NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490328351|ref|WP_004217808|]
View 

MULTISPECIES: ribokinase [Klebsiella]

Protein Classification

ribokinase( domain architecture ID 10793540)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11142 PRK11142
ribokinase; Provisional
5-309 0e+00

ribokinase; Provisional


:

Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 515.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   5 AGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKID 84
Cdd:PRK11142   2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  85 VAPVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTV 164
Cdd:PRK11142  82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 165 VLNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 244
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGF 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490328351 245 RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFLAQQ 309
Cdd:PRK11142 242 RVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
 
Name Accession Description Interval E-value
PRK11142 PRK11142
ribokinase; Provisional
5-309 0e+00

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 515.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   5 AGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKID 84
Cdd:PRK11142   2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  85 VAPVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTV 164
Cdd:PRK11142  82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 165 VLNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 244
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGF 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490328351 245 RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFLAQQ 309
Cdd:PRK11142 242 RVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
7-298 1.23e-117

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: 340.30  E-value: 1.23e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVL 166
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 167 NPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRV 246
Cdd:cd01174  161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490328351 247 QAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPW 298
Cdd:cd01174  241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
12-303 1.78e-114

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: 332.26  E-value: 1.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   12 GSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAV 91
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   92 AGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAPA 171
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  172 RE-LPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAID 250
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490328351  251 TIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEID 303
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
7-302 3.76e-76

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: 235.16  E-value: 3.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAekERIASAQALLMQL-----ESPLESVIAAAKIAHHHH 161
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 162 TTVVLNPA-------PARELPDELLALVDIITPNETEAEKLTGIrvesdEDAAKAANVLHAKGIGTVMITLGSRGVWLSA 234
Cdd:COG0524  159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490328351 235 EGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 302
Cdd:COG0524  234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
7-293 1.59e-60

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 194.87  E-value: 1.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351    7 KLVVLGSINADHILNLDAFPtpGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHT 162
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  163 T--VVLNPA-PARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESR 239
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490328351  240 RILGFR-VQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 293
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
 
Name Accession Description Interval E-value
PRK11142 PRK11142
ribokinase; Provisional
5-309 0e+00

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 515.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   5 AGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKID 84
Cdd:PRK11142   2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  85 VAPVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTV 164
Cdd:PRK11142  82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 165 VLNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 244
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGF 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490328351 245 RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFLAQQ 309
Cdd:PRK11142 242 RVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
7-298 1.23e-117

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: 340.30  E-value: 1.23e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVL 166
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 167 NPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRV 246
Cdd:cd01174  161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490328351 247 QAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPW 298
Cdd:cd01174  241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
12-303 1.78e-114

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: 332.26  E-value: 1.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   12 GSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAV 91
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   92 AGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAPA 171
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  172 RE-LPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAID 250
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490328351  251 TIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEID 303
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
7-302 3.76e-76

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: 235.16  E-value: 3.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAekERIASAQALLMQL-----ESPLESVIAAAKIAHHHH 161
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 162 TTVVLNPA-------PARELPDELLALVDIITPNETEAEKLTGIrvesdEDAAKAANVLHAKGIGTVMITLGSRGVWLSA 234
Cdd:COG0524  159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490328351 235 EGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 302
Cdd:COG0524  234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
7-293 1.59e-60

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 194.87  E-value: 1.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351    7 KLVVLGSINADHILNLDAFPtpGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHT 162
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  163 T--VVLNPA-PARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESR 239
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490328351  240 RILGFR-VQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 293
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
PTZ00292 PTZ00292
ribokinase; Provisional
4-302 1.05e-59

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 193.80  E-value: 1.05e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   4 AAGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKI 83
Cdd:PTZ00292  14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  84 DVAPVRAVAGEATGVALIFVNAE-GENVIGIHAGANAALSVSQVEAEKERIAS-AQALLMQLESPLESVIAAAKIAHHHH 161
Cdd:PTZ00292  94 NTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 162 TTVVLNPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRG-VWLSAE 235
Cdd:PTZ00292 174 CYTVFNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGcLIVEKE 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490328351 236 GESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 302
Cdd:PTZ00292 254 NEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
7-292 1.75e-33

