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Conserved domains on  [gi|2107956853|gb|UCD25950|]
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ribokinase [Gemmatimonadetes bacterium]

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 ...
 9-300 6.14e-110

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: 320.70  E-value: 6.14e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   9 GSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITD 88
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  89 SDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLNPAPA 168
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 169 QP-LGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVD 247
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2107956853 248 TTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIE 300
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 ...
 9-300 6.14e-110

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: 320.70  E-value: 6.14e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   9 GSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITD 88
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  89 SDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLNPAPA 168
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 169 QP-LGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVD 247
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2107956853 248 TTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIE 300
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
PRK11142 PRK11142
ribokinase; Provisional
 5-304 1.04e-107

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 315.27  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:PRK11142    5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLN 164
Cdd:PRK11142   85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 165 PAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVE 244
Cdd:PRK11142  165 PAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQ 244

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 245 AVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIEAVLA 304
Cdd:PRK11142  245 AVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 4-295 2.77e-107

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: 313.72  E-value: 2.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   4 GIVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTS 83
Cdd:cd01174     1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  84 HVITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVL 163
Cdd:cd01174    81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 164 NPAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEV 243
Cdd:cd01174   161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2107956853 244 EAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPS 295
Cdd:cd01174   241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-299 1.09e-69

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: 218.22  E-value: 1.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:COG0524     2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVlsARDAVTSADVLVTQL-----ETPLDTVRAAVELAAVNGV 159
Cdd:COG0524    82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDL--DEALLAGADILHLGGitlasEPPREALLAALEAARAAGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 160 RVVLNPA-------PAQPLGEEILQHVSVLTPNEIEAELLTGIAvssdgAALAAAKALNARGVEAVLITLGSRGALLFDS 232
Cdd:COG0524   160 PVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2107956853 233 DHAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEI 299
Cdd:COG0524   235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 5-269 5.69e-48

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 162.13  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPqpGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLV----TQLETPLDTVRAAVELAAVNG-- 158
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGtf 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 159 VRVVLNPA-PAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAEL 237
Cdd:pfam00294 160 DPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVH 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2107956853 238 IPSF-EVEAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:pfam00294 240 VPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSL 272
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 9-300 6.14e-110

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: 320.70  E-value: 6.14e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   9 GSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITD 88
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  89 SDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLNPAPA 168
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 169 QP-LGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVD 247
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2107956853 248 TTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIE 300
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
PRK11142 PRK11142
ribokinase; Provisional
 5-304 1.04e-107

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 315.27  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:PRK11142    5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLN 164
Cdd:PRK11142   85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 165 PAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVE 244
Cdd:PRK11142  165 PAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQ 244

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 245 AVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIEAVLA 304
Cdd:PRK11142  245 AVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 4-295 2.77e-107

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: 313.72  E-value: 2.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   4 GIVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTS 83
Cdd:cd01174     1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  84 HVITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVL 163
Cdd:cd01174    81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 164 NPAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEV 243
Cdd:cd01174   161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2107956853 244 EAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPS 295
Cdd:cd01174   241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
 1-303 5.61e-74

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 230.01  E-value: 5.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   1 MGSGIVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGI 80
Cdd:PTZ00292   14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  81 DTSHVITDSDAPSGVALIFVDQQ-GENSIAVASGANARLTPDDVLSARDAVTS-ADVLVTQLETPLDTVRAAVELAAVNG 158
Cdd:PTZ00292   94 NTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 159 VRVVLNPAPAQPLGE-----EILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSD 233
Cdd:PTZ00292  174 CYTVFNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKE 253

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2107956853 234 HAEL-IPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEIEAVL 303
Cdd:PTZ00292  254 NEPVhVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPADV 324
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-299 1.09e-69

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: 218.22  E-value: 1.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:COG0524     2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVlsARDAVTSADVLVTQL-----ETPLDTVRAAVELAAVNGV 159
Cdd:COG0524    82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDL--DEALLAGADILHLGGitlasEPPREALLAALEAARAAGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 160 RVVLNPA-------PAQPLGEEILQHVSVLTPNEIEAELLTGIAvssdgAALAAAKALNARGVEAVLITLGSRGALLFDS 232
Cdd:COG0524   160 PVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2107956853 233 DHAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQPSAPSREEI 299
Cdd:COG0524   235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 5-269 5.69e-48

