-value: 2.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  89 TPATSLEALTMARRSGVKTLFNPAPAIADLDPQ----FYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQV 164
Cdd:cd00287   69 APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKV 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 567316250 165 VIITLGAEGCVVLSQTEPEpKHIPTEKVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd00287  149 VIVTLGEKGAIVATRGGTE-VHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 7-250 1.44e-19

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 85.76  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   7 KVGKDSFGNDYIENLKQNDISTEFTYQtkDAATGTASIIV--NNEGQN--IIVIVAGANLLLNTEDLR------------ 70
Cdd:PRK09434  50 RVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVdlDDQGERsfTFMVRPSADLFLQPQDLPpfrqgewlhlcs 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  71 -AAANVISRAkvmvcqleitpaTSLEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVfcCNESEAEiLT 140
Cdd:PRK09434 128 iALSAEPSRS------------TTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALADV--VKLSEEE-LC 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 141 GLTVGSAADAGEAALVLLkRGCQVVIITLGAEGcvVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLS- 219
Cdd:PRK09434 193 FLSGTSQLEDAIYALADR-YPIALLLVTLGAEG--VLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTd 269

                        250       260       270
                 ....*....|....*....|....*....|....
gi 567316250 220 ---LEDMLNRSNFIAAVSVQAAGTQSSYPYKKDL 250
Cdd:PRK09434 270 eaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
132-241 2.79e-19

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 84.80  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAfy 211
Cdd:COG1105  184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFL-- 259

                         90       100       110
                 ....*....|....*....|....*....|
gi 567316250 212 LAYYPNLSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:COG1105  260 AGLARGLDLEEALRLAVAAGAAAALSPGTG 289
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 70-239 2.45e-16

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 77.95  E-value: 2.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  70 RAAANVISRAKVMVCQL----EITPATSLEALTMARRSGVKTLFNPAP---AIADLDP-------QFYTLSDVFCCNESE 135
Cdd:PLN02341 216 AEAKMAIRQSKALFCNGyvfdELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPderraleHLLRMSDVLLLTSEE 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 136 AEILTGLtvGSAADAGEAalvLLKRGC--QVVIITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFylA 213
Cdd:PLN02341 296 AEALTGI--RNPILAGQE---LLRPGIrtKWVVVKMGSKGSILV--TRSSVSCAPAFKVNVVDTVGCGDSFAAAIAL--G 366

                        170       180
                 ....*....|....*....|....*.
gi 567316250 214 YYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PLN02341 367 YIHNLPLVNTLTLANAVGAATAMGCG 392
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 103-239 1.96e-15

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: 74.00  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 103 SGVKTLFNPAPAIADLDPQFytLSDV------FCCNESEAEILTGlTVGSAADAgeAALVLLKRGCQVVIITLGAEGCVV 176
Cdd:cd01944  155 AGTTLVFDPGPRISDIPDTI--LQALmakrpiWSCNREEAAIFAE-RGDPAAEA--SALRIYAKTAAPVVVRLGSNGAWI 229

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567316250 177 LSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:cd01944  230 RLPDG-NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLA--KGMSLADAVLLANAAAAIVVTRSG 289
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 132-241 8.82e-15

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: 72.18  E-value: 8.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAfy 211
Cdd:cd01164  184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFV-- 259

                         90       100       110
                 ....*....|....*....|....*....|
gi 567316250 212 LAYYPNLSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:cd01164  260 AGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
PLN02323 PLN02323
probable fructokinase
 5-222 3.80e-14

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 70.81  E-value: 3.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   5 VCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIV--AGANLLLNTEDLRAaaNVISRAKVM 82
Cdd:PLN02323  63 IGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADMLLRESELDL--DLIRKAKIF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  83 ---VCQLEITPATS--LEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVFCCNESEAEILTGltvgSAA 148
Cdd:PLN02323 141 hygSISLITEPCRSahLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGIMSIWDEADIIKVSDEEVEFLTG----GDD 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567316250 149 DAGEAALVLLKRGCQVVIITLGAEGCVVLSqtePEPK-HIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLsLED 222
Cdd:PLN02323 217 PDDDTVVKLWHPNLKLLLVTEGEEGCRYYT---KDFKgRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSL-LED 287
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 8-244 6.54e-13