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: 124.23  E-value: 1.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHIlnldaFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01166    1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRAVAGEATGVALIFVNAEGENVIgIHAGANAALSVSQVEAEKER-IASAQAL------LMQLESPLESVIAAAKIAHH 159
Cdd:cd01166   76 HVRVDPGRPTGLYFLEIGAGGERRV-LYYRAGSAASRLTPEDLDEAaLAGADHLhlsgitLALSESAREALLEALEAAKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 160 HHTTVVL---------NPAPARELPDELLALVDIITPNETEAEKLTGIrvESDEDAAKAANVLHAkGIGTVMITLGSRGV 230
Cdd:cd01166  155 RGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGD--EDPTDAAERALALAL-GVKAVVVKLGAEGA 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490328351 231 WLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGA 292
Cdd:cd01166  232 LVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
8-293 1.88e-31

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: 118.57  E-value: 1.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   8 LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 87
Cdd:cd01942    2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  88 VRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVsqvEAEKERIASAQALLMQLESPLEsviAAAKIAHHHHTTVVLN 167
Cdd:cd01942   82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEP---NDEADPDGLADIVHLSSGPGLI---ELARELAAGGITVSFD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 168 PAPA-----RELPDELLALVDIITPNETEAE---KLTGIRVESDedaakaanvlhAKGIGTVMITLGSRGVWLSAEGESR 239
Cdd:cd01942  156 PGQElprlsGEELEEILERADILFVNDYEAEllkERTGLSEAEL-----------ASGVRVVVVTLGPKGAIVFEDGEEV 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490328351 240 RILGF-RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 293
Cdd:cd01942  225 EVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
7-274 2.86e-29

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: 113.18  E-value: 2.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQvAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01941    1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 PVRaVAGEATGVALIFVNAEGENVIGI-HAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVV 165
Cdd:cd01941   80 GIV-FEGRSTASYTAILDKDGDLVVALaDMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 166 LNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILG 243
Cdd:cd01941  159 FEPTSAPKLKKlfYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVETKL 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 490328351 244 FRVQAIDTIA----AGDTFNGALVTALLEGTALPE 274
Cdd:cd01941  239 FPAPQPETVVnvtgAGDAFVAGLVAGLLEGMSLDD 273
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
11-274 1.61e-27

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: 108.15  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  11 LGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRA 90
Cdd:cd01945    5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  91 VAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEkerIASAQALLMQLESPLESVIAAAKIAHHHHTTVV-LNPA 169
Cdd:cd01945   85 APGARSPISSITDITGDRATISITAIDTQAAPDSLPDAI---LGGADAVLVDGRQPEAALHLAQEARARGIPIPLdLDGG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 170 PARELpDELLALVDIITPNETEAEKLTGIrveSDEDAAKAanvLHAKGIGTVMITLGSRGV-WLSAEGESRRILGFRVQA 248
Cdd:cd01945  162 GLRVL-EELLPLADHAICSENFLRPNTGS---ADDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVEV 234
                        250       260
                 ....*....|....*....|....*.
gi 490328351 249 IDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:cd01945  235 VDTTGAGDVFHGAFAHALAEGMPLRE 260
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
42-272 8.20e-27

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


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 106.57  E-value: 8.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGAnAAL 121
Cdd:cd01167   28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGP-AAD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 122 SVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLALVDIIT 186
Cdd:cd01167  107 LLLDTELNPDLLSEADILhfgsIALASEPSRSALLELLEAAKKAGVLISfdpnlrpplwrDEEEARERIAELLELADIVK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 187 PNETEAEKLTGIrvesdEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTAL 266
Cdd:cd01167  187 LSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261