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 162.13  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPqpGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLV----TQLETPLDTVRAAVELAAVNG-- 158
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYisgsLPLGLPEATLEELIEAAKNGGtf 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 159 VRVVLNPA-PAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAEL 237
Cdd:pfam00294 160 DPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVH 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2107956853 238 IPSF-EVEAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:pfam00294 240 VPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSL 272
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 23-269 4.13e-34

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: 125.77  E-value: 4.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  23 PQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDSDAPSGVALIFVDQ 102
Cdd:cd01166    15 PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIGA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 103 QGENSIA--VASGANARLTPDDVlsARDAVTSADVLVT------QLETPLDTVRAAVELAAVNGVRVVL---------NP 165
Cdd:cd01166    95 GGERRVLyyRAGSAASRLTPEDL--DEAALAGADHLHLsgitlaLSESAREALLEALEAAKARGVTVSFdlnyrpklwSA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 166 APAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDgaaLAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEA 245
Cdd:cd01166   173 EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTD---AAERALALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEV 249

                         250       260
                  ....*....|....*....|....
gi 2107956853 246 VDTTAAGDVFNGALAVALSERSSL 269
Cdd:cd01166   250 VDTTGAGDAFAAGFLAGLLEGWDL 273
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 5-290 5.40e-32

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: 120.11  E-value: 5.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:cd01942     2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLsarDAVTSADVLVTQLETPLdtVRAAVELAAvNGVRVVLN 164
Cdd:cd01942    82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEA---DPDGLADIVHLSSGPGL--IELARELAA-GGITVSFD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 165 PAPAQPLG-----EEILQHVSVLTPNEIEAELLTGIAVSSDgaalaaakALNARGVEAVLITLGSRGALLFDSDHAELIP 239
Cdd:cd01942   156 PGQELPRLsgeelEEILERADILFVNDYEAELLKERTGLSE--------AELASGVRVVVVTLGPKGAIVFEDGEEVEVP 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2107956853 240 SF-EVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAQ 290
Cdd:cd01942   228 AVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 5-269 4.76e-28

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: 109.65  E-value: 4.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIiklaripqPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:cd01167     2 VVCFGEALIDFI--------PEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSArDAVTSADVLVT----QLETPL-DTVRAAVELAAVNGV 159
Cdd:cd01167    74 IQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNP-DLLSEADILHFgsiaLASEPSrSALLELLEAAKKAGV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 160 RVVL----------NPAPAQPLGEEILQHVSVLTPNEIEAELLTGIavssdGAALAAAKALNARGVEAVLITLGSRGALL 229
Cdd:cd01167   153 LISFdpnlrpplwrDEEEARERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALL 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2107956853 230 FDSDHAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:cd01167   228 YTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLL 267
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 5-265 3.73e-25

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: 102.01  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGeTVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTsH 84
Cdd:cd01941     2 IVVIGAANIDLRGKVSGSLVPG-TSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVAS-GANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVL 163
Cdd:cd01941    80 GIVFEGRSTASYTAILDKDGDLVVALADmDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 164 NPAPA---QPLgEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSD----HAE 236
Cdd:cd01941   160 EPTSApklKKL-FYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREggveTKL 238

                         250       260
                  ....*....|....*....|....*....
gi 2107956853 237 LIPSFEVEAVDTTAAGDVFNGALAVALSE 265
Cdd:cd01941   239 FPAPQPETVVNVTGAGDAFVAGLVAGLLE 267
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 8-265 1.54e-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: 91.97  E-value: 1.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   8 VGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVIT 87
Cdd:cd01945     5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  88 DSDAPSGVALIF---VDQQGENSIAVASGANARLTPDDVLSARDAVTsadVLVTQLETPLDTVRAAveLAAVNGVRVVLN 164
Cdd:cd01945    85 APGARSPISSITditGDRATISITAIDTQAAPDSLPDAILGGADAVL---VDGRQPEAALHLAQEA--RARGIPIPLDLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 165 PAPAQPLgEEILQHVSVLTPNEIEAELLTGIAvssdgaALAAAKALNARGVEAVLITLGSRGALLFDSDHA-ELIPSFEV 243
Cdd:cd01945   160 GGGLRVL-EELLPLADHAICSENFLRPNTGSA------DDEALELLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPV 232

