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Conserved domains on  [gi|446272410|ref|WP_000350265|]
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MULTISPECIES: ribokinase [Enterobacteriaceae]

Protein Classification

ribokinase( domain architecture ID 10797757)

ribokinase catalyzes the formation of D-ribose 5-phosphate from ribose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
7-299 4.16e-136

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: 386.96  E-value: 4.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    7 GSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKV 86
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   87 PCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLNPAPA 166
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  167 LRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVD 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446272410  247 TSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
7-299 4.16e-136

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: 386.96  E-value: 4.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    7 GSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKV 86
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   87 PCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLNPAPA 166
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  167 LRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVD 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446272410  247 TSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
2-294 2.26e-132

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: 377.66  E-value: 2.26e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL 161
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 162 NPAPAlRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK 241
Cdd:cd01174  161 NPAPA-RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446272410 242 VNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 294
Cdd:cd01174  240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
2-299 4.53e-94

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 281.63  E-value: 4.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:PTZ00292  17 DVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDL-KKCKLIVLQLEVQLETVYHAIEFGKKNGIEV 159
Cdd:PTZ00292  97 FVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 160 LLNPAPALRELDMSYACKC----DFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE- 234
Cdd:PTZ00292 177 VFNPAPAPKLAEVEIIKPFlkyvSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEp 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272410 235 VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:PTZ00292 257 VHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
2-298 1.42e-82

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: 251.34  E-value: 1.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQL-----EVQLETVYHAIEFGKKNG 156
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 157 IEVLLNPA------PALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALWMT 230
Cdd:COG0524  159 VPVSLDPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272410 231 RDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQF 298
Cdd:COG0524  234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
2-269 7.16e-57

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 185.24  E-value: 7.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    2 DIAVIGSNMVDLITYTNQMPkeGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIV----LQLEVQLETVYHAIEFGKKNGI 157
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  158 E--VLLNPAPALRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 235
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 446272410  236 HVPAF-KVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLE 273
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
7-299 4.16e-136

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: 386.96  E-value: 4.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    7 GSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKV 86
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   87 PCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLNPAPA 166
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  167 LRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVD 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446272410  247 TSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
2-294 2.26e-132

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: 377.66  E-value: 2.26e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLL 161
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 162 NPAPAlRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK 241
Cdd:cd01174  161 NPAPA-RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446272410 242 VNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 294
Cdd:cd01174  240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
2-299 4.53e-94

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 281.63  E-value: 4.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:PTZ00292  17 DVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDL-KKCKLIVLQLEVQLETVYHAIEFGKKNGIEV 159
Cdd:PTZ00292  97 FVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 160 LLNPAPALRELDMSYACKC----DFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE- 234
Cdd:PTZ00292 177 VFNPAPAPKLAEVEIIKPFlkyvSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEp 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272410 235 VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFN 299
Cdd:PTZ00292 257 VHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
2-298 1.42e-82

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: 251.34  E-value: 1.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQL-----EVQLETVYHAIEFGKKNG 156
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 157 IEVLLNPA------PALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALWMT 230
Cdd:COG0524  159 VPVSLDPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272410 231 RDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQF 298
Cdd:COG0524  234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PRK11142 PRK11142
ribokinase; Provisional
3-303 8.15e-72

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 223.98  E-value: 8.15e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:PRK11142   5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGIEVLLN 162
Cdd:PRK11142  85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 163 PAPAlRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKV 242
Cdd:PRK11142 165 PAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRV 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446272410 243 NAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPSIEQFNEFLT 303
Cdd:PRK11142 244 QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
2-269 7.16e-57

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 185.24  E-value: 7.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    2 DIAVIGSNMVDLITYTNQMPkeGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   82 YVEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAEDLKKCKLIV----LQLEVQLETVYHAIEFGKKNGI 157
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  158 E--VLLNPAPALRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 235
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 446272410  236 HVPAF-KVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLE 273
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
2-269 1.98e-41