                 ....*.
gi 490328351 267 LEGTAL 272
Cdd:cd01167  262 LSRGLL 267
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
7-267 3.87e-24

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: 97.17  E-value: 3.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIActgdddigerirrqlasdkidva 86
Cdd:cd00287    1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 pvravageatgvalifvnaegenVIGIHAGANAALSVSQVEAEKERIasaqallmqlesplesviaaakiahHHHTTVVL 166
Cdd:cd00287   58 -----------------------ADAVVISGLSPAPEAVLDALEEAR-------------------------RRGVPVVL 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 167 NPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRI 241
Cdd:cd00287   90 DPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVH 169
                        250       260
                 ....*....|....*....|....*..
gi 490328351 242 LG-FRVQAIDTIAAGDTFNGALVTALL 267
Cdd:cd00287  170 VPaFPVKVVDTTGAGDAFLAALAAGLA 196
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
7-291 3.31e-23

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: 96.72  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGkGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01944    1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 -PVRAvaGEATGVALIFVNAEGE----NVIGIHAGANAA-LSVSQVEAEKERIASAQallmQLESPLESVIA--AAKIAH 158
Cdd:cd01944   80 lPPRG--GDDGGCLVALVEPDGErsfiSISGAEQDWSTEwFATLTVAPYDYVYLSGY----TLASENASKVIllEWLEAL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 159 HHHTTVVLNPAPA-RELPD----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAanvLHAKGIGTVMITLGSRGVWL- 232
Cdd:cd01944  154 PAGTTLVFDPGPRiSDIPDtilqALMAKRPIWSCNREEAAIFAERGDPAAEASALR---IYAKTAAPVVVRLGSNGAWIr 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490328351 233 SAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKG 291
Cdd:cd01944  231 LPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
42-274 4.95e-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: 4.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRaVAGEATGVALIFVNAEGENVIGIHAGANAAL 121
Cdd:cd01168   55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 122 SVSQVEAEKerIASAQALLM---QLESPLESVIAAAKIAHHHHTTVVLN------PAPARELPDELLALVDIITPNETEA 192
Cdd:cd01168  134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 193 EKLTGIRVESDEDAAKAanvLHAKGIGTVMITLGSRGVWLSAEGESRRILGFR-VQAIDTIAAGDTFNGALVTALLEGTA 271
Cdd:cd01168  212 EALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP 288

                 ...
gi 490328351 272 LPE 274
Cdd:cd01168  289 LEE 291
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
17-274 2.56e-17

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 80.56  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGAD-IAFIACTGDDdiGERIRRQLASDKIDVAPVRaVAGEa 95
Cdd:COG1105   11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDvTALGFLGGFT--GEFIEELLDEEGIPTDFVP-IEGE- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  96 TGVALIFVNAEGENVIGIHaGANAALSVSQVEAEKERIASAqallmqlesplesviaaakiaHHHHTTVVLNPAPARELP 175
Cdd:COG1105   86 TRINIKIVDPSDGTETEIN-EPGPEISEEELEALLERLEEL---------------------LKEGDWVVLSGSLPPGVP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGS 227
Cdd:COG1105  144 PDFYaelirlarargakvvldtsgealkaaleAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGA 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490328351 228 RGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:COG1105  224 DGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
177-224 5.18e-14

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 70.88  E-value: 5.18e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490328351 177 ELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT 224
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
176-274 1.18e-13

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: 69.54  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT------LGSRGVWLSAEGESRRILGFRVQAI 249
Cdd:cd01173  131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFP 210
                         90       100
                 ....*....|....*....|....*.
gi 490328351 250 DTIA-AGDTFNGALVTALLEGTALPE 274
Cdd:cd01173  211 AYFNgTGDLFAALLLARLLKGKSLAE 236
PLN02978 PLN02978
pyridoxal kinase
176-269 8.07e-13