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: 66.67  E-value: 6.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   8 VGKDSFGNDYIENLKQNDIstEFTYQTKDAATGTASIIVNNEGQNIIVIVAGanlllNTEDLRAAANVISRAKVMvcqle 87
Cdd:cd01947   59 LGRDEIGIQSLEELESGGD--KHTVAWRDKPTRKTLSFIDPNGERTITVPGE-----RLEDDLKWPILDEGDGVF----- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  88 ITPATSL-EALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTgltvgsaadageAALVLLKRGCQVVI 166
Cdd:cd01947  127 ITAAAVDkEAIRKCRETKLVILQVTPRVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLI 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567316250 167 ITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAvsvQAAGTQSSY 244
Cdd:cd01947  195 VTEGELGAILY--PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLK--GWSIEEALELGAQCGA---ICVSHFGPY 265
PTZ00247 PTZ00247
adenosine kinase; Provisional
 8-250 1.02e-12

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 66.59  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   8 VGKDSFGNDYIENLKQNDISTEFTYqTKDAATGTASIIVNNEGQNIIVIVAGANLL----LNTEDLRAAanvISRAKVMV 83
Cdd:PTZ00247  89 VGDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTCAVLVCGKERSLVANLGAANHLsaehMQSHAVQEA---IKTAQLYY 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  84 CQ---LEITPATSLEALTMARRSGVKTLFN-PAP-AIADLDPQFYTL---SDVFCCNESEAEiltglTVGSAADAGEAAL 155
Cdd:PTZ00247 165 LEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyVDILFGNEEEAK-----TFAKAMKWDTEDL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 V-LLKRGCQ----------VVIITLGAEGCVVLSQTE----PEPkhiPTEKVKAVDTTGAGDSFVGAlafYLAYYPN-LS 219
Cdd:PTZ00247 240 KeIAARIAMlpkysgtrprLVVFTQGPEPTLIATKDGvtsvPVP---PLDQEKIVDTNGAGDAFVGG---FLAQYANgKD 313

                        250       260       270
                 ....*....|....*....|....*....|.
gi 567316250 220 LEDMLNRSNFIAAVSVQAAGtqSSYPYKKDL 250
Cdd:PTZ00247 314 IDRCVEAGHYSAQVIIQHNG--CTYPEKPPF 342
PLN02548 PLN02548
adenosine kinase
 2-250 1.81e-11

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 63.20  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   2 TSMVCKVGKDSFGNDYIENLKQNDISTEFtYQTKDAATGTASIIVNNEGQNIIVIVAGANLLlNTEDLRAAAN--VISRA 79
Cdd:PLN02548  72 TSYMGCIGKDKFGEEMKKCATAAGVNVHY-YEDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENwaLVEKA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  80 KVMVCQ---LEITPATSLEALTMARRSGVKTLFN-PAPAIADL--DPQFYTLS--DVFCCNESEAEILTGLTVGSAADAG 151
Cdd:PLN02548 150 KFYYIAgffLTVSPESIMLVAEHAAANNKTFMMNlSAPFICEFfkDQLMEALPyvDFLFGNETEARTFAKVQGWETEDVE 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 152 EAALVL----LKRGCQ--VVIITLGAEGCVVL--SQTEPEPKhIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDM 223
Cdd:PLN02548 230 EIALKIsalpKASGTHkrTVVITQGADPTVVAedGKVKEFPV-IPLPKEKLVDTNGAGDAFVG--GFLSQLVQGKDIEEC 306

                        250       260
                 ....*....|....*....|....*..
gi 567316250 224 LNRSNFIAAVSVQAAGTqsSYPYKKDL 250
Cdd:PLN02548 307 VRAGNYAANVIIQRSGC--TYPEKPDF 331
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 127-223 6.50e-09

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


Pssm-ID: 238921 [Multi-domain]  Cd Length: 277  Bit Score: 55.16  E-value: 6.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 127 DVFCCNESEAEILTGltvgsAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTE----PEpkhIPTEKVkaVDTTGAGD 202
Cdd:cd01946  165 DVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGyfaaPA---YPLESV--FDPTGAGD 234

                         90       100
                 ....*....|....*....|.
gi 567316250 203 SFVGALAFYLAYYPNLSLEDM 223
Cdd:cd01946  235 TFAGGFIGYLASQKDTSEANM 255
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 132-222 9.20e-09

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 55.18  E-value: 9.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGltvGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTepEPKHIP-TEKVKAVDTTGAGDSFVGalAF 210
Cdd:PLN02379 239 NEDEARELLR---GEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGK--EVVRVPaIGETNAVDATGAGDLFAS--GF 311

                         90
                 ....*....|..
gi 567316250 211 YLAYYPNLSLED 222
Cdd:PLN02379 312 LYGLIKGLSLEE 323
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 4-241 1.29e-08

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 54.81  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   4 MVCKVGKDSFGNDYIENLKQNDIstEFTYQ-TKDAATGTASIIVNNEGQNIIVIVAGANLLLN-TEDLRAAanvISRAKV 81
Cdd:PLN02813 153 MAGSVGSDPLGDFYRTKLRRANV--HFLSQpVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNyDSCLASA---ISKSRV 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  82 MVCQ-----LEITPATSLEALTMARRSGVK---TLFNPApAIADLDPQFYTL----SDVFCCNESEAEILTGLtvgSAAD 149
Cdd:PLN02813 228 LVVEgylweLPQTIEAIAQACEEAHRAGALvavTASDVS-CIERHRDDFWDVmgnyADILFANSDEARALCGL---GSEE 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 150 AGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFV-GALAFYLAYYPNL-SLEDMLNRs 227
Cdd:PLN02813 304 SPESATRYLSHFCPLVSVTDGARGSYIGVKGEAV--YIPPSPCVPVDTCGAGDAYAaGILYGLLRGVSDLrGMGELAAR- 380

                        250
                 ....*....|....
gi 567316250 228 nfIAAVSVQAAGTQ 241
Cdd:PLN02813 381 --VAATVVGQQGTR 392
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 125-233 2.27e-07

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: 50.28  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT----LGAEGCVVLSQTEPEPKHIPTEKVKAVDT-TG 199
Cdd:cd01173  136 LADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelADDDRIEMLGSTATEAWLVQRPKIPFPAYfNG 215

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567316250 200 AGDSFVGALAFYLAYYPnlSLEDMLNRS-NFIAAV 233
Cdd:cd01173  216 TGDLFAALLLARLLKGK--SLAEALEKAlNFVHEV 248
PRK09850 PRK09850
pseudouridine kinase; Provisional
 4-209 2.71e-07

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 50.76  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250   4 MVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIvagaNLLLNTEDLRAA-----ANVISR 78
Cdd:PRK09850  59 LLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAI----NDMNISNAITAEylaqhREFIQR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  79 AKVMVCQLEITPATSLEALTMArrSGVKTLFNPAPA-----IADLDPQFYTLSDvfccNESEAEILTGLTVGSAADAGEA 153
Cdd:PRK09850 135 AKVIVADCNISEEALAWILDNA--ANVPVFVDPVSAwkcvkVRDRLNQIHTLKP----NRLEAETLSGIALSGREDVAKV 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 567316250 154 ALVLLKRGCQVVIITLGAEGcVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALA 209
Cdd:PRK09850 209 AAWFHQHGLNRLVLSMGGDG-VYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLA 263
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 132-213 4.66e-07

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: 49.65  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT---LGAEGCV-VLsQTEPEPKHIPTEKVKAVDTTGAGDSFVGA 207
Cdd:COG0351  133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghLPGDEAVdVL-YDGDGVREFSAPRIDTGNTHGTGCTLSSA 211


                 ....*.
gi 567316250 208 LAFYLA 213
Cdd:COG0351  212 IAALLA 217
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 132-234 8.19e-07

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


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 48.94  E-value: 8.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADageaalvLLKR-GCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALaF 210
Cdd:cd01937  160 KLSRVEAEVISTPTELAR-------LIKEtGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPTGAGDVFLAAF-L 229

                         90       100
                 ....*....|....*....|....
gi 567316250 211 YLAYYPNLSLEdmlnRSNFIAAVS 234
Cdd:cd01937  230 YSRLSGKDIKE----AAEFAAAAA 249
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 164-213 1.36e-06

MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 48.49  E-value: 1.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567316250 164 VVIITLGAEGCVVLSQTEPEPKHIP---TEKVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd01943  227 GVVLRCGKLGCYVGSADSGPELWLPayhTKSTKVVDPTGGGNSFLGGFAAGLA 279
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 145-213 2.10e-06

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: 47.73  E-value: 2.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567316250 145 GSAADAG-EAALVLLK----RGCQVVIITLGAEGCVVLS-----QTEPEPkhiptekVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd01940  166 FSASDLSdEEVKAKLKeavsRGAKLVIVTRGEDGAIAYDgavfySVAPRP-------VEVVDTLGAGDSFIAGFLLSLL 237
fruK PRK09513
1-phosphofructokinase; Provisional
 132-235 2.65e-06

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 47.38  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLS-----QTEPepkhiptEKVKAVDTTGAGDSFVG 206
Cdd:PRK09513 187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNasgewIAKP-------PACDVVSTVGAGDSMVG 259

                         90       100
                 ....*....|....*....|....*....
gi 567316250 207 ALAFYLAYypNLSLEDMLNRSNFIAAVSV 235
Cdd:PRK09513 260 GLIYGLLM--RESSEHTLRLATAVSALAV 286
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 132-223 3.91e-06

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 47.09  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRG-CQVVIITLGAEGCVVLS-----QTEPEPkhiptekVKAVDTTGAGDSFV 205
Cdd:PRK10294 187 NQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDsenciQVVPPP-------VKSQSTVGAGDSMV 259

                         90
                 ....*....|....*...
gi 567316250 206 GALAFYLAyyPNLSLEDM 223
Cdd:PRK10294 260 GAMTLKLA--ENASLEEM 275
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 135-213 6.18e-06

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: 45.94  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250  135 EAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT---LGAEGCVVLSQ--TEPEPKHIPTEKVKAVDTTGAGDSFVGALA 209
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAVVTDVlyDGGGFYTLEAPRIPTKNTHGTGCTLSAAIA 208


                  ....
gi 567316250  210 FYLA 213
Cdd:pfam08543 209 ANLA 212
PLN02978 PLN02978
pyridoxal kinase
 125-248 1.27e-05

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 45.50  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT-LGAEGCVVLSQTEPEPKHIPTEKVK-AVDT----- 197
Cdd:PLN02978 149 LATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITsIDIDGKLLLVGSHRKEKGARPEQFKiVIPKipayf 228

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567316250 198 TGAGDSFVGALAFYLAYYPnlsleDMLNRSNFIAAVSVQAAGTQSSYPYKK 248
Cdd:PLN02978 229 TGTGDLMAALLLGWSHKYP-----DNLDKAAELAVSSLQAVLRRTLADYKR 274
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 135-218 1.41e-05

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 45.12  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 135 EAEILTGLTVGSAADAG-EAALVLLKRGCQVVIIT-----LGAEGCVVL-SQTEPEpkHIPTEKVKAVDTTGAGDSFVGA 207
Cdd:PRK06427 143 EAEALTGLPIADTEDEMkAAARALHALGCKAVLIKgghllDGEESVDWLfDGEGEE--RFSAPRIPTKNTHGTGCTLSAA 220

                         90
                 ....*....|.
gi 567316250 208 LAFYLAYYPNL 218
Cdd:PRK06427 221 IAAELAKGASL 231
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
 160-239 1.42e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 45.57  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PLN02630 201 RQKCCVIVTNGKKGCRIYWKDGE--MRVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 113-233 2.45e-05

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: 44.37  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 113 PAIADLDPQFYTLSDVFCC--------------NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT-----LGAEG 173
Cdd:COG2240  112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvpldDTPAD 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567316250 174 CV-VLSQTEPEPKHIPTEKVkAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNR-SNFIAAV 233
Cdd:COG2240  192 KIgNLAVTADGAWLVETPLL-PFSPNGTGDLFAALLLAHLLR--GKSLEEALERaAAFVYEV 250
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 160-239 1.43e-04

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 42.03  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCvvLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PRK09813 183 RGAGVVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIA--GFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 125-168 6.51e-04

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 40.06  E-value: 6.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT 168
Cdd:PTZ00344 139 YADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
PRK05756 PRK05756
pyridoxal kinase PdxY;
112-168 8.50e-04

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 39.85  E-value: 8.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 567316250 112 APAIAD-LDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT 168
Cdd:PRK05756 124 APGVAEfLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 132-240 1.12e-03

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 39.81  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEiltgLTVGSAADagEAALVllKRGCQVV--------IITLGAEGCVVLSQTEPePKHIPTEKVKAVDTTGAGDS 203
Cdd:PRK11316 195 NLSEFE----AVVGKCKD--EAELV--EKGMKLIadydlsalLVTRSEQGMTLLQPGKA-PLHLPTQAREVYDVTGAGDT 265

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567316250 204 FVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:PRK11316 266 VISVLAAALA--AGNSLEEACALANAAAGVVVGKLGT 300
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 146-240 2.76e-03

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 38.16  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 146 SAADAGEAALVLLKRGCqVVIITLGAEGCVVLSqTEPEPKHIPTEK-VKAVDTTGAGDSFVGALAFYLAYYPNlSLEDML 224
Cdd:cd01939  197 SPEECLRGEGPRAKKAA-LLVCTWGDQGAGALG-PDGEYVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD-DLSEAL 273

                         90
                 ....*....|....*.
gi 567316250 225 NRSNFIAAVSVQAAGT 240
Cdd:cd01939  274 DFGNRVASQKCTGVGF 289
 
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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