|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-288 |
4.31e-71 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 221.27 E-value: 4.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIE 84
Cdd:cd01174 4 VVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 85 -MEDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILSTAGSGDLMILQGNLSDRTTRDILEHARAIGMVTAFNPS 163
Cdd:cd01174 84 vVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILNPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 164 PVRSYFSDLWDLIDIAFLNKGEAQALTGTTG------RDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVV 237
Cdd:cd01174 164 PARPLPAELLALVDILVPNETEAALLTGIEVtdeedaEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499969019 238 DTTGAGDTFMaAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTRKAFPT 288
Cdd:cd01174 244 DTTGAGDTFI-GALAAALARGLSLEE-AIRFANAAAALSVTRPGAQPSIPT 292
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-292 |
1.26e-55 |
|
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: 182.01 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 2 RAYIVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSE 81
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 82 LIE-MEDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILstAGSGDLMILQG-----NLSDRTTRDILEHARAIG 155
Cdd:COG0524 81 GVRrDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 156 MVTAFNPS-------PVRSYFSDLWDLIDIAFLNKGEAQALTGTTG-RDAAEYLLSRGLREIVLTLGGDGATLVNRHDSI 227
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGETDpEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499969019 228 EVPAQVCEVVDTTGAGDTFMAAALASCaLRGQRLDRlAIEHAVAAAAITVSRHGTRKAFPTISEL 292
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGL-LEGLDLEE-ALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
7-293 |
5.94e-50 |
|
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: 167.01 E-value: 5.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 7 GNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIE-M 85
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGtV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 86 EDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILSTAGSGDLMILQGNLSDRTTRDILEHARAIGMVTAFNPSPV 165
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 166 RSYFS-DLWDLIDIAFLNKGEAQALTGT------TGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVD 238
Cdd:TIGR02152 161 IKDLDdELLSLVDIITPNETEAEILTGIevtdeeDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499969019 239 TTGAGDTFMaAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTRKAFPTISELE 293
Cdd:TIGR02152 241 TTAAGDTFN-GAFAVALAEGKSLED-AIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
5-297 |
7.07e-39 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 139.10 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDAR-ADTIRHYLADEPLRSELI 83
Cdd:PTZ00292 20 VVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFgSDTIKNFKRNGVNTSFVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 84 EMEDASSDVSIIF-RLPGGENAIVTTTESAQSLSLSDVRRILSTAGS-GDLMILQGNLSDRTTRDILEHARAIGMVTAFN 161
Cdd:PTZ00292 100 RTENSSTGLAMIFvDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERGCYTVFN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 162 PSPVRSYFS-----DLWDLIDIAFLNKGEAQALTGTTGRD------AAEYLLSRGLREIVLTLGGDGATLV-NRHDSIEV 229
Cdd:PTZ00292 180 PAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDtesafkASKELQQLGVENVIITLGANGCLIVeKENEPVHV 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499969019 230 PAQVCEVVDTTGAGDTFMaAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTRKAFPTISELEAILR 297
Cdd:PTZ00292 260 PGKRVKAVDTTGAGDCFV-GSMAYFMSRGKDLKE-SCKRANRIAAISVTRHGTQSSYPHPSELPADVK 325
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
5-296 |
3.01e-34 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 126.14 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIE 84
Cdd:PRK11142 7 VLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 85 M-EDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILSTAGSGDLMILQGNLSDRTTRDILEHARAIGMVTAFNPS 163
Cdd:PRK11142 87 ViKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILNPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 164 PVRSYFSDLWDLIDIAFLNKGEAQALTGTTGRD------AAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVV 237
Cdd:PRK11142 167 PARELPDELLALVDIITPNETEAEKLTGIRVEDdddaakAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAV 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499969019 238 DTTGAGDTFmAAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTRKAFPTISELEAIL 296
Cdd:PRK11142 247 DTIAAGDTF-NGALVTALLEGKPLPE-AIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-283 |
7.35e-32 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 119.76 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 6 VGNVAIDETIAVSELPvtGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSE-LIE 84
Cdd:pfam00294 5 IGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDyVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 85 MEDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILSTAGSGDLM----ILQGNLSDRTTRDILEHARAIGMVTA- 159
Cdd:pfam00294 83 DEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGTFDPn 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 160 -FNPS-PVRSYFSDLWDLIDIAFLNKGEAQALTGTTGRDAAEY------LLSRGLREIVLTLGGDGATLVNRHDSIEVPA 231
Cdd:pfam00294 163 lLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEAlaalhkLLAKGIKTVIVTLGADGALVVEGDGEVHVPA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499969019 232 QVC-EVVDTTGAGDTFmAAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTR 283
Cdd:pfam00294 243 VPKvKVVDTTGAGDSF-VGGFLAGLLAGKSLEE-ALRFANAAAALVVQKSGAQ 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-283 |
3.09e-27 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 107.01 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPL-RSELI 83
Cdd:cd01942 4 VVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVdTSHVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 84 EMEDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRILSTAGSgdlmilqgnLSDRTTRDILEHARAI---GMVTAF 160
Cdd:cd01942 84 VVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPDGLADI---------VHLSSGPGLIELARELaagGITVSF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 161 NPSPVRSYFS--DLWD---LIDIAFLNKGEAQALTGTTGRDAAEylLSRGLREIVLTLGGDGATLVNRHDSIEVPA-QVC 234
Cdd:cd01942 155 DPGQELPRLSgeELEEileRADILFVNDYEAELLKERTGLSEAE--LASGVRVVVVTLGPKGAIVFEDGEEVEVPAvPAV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499969019 235 EVVDTTGAGDTFmAAALASCALRGQRLDRlAIEHAVAAAAITVSRHGTR 283
Cdd:cd01942 233 KVVDTTGAGDAF-RAGFLYGLLRGYDLEE-SLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
36-281 |
1.14e-23 |
|
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: 97.65 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 36 LGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIEMeDASSDVSIIFRLPGGENAIVTTTESAQS- 114
Cdd:cd01166 30 FGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV-DPGRPTGLYFLEIGAGGERRVLYYRAGSa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 115 ---LSLSDV-RRILSTAG----SGDLMILQGNLSDrTTRDILEHARAIGMVTAF--NPSPV-------RSYFSDLWDLID 177
Cdd:cd01166 109 asrLTPEDLdEAALAGADhlhlSGITLALSESARE-ALLEALEAAKARGVTVSFdlNYRPKlwsaeeaREALEELLPYVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 178 IAFLNKGEAQALTG-TTGRDAAEYLLS--RGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAAALAsC 254
Cdd:cd01166 188 IVLPSEEEAEALLGdEDPTDAAERALAlaLGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLA-G 266
|
250 260
....*....|....*....|....*..
gi 499969019 255 ALRGQRLDRlAIEHAVAAAAITVSRHG 281
Cdd:cd01166 267 LLEGWDLEE-ALRFANAAAALVVTRPG 292
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
5-268 |
2.24e-20 |
|
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: 88.52 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASilgNAGGS--DLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYL--ADEPLRS 80
Cdd:cd01941 4 VIGAANIDLRGKVSGSLVPGTS---NPGHVkqSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESekAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 81 ELIEMEDASSDVSIIFRlpGGE--------NAIVTTTEsaqsLSLSDVRRILSTAgsgDLMILQGNLSDRTTRDILEHAR 152
Cdd:cd01941 81 IVFEGRSTASYTAILDK--DGDlvvaladmDIYELLTP----DFLRKIREALKEA---KPIVVDANLPEEALEYLLALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 153 AIGMVTAFNP--SPVRSYFSDLWDLIDIAFLNKGEAQALTGTTGRD------AAEYLLSRGLREIVLTLGGDGATLVNRH 224
Cdd:cd01941 152 KHGVPVAFEPtsAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENnedenkAAKILLLPGIKNVIVTLGAKGVLLSSRE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499969019 225 DSIEV----PAQVCEVVDTTGAGDTFMAAALAS---------CALRGQRLDRLAIEH 268
Cdd:cd01941 232 GGVETklfpAPQPETVVNVTGAGDAFVAGLVAGllegmslddSLRFAQAAAALTLES 288
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
37-252 |
7.94e-20 |
|
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: 87.28 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIEMEDASSDVSIIFRLPGGENAIVTTTESAQSLS 116
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 117 LSDV-RRILSTAgsgDLMILQG---NLSDRTTRDILEHARAIGMVTAFN---PSPVRSYFSDLWDLI---DIAFLNKGEA 186
Cdd:cd01168 135 PDDLdWSLLAKA---KYLYLEGyllTVPPEAILLAAEHAKENGVKIALNlsaPFIVQRFKEALLELLpyvDILFGNEEEA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 187 QALTGTTGRD---AAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPA-QVCEVVDTTGAGDTFMAAALA 252
Cdd:cd01168 212 EALAEAETTDdleAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAiPVEKIVDTNGAGDAFAGGFLY 281
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
8-297 |
1.11e-19 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 86.86 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 8 NVAIDETIAVSELpVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADtIRHYLADEPLRSELIEMED 87
Cdd:TIGR03168 7 NPAIDLTIEVDGL-TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEF-IEALLAEEGIKNDFVEVKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 88 AS-SDVSIIfrlpggENAIVTTTESAQSLSLSD------VRRILSTAGSGDLMILQG----NLSDRTTRDILEHARAIGM 156
Cdd:TIGR03168 85 ETrINVKIK------ESSGEETELNEPGPEISEeeleqlLEKLRELLASGDIVVISGslppGVPPDFYAQLIAIARKKGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 157 VTAFNPSPVRsyfsdLWDLIDIA-FL---NKGEAQALTGTTG------RDAAEYLLSRGLREIVLTLGGDGATLVNRHDS 226
Cdd:TIGR03168 159 KVILDTSGEA-----LREALAAKpFLikpNHEELEELFGRELktleeiIEAARELLDRGAENVLVSLGADGALLVTKEGA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499969019 227 IEVPAQVCEVVDTTGAGDTfMAAALASCALRGQRLD---RLAIEHAVAaaaiTVSRHGTRkaFPTISELEAILR 297
Cdd:TIGR03168 234 LKATPPKVEVVNTVGAGDS-MVAGFLAGLARGLSLEealRFAVAAGSA----AAFSPGTG--LPDPEDVEELLD 300
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
8-255 |
4.98e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 85.19 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 8 NVAIDETIAVSELpVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDArADTIRHYLADEPLRSELIEMED 87
Cdd:COG1105 7 NPALDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 88 AS-SDVSIIFRLPGGENAIVtttESAQSLSLSDVRRILST----AGSGDLMILQG----NLSDRTTRDILEHARAIGMVT 158
Cdd:COG1105 85 ETrINIKIVDPSDGTETEIN---EPGPEISEEELEALLERleelLKEGDWVVLSGslppGVPPDFYAELIRLARARGAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 159 AFnpspvrsyfsD-----LWDLID-IAFL---NKGEAQALTGTTG------RDAAEYLLSRGLREIVLTLGGDGATLVNR 223
Cdd:COG1105 162 VL----------DtsgeaLKAALEaGPDLikpNLEELEELLGRPLetlediIAAARELLERGAENVVVSLGADGALLVTE 231
|
250 260 270
....*....|....*....|....*....|..
gi 499969019 224 HDSIEVPAQVCEVVDTTGAGDTFMAAALASCA 255
Cdd:COG1105 232 DGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLA 263
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
6-288 |
2.83e-18 |
|
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: 82.73 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 6 VGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLR-SELIE 84
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDtSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 85 MEDASSDVSIIFRlPGGENAIVTTT-----ESAQSLSLSDVRRIlstagsgDLMILQGNLSDRTTrDILEHARA--IGMV 157
Cdd:cd01945 85 APGARSPISSITD-ITGDRATISITaidtqAAPDSLPDAILGGA-------DAVLVDGRQPEAAL-HLAQEARArgIPIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 158 TAFNPSPVRSyFSDLWDLIDIAFLNKGEAQALTGTTGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDS-IEVPAQVCEV 236
Cdd:cd01945 156 LDLDGGGLRV-LEELLPLADHAICSENFLRPNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPVEV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499969019 237 VDTTGAGDTFMAAALASCALRGQRLDRLAIEHAVAAAAITvsRHGTRKAFPT 288
Cdd:cd01945 235 VDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCR--GLGGRAGLPT 284
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
8-296 |
1.46e-17 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 81.10 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 8 NVAIDETIAVSELpVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDArADTIRHYLADEPLRSELIEMED 87
Cdd:TIGR03828 7 NPAIDLTIELDGL-TLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 88 AS-SDVSIIfrlpggENAIVTTTESAQSLSLSD------VRRILSTAGSGDLMILQG----NLSDRTTRDILEHARAIGM 156
Cdd:TIGR03828 85 ETrINVKIK------EPSGTETKLNGPGPEISEeelealLEKLRAQLAEGDWLVLSGslppGVPPDFYAELIALAREKGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 157 VTAFNPSPVRsyfsdLWDLIDI-AFL---NKGEAQALTGTT------GRDAAEYLLSRGLREIVLTLGGDGATLVNRHDS 226
Cdd:TIGR03828 159 KVILDTSGEA-----LRDGLKAkPFLikpNDEELEELFGRElktleeIIEAARELLDLGAENVLISLGADGALLVTKEGA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499969019 227 IEVPAQVCEVVDTTGAGDTfMAAALASCALRGQRLD---RLAIEHAVAaaaiTVSRHGTRkaFPTISELEAIL 296
Cdd:TIGR03828 234 LFAQPPKGEVVSTVGAGDS-MVAGFLAGLESGLSLEealRLAVAAGSA----AAFSEGTG--LPDPEDIEELL 299
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
33-281 |
9.81e-16 |
|
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: 75.75 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 33 GSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLA-----------DEPLRSELIEME-DASSDVSIIFRLPG 100
Cdd:cd01167 24 TKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKeagvdtrgiqfDPAAPTTLAFVTlDADGERSFEFYRGP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 101 GENAIVTTtesAQSLSLSDVRRILSTagsGDLMILQGNLSDrTTRDILEHARAIGMVTAFNPS----------PVRSYFS 170
Cdd:cd01167 104 AADLLLDT---ELNPDLLSEADILHF---GSIALASEPSRS-ALLELLEAAKKAGVLISFDPNlrpplwrdeeEARERIA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 171 DLWDLIDIAFLNKGEAQALTGTTGRDAAEYLLSR-GLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAA 249
Cdd:cd01167 177 ELLELADIVKLSDEELELLFGEEDPEEIAALLLLfGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAG 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 499969019 250 ALASCALRGQRLD-----RLAIEHAVAAAAITVSRHG 281
Cdd:cd01167 257 LLAQLLSRGLLALdedelAEALRFANAVGALTCTKAG 293
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
8-259 |
4.92e-15 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 73.72 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 8 NVAIDETIAVSELpVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDArADTIRHYLADEPLRSELIEMED 87
Cdd:cd01164 8 NPAIDLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVEVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 88 AS-SDVSIIfrlpggENAIVTTTESAQSLSLSD------VRRILSTAGSGDLMILQG----NLSDRTTRDILEHARAIGM 156
Cdd:cd01164 86 ETrINVKIK------EEDGTETEINEPGPEISEeelealLEKLKALLKKGDIVVLSGslppGVPADFYAELVRLAREKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 157 VTAFNPS--PVRSYFSDLWDLIDiafLNKGEAQALTGTTGRD------AAEYLLSRGLREIVLTLGGDGATLVNRHDSIE 228
Cdd:cd01164 160 RVILDTSgeALLAALAAKPFLIK---PNREELEELFGRPLGDeedviaAARKLIERGAENVLVSLGADGALLVTKDGVYR 236
|
250 260 270
....*....|....*....|....*....|.
gi 499969019 229 VPAQVCEVVDTTGAGDTfMAAALASCALRGQ 259
Cdd:cd01164 237 ASPPKVKVVSTVGAGDS-MVAGFVAGLAQGL 266
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-281 |
7.73e-15 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 73.23 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 6 VGNVAIDETIAVSELPVTGASILGNAGGSDLGGkGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIEM 85
Cdd:cd01944 5 IGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 86 EDASSDVSIIFRLPGGENAIVTTTESAQSLSLSDVRRIlsTAGSGDLMILQGN-LSDRTTRD--ILEHARAIGMVTA--F 160
Cdd:cd01944 84 GGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATL--TVAPYDYVYLSGYtLASENASKviLLEWLEALPAGTTlvF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 161 NPSPV-----RSYFSDLWDLIDIAFLNKGEAQALTGTTGRDAAEYLLSRGLRE---IVLTLGGDGATLVNRHD-SIEVPA 231
Cdd:cd01944 162 DPGPRisdipDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTaapVVVRLGSNGAWIRLPDGnTHIIPG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499969019 232 QVCEVVDTTGAGDTFMAAALASCAlRGQRLDRlAIEHAVAAAAITVSRHG 281
Cdd:cd01944 242 FKVKAVDTIGAGDTHAGGMLAGLA-KGMSLAD-AVLLANAAAAIVVTRSG 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
68-255 |
8.11e-15 |
|
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: 71.36 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 68 TIRHYLADEPLRSELIEMEDASSDVSIIFRLPGGENAIVTTTesAQSLSLSdvrrilSTAGSGDLMILQG-NLSDRTTRD 146
Cdd:cd00287 4 VVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVA--LARLGVS------VTLVGADAVVISGlSPAPEAVLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 147 ILEHARAIGMVTAFNPSP-----VRSYFSDLWDLIDIAFLNKGEAQALTGTTGRDAAEY------LLSRGLREIVLTLGG 215
Cdd:cd00287 76 ALEEARRRGVPVVLDPGPravrlDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAaeaaalLLSKGPKVVIVTLGE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499969019 216 DGATLVNRHDSI-EVPAQVCEVVDTTGAGDTFMAAALASCA 255
Cdd:cd00287 156 KGAIVATRGGTEvHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
36-253 |
1.36e-14 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 72.92 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 36 LGGKGtNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIEMEDA---------SSDVSIIFRLPGGENAIV 106
Cdd:COG2870 55 PGGAA-NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRrptttktrvIAGGQQLLRLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 107 TTTESAQSLSLsdVRRILSTAgsgDLMILQ----GNLSDRTTRDILEHARAIGMVTAFNPSPVR--SYFSdlwdlIDIAF 180
Cdd:COG2870 134 SAELEARLLAA--LEAALPEV---DAVILSdygkGVLTPELIQALIALARAAGKPVLVDPKGRDfsRYRG-----ATLLT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 181 LNKGEAQALTGTTGRD------AAEYLLSR-GLREIVLTLGGDGATLVNR-HDSIEVPAQVCEVVDTTGAGDTF---MAA 249
Cdd:COG2870 204 PNLKEAEAAVGIPIADeeelvaAAAELLERlGLEALLVTRGEEGMTLFDAdGPPHHLPAQAREVFDVTGAGDTViatLAL 283
|
....
gi 499969019 250 ALAS 253
Cdd:COG2870 284 ALAA 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
5-253 |
1.76e-14 |
|
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: 72.21 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVS------ELPVtgASILGNAGGSDLGGKGtNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPL 78
Cdd:cd01172 4 VVGDVILDEYLYGDverispEAPV--PVVKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 79 RSELIEMEDASSDVSI--------IFRLPGGENAIVTTTESAQSLslsdvRRILSTAGSGDLMIL----QGNLSDRTTRD 146
Cdd:cd01172 81 DTDGIVDEGRPTTTKTrviarnqqLLRVDREDDSPLSAEEEQRLI-----ERIAERLPEADVVILsdygKGVLTPRVIEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 147 ILEHARAIGMVTAFNP-SPVRSYFSDLwDLIDIaflNKGEAQALTGTTGRD------AAEYLLSR-GLREIVLTLGGDGA 218
Cdd:cd01172 156 LIAAARELGIPVLVDPkGRDYSKYRGA-TLLTP---NEKEAREALGDEINDddeleaAGEKLLELlNLEALLVTLGEEGM 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 499969019 219 TLVNRHDSIE-VPAQVCEVVDTTGAGDTF---MAAALAS 253
Cdd:cd01172 232 TLFERDGEVQhIPALAKEVYDVTGAGDTViatLALALAA 270
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
37-253 |
2.07e-12 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 65.84 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSELIEMEDASSDVSIIfRLPGGENAIVTTTE--SAQS 114
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADV-ELVDGDRIFGLSNKggVARE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 115 LSLSDVRRILSTAgsgDLMILQGNLSDRTTRDILEHARAIGMVTAFNpspvrsyFSDLWDL---------IDIAFLNKGE 185
Cdd:cd01940 101 HPFEADLEYLSQF---DLVHTGIYSHEGHLEKALQALVGAGALISFD-------FSDRWDDdylqlvcpyVDFAFFSASD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499969019 186 aqaLTGTTGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAAALAS 253
Cdd:cd01940 171 ---LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLS 235
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
37-283 |
2.42e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 66.76 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVVMARCGVSTT--------LVAPVGKDARADTIRHYLADEPLRSELIEMEDASSDVSIIFRLPGGENAIVTT 108
Cdd:PLN02813 126 GGSLSNTLVALARLGSQSAagpalnvaMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDAQRTMLSY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 109 TESAQSLSLSDvrRILSTAGSGDLMILQGNL-----SDRTTRDILEHARAIGM---VTAFNPSPVRSYFSDLWDLI---- 176
Cdd:PLN02813 206 QGTSSTVNYDS--CLASAISKSRVLVVEGYLwelpqTIEAIAQACEEAHRAGAlvaVTASDVSCIERHRDDFWDVMgnya 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 177 DIAFLNKGEAQALTG----TTGRDAAEYLlSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAAALA 252
Cdd:PLN02813 284 DILFANSDEARALCGlgseESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILY 362
|
250 260 270
....*....|....*....|....*....|.
gi 499969019 253 SCaLRGQRLDRLAIEHAVAAAAITVSRHGTR 283
Cdd:PLN02813 363 GL-LRGVSDLRGMGELAARVAATVVGQQGTR 392
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
5-252 |
5.95e-12 |
|
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: 64.36 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 5 IVGNVAIDETIAVSELPVTGASILGNAGGSDLGGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRhyladEPLRSELIE 84
Cdd:cd01947 4 VVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSL-----EELESGGDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 85 MEDASSDVsiifrlPGGENAIVTTTESAQSLSLSDVRRI----LSTAGSGDLMILQGNLSDRTtrdILEHARAIGMVTAF 160
Cdd:cd01947 79 HTVAWRDK------PTRKTLSFIDPNGERTITVPGERLEddlkWPILDEGDGVFITAAAVDKE---AIRKCRETKLVILQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 161 NPSPVRS-YFSDLWDLIDIAFLNKGEAQaltgttGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDT 239
Cdd:cd01947 150 VTPRVRVdELNQALIPLDILIGSRLDPG------ELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDS 223
|
250
....*....|...
gi 499969019 240 TGAGDTFMAAALA 252
Cdd:cd01947 224 TGAGDSFAAGFIY 236
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
175-258 |
8.81e-10 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 58.41 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 175 LIDIAFLNKGEAQALTGTTGRDAAEYLLSR--GLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAAALA 252
Cdd:PRK09434 180 LADVVKLSEEELCFLSGTSQLEDAIYALADryPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLA 259
|
....*.
gi 499969019 253 SCALRG 258
Cdd:PRK09434 260 GLSQAG 265
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
148-262 |
3.23e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 57.53 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 148 LEHARAIGMVTAFNPSP-----------VRSYFSDLWDLIDIAFLNKGEAQALTGTTG-RDAAEYLLSRGLRE--IVLTL 213
Cdd:PLN02341 247 VDYAIDVGTAVFFDPGPrgksllvgtpdERRALEHLLRMSDVLLLTSEEAEALTGIRNpILAGQELLRPGIRTkwVVVKM 326
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499969019 214 GGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFmAAALASCALRGQRLD 262
Cdd:PLN02341 327 GSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSF-AAAIALGYIHNLPLV 374
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
161-253 |
2.18e-08 |
|
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: 53.94 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 161 NPSPVRSYFSDLWDLIDIAFLNKGEAQalTGTTGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTT 240
Cdd:cd01937 141 RANQEKLIKCVILKLHDVLKLSRVEAE--VISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPT 218
|
90
....*....|...
gi 499969019 241 GAGDTFMAAALAS 253
Cdd:cd01937 219 GAGDVFLAAFLYS 231
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
142-246 |
5.60e-07 |
|
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: 49.77 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 142 RTTRDILEHARAIGMVTA-FNPSPVRSYFSDLWDLIDIAFLNKGEAQALTGTTGR-DAAEYLLSRGLREIVLTLGGDGAT 219
Cdd:cd01946 129 REVLEQVKDPKLVVMDTMnFWISIKPEKLKKVLAKVDVVIINDGEARQLTGAANLvKAARLILAMGPKALIIKRGEYGAL 208
|
90 100
....*....|....*....|....*...
gi 499969019 220 LVNRHDSIEVPAQVCE-VVDTTGAGDTF 246
Cdd:cd01946 209 LFTDDGYFAAPAYPLEsVFDPTGAGDTF 236
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
37-258 |
9.86e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 49.22 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLRSE---LIEMEDASSDVSIIFRLpgGENAI----VTTT 109
Cdd:PRK09850 40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDkclIVPGENTSSYLSLLDNT--GEMLVaindMNIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 110 ESAQSLSLSDVRRILSTAgsgDLMILQGNLSDRTTRDILEHARAIGM----VTAFNPSPVRSYFSDLWDLIDiaflNKGE 185
Cdd:PRK09850 118 NAITAEYLAQHREFIQRA---KVIVADCNISEEALAWILDNAANVPVfvdpVSAWKCVKVRDRLNQIHTLKP----NRLE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 186 AQALTGT--TGRD----AAEYLLSRGLREIVLTLGGDGA--TLVNRHDSIEVPAQVcEVVDTTGAGDTFMaAALASCALR 257
Cdd:PRK09850 191 AETLSGIalSGREdvakVAAWFHQHGLNRLVLSMGGDGVyySDISGESGWSAPIKT-NVINVTGAGDAMM-AGLASCWVD 268
|
.
gi 499969019 258 G 258
Cdd:PRK09850 269 G 269
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
172-296 |
2.63e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.00 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 172 LWDLIDIAFLNKGEAQALTG--TTGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAA 249
Cdd:PLN02323 194 IWDEADIIKVSDEEVEFLTGgdDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGG 273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499969019 250 ALASCALRGQRLD-----RLAIEHAVAAAAITVSRHGTRKAFPTISELEAIL 296
Cdd:PLN02323 274 LLSQLAKDLSLLEdeerlREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
165-246 |
2.79e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 45.17 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 165 VRSYFSDLWDL-----IDIAFLNKGEAQALTG---TTGRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQV-CE 235
Cdd:PLN02379 217 VRNFRSPLLQLlesgkIDLCFANEDEARELLRgeqESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTN 296
|
90
....*....|.
gi 499969019 236 VVDTTGAGDTF 246
Cdd:PLN02379 297 AVDATGAGDLF 307
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
37-263 |
3.77e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 44.63 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVV---MARCGVST-TLVAPVGKDARADTIRHYLADEPLRSELIEMEDASSDVSIIFrLPGGENAIVTTTESA 112
Cdd:PTZ00247 62 GGSALNTARVaqwMLQAPKGFvCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVL-VCGKERSLVANLGAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 113 QSLSL-----SDVRRILSTAGsgdLMILQG---NLSDRTTRDILEHARAIGMVTAFNPSPV--RSYFSD----LWDLIDI 178
Cdd:PTZ00247 141 NHLSAehmqsHAVQEAIKTAQ---LYYLEGfflTVSPNNVLQVAKHARESGKLFCLNLSAPfiSQFFFErllqVLPYVDI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 179 AFLNKGEAQALT-----GTTG------RDAAE--YLLSRGlREIVLTLGGDgATLVNRHD---SIEVPA-QVCEVVDTTG 241
Cdd:PTZ00247 218 LFGNEEEAKTFAkamkwDTEDlkeiaaRIAMLpkYSGTRP-RLVVFTQGPE-PTLIATKDgvtSVPVPPlDQEKIVDTNG 295
|
250 260
....*....|....*....|..
gi 499969019 242 AGDTFMAAALASCALrGQRLDR 263
Cdd:PTZ00247 296 AGDAFVGGFLAQYAN-GKDIDR 316
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
196-251 |
4.17e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 44.30 E-value: 4.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499969019 196 DAAEYLLSRGLREIVLTLGGDGATLVNrhDSIEVPAQ--VCEVVDTTGAGDTfMAAAL 251
Cdd:PRK09513 207 EAAHALREQGIAHVVISLGAEGALWVN--ASGEWIAKppACDVVSTVGAGDS-MVGGL 261
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
142-261 |
4.21e-05 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 44.32 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 142 RTTRDILEHARAIGMVTAFNPSPVRSYFSDLWDLI---DIAFLNKGEAQALTGTTGRDAAEYLLSRGLREIVL--TLGGD 216
Cdd:cd01939 143 RMMQHIEEHNNRRPEIRITISVEVEKPREELLELAaycDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLvcTWGDQ 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499969019 217 GATLVNRHDSI-EVPAQVCE-VVDTTGAGDTFMAAALASCALRGQRL 261
Cdd:cd01939 223 GAGALGPDGEYvHSPAHKPIrVVDTLGAGDTFNAAVIYALNKGPDDL 269
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
37-251 |
1.12e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.80 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 37 GGKGTNQAVVMARCGVSTTLVAPVGKDARADTIRHYLADEPLrseliemedassDVSIIFRLPGgeNAIVTTTEsaqsls 116
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGV------------DISHVHTKHG--VTAQTQVE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 117 LSDVRRILSTAGSG---DLMILQGNLSDRTTRDILEHA------------RAIGMVTAFNpspvrsyFSDLWD------- 174
Cdd:PRK09813 83 LHDNDRVFGDYTEGvmaDFALSEEDYAWLAQYDIVHAAiwghaedafpqlHAAGKLTAFD-------FSDKWDsplwqtl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969019 175 --LIDIAF-LNKGEAQALtgttgRDAAEYLLSRGLREIVLTLGGDGATLVNRHDSIEVPAQVCEVVDTTGAGDTFMAAAL 251
Cdd:PRK09813 156 vpHLDYAFaSAPQEDEFL-----RLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFL 230
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
205-256 |
5.31e-03 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 38.27 E-value: 5.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499969019 205 GLREIVLTLGGDGATLVNR-HDSIEVPAQVCEVVDTTGAGDTF---MAAALA-------SCAL 256
Cdd:PRK11316 224 DLSALLVTRSEQGMTLLQPgKAPLHLPTQAREVYDVTGAGDTVisvLAAALAagnsleeACAL 286
|
|
| |