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 67.84  E-value: 8.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQ----AIDT 251
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEqfkiVIPK 223
                         90
                 ....*....|....*...
gi 490328351 252 IAAGDTFNGALVTALLEG 269
Cdd:PLN02978 224 IPAYFTGTGDLMAALLLG 241
PRK09850 PRK09850
pseudouridine kinase; Provisional
2-269 9.36e-13

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 67.71  E-value: 9.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   2 MKAAGKLVVLGSINAD------HILNLdAFPTPGetvtghhyQVAF--GGKGANQAVAAGRSGADIAFIACTGDDDIGER 73
Cdd:PRK09850   1 MREKDYVVIIGSANIDvagyshESLNY-ADSNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  74 IRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQL---ESPLES 149
Cdd:PRK09850  72 LLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAW 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 150 VIAAAKIahhhhTTVVLNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGS 227
Cdd:PRK09850 152 ILDNAAN-----VPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGG 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 490328351 228 RGVWLS-AEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK09850 227 DGVYYSdISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
42-303 4.12e-12

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 65.73  E-value: 4.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGEN--VIGIHAGANA 119
Cdd:PRK09434  28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 120 ALSVSQVEAEKER-------IASAQallmqleSPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLAL 181
Cdd:PRK09434 108 FLQPQDLPPFRQGewlhlcsIALSA-------EPSRSTTFEAMRRIKAAGGFVSfdpnlredlwqDEAELRECLRQALAL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 182 VDIITPNETEAEKLTGirvESDEDAAKAAnVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGA 261
Cdd:PRK09434 181 ADVVKLSEEELCFLSG---TSQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAG 256
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 490328351 262 LVTALLEGTALPEAIRFAHAAAAI------AVTRKGAQPSVPWRTEID 303
Cdd:PRK09434 257 LLAGLSQAGLWTDEAELAEIIAQAqacgalATTAKGAMTALPNRQELE 304
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
176-274 2.05e-11

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: 62.88  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT----LGSRGV---WLSAEGESRRILGFRVQA 248
Cdd:pfam08543 114 EELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVvtdVLYDGGGFYTLEAPRIPT 193
                          90       100
                  ....*....|....*....|....*.
gi 490328351  249 IDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:pfam08543 194 KNTHGTGCTLSAAIAANLAKGLSLPE 219
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
7-269 3.34e-11

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: 62.44  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVa 86
Cdd:cd01947    1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  87 pVRAVAGEATGVALIFVNAEGENVIGIHAGanaalsvsQVEAEKERIASAQALLMQLESplESVIAAAKIAHHHHTTVVL 166
Cdd:cd01947   80 -TVAWRDKPTRKTLSFIDPNGERTITVPGE--------RLEDDLKWPILDEGDGVFITA--AAVDKEAIRKCRETKLVIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 167 NPAP--ARELPDELLALVDIITPNETEAEKLTgirvesdedaakAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 244
Cdd:cd01947  149 QVTPrvRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
                        250       260
                 ....*....|....*....|....*
gi 490328351 245 RVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:cd01947  217 KAKVPDSTGAGDSFAAGFIYGLLKG 241
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
17-274 4.37e-11

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: 62.55  E-value: 4.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDdIGERIRRQLASDKIDVAPVRaVAGEA- 95
Cdd:cd01164   12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-VAGETr 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  96 TGVALIfvnaEGENVIGIHAGANAALSVSQVEAEKERIASAQAllmqlesplesviaaakiahhHHTTVVLNPAPARELP 175
Cdd:cd01164   89 INVKIK----EEDGTETEINEPGPEISEEELEALLEKLKALLK---------------------KGDIVVLSGSLPPGVP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGS 227
Cdd:cd01164  144 ADFYaelvrlarekgarvildtsgeallaalaAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGA 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490328351 228 RGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:cd01164  224 DGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
176-274 5.85e-11

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: 61.70  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT----------------LGSRGVWLSaegESR 239
Cdd:COG2240  133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpadkignlaVTADGAWLV---ETP 209
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490328351 240 RIlgfrvqAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:COG2240  210 LL------PFSPNGTGDLFAALLLAHLLRGKSLEE 238
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
183-274 2.31e-10