                         250       260
                  ....*....|....*....|..
gi 2107956853 244 EAVDTTAAGDVFNGALAVALSE 265
Cdd:cd01945   233 EVVDTTGAGDVFHGAFAHALAE 254
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 14-269 4.86e-21

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: 91.14  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  14 DMIikLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTsHVITDSDAPS 93
Cdd:cd01168    32 DMI--LADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  94 GVALIFVDQQGENSIAVASGANARLTPDDVLSArdAVTSADVLVT---QLETPLDTVRAAVELAAVNGVRVVLN---PAP 167
Cdd:cd01168   109 GTCAVLVTPDAERTMCTYLGAANELSPDDLDWS--LLAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsaPFI 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 168 AQPLGE---EILQHVSVLTPNEIEAELLTGIAVSSDgaaLAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSF-EV 243
Cdd:cd01168   187 VQRFKEallELLPYVDILFGNEEEAEALAEAETTDD---LEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIpVE 263

                         250       260
                  ....*....|....*....|....*.
gi 2107956853 244 EAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:cd01168   264 KIVDTNGAGDAFAGGFLYGLVQGEPL 289
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 124-263 5.97e-19

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: 82.91  E-value: 5.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 124 LSARDAVTSADVLVTQLETP-LDTVRAAVELAAVNGVRVVLNPAPAQ-----PLGEEILQHVSVLTPNEIEAELLTGIAV 197
Cdd:cd00287    49 LGVSVTLVGADAVVISGLSPaPEAVLDALEEARRRGVPVVLDPGPRAvrldgEELEKLLPGVDILTPNEEEAEALTGRRD 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2107956853 198 SSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAEL-IPSFEVEAVDTTAAGDVFNGALAVAL 263
Cdd:cd00287   129 LEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVhVPAFPVKVVDTTGAGDAFLAALAAGL 195
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 53-301 1.72e-17

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 81.01  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  53 GGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDSDAP---------SGVALIFVDQqgENSIAVASGANARLtpddV 123
Cdd:COG2870    69 GAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPtttktrviaGGQQLLRLDF--EDRFPLSAELEARL----L 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 124 LSARDAVTSADVLVtqLE-------TPLDtVRAAVELAAVNGVRVVLNPAPAQPlgeEILQHVSVLTPNEIEAELLTGIA 196
Cdd:COG2870   143 AALEAALPEVDAVI--LSdygkgvlTPEL-IQALIALARAAGKPVLVDPKGRDF---SRYRGATLLTPNLKEAEAAVGIP 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 197 VSSDGAALAAAKALNAR-GVEAVLITLGSRGALLFDSDHAEL-IPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAAR 274
Cdd:COG2870   217 IADEEELVAAAAELLERlGLEALLVTRGEEGMTLFDADGPPHhLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAE 296

                         250       260
                  ....*....|....*....|....*..
gi 2107956853 275 FANAAAALAVTKLGAqpSAPSREEIEA 301
Cdd:COG2870   297 LANLAAGIVVGKLGT--ATVSPEELLA 321
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 5-259 1.46e-16

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: 77.84  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIdtSH 84
Cdd:cd01947     2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAV--TSADVLVTqletpldtvraAVELAAVNGVrVV 162
Cdd:cd01947    80 TVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGDGVfiTAAAVDKE-----------AIRKCRETKL-VI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 163 LNPAPAQPLGE--EILQHVSVLTPNEIEAELLTgiavssdgaalaAAKALNARGVEAVLITLGSRGALLFDSDHAELIPS 240
Cdd:cd01947   148 LQVTPRVRVDElnQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPA 215

                         250
                  ....*....|....*....
gi 2107956853 241 FEVEAVDTTAAGDVFNGAL 259
Cdd:cd01947   216 KKAKVPDSTGAGDSFAAGF 234
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 53-294 3.09e-15

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: 74.52  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  53 GGKVTFVARVGDDVFGQQAVEGFVADGIDTsHVITDSDAP---------SGVALIFVDQQGENSIAVASGANARLTPDDV 123
Cdd:cd01172    53 GAKVTLLGVVGDDEAGDLLRKLLEKEGIDT-DGIVDEGRPtttktrviaRNQQLLRVDREDDSPLSAEEEQRLIERIAER 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 124 LSARDAVTSAD----VLVTQLetpldtVRAAVELAAVNGVRVVLNPapaQPLGEEILQHVSVLTPNEIEAELLTGIAVSS 199
Cdd:cd01172   132 LPEADVVILSDygkgVLTPRV------IEALIAAARELGIPVLVDP---KGRDYSKYRGATLLTPNEKEAREALGDEIND 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 200 DGAALAAAKALNAR-GVEAVLITLGSRGALLFDSD-HAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFAN 277
Cdd:cd01172   203 DDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDgEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLAN 282

                         250
                  ....*....|....*..
gi 2107956853 278 AAAALAVTKLGAQPSAP 294
Cdd:cd01172   283 AAAGVVVGKVGTAPVTP 299
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
14-269 3.01e-14

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 71.70  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  14 DMIIKLARIpQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVfGQQAVEGFVADGIDTSHVITDSDAPS 93
Cdd:COG1105    11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  94 GVALIfVDQQGENSIAVASGAnaRLTPDDV--LSAR--DAVTSADVLVtqL------ETPLDTVRAAVELAAVNGVRVVL 163
Cdd:COG1105    89 NIKIV-DPSDGTETEINEPGP--EISEEELeaLLERleELLKEGDWVV--LsgslppGVPPDFYAELIRLARARGAKVVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 164 NpAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEV 243
Cdd:COG1105   164 D-TSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKV 242

                         250       260
                  ....*....|....*....|....*.
gi 2107956853 244 EAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:COG1105   243 EVVSTVGAGDSMVAGFLAGLARGLDL 268
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 5-288 5.25e-14

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: 70.91  E-value: 5.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDMIIKLARIPQPGETVLGGDFSTAAGGkGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDtsH 84
Cdd:cd01944     2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE--I 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDS-DAPSGVALIFVDQQGENSIAVASGANARLTPDDVlsARDAVTSADVLVT---QLETPLDTVRAAVEL--AAVNG 158
Cdd:cd01944    79 LLPPRgGDDGGCLVALVEPDGERSFISISGAEQDWSTEWF--ATLTVAPYDYVYLsgyTLASENASKVILLEWleALPAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 159 VRVVLNPAP-----AQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVeavLITLGSRGALLFDSD 233
Cdd:cd01944   157 TTLVFDPGPrisdiPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAPV---VVRLGSNGAWIRLPD 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2107956853 234 -HAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLG 288
Cdd:cd01944   234 gNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 53-269 1.11e-12

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 67.27  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  53 GGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDSDAPSGVALIFVDQQGENSIA--VASGANARLTPDDV------- 123
Cdd:PRK09434   42 GGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTfmVRPSADLFLQPQDLppfrqge 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 124 --------LSARDAVTSAdvlvtqlETPLDTVRAAvelaavnGVRVVL----------NPAPAQPLGEEILQHVSVLTPN 185
Cdd:PRK09434  122 wlhlcsiaLSAEPSRSTT-------FEAMRRIKAA-------GGFVSFdpnlredlwqDEAELRECLRQALALADVVKLS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 186 EIEAELLTGIAVSSDGAALAAAKAlnarGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVDTTAAGDVFNGALAVALSE 265
Cdd:PRK09434  188 EEELCFLSGTSQLEDAIYALADRY----PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQ 263


                  ....
gi 2107956853 266 RSSL 269
Cdd:PRK09434  264 AGLW 267
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 151-269 4.11e-10

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: 59.47  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 151 VELAAVNGVRVVLNpAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLF 230
Cdd:cd01164   151 VRLAREKGARVILD-TSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLV 229

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2107956853 231 DSDHAELIPSFEVEAVDTTAAGDVFNGALAVALSERSSL 269
Cdd:cd01164   230 TKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSL 268
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 59-260 6.36e-10

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 59.46  E-value: 6.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  59 VARVGDDVFGQQAVEGFVADGIDTSHVITDSDAPSGVA------LIFVDQQGENSIAVASGANarLTPDDVLS------- 125
Cdd:PLN02341  139 IGHVGDEIYGKFLLDVLAEEGISVVGLIEGTDAGDSSSasyetlLCWVLVDPLQRHGFCSRAD--FGPEPAFSwisklsa 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 126 -ARDAVTSADVLVTQ----LETPLDTVRAAVELAAVNGVRVVLNPAP-------AQPLGEEILQHV----SVLTPNEIEA 189
Cdd:PLN02341  217 eAKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgksllvGTPDERRALEHLlrmsDVLLLTSEEA 296

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2107956853 190 ELLTGIavsSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVDTTAAGDVFNGALA 260
Cdd:PLN02341  297 EALTGI---RNPILAGQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIA 364
PRK09954 PRK09954
sugar kinase;
6-269 3.01e-08

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 54.17  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   6 VVVGSSNTDmIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHV 85
Cdd:PRK09954   61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  86 ITDSDAPSGVALIFVDQQGENSIAVA-SGANARLTPDDVLSARDAVTSADVLVTQLETPLDTVRAAVELAavNGVRVVLN 164
Cdd:PRK09954  140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLA--DEIPVFVD 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 165 PAPAQPLG--EEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFE 242
Cdd:PRK09954  218 TVSEFKAGkiKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTAP 297

                         250       260
                  ....*....|....*....|....*...
gi 2107956853 243 VEA-VDTTAAGDVFNGALAVALSERSSL 269
Cdd:PRK09954  298 AHTtVDSFGADDGFMAGLVYSFLEGYSF 325
PLN02323 PLN02323
probable fructokinase
 34-303 3.33e-08

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 53.86  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  34 FSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDSDAPSGVALIFVDQQGENsiavasg 113
Cdd:PLN02323   38 FKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGER------- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 114 anarltpdDVLSARDAvtSADVLVTQLETPLDTVR----------------------AAVELAAVNGVRVVLNPAPAQPL 171
Cdd:PLN02323  111 --------EFMFYRNP--SADMLLRESELDLDLIRkakifhygsislitepcrsahlAAMKIAKEAGALLSYDPNLRLPL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 172 -------GEEIL---QHVSVLTPNEIEAELLTGiavsSDGAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSF 241
Cdd:PLN02323  181 wpsaeaaREGIMsiwDEADIIKVSDEEVEFLTG----GDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGF 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2107956853 242 EVEAVDTTAAGDVFNGALAVALSERSS-------LAEAARFANAAAALAVTKLGAQPSAPSREEIEAVL 303
Cdd:PLN02323  257 KVKAVDTTGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
PRK09850 PRK09850
pseudouridine kinase; Provisional
 5-260 2.25e-07

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 51.53  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853   5 IVVVGSSNTDmIIKLARIPQPGETVLGGDFSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSH 84
Cdd:PRK09850    7 VVIIGSANID-VAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  85 VITDSDAPSGVALIFVDQQGENSIAVASganarLTPDDVLSA------RDAVTSADVLVTQLETPLDTVRAAVELAAvnG 158
Cdd:PRK09850   86 CLIVPGENTSSYLSLLDNTGEMLVAIND-----MNISNAITAeylaqhREFIQRAKVIVADCNISEEALAWILDNAA--N 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 159 VRVVLNPAPAQPLGE--EILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGALLFD-SDHA 235
Cdd:PRK09850  159 VPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDiSGES 238

                         250       260
                  ....*....|....*....|....*
gi 2107956853 236 ELIPSFEVEAVDTTAAGDVFNGALA 260
Cdd:PRK09850  239 GWSAPIKTNVINVTGAGDAMMAGLA 263
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 53-255 1.03e-06

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 48.97  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  53 GGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDsdaPSGVALIFVDQQGENSI--AVASG--ANARLTPDDV--LSA 126
Cdd:PRK09813   37 GIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK---HGVTAQTQVELHDNDRVfgDYTEGvmADFALSEEDYawLAQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 127 RDAVTSAdvLVTQLETPLDTVRAAvelaavnGVRVVLNPA--PAQPLGEEILQHVsvltpneieaELLTGIAVSSDGAAL 204
Cdd:PRK09813  114 YDIVHAA--IWGHAEDAFPQLHAA-------GKLTAFDFSdkWDSPLWQTLVPHL----------DYAFASAPQEDEFLR 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2107956853 205 AAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVDTTAAGDVF 255
Cdd:PRK09813  175 LKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSF 225
PRK15074 PRK15074
inosine/guanosine kinase; Provisional
 90-196 2.61e-06

inosine/guanosine kinase; Provisional


Pssm-ID: 185033  Cd Length: 434  Bit Score: 48.47  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  90 DAPSGVALIFVDQQGENSIAVASGANARLTPDDVLSARDAVTSADVLVTQL-----ETPL-DTVRAAVELAAVNGVRVVL 163
Cdd:PRK15074  146 DGPIGRCFTLISEDGERTFAISPGHMNQLRPESIPEDVIAGASALVLTAYLvrckpGEPMpEATMKAIEYAKKHNVPVVL 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2107956853 164 ----------NPapaQPLGEEILQHVSVLTPNEIEAELLTGIA 196
Cdd:PRK15074  226 tlgtkfviedNP---QWWQEFLKEHVSILAMNEDEAEALTGES 265
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 39-265 2.76e-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: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  39 GGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITdSDAPSGVALIFVDQQGENSIAVASGANARL 118
Cdd:cd01940    22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV-KEGENAVADVELVDGDRIFGLSNKGGVARE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 119 TPDDvlSARDAVTSADVLVTQLETPLDTVRAAVELAAVNGVRVVLNPAP--AQPLGEEILQHVSV-------LTPNEIEA 189
Cdd:cd01940   101 HPFE--ADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFSDrwDDDYLQLVCPYVDFaffsasdLSDEEVKA 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2107956853 190 ELLTGIAvssdgaalaaakalnaRGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVDTTAAGDVFNGALAVALSE 265
Cdd:cd01940   179 KLKEAVS----------------RGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLA 238
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 174-257 8.54e-06

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: 46.30  E-value: 8.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 174 EILQHVSVLTPNEIEAELLTGIAvssdgAALAAAKALNARGVEAVLITLGSRGALLFDSDHAELIPSFEVEAV-DTTAAG 252
Cdd:cd01946   159 KVLAKVDVVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAG 233


                  ....*
gi 2107956853 253 DVFNG 257
Cdd:cd01946   234 DTFAG 238
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 173-269 1.07e-04

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: 42.77  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 173 EEILQHVSVLTPNEIEAELLTGIAVSSDGAALAaakalnarGVEAVLITLGSRGALLFDSDHAELIPSFEVEAVDTTAAG 252
Cdd:cd01937   150 CVILKLHDVLKLSRVEAEVISTPTELARLIKET--------GVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAG 221

                          90
                  ....*....|....*..
gi 2107956853 253 DVFNGALAVALSERSSL 269
Cdd:cd01937   222 DVFLAAFLYSRLSGKDI 238
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 174-266 1.09e-04

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 43.15  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 174 EILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITlgsrgALLFDSDHAELIPSFEVEAVDT----- 248
Cdd:PTZ00344  135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT-----SFREDEDPTHLRFLLSCRDKDTknnkr 209

                          90       100       110
                  ....*....|....*....|....*....|
gi 2107956853 249 ------------TAAGDVFnGALAVALSER 266
Cdd:PTZ00344  210 ftgkvpyiegryTGTGDLF-AALLLAFSHQ 238
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 144-305 2.65e-04

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: 42.12  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 144 LDTVRAAVELAAVNGVRVVLNPAPAQplgEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLG 223
Cdd:PRK11316  157 LASVQAMIQLARKAGVPVLIDPKGTD---FERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRS 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 224 SRGALLFDSDHAEL-IPSFEVEAVDTTAAGDVFNGALAVALSERSSLAEAARFANAAAALAVTKLGAqpSAPSREEIEAV 302
Cdd:PRK11316  234 EQGMTLLQPGKAPLhLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT--STVSPIELENA 311


                  ...
gi 2107956853 303 LAR 305
Cdd:PRK11316  312 LRG 314
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 157-269 2.72e-04

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: 41.80  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 157 NGVRVVLNPAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITlgsrGALLFDSDHAE 236
Cdd:cd01173   115 NGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT----SVELADDDRIE 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2107956853 237 LIPS-------FEVEAVDTTA----AGDVFNGALAVALSERSSL 269
Cdd:cd01173   191 MLGStateawlVQRPKIPFPAyfngTGDLFAALLLARLLKGKSL 234
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 145-264 3.08e-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: 41.31  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 145 DTVRAAVELAAVNGVRVVLNP--------APAQP-----LGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALN 211
Cdd:pfam08543  73 EIIEAVAEKLDKYGVPVVLDPvmvaksgdSLLDDeaieaLKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 212 ARGVEAVLIT---LGSRGA----LLFDSDHAELIPSFEVEAVDTTAAGDVFNGALAVALS 264
Cdd:pfam08543 153 ALGAKAVLIKgghLEGEEAvvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLA 212
PTZ00247 PTZ00247
adenosine kinase; Provisional
 54-257 4.68e-04

