|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-309 |
2.14e-80 |
|
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: 246.31 E-value: 2.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAH 80
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDafGDELLENLREEGIDVSY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 VEMRADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVSDLKQGDVLLLQNETN--AIRDAIEIGLEKGLRIVFN 158
Cdd:cd01174 82 VEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPleTVLAALRAARRAGVTVILN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 159 PAPFdRSVPLLPLNQTAALILNEGEARGLYSMDEAAAEnlDDLELLTALGERYPNsTLLITLGARGVAVRIPGQSpKLFP 238
Cdd:cd01174 162 PAPA-RPLPAELLALVDILVPNETEAALLTGIEVTDEE--DAEKAARLLLAKGVK-NVIVTLGAKGALLASGGEV-EHVP 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821498934 239 AYRVDaVVDTTAAGDTFTGYAVRALTlawnaeeKGEDparcraiLEDGIKYAVTAAALSVTRAGAAESIPH 309
Cdd:cd01174 237 AFKVK-AVDTTGAGDTFIGALAAALA-------RGLS-------LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
7-308 |
5.41e-63 |
|
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: 201.68 E-value: 5.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 7 GSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHVEMR 84
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDafGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 85 ADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVSDLKQGDVLLLQNET--NAIRDAIEIGLEKGLRIVFNPAPF 162
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIplETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 163 DRSVPLLPLNQTAALILNEGEAR---GLYSMDEAAAEnlddlELLTALGERYPNsTLLITLGARGVAVRIPGQSpKLFPA 239
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEiltGIEVTDEEDAE-----KAAEKLLEKGVK-NVIITLGSKGALLVSKDES-KLIPA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821498934 240 YRVDAVvDTTAAGDTFTGYAVRALtlawnaeEKGEDparcraiLEDGIKYAVTAAALSVTRAGAAESIP 308
Cdd:TIGR02152 234 FKVKAV-DTTAAGDTFNGAFAVAL-------AEGKS-------LEDAIRFANAAAAISVTRKGAQSSIP 287
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-313 |
9.36e-58 |
|
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: 188.55 E-value: 9.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 2 HVLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVA 79
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDpfGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 80 HVEMRADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVsdLKQGDVLLLQNET-------NAIRDAIEIGLEKG 152
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGITlasepprEALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 153 LRIVFNPAP----FDRSVPLLP--LNQTAALILNEGEARGLYSMDEAAaenlddlELLTALGERYPnSTLLITLGARGVA 226
Cdd:COG0524 159 VPVSLDPNYrpalWEPARELLRelLALVDILFPNEEEAELLTGETDPE-------EAAAALLARGV-KLVVVTLGAEGAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 227 VRIPGQSpKLFPAYRVDaVVDTTAAGDTFTGYAVRALTlawnaeeKGEDPARCrailedgIKYAVTAAALSVTRAGAAES 306
Cdd:COG0524 231 LYTGGEV-VHVPAFPVE-VVDTTGAGDAFAAGFLAGLL-------EGLDLEEA-------LRFANAAAALVVTRPGAQPA 294
|
....*..
gi 1821498934 307 IPHFEVV 313
Cdd:COG0524 295 LPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
6-315 |
2.20e-52 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 174.67 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 6 IGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHVEM 83
Cdd:PRK11142 8 LGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDsiGESMRQQLAKDGIDTAPVSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 84 RADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVSDLKQGDVLLLQNET--NAIRDAIEIGLEKGLRIVFNPAP 161
Cdd:PRK11142 88 IKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETplETVLAAAKIAKQHGTKVILNPAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 162 fDRSVP--LLPL------NQTAALILNEGEARGLYSMDEAAAenlddleLLTALGErypnSTLLITLGARGVAVRIPGQS 233
Cdd:PRK11142 168 -ARELPdeLLALvdiitpNETEAEKLTGIRVEDDDDAAKAAQ-------VLHQKGI----ETVLITLGSRGVWLSENGEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 234 pKLFPAYRVDAvVDTTAAGDTFTGYAVRALTlawnaEEKGedparcraiLEDGIKYAVTAAALSVTRAGAAESIPHFEVV 313
Cdd:PRK11142 236 -QRVPGFRVQA-VDTIAAGDTFNGALVTALL-----EGKP---------LPEAIRFAHAAAAIAVTRKGAQPSIPWREEI 299
|
..
gi 1821498934 314 DA 315
Cdd:PRK11142 300 DA 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-317 |
8.82e-47 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 160.67 E-value: 8.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPHFLRGGETVAAyrRTLHV--GGKGLNQSVALARAGIASSHAGIIGRDG---EVLKNFlEAEGVN 77
Cdd:PTZ00292 18 VVVVGSSNTDLIGYVDRMPQVGETLHG--TSFHKgfGGKGANQAVMASKLGAKVAMVGMVGTDGfgsDTIKNF-KRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 78 VAHVEMRADEASGHTVIQISPE-GENAILYYPGTNTCLTREFVKNAVSDLKQ-GDVLLLQNET--NAIRDAIEIGLEKGL 153
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIplETTLDALKEAKERGC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 154 RIVFNPAP------FDRSVPLLPLNQTaaLILNEGEARGLYSMDEA-AAENLDDLELLTALGERypnsTLLITLGARGVA 226
Cdd:PTZ00292 175 YTVFNPAPapklaeVEIIKPFLKYVSL--FCVNEVEAALITGMEVTdTESAFKASKELQQLGVE----NVIITLGANGCL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 227 VRIPGQSPKLFPAYRVDAVvDTTAAGDTFTGYAVRALTLAWNaeekgedparcraiLEDGIKYAVTAAALSVTRAGAAES 306
Cdd:PTZ00292 249 IVEKENEPVHVPGKRVKAV-DTTGAGDCFVGSMAYFMSRGKD--------------LKESCKRANRIAAISVTRHGTQSS 313
|
330
....*....|.
gi 1821498934 307 IPHFEVVDAVV 317
Cdd:PTZ00292 314 YPHPSELPADV 324
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-305 |
1.22e-33 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 125.15 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 6 IGSLNID---NVYQVPhflrgGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAH 80
Cdd:pfam00294 5 IGEANIDligNVEGLP-----GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDnfGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 VEMRADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVSDLKQGDV------LLLQNETNAIRDAIEIGLEKGL- 153
Cdd:pfam00294 80 VVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLlyisgsLPLGLPEATLEELIEAAKNGGTf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 154 -RIVFNPAPFDRSVPLLPLNQTAALILNEGEARGLYSMDEAAAENLddLELLTALGERYPNsTLLITLGARGVAVRIPGQ 232
Cdd:pfam00294 160 dPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEA--LAALHKLLAKGIK-TVIVTLGADGALVVEGDG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821498934 233 SPKLFPAYRVDaVVDTTAAGDTFTGyavrALTLAWNAEEKgedparcraiLEDGIKYAVTAAALSVTRAGAAE 305
Cdd:pfam00294 237 EVHVPAVPKVK-VVDTTGAGDSFVG----GFLAGLLAGKS----------LEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
3-303 |
5.07e-29 |
|
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: 112.40 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAH 80
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDfhGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 VEMRADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVSDLkqgDVLLLQNETNAIRDAIEIGLEkGLRIVFNP- 159
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPDGLA---DIVHLSSGPGLIELARELAAG-GITVSFDPg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 160 ---APFDRSVPLLPLNQTAALILNEGEARGLYSMDeaaaeNLDDLELLTALGerypnsTLLITLGARGVAVRIPGQSpKL 236
Cdd:cd01942 158 qelPRLSGEELEEILERADILFVNDYEAELLKERT-----GLSEAELASGVR------VVVVTLGPKGAIVFEDGEE-VE 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821498934 237 FPAYRVDAVVDTTAAGDTFTGyavrALTLAWnaeEKGEDparcraiLEDGIKYAVTAAALSVTRAGA 303
Cdd:cd01942 226 VPAVPAVKVVDTTGAGDAFRA----GFLYGL---LRGYD-------LEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-303 |
3.63e-24 |
|
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: 99.63 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQvphflrGGETVAAYRRtlHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAH 80
Cdd:cd01167 2 VVCFGEALIDFIPE------GSGAPETFTK--APGGAPANVAVALARLGGKAAFIGKVGDDefGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 VEMRADEASGHTVIQISPEGE-NAILYYPGTNTCLTREFVKNAVsdLKQGDVLL-----LQNETN--AIRDAIEIGLEKG 152
Cdd:cd01167 74 IQFDPAAPTTLAFVTLDADGErSFEFYRGPAADLLLDTELNPDL--LSEADILHfgsiaLASEPSrsALLELLEAAKKAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 153 LRIVFNP-----------APFDRSVPLLPLnqtAALI-LNEGEARGLYSMDeaaaenldDLELLTALGERYPNSTLLITL 220
Cdd:cd01167 152 VLISFDPnlrpplwrdeeEARERIAELLEL---ADIVkLSDEELELLFGEE--------DPEEIAALLLLFGLKLVLVTR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 221 GARGVAVRIPGQSpKLFPAYRVDaVVDTTAAGDTFTGYAVRALTlawnaeeKGEDPARCRAILEDGIKYAVTAAALSVTR 300
Cdd:cd01167 221 GADGALLYTKGGV-GEVPGIPVE-VVDTTGAGDAFVAGLLAQLL-------SRGLLALDEDELAEALRFANAVGALTCTK 291
|
...
gi 1821498934 301 AGA 303
Cdd:cd01167 292 AGA 294
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-302 |
4.96e-20 |
|
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: 88.25 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGkGLNQSVALARAGIASSHAGIIG--RDGEVLKNFLEAEGVNVAh 80
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGngNWADQIRQAMRDEGIEIL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 VEMRADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAvsDLKQGDVLLLQNET----NAIRDAI---EIGLEKGL 153
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATL--TVAPYDYVYLSGYTlaseNASKVILlewLEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 154 RIVFNPAPFDRSVPLLPLNQTAALI----LNEGEArglysmdEAAAENLDDLELLTALGERYP-NSTLLITLGARGVAVR 228
Cdd:cd01944 158 TLVFDPGPRISDIPDTILQALMAKRpiwsCNREEA-------AIFAERGDPAAEASALRIYAKtAAPVVVRLGSNGAWIR 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821498934 229 IPGQSPKLFPAYRVDAvVDTTAAGDTFTGYAVRALTlawnaeeKGEDPArcraileDGIKYAVTAAALSVTRAG 302
Cdd:cd01944 231 LPDGNTHIIPGFKVKA-VDTIGAGDTHAGGMLAGLA-------KGMSLA-------DAVLLANAAAAIVVTRSG 289
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
34-304 |
5.19e-20 |
|
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: 88.40 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 34 LHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHVEMRADEASGHTVIQISPEGENAILYYpgTN 111
Cdd:cd01166 28 KFFGGAEANVAVGLARLGHRVALVTAVGDDpfGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIGAGGERRVLYY--RA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 112 TCLTREFVKNAVS--DLKQGDVL--------LLQNETNAIRDAIEIGLEKGLRIVFNPapfdrsvpllplNQTAALILNE 181
Cdd:cd01166 106 GSAASRLTPEDLDeaALAGADHLhlsgitlaLSESAREALLEALEAAKARGVTVSFDL------------NYRPKLWSAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 182 gEARGLYSmdEAAAE------NLDDLELLT-----------ALGERYPNSTLLITLGARGVAVRIPGQSpKLFPAYRVDa 244
Cdd:cd01166 174 -EAREALE--ELLPYvdivlpSEEEAEALLgdedptdaaerALALALGVKAVVVKLGAEGALVYTGGGR-VFVPAYPVE- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 245 VVDTTAAGDTFTGYAVRALTlawnaeeKGEDPARCrailedgIKYAVTAAALSVTRAGAA 304
Cdd:cd01166 249 VVDTTGAGDAFAAGFLAGLL-------EGWDLEEA-------LRFANAAAALVVTRPGDI 294
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
2-309 |
1.51e-14 |
|
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: 72.71 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 2 HVLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVA 79
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDaiGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 80 HVEMRADEASGHTVIqISPEGENAILYYPGTNTCLTREFVKNAvsDLKQGDVLLLQN-----ETNAIRDAIEIGLEKGLR 154
Cdd:cd01945 81 FIVVAPGARSPISSI-TDITGDRATISITAIDTQAAPDSLPDA--ILGGADAVLVDGrqpeaALHLAQEARARGIPIPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 155 I-VFNPAPFDRsvpLLPLNQTAALILNEGEARGLYSMDEAaaenlddLELLTALGerypNSTLLITLGARGVAVRIPGQS 233
Cdd:cd01945 158 LdGGGLRVLEE---LLPLADHAICSENFLRPNTGSADDEA-------LELLASLG----IPFVAVTLGEAGCLWLERDGE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821498934 234 PKLFPAYRVDaVVDTTAAGDTFTGyavrALTLAWNAeekGEDparcraiLEDGIKYAVTAAALSVTRAGAAESIPH 309
Cdd:cd01945 224 LFHVPAFPVE-VVDTTGAGDVFHG----AFAHALAE---GMP-------LREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-298 |
2.56e-14 |
|
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: 71.96 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPHFLRGGETVAAyRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNvah 80
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPG-HVKQSPGGVGRNIAENLARLGVSVALLSAVGDDseGESILEESEKAGLN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 81 veMRADEASGH-TVIQISPEGENAILYY----PGTNTCLTREFVKNAVSDLKQGDVLLLqnETN----AIRDAIEIGLEK 151
Cdd:cd01941 78 --VRGIVFEGRsTASYTAILDKDGDLVValadMDIYELLTPDFLRKIREALKEAKPIVV--DANlpeeALEYLLALAAKH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 152 GLRIVFNPAPFDRSVPLL-PLNQTAALILNEGEARGLYsmdEAAAENLDDL--ELLTALGERYPNstLLITLGARGVAV- 227
Cdd:cd01941 154 GVPVAFEPTSAPKLKKLFyLLHAIDLLTPNRAELEALA---GALIENNEDEnkAAKILLLPGIKN--VIVTLGAKGVLLs 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821498934 228 -RIPGQSPKLFPAYRVDAVVDTTAAGDTFTGYAVRALTlawnaeeKGEDPARCrailedgIKYAVTAAALSV 298
Cdd:cd01941 229 sREGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLL-------EGMSLDDS-------LRFAQAAAALTL 286
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
37-309 |
1.44e-13 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 69.96 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 37 GGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHveMRADEAsgHT----VIQISPEGENAILYY--P 108
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDpfGRFMQQTLQDEGVDTTY--LRLDPA--HRtstvVVDLDDQGERSFTFMvrP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 109 GTNTCLTrefvknaVSDL---KQGDVLL-----LQNETN---------AIRDAieiglekGLRIVFNPAPFD---RSVPL 168
Cdd:PRK09434 104 SADLFLQ-------PQDLppfRQGEWLHlcsiaLSAEPSrsttfeamrRIKAA-------GGFVSFDPNLREdlwQDEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 169 LP--LNQTAALI----LNEGEARGLysmdeaaaENLDDLEL-LTALGERYPNSTLLITLGARGVAVRIPGQSpKLFPAYR 241
Cdd:PRK09434 170 LRecLRQALALAdvvkLSEEELCFL--------SGTSQLEDaIYALADRYPIALLLVTLGAEGVLVHTRGQV-QHFPAPS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821498934 242 VDaVVDTTAAGDTFTGYAVRALTLAWNAEEKgedparcrAILEDGIKYAVTAAALSVTRAGAAESIPH 309
Cdd:PRK09434 241 VD-PVDTTGAGDAFVAGLLAGLSQAGLWTDE--------AELAEIIAQAQACGALATTAKGAMTALPN 299
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-303 |
4.61e-13 |
|
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: 68.79 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 3 VLNIGSLNIDNVYQVPH-FL----------------RGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD-- 63
Cdd:cd01168 4 VLGLGNALVDILAQVDDaFLeklglkkgdmiladmeEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDkl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 64 GEVLKNFLEAEGVNVAHVEMrADEASGHTVIQISPEGENAILYYPGTNTCLTREFVKNAVsdLKQGDVL-----LLQNET 138
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQVQ-PDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAKYLylegyLLTVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 139 NAIRDAIEIGLEKGLRIVFN-PAPF--DRS-VPLLPLNQTAALIL-NEGEARGLYSmdeaaAENLDDLELLTALGERYPn 213
Cdd:cd01168 161 EAILLAAEHAKENGVKIALNlSAPFivQRFkEALLELLPYVDILFgNEEEAEALAE-----AETTDDLEAALKLLALRC- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 214 STLLITLGARGVAVRIPGQSPKLfPAYRVDAVVDTTAAGDTFTGYAVRALTlawnaeeKGEDPARCrailedgIKYAVTA 293
Cdd:cd01168 235 RIVVITQGAKGAVVVEGGEVYPV-PAIPVEKIVDTNGAGDAFAGGFLYGLV-------QGEPLEEC-------IRLGSYA 299
|
330
....*....|
gi 1821498934 294 AALSVTRAGA 303
Cdd:cd01168 300 AAEVIQQLGP 309
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-283 |
1.45e-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: 63.59 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 6 IGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRDGEVLKNFLEAEGVNVAHVEMRA 85
Cdd:cd01947 5 VGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 86 DEASGHTVIQISPEGENAILYyPGTNTCLTREFVknavsDLKQGDVLLLqNETNAIRDAIEIGLEKGLRIvFNPAPFDRS 165
Cdd:cd01947 85 DKPTRKTLSFIDPNGERTITV-PGERLEDDLKWP-----ILDEGDGVFI-TAAAVDKEAIRKCRETKLVI-LQVTPRVRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 166 VPLLPLNQ-TAALILNEGEARGLYSMDEAAAENLDdlelltalgerypnsTLLITLGARGVAVrIPGQSPKLFPAYRVDa 244
Cdd:cd01947 157 DELNQALIpLDILIGSRLDPGELVVAEKIAGPFPR---------------YLIVTEGELGAIL-YPGGRYNHVPAKKAK- 219
|
250 260 270
....*....|....*....|....*....|....*....
gi 1821498934 245 VVDTTAAGDTFTGYAVRALTLAWNAEEKGEDPARCRAIL 283
Cdd:cd01947 220 VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAIC 258
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
9-320 |
1.80e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 64.00 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 9 LN--IDNVYQVPHFLRGgETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD-GEVLKNFLEAEGVNVAHVEMRA 85
Cdd:COG1105 6 LNpaLDRTYEVDELEPG-EVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFtGEFIEELLDEEGIPTDFVPIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 86 D--------EASGHTVIQISPEG----ENAIlyypgtntcltREFVKNAVSDLKQGDVLLL-----QN-ETNAIRDAIEI 147
Cdd:COG1105 85 EtrinikivDPSDGTETEINEPGpeisEEEL-----------EALLERLEELLKEGDWVVLsgslpPGvPPDFYAELIRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 148 GLEKGLRIVF--NPAPFDRSVPLLPLnqtaaLI-LNEGEARGLYSMDeaaaenLDDLELLTALGERYPNS---TLLITLG 221
Cdd:COG1105 154 ARARGAKVVLdtSGEALKAALEAGPD-----LIkPNLEELEELLGRP------LETLEDIIAAARELLERgaeNVVVSLG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 222 ARGVAVRIPGQspklfpAYRVDA----VVDTTAAGDTFTGyavrALTLAWnaeEKGEDParcrailEDGIKYAVTAAALS 297
Cdd:COG1105 223 ADGALLVTEDG------VYRAKPpkveVVSTVGAGDSMVA----GFLAGL---ARGLDL-------EEALRLAVAAGAAA 282
|
330 340
....*....|....*....|...
gi 1821498934 298 VTRAGAAesIPHFEVVDAVVADL 320
Cdd:COG1105 283 ALSPGTG--LPDREDVEELLAQV 303
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
27-308 |
3.88e-11 |
|
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: 62.96 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 27 VAAYRRTLHVGGKGlNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHVEmraDE-----------ASGHTV 93
Cdd:cd01172 30 VKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDDeaGDLLRKLLEKEGIDTDGIV---DEgrptttktrviARNQQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 94 IQISPEGEnailyYPGTNTCLTREfVKNAVSDLKQGDVLLLQN------ETNAIRDAIEIGLEKGLRIVFNPAPFDRSvp 167
Cdd:cd01172 106 LRVDREDD-----SPLSAEEEQRL-IERIAERLPEADVVILSDygkgvlTPRVIEALIAAARELGIPVLVDPKGRDYS-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 168 llpLNQTAALI-LNEGEARGLYSMDEAAAENLDdlELLTALGERYPNSTLLITLGARGVAVRIPGQSPKLFPAYrVDAVV 246
Cdd:cd01172 178 ---KYRGATLLtPNEKEAREALGDEINDDDELE--AAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQHIPAL-AKEVY 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821498934 247 DTTAAGDTFTgyAVRALTLAwnaeekgedpARCRaiLEDGIKYAVTAAALSVTRAGAAESIP 308
Cdd:cd01172 252 DVTGAGDTVI--ATLALALA----------AGAD--LEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
11-315 |
2.04e-09 |
|
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: 57.59 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 11 IDNVYQVPHFLRGGETVAAYRRtLHVGGKGLNQSVALARAGIASSHAGIIGRD-GEVLKNFLEAEGVNVAHVemradEAS 89
Cdd:TIGR03168 10 IDLTIEVDGLTPGEVNRVAAVR-KDAGGKGINVARVLARLGAEVVATGFLGGFtGEFIEALLAEEGIKNDFV-----EVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 90 GHTVIQI---SPEGENAILYYPG---TNTCLtREFVKNAVSDLKQGDVLLLQN------ETNAIRDAIEIGLEKGLRIVf 157
Cdd:TIGR03168 84 GETRINVkikESSGEETELNEPGpeiSEEEL-EQLLEKLRELLASGDIVVISGslppgvPPDFYAQLIAIARKKGAKVI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 158 npapFDRSVPLLplnqTAALilnegEARGLYSM---DEAAA------ENLDDL-----ELLTALGERypnstLLITLGAR 223
Cdd:TIGR03168 162 ----LDTSGEAL----REAL-----AAKPFLIKpnhEELEElfgrelKTLEEIieaarELLDRGAEN-----VLVSLGAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 224 GVAVRIPGQspklfpAYRVDA----VVDTTAAGDTFtgyaVRALTLAWnaeEKGEDPARCrailedgIKYAVTAAALSVT 299
Cdd:TIGR03168 224 GALLVTKEG------ALKATPpkveVVNTVGAGDSM----VAGFLAGL---ARGLSLEEA-------LRFAVAAGSAAAF 283
|
330
....*....|....*.
gi 1821498934 300 RAGAAesIPHFEVVDA 315
Cdd:TIGR03168 284 SPGTG--LPDPEDVEE 297
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
11-304 |
2.18e-08 |
|
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: 54.46 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 11 IDNVYQVPHFLRGgETVAAYRRTLHVGGKGLNQSVALARAGIASSHAGIIGRD-GEVLKNFLEAEGVNVAHVemradEAS 89
Cdd:cd01164 11 IDLTIELDQLQPG-EVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFtGDFFEALLKEEGIPDDFV-----EVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 90 GHTVIQI---SPEGENAILYYPG---TNTCLtREFVKNAVSDLKQGDVLLLQNE------TNAIRDAIEIGLEKGLRIVF 157
Cdd:cd01164 85 GETRINVkikEEDGTETEINEPGpeiSEEEL-EALLEKLKALLKKGDIVVLSGSlppgvpADFYAELVRLAREKGARVIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 158 --NPAPFDRSVPLLPLnqtaaLI-LNEGEARGLYSmdeAAAENLDDL-ELLTALGERYPnSTLLITLGARGvAVRIPGQS 233
Cdd:cd01164 164 dtSGEALLAALAAKPF-----LIkPNREELEELFG---RPLGDEEDViAAARKLIERGA-ENVLVSLGADG-ALLVTKDG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821498934 234 pklfpAYRVDA----VVDTTAAGDTFtgyaVRALTLAWnaeEKGEDParcrailEDGIKYAVTAAALSVTRAGAA 304
Cdd:cd01164 234 -----VYRASPpkvkVVSTVGAGDSM----VAGFVAGL---AQGLSL-------EEALRLAVAAGSATAFSPGTG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
31-281 |
2.61e-08 |
|
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: 53.90 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 31 RRTLHVGGKGLNQSVALARAGIASSHAGIIGRD--GEVLKNFLEAEGVNVAHVEMRadeasghtviqispEGENAIlyyp 108
Cdd:cd01940 16 LGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDdaGAHVRSTLKRLGVDISHCRVK--------------EGENAV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 109 gtnTCLT-----REFV---KNAVSDLkqgdvLLLQNETNAIR--DAIEIG-------LEKGLR-IVFNPAP--FDRSVpl 168
Cdd:cd01940 78 ---ADVElvdgdRIFGlsnKGGVARE-----HPFEADLEYLSqfDLVHTGiysheghLEKALQaLVGAGALisFDFSD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 169 lplNQTAALIlnegeARGLYSMDEAA--AENLDDLELLTALGE--RYPNSTLLITLGARGVAVRIPGQSpkLFPAYRVDA 244
Cdd:cd01940 148 ---RWDDDYL-----QLVCPYVDFAFfsASDLSDEEVKAKLKEavSRGAKLVIVTRGEDGAIAYDGAVF--YSVAPRPVE 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1821498934 245 VVDTTAAGDTF-TGYAVRALTLAWNAEEKGEDPARCRA 281
Cdd:cd01940 218 VVDTLGAGDSFiAGFLLSLLAGGTAIAEAMRQGAQFAA 255
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
2-257 |
3.14e-08 |
|
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: 52.87 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 2 HVLNIGSLNIDNVYQVPHFLRGGETVAAYRRTLHVGGKGLNQSVALARAGIassHAGIIGRDGEVLknfleaegvnvahv 81
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGV---SVTLVGADAVVI-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 82 emradeasghTVIQISPEgenailyypgtntcltrefvknavsdlkqgdvlllqnetnAIRDAIEIGLEKGLRIVFNPAP 161
Cdd:cd00287 64 ----------SGLSPAPE----------------------------------------AVLDALEEARRRGVPVVLDPGP 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 162 FDRSVPLLP----LNQTAALILNEGEARGLysMDEAAAENLDDLELLTALGERYPNsTLLITLGARGVAVRIPGQSPKLF 237
Cdd:cd00287 94 RAVRLDGEEleklLPGVDILTPNEEEAEAL--TGRRDLEVKEAAEAAALLLSKGPK-VVIVTLGEKGAIVATRGGTEVHV 170
|
250 260
....*....|....*....|
gi 1821498934 238 PAYRVDaVVDTTAAGDTFTG 257
Cdd:cd00287 171 PAFPVK-VVDTTGAGDAFLA 189
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
177-257 |
3.18e-05 |
|
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: 44.76 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 177 LILNEGEAR---GLYSMDEAAaenlddlELLTALGERypnsTLLITLGARGVAVrIPGQSPKLFPAYRVDAVVDTTAAGD 253
Cdd:cd01946 167 VIINDGEARqltGAANLVKAA-------RLILAMGPK----ALIIKRGEYGALL-FTDDGYFAAPAYPLESVFDPTGAGD 234
|
....
gi 1821498934 254 TFTG 257
Cdd:cd01946 235 TFAG 238
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
154-324 |
1.58e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 39.63 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 154 RIVFNPAPfDRSVP--LLPLNQTAALIL----NEGEARGLYSMDEAAAENLD------DLELLTALGERyPNSTLLITLG 221
Cdd:cd01943 156 KIVWEPLP-DSCDPenLEDLLQALPRVDvfspNLEEAARLLGLPTSEPSSDEekeavlQALLFSGILQD-PGGGVVLRCG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 222 ARGVAVRIPGQSPKL-FPAYRVDA--VVDTTAAGDTFTGYAVRALtlawnAEEKGEDPARCrailedgikYAVTAAALSV 298
Cdd:cd01943 234 KLGCYVGSADSGPELwLPAYHTKStkVVDPTGGGNSFLGGFAAGL-----ALTKSIDEACI---------YGSVAASFAI 299
|
170 180
....*....|....*....|....*.
gi 1821498934 299 TRAGaaesIPHFEVVDAvvADLWDTE 324
Cdd:cd01943 300 EQVG----LPRLTKVEG--EELWNGE 319
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
216-313 |
7.87e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 37.68 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821498934 216 LLITLGARGVAVRIPGQSPKLfPAYRVDAVvDTTAAGDTFTGYAVRALtlawnAEEKG--EDPARCRAILedgiKYAVTA 293
Cdd:PLN02323 233 LLVTEGEEGCRYYTKDFKGRV-EGFKVKAV-DTTGAGDAFVGGLLSQL-----AKDLSllEDEERLREAL----RFANAC 301
|
90 100
....*....|....*....|
gi 1821498934 294 AALSVTRAGAAESIPHFEVV 313
Cdd:PLN02323 302 GAITTTERGAIPALPTKEAV 321
|
|
| |