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: 60.23  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  183 DIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT----LGS-------------RGVWLSaegeSRRILGFR 245
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThlirAGSqrdrsfeglvatqEGRWHI----SRPLAVFD 215
                          90       100
                  ....*....|....*....|....*....
gi 490328351  246 VQAIDTiaaGDTFNGALVTALLEGTALPE 274
Cdd:TIGR00687 216 PPPVGT---GDLIAALLLATLLHGNSLKE 241
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
35-274 5.29e-10

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: 58.90  E-value: 5.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  35 HHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEaTGVALIFVnaEGENVIGIH 114
Cdd:cd01940   15 HLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVEL--VDGDRIFGL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 115 AGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPApARELPDELLALVDIITPNETEAEK 194
Cdd:cd01940   92 SNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFS-DRWDDDYLQLVCPYVDFAFFSASD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 195 ltgirvESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEG-TALP 273
Cdd:cd01940  171 ------LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGgTAIA 244

                 .
gi 490328351 274 E 274
Cdd:cd01940  245 E 245
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
176-274 8.75e-10

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: 58.13  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT----LGSRGV-WLSAEGESRRILGFRVQAID 250
Cdd:COG0351  121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlPGDEAVdVLYDGDGVREFSAPRIDTGN 200
                         90       100
                 ....*....|....*....|....
gi 490328351 251 TIAAGDTFNGALVTALLEGTALPE 274
Cdd:COG0351  201 THGTGCTLSSAIAALLAKGLDLEE 224
PRK09954 PRK09954
sugar kinase;
9-274 1.19e-09

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 58.40  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351   9 VVLGSINADhILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPV 88
Cdd:PRK09954  61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  89 RAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQLE---SPLESVIAAAKIAHHHHTTV 164
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNltaEALEWVFTLADEIPVFVDTV 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 165 VLNPAparELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 244
Cdd:PRK09954 220 SEFKA---GKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTA 296
                        250       260       270
                 ....*....|....*....|....*....|.
gi 490328351 245 RVQA-IDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PRK09954 297 PAHTtVDSFGADDGFMAGLVYSFLEGYSFRD 327
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
43-272 1.47e-09

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 58.69  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  43 GKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVapVRAVAGEATGVAlifVNAEGENVI--------GIH 114
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwvlvdplQRH 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 115 A-------GANAALS-VSQVEAE-KERIASAQALLMQ----LESPLESVIAAAKIAHHHHTTVVLNPAP-----ARELPD 176
Cdd:PLN02341 195 GfcsradfGPEPAFSwISKLSAEaKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPD 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 177 E------LLALVDIITPNETEAEKLTGIRvesdeDAAKAANVLHAKGIGT--VMITLGSRGVWLSAEGESRRILGFRVQA 248
Cdd:PLN02341 275 ErralehLLRMSDVLLLTSEEAEALTGIR-----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
                        250       260
                 ....*....|....*....|....
gi 490328351 249 IDTIAAGDTFNGALVTALLEGTAL 272
Cdd:PLN02341 350 VDTVGCGDSFAAAIALGYIHNLPL 373
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
173-269 2.09e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 57.00  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 173 ELPDELLAL---VDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRgvwLSAE--------GESRRI 241
Cdd:PRK12413 118 ELRQELIQFfpyVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR---LSQKkaidlfydGKEFVI 194
                         90       100
                 ....*....|....*....|....*...
gi 490328351 242 LGFRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK12413 195 LESPVLEKNNIGAGCTFASSIASQLVKG 222
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
182-297 3.99e-09

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: 56.80  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 182 VDIITPNETEAEKLTGIRVESDEDAAKAANVLHAK-GIGTVMITLGSRGV-WLSAEGESRRILGFRVQAIDTIAAGDTFN 259
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTVI 261
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490328351 260 GALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVP 297
Cdd:cd01172  262 ATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
PLN02323 PLN02323
probable fructokinase
40-306 5.33e-09