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 41.17  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853  54 GKVTFVARVGDDVFGQQAVEGFVADGIDTsHVITDSDAPSGVALIFVDQQgENSIAVASGANARLTPDDVLS--ARDAVT 131
Cdd:PTZ00247   81 GFVCYVGCVGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTCAVLVCGK-ERSLVANLGAANHLSAEHMQShaVQEAIK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 132 SADVLVTQ---LETPLDTVRAAVELAAVNGVRVVLN---PAPAQPLGEEILQ---HVSVLTPNEIEAELL-------TGI 195
Cdd:PTZ00247  159 TAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlsaPFISQFFFERLLQvlpYVDILFGNEEEAKTFakamkwdTED 238

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2107956853 196 AVSSDGAALAAAKALNARGvEAVLITLGSRGALLFDSDHAELIPSFEVEA---VDTTAAGDVFNG 257
Cdd:PTZ00247  239 LKEIAARIAMLPKYSGTRP-RLVVFTQGPEPTLIATKDGVTSVPVPPLDQekiVDTNGAGDAFVG 302
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 173-263 5.19e-04

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


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 40.79  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 173 EEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGA-----LLFDSDHAELIPSFEVEAVD 247
Cdd:COG0351   121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGdeavdVLYDGDGVREFSAPRIDTGN 200

                          90
                  ....*....|....*.
gi 2107956853 248 TTAAGDVFNGALAVAL 263
Cdd:COG0351   201 THGTGCTLSSAIAALL 216
PLN02978 PLN02978
pyridoxal kinase
 173-221 9.46e-04

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 40.11  E-value: 9.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2107956853 173 EEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLIT 221
Cdd:PLN02978  144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVIT 192
PLN02967 PLN02967
kinase
 34-104 1.59e-03

kinase


Pssm-ID: 215521 [Multi-domain]  Cd Length: 581  Bit Score: 40.03  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2107956853  34 FSTAAGGKGANQAVAAARAGGKVTFVARVGDDVFGQQAVEGFVADGIDTSHVITDSDAPSGVALIFVDQQG 104
Cdd:PLN02967  238 FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRG 308
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
163-265 2.80e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 38.80  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 163 LNPAPAQPLGEEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSRGA------LLFDSDHAE 236
Cdd:PRK12412  117 LHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKLGtetaidVLYDGETFD 196

                          90       100
                  ....*....|....*....|....*....
gi 2107956853 237 LIPSFEVEAVDTTAAGDVFNGALAVALSE 265
Cdd:PRK12412  197 LLESEKIDTTNTHGAGCTYSAAITAELAK 225
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 173-263 3.04e-03

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


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 38.59  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 173 EEILQHVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLIT--------LGSRGALLFDSDHAELI--PSFE 242
Cdd:COG2240   133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTADGAWLVetPLLP 212

                          90       100
                  ....*....|....*....|.
gi 2107956853 243 VEAVDTtaaGDVFNGALAVAL 263
Cdd:COG2240   213 FSPNGT---GDLFAALLLAHL 230
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 171-263 3.53e-03

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 38.18  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 171 LGEEILQHVSVLTPNEIEAELLTGIAV-SSDGAALAAAKALNARGVEAVLITLGSRGA------LLFDSDHAELIPSFEV 243
Cdd:PRK06427  126 LRERLLPLATLITPNLPEAEALTGLPIaDTEDEMKAAARALHALGCKAVLIKGGHLLDgeesvdWLFDGEGEERFSAPRI 205

                          90       100
                  ....*....|....*....|
gi 2107956853 244 EAVDTTAAGDVFNGALAVAL 263
Cdd:PRK06427  206 PTKNTHGTGCTLSAAIAAEL 225
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
158-235 8.89e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 36.96  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2107956853 158 GVRVVLNPA---------PAQPLGEEILQ---HVSVLTPNEIEAELLTGIAVSSDGAALAAAKALNARGVEAVLITLGSR 225
Cdd:PRK12413   97 GIPVVLDPVlvckethdvEVSELRQELIQffpYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR 176

                          90
                  ....*....|
gi 2107956853 226 gallFDSDHA 235
Cdd:PRK12413  177 ----LSQKKA 182
 
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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