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: 145.03  E-value: 1.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLitytnqMPKEGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 80
Cdd:cd01166    1 DVVTIGEVMVDL------SPPGGGRLEqADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  81 TYVEKVPCTSSGVAPIFVNANSSNSILI-IKG-ANKFLSPEDIDRAAedLKKCKLIVL------QLEVQLETVYHAIEFG 152
Cdd:cd01166   75 SHVRVDPGRPTGLYFLEIGAGGERRVLYyRAGsAASRLTPEDLDEAA--LAGADHLHLsgitlaLSESAREALLEALEAA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 153 KKNGIEVL--LNPAPALR-ELDMSYAC-----KCDFFIPNETELEILTGMSVDTydhiRLAARSL-VDKGLNNIIVTMSE 223
Cdd:cd01166  153 KARGVTVSfdLNYRPKLWsAEEAREALeellpYVDIVLPSEEEAEALLGDEDPT----DAAERALaLALGVKAVVVKLGA 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446272410 224 KGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01166  229 EGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLE 274
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
2-269 1.18e-38

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: 137.44  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   2 DIAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:cd01942    1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPCTSSGVApiFVNANSSNSILII--KGANKFLSPEDIDRAAEDLKkckliVLQLEVQLETVYHAIEFgKKNGIEV 159
Cdd:cd01942   81 HVRVVDEDSTGVA--FILTDGDDNQIAYfyPGAMDELEPNDEADPDGLAD-----IVHLSSGPGLIELAREL-AAGGITV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 160 LLNPAPALRELDMSYA----CKCDFFIPNETELEILtgmsvdtydhIRLAARSL--VDKGLNNIIVTMSEKGALWMTRDQ 233
Cdd:cd01942  153 SFDPGQELPRLSGEELeeilERADILFVNDYEAELL----------KERTGLSEaeLASGVRVVVVTLGPKGAIVFEDGE 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446272410 234 EVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01942  223 EVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLE 259
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
6-294 8.30e-33

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: 122.40  E-value: 8.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   6 IGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDD-----IFADntirnLESWGINT 80
Cdd:cd01945    5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDaigrlILAE-----LAAEGVDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  81 TYVEKVPCTSSGVAPIFVNANSSNSILIIKGANKF----LSPEDIDRAAedlkkcklIVLQLEVQLETVYHAIEFGKKNG 156
Cdd:cd01945   80 SFIVVAPGARSPISSITDITGDRATISITAIDTQAapdsLPDAILGGAD--------AVLVDGRQPEAALHLAQEARARG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 157 IEVLLN----PAPALRELdmsyACKCDFFIPNETELEILTGMSVDtydhirLAARSLVDKGLNNIIVTMSEKGALWMTRD 232
Cdd:cd01945  152 IPIPLDldggGLRVLEEL----LPLADHAICSENFLRPNTGSADD------EALELLASLGIPFVAVTLGEAGCLWLERD 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446272410 233 QEV-HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVEAALKKAALFAAFSVTGKGTQSSYPS 294
Cdd:cd01945  222 GELfHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
3-256 5.65e-31

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: 117.74  E-value: 5.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITytNQMPKEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01167    2 VVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAeDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:cd01167   74 IQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPD-LLSEADIlhfgsIALASEPSRSALLELLEAAKKAGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 158 EVLLNP---------APALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDKGLNNIIVTMSEKGALW 228
Cdd:cd01167  153 LISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALL 227
                        250       260
                 ....*....|....*....|....*...
gi 446272410 229 MTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:cd01167  228 YTKGGVGEVPGIPVEVVDTTGAGDAFVA 255
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
1-269 2.12e-28

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: 111.17  E-value: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   1 MDIAVIGSNMVDLITYTN-----------------QMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDD 63
Cdd:cd01168    2 YDVLGLGNALVDILAQVDdafleklglkkgdmilaDMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  64 IFADNTIRNLESWGINTTYVEKvPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVL---QLEV 140
Cdd:cd01168   82 KLGDFLLKDLRAAGVDTRYQVQ-PDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAKYLYLegyLLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 141 QLETVYHAIEFGKKNGIEVLLN-PAP--------ALRELdmsyACKCDFFIPNETELEILTGMSVDtydHIRLAARSLVD 211
Cdd:cd01168  159 PPEAILLAAEHAKENGVKIALNlSAPfivqrfkeALLEL----LPYVDILFGNEEEAEALAEAETT---DDLEAALKLLA 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446272410 212 KGLNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01168  232 LRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEPLE 290
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
1-269 6.30e-28

5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]


Pssm-ID: 275175 [Multi-domain]  Cd Length: 309  Bit Score: 109.61  E-value: 6.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410    1 MDIAVIGSNMVDLitYTNQMpkeGETLE-APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGIN 79
Cdd:TIGR04382   2 LDVITIGRVGVDL--YPQQI---GVPLEdVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   80 TTYVEKVPCTSSGVApifvnanssnsILIIKGANKF-------------LSPEDIDraAEDLKKCKLIV-----LQLEVQ 141
Cdd:TIGR04382  77 TSHVVTDPGRRTSLV-----------FLEIKPPDEFpllfyrenaadlaLTPDDVD--EDYIASARALLvsgtaLSQEPS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  142 LETVYHAIEFGKKNGIEVLL----------NPAPALRELDMSYAcKCDFFIPNETELEILTGMSVDtydhiRLAARSLVD 211
Cdd:TIGR04382 144 REAVLKALEYARAAGVRVVLdidyrpylwkSPEEAGIYLRLVLP-LVDVIIGTREEFDIAGGEGDD-----EAAARALLD 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446272410  212 KGLNNIIVTMSEKGALWMTRDQE-VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:TIGR04382 218 AGVEILVVKRGPEGSLVYTGDGEgVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLE 276
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
3-269 5.31e-27

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: 107.01  E-value: 5.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAfKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 82
Cdd:cd01941    2 IVVIGAANIDLRGKVSGSLVPGTSNPGHV-KQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 vekvPCTSSGVA-PIFVNANSSNSILIIKGAN----KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:cd01941   80 ----GIVFEGRStASYTAILDKDGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 158 EVLLNPAPALRELDMSYACK-CDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV- 235
Cdd:cd01941  156 PVAFEPTSAPKLKKLFYLLHaIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVe 235
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446272410 236 --HVPAFKV-NAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01941  236 tkLFPAPQPeTVVNVTGAGDAFVAGLVAGLLEGMSLD 272
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
3-263 4.44e-26

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: 102.17  E-value: 4.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLnskvlmltkvgddifadntirnleswgintty 82
Cdd:cd00287    2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARL-------------------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 vekvpctssGVAPIFVNAnssnSILIIKGANkflspedidraaedlkkcklivLQLEVQLETVYHAIEFGKKngieVLLN 162
Cdd:cd00287   50 ---------GVSVTLVGA----DAVVISGLS----------------------PAPEAVLDALEEARRRGVP----VVLD 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 163 PAPALRELD----MSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRD-QEVHV 237
Cdd:cd00287   91 PGPRAVRLDgeelEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHV 170
                        250       260
                 ....*....|....*....|....*.
gi 446272410 238 PAFKVNAVDTSGAGDAFIGCFSHYYV 263
Cdd:cd00287  171 PAFPVKVVDTTGAGDAFLAALAAGLA 196
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
3-259 6.61e-25

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: 101.48  E-value: 6.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQmpkEGETLEAP--AFKIG-----CGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLES 75
Cdd:cd01172    2 VLVVGDVILDEYLYGDV---ERISPEAPvpVVKVEreeirLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  76 WGINTTYVekvpcTSSGVAPIFVNAnssnsilIIKGANK-----FLSPEDIDRAAED---------LKKCKLIVLQ---- 137
Cdd:cd01172   78 EGIDTDGI-----VDEGRPTTTKTR-------VIARNQQllrvdREDDSPLSAEEEQrlieriaerLPEADVVILSdygk 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 138 --LEVQLetVYHAIEFGKKNGIEVLLNPapalRELDMSYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDK-GL 214
Cdd:cd01172  146 gvLTPRV--IEALIAAARELGIPVLVDP----KGRDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNL 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446272410 215 NNIIVTMSEKGALWMTRDQEV-HVPAFKVNAVDTSGAGDAFIGCFS 259
Cdd:cd01172  220 EALLVTLGEEGMTLFERDGEVqHIPALAKEVYDVTGAGDTVIATLA 265
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
11-269 1.08e-22

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 95.59  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  11 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDdiFADNTIRN-LESWGINTTYVEkvpct 89
Cdd:COG1105   10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGG--FTGEFIEElLDEEGIPTDFVP----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  90 ssgVAP-----IFVNANSSNSILIIKGANKFLSPEDIDRAAEDL----KKCKLIVL----------QLEVQLetvyhaIE 150
Cdd:COG1105   82 ---IEGetrinIKIVDPSDGTETEINEPGPEISEEELEALLERLeellKEGDWVVLsgslppgvppDFYAEL------IR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 151 FGKKNGIEVLLN-PAPALRE-LDMS-YACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGAL 227
Cdd:COG1105  153 LARARGAKVVLDtSGEALKAaLEAGpDLIK-----PNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGAL 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446272410 228 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:COG1105  228 LVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLE 269
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
11-269 1.44e-19

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 86.86  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   11 VDLITYTNQMpKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLML----TKVGDDIFAdntirNLESWGINTTYVEKV 86
Cdd:TIGR03168  10 IDLTIEVDGL-TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATgflgGFTGEFIEA-----LLAEEGIKNDFVEVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   87 PCTSSGVApiFVNANSSNSILIIKGANkfLSPEDIDRAAED----LKKCKLIV----LQLEVQLETVYHAIEFGKKNGIE 158
Cdd:TIGR03168  84 GETRINVK--IKESSGEETELNEPGPE--ISEEELEQLLEKlrelLASGDIVVisgsLPPGVPPDFYAQLIAIARKKGAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  159 VLLNPA-PALRE-LDMS-YACKcdffiPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEV 235
Cdd:TIGR03168 160 VILDTSgEALREaLAAKpFLIK-----PNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGAL 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 446272410  236 HVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:TIGR03168 235 KATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLE 268
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
11-269 1.20e-18

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: 84.12  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  11 VDLITYTNQmPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDiFADNTIRNLESWGINTTYVEkvpctS 90
Cdd:cd01164   11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-----V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  91 SGVAPIFVN-ANSSNSILIIKGANKFLSPEDIDRAAEDLK----KCKLIVL----------QLEVQLetvyhaIEFGKKN 155
Cdd:cd01164   84 AGETRINVKiKEEDGTETEINEPGPEISEEELEALLEKLKallkKGDIVVLsgslppgvpaDFYAEL------VRLAREK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 156 GIEVLLNPA-PALRELdmsYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE 234
Cdd:cd01164  158 GARVILDTSgEALLAA---LAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGV 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446272410 235 VHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01164  235 YRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLE 269
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
3-260 4.73e-18

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: 82.08  E-value: 4.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGI-NTT 81
Cdd:cd01947    2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPctsSGVAPIFVNANSSNSILIIKGANKFLSPEDIdraaedLKKCKLIVLQLEVQLETVYHAIEFGKKngieVLL 161
Cdd:cd01947   82 AWRDKP---TRKTLSFIDPNGERTITVPGERLEDDLKWPI------LDEGDGVFITAAAVDKEAIRKCRETKL----VIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 162 NPAPALRELDMSYACK-CDFFIPNETELEILTGMSVDtydhirlaarslVDKGLNNIIVTMSEKGALWMTRDQEVHVPAF 240
Cdd:cd01947  149 QVTPRVRVDELNQALIpLDILIGSRLDPGELVVAEKI------------AGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
                        250       260
                 ....*....|....*....|
gi 446272410 241 KVNAVDTSGAGDAFIGCFSH 260
Cdd:cd01947  217 KAKVPDSTGAGDSFAAGFIY 236
PLN02323 PLN02323
probable fructokinase
28-256 1.86e-17

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 81.21  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  28 EAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSNSIL 107
Cdd:PLN02323  34 EAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 108 IIK--GANKFLSPEDIDraAEDLKKCKL-----IVLQLEVQLETVYHAIEFGKKNGIEVLLNP---------APALRELD 171
Cdd:PLN02323 114 FYRnpSADMLLRESELD--LDLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGI 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 172 MSYACKCDFFIPNETELEILTGmSVDTYDHirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAG 251
Cdd:PLN02323 192 MSIWDEADIIKVSDEEVEFLTG-GDDPDDD---TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAG 267

                 ....*
gi 446272410 252 DAFIG 256
Cdd:PLN02323 268 DAFVG 272
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
3-267 8.70e-17

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 78.82  E-value: 8.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLItytnqmP-KEGETLEAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTT 81
Cdd:PRK09434   5 VWVLGDAVVDLI------PeGENRYLKCP------GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  82 YVEKVPC--TSSGVAPIFVNANSSNSILIIKGANKFLSPEDID--RAAEDLKKCKlIVLQLEVQLETVYHAIEFGKKNGI 157
Cdd:PRK09434  73 YLRLDPAhrTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPpfRQGEWLHLCS-IALSAEPSRSTTFEAMRRIKAAGG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 158 EVLLNP---------APALRELDMSYACKCDFFIPNETELEILTGMsvdtyDHIRLAARSLVDK-GLNNIIVTMSEKGAL 227
Cdd:PRK09434 152 FVSFDPnlredlwqdEAELRECLRQALALADVVKLSEEELCFLSGT-----SQLEDAIYALADRyPIALLLVTLGAEGVL 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446272410 228 WMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:PRK09434 227 VHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGL 266
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
1-256 1.52e-16

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 79.49  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   1 MDIAVIGSNMVDLITYTNQMP-----KEGETLE-----APAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTI 70
Cdd:PLN02341  73 IDVATLGNLCVDIVLPVPELPppsreERKAYMEelaasPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  71 RNLESWGINTtyVEKVPCTSSGVApifVNANSSNSI--LIIKGANK--FLSPEDI-------------DRAAEDLKKCKL 133
Cdd:PLN02341 153 DVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwVLVDPLQRhgFCSRADFgpepafswisklsAEAKMAIRQSKA 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 134 IVLQ----LEVQLETVYHAIEFGKKNGIEVLLNPAP--------------ALRE-LDMSyackcDFFIPNETELEILTGM 194
Cdd:PLN02341 228 LFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgksllvgtpderrALEHlLRMS-----DVLLLTSEEAEALTGI 302
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446272410 195 SVDTydhirLAARSLVDKGLNN--IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PLN02341 303 RNPI-----LAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAA 361
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
3-267 5.32e-12

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: 64.68  E-value: 5.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMpkegetleAPafkigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01940    2 LAAIGDNVVDKYLHLGKM--------YP------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 VEKVPcTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIvlqlevqletvyHAIEFGKKNGIEVLL- 161
Cdd:cd01940   68 CRVKE-GENAVADVELVDGDRIFGLSNKGGVAREHPFEADLEY--LSQFDLV------------HTGIYSHEGHLEKALq 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 162 --NPAPALRELDMSY---ACKCDFFIPNeTELEILTGMSVDTyDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH 236
Cdd:cd01940  133 alVGAGALISFDFSDrwdDDYLQLVCPY-VDFAFFSASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYS 210
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446272410 237 VPAFKVNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:cd01940  211 VAPRPVEVVDTLGAGDSFIAGFLLSLLAGGT 241
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
3-258 2.32e-11

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: 63.21  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGkGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTy 82
Cdd:cd01944    2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 VEKVPCTSSGVAPIFVNANSSNSILIIKGANKFLSPEDIDR---AAEDL---------KKCKLIVLQLEVQLETvyhaie 150
Cdd:cd01944   80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATltvAPYDYvylsgytlaSENASKVILLEWLEAL------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 151 fgkKNGIEVLLNPAPALRELD---MSYACKCDFFIP-NETELEILTGmsvdTYD-HIRLAARSLVDKGLNNIIVTMSEKG 225
Cdd:cd01944  154 ---PAGTTLVFDPGPRISDIPdtiLQALMAKRPIWScNREEAAIFAE----RGDpAAEASALRIYAKTAAPVVVRLGSNG 226
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446272410 226 AlWM--TRDQEVHVPAFKVNAVDTSGAGDAFIGCF 258
Cdd:cd01944  227 A-WIrlPDGNTHIIPGFKVKAVDTIGAGDTHAGGM 260
fruK PRK09513
1-phosphofructokinase; Provisional
183-256 1.25e-09

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 58.17  E-value: 1.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446272410 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVG 259
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
177-269 4.64e-09

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: 56.31  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 177 KCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEVHVPAFKVNaVDTS 248
Cdd:COG2240  138 LADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtPADKiGNLAVTADGAWLVETPLLP-FSPN 216
                         90       100
                 ....*....|....*....|.
gi 446272410 249 GAGDAFIGCFSHYYVQSGDVE 269
Cdd:COG2240  217 GTGDLFAALLLAHLLRGKSLE 237
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
165-269 8.02e-09

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: 55.28  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 165 PALRELDMSYAckcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT------MSEKGALWMTRDQ--EVH 236
Cdd:cd01173  127 PVYRDLLVPLA---DIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEawLVQ 203
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446272410 237 VPAFKVNAvDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01173  204 RPKIPFPA-YFNGTGDLFAALLLARLLKGKSLA 235
PRK09850 PRK09850
pseudouridine kinase; Provisional
3-264 8.50e-09

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 55.76  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETlEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:PRK09850   7 VVIIGSANIDVAGYSHESLNYADS-NPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 VEKVP--CTSSGVAPIfvnANSSNSILIIKGAN--KFLSPEDIDRAAEDLKKCKLIVLQLEVQLETVYHAIEFGKKngIE 158
Cdd:PRK09850  86 CLIVPgeNTSSYLSLL---DNTGEMLVAINDMNisNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN--VP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 159 VLLNPAPALRELDM-SYACKCDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQEVH- 236
Cdd:PRK09850 161 VFVDPVSAWKCVKVrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGw 240
                        250       260
                 ....*....|....*....|....*...
gi 446272410 237 VPAFKVNAVDTSGAGDAFIGCFSHYYVQ 264
Cdd:PRK09850 241 SAPIKTNVINVTGAGDAMMAGLASCWVD 268
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
126-258 1.47e-08

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 55.18  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 126 EDLKKCKLIVLQLEVQ-LETVYHAIEFGKKNGI---------EVLLNPAPALRELDMSYacKCDFFIPNETE-LEILTGM 194
Cdd:PLN02379 173 EDFKGSKWLVLRYGFYnLEVIEAAIRLAKQEGLsvsldlasfEMVRNFRSPLLQLLESG--KIDLCFANEDEaRELLRGE 250
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272410 195 SVDTYDhirlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFK-VNAVDTSGAGDAFIGCF 258
Cdd:PLN02379 251 QESDPE----AALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGF 311
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
177-268 2.51e-08

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: 54.01  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 177 KCDFFIPNETELEILTGMsvdtYDHIRlAARSLVDKGLNNIIVTMSEKGALWMTRDQEVHVPAFKVNAV-DTSGAGDAFI 255
Cdd:cd01946  163 KVDVVIINDGEARQLTGA----ANLVK-AARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTFA 237
                         90
                 ....*....|...
gi 446272410 256 GCFSHYYVQSGDV 268
Cdd:cd01946  238 GGFIGYLASQKDT 250
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
1-258 3.24e-08

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 53.59  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   1 MDIAVIGSNMVDLitytnqMPKEGEtleapAFKigcGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINT 80
Cdd:PRK09813   1 KKLATIGDNCVDI------YPQLGK-----AFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  81 TYVEkvpcTSSGVAPI-FVNANSSNSIL--IIKG--ANKFLSPEDIDRAAE-DLkkcklivlqlevqletVYHAIeFGKK 154
Cdd:PRK09813  67 SHVH----TKHGVTAQtQVELHDNDRVFgdYTEGvmADFALSEEDYAWLAQyDI----------------VHAAI-WGHA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 155 NgiEVLlnpaPALRE----LDMSYACKCDffipneTELEILTGMSVD---TYDH-----IRLAARSLVDKGLNNIIVTMS 222
Cdd:PRK09813 126 E--DAF----PQLHAagklTAFDFSDKWD------SPLWQTLVPHLDyafASAPqedefLRLKMKAIVARGAGVVIVTLG 193
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446272410 223 EKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCF 258
Cdd:PRK09813 194 ENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGF 229
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
3-267 3.45e-07

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: 50.87  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITYTNQMPKEGETLEAPAFKIGCGGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTY 82
Cdd:cd01939    2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  83 V----EKVPCTSSgvapIFVNANSSNSILIIKGANKFLSPEDIDRAaeDLKKCKLIVLQ---LEVQLETVYHAIEFGKKN 155
Cdd:cd01939   82 CyrkdIDEPASSY----IIRSRAGGRTTIVNDNNLPEVTYDDFSKI--DLTQYGWIHFEgrnPDETLRMMQHIEEHNNRR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 156 GIEV------LLNPAPALRELdMSYackCDFFIPNETELEILTGMSVDTydhiRLAARSLVDKGLNNIIVTMSEKGALWM 229
Cdd:cd01939  156 PEIRitisveVEKPREELLEL-AAY---CDVVFVSKDWAQSRGYKSPEE----CLRGEGPRAKKAALLVCTWGDQGAGAL 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446272410 230 TRDQE-VHVPAFK-VNAVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:cd01939  228 GPDGEyVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD 267
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
217-269 4.31e-07

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 50.58  E-value: 4.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446272410 217 IIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVP 258
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
3-269 6.26e-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: 49.71  E-value: 6.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410   3 IAVIGSNMVDLITyTNQMPKegetleapafkIGCGGKGANQAVAAAKLNSKVLMLTKVGDD------IFADNTIRNLESW 76
Cdd:cd01937    2 IVIIGHVTIDEIV-TNGSGV-----------VKPGGPATYASLTLSRLGLTVKLVTKVGRDypdkwsDLFDNGIEVISLL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  77 GINTTYVEKVPCTSS--------GVAPIFVNANSSnsilIIKGANKFLSP--EDIDRaaEDLKKCKLIVLQLEVQLEtvy 146
Cdd:cd01937   70 STETTTFELNYTNEGrtrtllakCAAIPDTESPLS----TITAEIVILGPvpEEISP--SLFRKFAFISLDAQGFLR--- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 147 haiEFGKKNGIEVLLNPapalreldmsyacKCDFFIPNETELE-ILTGMSvdtydhirlAARSLVDKGLNNIIVTMSEKG 225
Cdd:cd01937  141 ---RANQEKLIKCVILK-------------LHDVLKLSRVEAEvISTPTE---------LARLIKETGVKEIIVTDGEEG 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446272410 226 ALWMTRDQEVHVPAFKVNAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01937  196 GYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
183-256 1.09e-06

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 49.40  E-value: 1.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272410 183 PNETELEILTGMSVDTYDHIRLAARSLVDKG-LNNIIVTMSEKGALWMTRDQEVHVPAFKVNAVDTSGAGDAFIG 256
Cdd:PRK10294 186 PNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVG 260
PTZ00247 PTZ00247
adenosine kinase; Provisional
19-269 1.84e-06

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 48.87  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  19 QMPKEGETLEAPAFKIGCGGKGANQA-VAAAKL---NSKVLMLTKVGDDIFADNTIRNLESWGINTT--YVEKVPctsSG 92
Cdd:PTZ00247  44 QLPIFEELESIPNVSYVPGGSALNTArVAQWMLqapKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLfeYTTKAP---TG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  93 VAPIFVNaNSSNSILIIKGANKFLSPEDIDRAA--EDLKKCKLIVLQ---LEVQLETVYHAIEFGKKNGIEVLLN-PAP- 165
Cdd:PTZ00247 121 TCAVLVC-GKERSLVANLGAANHLSAEHMQSHAvqEAIKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPf 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 166 -------ALRELdMSYackCDFFIPNETELEIL-TGMSVDTYDHIRLAARSLVDKGLNN-----IIVTMSEKGALWMTRD 232
Cdd:PTZ00247 200 isqfffeRLLQV-LPY---VDILFGNEEEAKTFaKAMKWDTEDLKEIAARIAMLPKYSGtrprlVVFTQGPEPTLIATKD 275
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446272410 233 QEVHVPAFKVNA---VDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PTZ00247 276 GVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKDID 315
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
183-254 1.54e-05

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 45.80  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVTmSEKGA--------LWMTRDQeVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK08176 158 PNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT-SAAGNeenqemqvVVVTADS-VNVISHPRVDTDLKGTGDLF 235
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
183-254 1.95e-05

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


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 45.03  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVtmseKGA---------LWMTRDQEVHVPAFKVNAVDTSGAGDA 253
Cdd:COG0351  132 PNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLV----KGGhlpgdeavdVLYDGDGVREFSAPRIDTGNTHGTGCT 207

                 .
gi 446272410 254 F 254
Cdd:COG0351  208 L 208
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
183-254 1.28e-04

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: 42.47  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446272410  183 PNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT---MSEKGA----LWMTRDQEVHVPAFKVNAVDTSGAGDAF 254
Cdd:pfam08543 125 PNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAvvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTL 203
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
25-254 1.94e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 42.49  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  25 ETLEAPAFKIGCGGKGANQAVAAAKLNSK--------VLMLTKVGDDIFADNTIRNLESWGINTTyVEKVPCTSSGVAPI 96
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFL-SQPVKDGTTGTVIV 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  97 FVNANSSNSILIIKGANKFLSPEDIDRAAedLKKCKLIVLQ-----LEVQLETVYHAIEFGKKNGIEVLLNPA------- 164
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASA--ISKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALVAVTASdvscier 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 165 --PALRELDMSYAckcDFFIPNETELEILTGMSVDTydhirlaARSLVDKGLNN----IIVTMSEKGALWMTRDQEVHVP 238
Cdd:PLN02813 271 hrDDFWDVMGNYA---DILFANSDEARALCGLGSEE-------SPESATRYLSHfcplVSVTDGARGSYIGVKGEAVYIP 340
                        250
                 ....*....|....*.
gi 446272410 239 AFKVNAVDTSGAGDAF 254
Cdd:PLN02813 341 PSPCVPVDTCGAGDAY 356
PRK05756 PRK05756
pyridoxal kinase PdxY;
164-269 2.62e-04

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 41.78  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 164 APALRELDMSYAckcDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT-------MSEK-GALWMTRDQEV 235
Cdd:PRK05756 128 AEFLRDRALPAA---DIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragyPADRfEMLLVTADGAW 204
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446272410 236 HVPAFKV-NAVDTSGAGDAFIGCFSHYYVQSGDVE 269
Cdd:PRK05756 205 HISRPLVdFMRQPVGVGDLTSALFLARLLQGGSLE 239
PRK09954 PRK09954
sugar kinase;
37-267 4.34e-04

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 41.46  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  37 GGKGANQAVAAAKLNSKVLMLTKVGDDIFADNTIRNLESWGINTTYVEKVPCTSSGVAPIFVNANSSnSILIIKGAN--K 114
Cdd:PRK09954  93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDE-TVLAINDTHilQ 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 115 FLSPEDIDrAAEDLKKCKLIVLqleVQLETVYHAIE--FGKKNGIEVLLNPAPALRELDM-SYACKCDFFIPNETELEIL 191
Cdd:PRK09954 172 QLTPQLLN-GSRDLIRHAGVVL---ADCNLTAEALEwvFTLADEIPVFVDTVSEFKAGKIkHWLAHIHTLKPTQPELEIL 247
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446272410 192 TGMSVDTYDHIRLAARSLVDKGLNNIIVTMSEKGALWMTRDQE---VHVPAFKVnaVDTSGAGDAFIGCFSHYYVQSGD 267
Cdd:PRK09954 248 WGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEqflLTAPAHTT--VDSFGADDGFMAGLVYSFLEGYS 324
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
164-220 1.06e-03

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 40.20  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446272410  164 APALRELDMSYACK-CDFFIPNETELEILTGMSVDTYDHIRLAARSLVDKGLNNIIVT 220
Cdd:TIGR00687 124 APDLLEVYREKAIPvADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT 181
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
148-254 1.97e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 38.89  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 148 AIEFGK-KNGIEVLLNPAPALREL-DMSYACKCDFFI----------PNETELEILTGMSVDTYDHIRLAARSLVDKGLN 215
Cdd:PRK12413  88 ALDFIKgHPGIPVVLDPVLVCKEThDVEVSELRQELIqffpyvtvitPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAK 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446272410 216 NIIVT----MSEKGALWMTRD-QEVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK12413 168 AVVIKggnrLSQKKAIDLFYDgKEFVILESPVLEKNNIGAGCTF 211
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
40-269 4.24e-03

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: 38.48  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410  40 GANQAVAAAKLNSKvLMLTKVGDDiFADNTIRNLESWGINTTYVEKVP-CTSSGVApIFVNAN-----SSNSILIIKGAN 113
Cdd:cd01943   35 GARLFLPPPLSRSI-SWIVDKGSD-FPKSVEDELESWGTGMVFRRDPGrLTTRGLN-IYDGNDrrffkYLTPKKRIDVSD 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 114 KFLSPEDIDRAA----EDLKKCKLIVLQLEVQLETvyhaIEFGKKNGIEVLLNPAPALRE----LDMSYAC-KCDFFIPN 184
Cdd:cd01943  112 DLNSTPLIRSSCihliCSPERCASIVDDIINLFKL----LKGNSPTRPKIVWEPLPDSCDpenlEDLLQALpRVDVFSPN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272410 185 ETELEILTGMSVDT---------YDHIRLAARSLvDKGLNNIIVTMSEKGALWMTRDQ--EVHVPAF-----KVnaVDTS 248
Cdd:cd01943  188 LEEAARLLGLPTSEpssdeekeaVLQALLFSGIL-QDPGGGVVLRCGKLGCYVGSADSgpELWLPAYhtkstKV--VDPT 264
                        250       260
                 ....*....|....*....|.
gi 446272410 249 GAGDAFIGCFSHYYVQSGDVE 269
Cdd:cd01943  265 GGGNSFLGGFAAGLALTKSID 285
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
183-254 9.31e-03

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 37.03  E-value: 9.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446272410 183 PNETELEILTGMSVDTYDHI-RLAARSLVDKGLNNIIVT---MSEKGA---LWMTRDQEVHVPAFKVNAVDTSGAGDAF 254
Cdd:PRK06427 139 PNLPEAEALTGLPIADTEDEmKAAARALHALGCKAVLIKgghLLDGEEsvdWLFDGEGEERFSAPRIPTKNTHGTGCTL 217
 
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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