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 56.55  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  40 AFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGANA 119
Cdd:PLN02323  41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 120 ALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVV---------LNPAP--ARELPDELLALVDI 184
Cdd:PLN02323 121 DMLLRESELDLDLIRKAKIFhygsISLITEPCRSAHLAAMKIAKEAGALLsydpnlrlpLWPSAeaAREGIMSIWDEADI 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 185 ITPNETEAEKLTGIRVESDEDAAKaanvLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVT 264
Cdd:PLN02323 201 IKVSDEEVEFLTGGDDPDDDTVVK----LWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLS 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 490328351 265 ------ALLEGTA-LPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFL 306
Cdd:PLN02323 277 qlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
174-267 1.07e-08

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 55.13  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 174 LPDELLALVDIITPNETEAEKLTGIRVESDEDAAK-AANVLHAKGIGTVMITLG-------SRGVWLSAEGESRrilgFR 245
Cdd:PRK06427 126 LRERLLPLATLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhlldgeeSVDWLFDGEGEER----FS 201
                         90       100
                 ....*....|....*....|....*
gi 490328351 246 VQAIDTIA---AGDTFNGALvTALL 267
Cdd:PRK06427 202 APRIPTKNthgTGCTLSAAI-AAEL 225
PRK05756 PRK05756
pyridoxal kinase PdxY;
168-274 7.42e-08

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 52.56  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 168 PAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMIT----------------LGSRGVW 231
Cdd:PRK05756 125 PGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypadrfemllVTADGAW 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490328351 232 LSaegeSRRILGFRVQaidTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PRK05756 205 HI----SRPLVDFMRQ---PVGVGDLTSALFLARLLQGGSLEE 240
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
30-269 1.12e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 49.81  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  30 ETVTGHHYQVAFGGKGANQAVAAGRSGA--------DIAFIACTGDDDIGERIRRQLASdkidvAPVR----AVAGEATG 97
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRR-----ANVHflsqPVKDGTTG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  98 VALIFVNAEGENVIGIHAGANAALSVSQVEAE---KERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAP---- 170
Cdd:PLN02813 189 TVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASaisKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDvsci 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 171 ARELPDELLAL---VDIITPNETEAEKLTGIrvESDEDAAKAANVLhAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQ 247
Cdd:PLN02813 269 ERHRDDFWDVMgnyADILFANSDEARALCGL--GSEESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCV 345
                        250       260
                 ....*....|....*....|..
gi 490328351 248 AIDTIAAGDTFNGALVTALLEG 269
Cdd:PLN02813 346 PVDTCGAGDAYAAGILYGLLRG 367
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
166-274 1.87e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 48.43  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 166 LNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSR-----GVWLSAEGESRR 240
Cdd:PRK12412 117 LHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetAIDVLYDGETFD 196
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490328351 241 IL-GFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PRK12412 197 LLeSEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
178-214 3.41e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 48.19  E-value: 3.41e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490328351 178 LLALVDIITPNETEAEKLTGIRVESDEDAAKAANVLH 214
Cdd:PRK08573 127 LLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIV 163
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
10-274 3.98e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 44.78  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  10 VLGSINAdHILNLDAFPTPGETVTGhhyqvafgGKGAN--QAVAAGrSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 87
Cdd:PLN02379  63 ILREVNA-HILPSPDDLSPIKTMAG--------GSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  88 VRAVAGEaTGVALIFVNAEGENVIgiHAGANAALSVSQVEAEKERIASAQALLMQLE-SPLESVIAAAKIAHHHHTTVVL 166
Cdd:PLN02379 133 LRAKKGP-TAQCVCLVDALGNRTM--RPCLSSAVKLQADELTKEDFKGSKWLVLRYGfYNLEVIEAAIRLAKQEGLSVSL 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 167 NPAP---ARELPDELLAL-----VDIITPNETEAEKLtgIRVESDEDAAKAANVLhAKGIGTVMITLGSRG--------- 229
Cdd:PLN02379 210 DLASfemVRNFRSPLLQLlesgkIDLCFANEDEAREL--LRGEQESDPEAALEFL-AKYCNWAVVTLGSKGciarhgkev 286
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490328351 230 VWLSAEGESRrilgfrvqAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PLN02379 287 VRVPAIGETN--------AVDATGAGDLFASGFLYGLIKGLSLEE 323
fruK PRK09513
1-phosphofructokinase; Provisional
184-308 4.33e-05

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 44.30  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 184 IITPNETEAEKLTGIRVESDEDAAKAANVLHAKGIGTVMITLGSRG-VWLSAEGESRrILGFRVQAIDTIAAGDTFNGAL 262
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGaLWVNASGEWI-AKPPACDVVSTVGAGDSMVGGL 261
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490328351 263 VTALLEGTALPEAIRFAHAAAAIAVTrkgaQPSVPW--RTEIDEFLAQ 308
Cdd:PRK09513 262 IYGLLMRESSEHTLRLATAVSALAVS----QSNVGItdRPQLAAMMAR 305
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
175-260 1.38e-04

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: 42.84  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 175 PDEL---LALVDIITPNETEAEKLTGirvesDEDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAI-D 250
Cdd:cd01946  154 PEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
                         90
                 ....*....|
gi 490328351 251 TIAAGDTFNG 260
Cdd:cd01946  229 PTGAGDTFAG 238
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
177-269 2.53e-03

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: 38.92  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 177 ELLALVDIITPNETEAEKLTgirvesdeDAAKAANVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGD 256
Cdd:cd01937  151 VILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGD 222
                         90
                 ....*....|...
gi 490328351 257 TFNGALVTALLEG 269
Cdd:cd01937  223 VFLAAFLYSRLSG 235
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
164-226 3.75e-03

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 38.60  E-value: 3.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490328351 164 VVLNPAPARELPDELLALVDIITPNETEAEKLTG-IRVESDEDAAKAANVLHAKGIGTVMITLG 226
Cdd:PLN02898 121 VLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMRSAAKELHKLGPRYVLVKGG 184
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
42-274 6.08e-03

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 37.79  E-value: 6.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351  42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEAtgvALIFVNAEG-ENVIGIHA-GANA 119
Cdd:PRK09813  23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT---AQTQVELHDnDRVFGDYTeGVMA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 120 ALSVSQveaEKERIASAQ-----ALLMQLESPLESVIAAAkiahhhhTTVVLNPA--PARELPDELLALVDIitpnetea 192
Cdd:PRK09813 100 DFALSE---EDYAWLAQYdivhaAIWGHAEDAFPQLHAAG-------KLTAFDFSdkWDSPLWQTLVPHLDY-------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 193 ekltGIRVESDEDA--AKAANVLHAKGIGTVMITLGSRGVwLSAEGESRRILG-FRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK09813 162 ----AFASAPQEDEflRLKMKAIVARGAGVVIVTLGENGS-IAWDGAQFWRQApEPVTVVDTMGAGDSFIAGFLCGWLAG 236

                 ....*
gi 490328351 270 TALPE 274
Cdd:PRK09813 237 MTLPQ 241
PLN02548 PLN02548
adenosine kinase
177-274 6.45e-03

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 37.77  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490328351 177 ELLALVDIITPNETEAEKLTGIRVESDED----AAKAANVLHAKGIG--TVMITLGSRGVWLSAEGesrRILGFRVQAI- 249
Cdd:PLN02548 199 EALPYVDFLFGNETEARTFAKVQGWETEDveeiALKISALPKASGTHkrTVVITQGADPTVVAEDG---KVKEFPVIPLp 275
                         90       100       110
                 ....*....|....*....|....*....|
gi 490328351 250 -----DTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PLN02548 276 keklvDTNGAGDAFVGGFLSQLVQGKDIEE 305
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH