|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
70-367 |
8.62e-116 |
|
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: 338.37 E-value: 8.62e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcGVH 149
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE--GID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEiMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVP 229
Cdd:cd01174 79 VSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPA-DVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 230 VILDVGGMDtPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEkpiqQ 309
Cdd:cd01174 158 VILNPAPAR-PLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGE----V 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 310 SIIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPD 367
Cdd:cd01174 233 EHVPAFKVkaVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
75-371 |
3.47e-93 |
|
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: 280.64 E-value: 3.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 75 GSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVR 154
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNG--IDTEYVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 155 SVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDV 234
Cdd:TIGR02152 79 TVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDI-DAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 235 GGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGEKpiqQSIIPA 314
Cdd:TIGR02152 158 APAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKG-ALLVSKDE---SKLIPA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220039 315 --AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSV 371
Cdd:TIGR02152 234 fkVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
71-371 |
9.15e-84 |
|
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: 257.12 E-value: 9.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHL 150
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAEL--RAEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEimsDDDLEIVRNAGIVLLQ-----REIPDSINIQVAKAVKK 225
Cdd:COG0524 80 SGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPE---DLDEALLAGADILHLGgitlaSEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 226 AGVPVILDVGGMD------TPIPNELLDSIDILSPNETELSRLTGMPTetfeqISQAVAKCHKLGVKQVLVKLGSKGSAL 299
Cdd:COG0524 157 AGVPVSLDPNYRPalwepaRELLRELLALVDILFPNEEEAELLTGETD-----PEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220039 300 FIQGEkpiqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSV 371
Cdd:COG0524 232 YTGGE----VVHVPAfpVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
71-375 |
1.49e-68 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 218.20 E-value: 1.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHL 150
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDG--IDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPV 230
Cdd:PRK11142 83 APVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALV-EAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 231 ILDVGGMdTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGekpiQQS 310
Cdd:PRK11142 162 ILNPAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENG----EGQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220039 311 IIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLL 375
Cdd:PRK11142 237 RVPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
71-362 |
4.31e-65 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 208.74 E-value: 4.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPkeGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHL 150
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQEL--KKEGVDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIV----LLQREIPDSINIQVAKAVKKA 226
Cdd:pfam00294 78 DYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEEL-EENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 227 G--VPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGE 304
Cdd:pfam00294 157 GtfDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADG-ALVVEGD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220039 305 KPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAI 362
Cdd:pfam00294 236 GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
68-368 |
9.35e-58 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 191.10 E-value: 9.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 68 APPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcG 147
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRN--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 148 VHLDYVRSVNNEPTGHAVVML-QSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKA 226
Cdd:PTZ00292 93 VNTSFVSRTENSSTGLAMIFVdTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 227 GVPVILDVggmdTPIPN--------ELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSA 298
Cdd:PTZ00292 173 GCYTVFNP----APAPKlaeveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCL 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220039 299 LFIQGEKPIQqsiIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDR 368
Cdd:PTZ00292 249 IVEKENEPVH---VPGKRVkaVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHP 317
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
70-362 |
3.93e-44 |
|
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: 154.01 E-value: 3.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVH 149
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEG--VD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LDYVRSVNNEPTGHAVVMlqSDGQNSIIIVG--GANMKAWPEIMSDDDleivRNAGIVLLQREIPDsinIQVAKAVKKAG 227
Cdd:cd01942 79 TSHVRVVDEDSTGVAFIL--TDGDDNQIAYFypGAMDELEPNDEADPD----GLADIVHLSSGPGL---IELARELAAGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 228 VPVILDVGGMDTPIPNELLDSI----DILSPNETE---LSRLTGMPTEtfeqisqAVAKchklGVKQVLVKLGSKGSALF 300
Cdd:cd01942 150 ITVSFDPGQELPRLSGEELEEIleraDILFVNDYEaelLKERTGLSEA-------ELAS----GVRVVVVTLGPKGAIVF 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220039 301 IQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAI 362
Cdd:cd01942 219 EDGEE-VEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
105-362 |
3.20e-41 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 146.57 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 105 GGKGANqAACG-AKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHldYVRSVNNEPTGHAVVMLQSDGQNSIIIV--GG 181
Cdd:cd01166 31 GGAEAN-VAVGlARLGHRVALVTAVGDDPFGRFILAELRREGVDTS--HVRVDPGRPTGLYFLEIGAGGERRVLYYraGS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 182 ANMKAWPEimsDDDLEIVRNA------GIVLLQREIPDSINIQVAKAVKKAGVPVILDV------GGMDTPIP--NELLD 247
Cdd:cd01166 108 AASRLTPE---DLDEAALAGAdhlhlsGITLALSESAREALLEALEAAKARGVTVSFDLnyrpklWSAEEAREalEELLP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 248 SIDILSPNETELSRLTGMPTETfEQIsqAVAKCHKLGVKQVLVKLGSKGSALFIQGEKpiQQSIIPAAQVVDTTGAGDTF 327
Cdd:cd01166 185 YVDIVLPSEEEAEALLGDEDPT-DAA--ERALALALGVKAVVVKLGAEGALVYTGGGR--VFVPAYPVEVVDTTGAGDAF 259
|
250 260 270
....*....|....*....|....*....|....*
gi 15220039 328 TAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAI 362
Cdd:cd01166 260 AAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
80-376 |
3.42e-39 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 141.43 E-value: 3.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 80 DIYVEIERLpKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAhGKLIAEALgdDGCGVHLDYVRSvnNE 159
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELL--DEEGIPTDFVPI--EG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 160 PTGHAVVML-QSDGQNSIIIVGGanmkawPEImSDDDLE--------IVRNAGIVL----LQREIPDSINIQVAKAVKKA 226
Cdd:COG1105 85 ETRINIKIVdPSDGTETEINEPG------PEI-SEEELEallerleeLLKEGDWVVlsgsLPPGVPPDFYAELIRLARAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 227 GVPVILDVGGmdtpipnELLD-----SIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFI 301
Cdd:COG1105 158 GAKVVLDTSG-------EALKaaleaGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADG-ALLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220039 302 QGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAipSMPDRKSVLKLLK 376
Cdd:COG1105 230 TEDG-VYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGT--GLPDREDVEELLA 301
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
80-360 |
7.77e-36 |
|
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: 132.27 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 80 DIYVEIERLpKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDaHGKLIAEALGDDGcgvhLDYVRSVNNE 159
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEG----IPDDFVEVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 160 PTGHAVVMLQSDGQNSIIivggaNMKAwPEImSDDDLE--------IVRNAGIVL----LQREIPDSINIQVAKAVKKAG 227
Cdd:cd01164 86 ETRINVKIKEEDGTETEI-----NEPG-PEI-SEEELEalleklkaLLKKGDIVVlsgsLPPGVPADFYAELVRLAREKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 228 VPVILDVGGmdtpipNELLDSI----DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQG 303
Cdd:cd01164 159 ARVILDTSG------EALLAALaakpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADG-ALLVTK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220039 304 EKPIQqSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKG 360
Cdd:cd01164 232 DGVYR-ASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
70-357 |
4.82e-35 |
|
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: 130.13 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 70 PLVVVGSANADI--YVEIERLPkeGETISAKTGQTlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEAL---GDD 144
Cdd:cd01941 1 EIVVIGAANIDLrgKVSGSLVP--GTSNPGHVKQS-PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESekaGLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 145 gcgvhlDYVRSVNNEPTGHAVVMLQSDGQnsiIIVGGANMKAWpEIMSDDDL----EIVRNAGIVLLQREIPDSINIQVA 220
Cdd:cd01941 78 ------VRGIVFEGRSTASYTAILDKDGD---LVVALADMDIY-ELLTPDFLrkirEALKEAKPIVVDANLPEEALEYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 221 KAVKKAGVPVILDVGGMD-TPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSAL 299
Cdd:cd01941 148 ALAAKHGVPVAFEPTSAPkLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220039 300 FiQGEKPIQQSIIPAAQ---VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQ 357
Cdd:cd01941 228 S-SREGGVETKLFPAPQpetVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
72-362 |
8.32e-35 |
|
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: 129.68 E-value: 8.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 72 VVVGSANADIyveIERLPKEGETISAKtgqtlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHLD 151
Cdd:cd01167 3 VCFGEALIDF---IPEGSGAPETFTKA-----PGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKE--AGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 152 YVRSVNNEPTGHAVVMLQSDGQNSIIIVGG--ANMKAWPEIMSD--DDLEIVRNAGIVLLQREIPDSINiQVAKAVKKAG 227
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADLLLDTELNPDllSEADILHFGSIALASEPSRSALL-ELLEAAKKAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 228 VPVILDVGGMDTPIPN---------ELLDSIDILSPNETELSRLTGMptetfEQISQAVAKCHKLGVKQVLVKLGSKGSA 298
Cdd:cd01167 152 VLISFDPNLRPPLWRDeeeareriaELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGAL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220039 299 LFIQGEKPIQQSiiPAAQVVDTTGAGDTFTAAFAVAMVEGKSH-------EECLRFAAAAASLCVQVKGAI 362
Cdd:cd01167 227 LYTKGGVGEVPG--IPVEVVDTTGAGDAFVAGLLAQLLSRGLLaldedelAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
74-367 |
2.73e-33 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 125.48 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 74 VGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHldYV 153
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS--FI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 154 RSVNNEPTGHAVVMlQSDGQNSIIIVGGANMKAWPEIMSDDDLEivrNAGIVLLQREIPDSiNIQVAKAVKKAGVPVILD 233
Cdd:cd01945 83 VVAPGARSPISSIT-DITGDRATISITAIDTQAAPDSLPDAILG---GADAVLVDGRQPEA-ALHLAQEARARGIPIPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 234 VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTEtfeqisQAVAKCHKLGVKQVLVKLGSKGSaLFIQGEKPIQQSIIP 313
Cdd:cd01945 158 LDGGGLRVLEELLPLADHAICSENFLRPNTGSADD------EALELLASLGIPFVAVTLGEAGC-LWLERDGELFHVPAF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15220039 314 AAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPD 367
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
71-364 |
7.01e-29 |
|
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: 114.25 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKE-----------------GETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAH 133
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEklglkkgdmiladmeeqEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 134 GKLIAEALGDdgCGVHLDYVrSVNNEPTGHAVVMLQSDGQNSIIIVGGAnmkAWPEIMSDDDLEIVRNAGIVLL---QRE 210
Cdd:cd01168 84 GDFLLKDLRA--AGVDTRYQ-VQPDGPTGTCAVLVTPDAERTMCTYLGA---ANELSPDDLDWSLLAKAKYLYLegyLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 211 IPDSINIQVAKAVKKAGVPVILDVGgmDTPIPN-------ELLDSIDILSPNETELSRLTGM-PTETFEQisqAVAKCHk 282
Cdd:cd01168 158 VPPEAILLAAEHAKENGVKIALNLS--APFIVQrfkeallELLPYVDILFGNEEEAEALAEAeTTDDLEA---ALKLLA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 283 LGVKQVLVKLGSKGSALFIQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAI 362
Cdd:cd01168 232 LRCRIVVITQGAKGAVVVEGGEV-YPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
..
gi 15220039 363 PS 364
Cdd:cd01168 311 LP 312
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
72-367 |
5.85e-27 |
|
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: 108.80 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 72 VVVGSANADIYV--EIERLPKEGETISA--KTGQTLAGGKGA---NQAACGAKlmypTYFVGRLGEDAHGKLIAEALGDD 144
Cdd:cd01172 3 LVVGDVILDEYLygDVERISPEAPVPVVkvEREEIRLGGAANvanNLASLGAK----VTLLGVVGDDEAGDLLRKLLEKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 145 GcgVHLDYVRSvNNEPT---------GHAVVMLQSDGQNSIIIVGGANMKAW-PEIMSDDDLEIVRNAGIVLLQREIPDS 214
Cdd:cd01172 79 G--IDTDGIVD-EGRPTttktrviarNQQLLRVDREDDSPLSAEEEQRLIERiAERLPEADVVILSDYGKGVLTPRVIEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 215 InIQVAKavkKAGVPVILDVGGMDTpipnELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKC-HKLGVKQVLVKLG 293
Cdd:cd01172 156 L-IAAAR---ELGIPVLVDPKGRDY----SKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLlELLNLEALLVTLG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220039 294 SKGSALFiQGEKPIQqsIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPD 367
Cdd:cd01172 228 EEGMTLF-ERDGEVQ--HIPAlaKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPK 300
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
104-357 |
8.36e-25 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 102.97 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 104 AGGKG---ANQAACGAKlmypTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPT-------GHAVVMLQSDGQ 173
Cdd:COG2870 55 PGGAAnvaANLAALGAQ----VTLVGVVGDDEAGRELRRLLEEAG--IDTDGLVVDPRRPTttktrviAGGQQLLRLDFE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 174 NSIIIVGGAnmkawPEIMSDDDLEIVRNAGIVLLQR----EIPDSINIQVAKAVKKAGVPVILDVGGMDtpipNELLDSI 249
Cdd:COG2870 129 DRFPLSAEL-----EARLLAALEAALPEVDAVILSDygkgVLTPELIQALIALARAAGKPVLVDPKGRD----FSRYRGA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 250 DILSPNETELSRLTGMPTETFEQISQAVAK-CHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIiPAAQVVDTTGAGDTFT 328
Cdd:COG2870 200 TLLTPNLKEAEAAVGIPIADEEELVAAAAElLERLGLEALLVTRGEEGMTLFDADGPPHHLPA-QAREVFDVTGAGDTVI 278
|
250 260
....*....|....*....|....*....
gi 15220039 329 AAFAVAMVEGKSHEECLRFAAAAASLCVQ 357
Cdd:COG2870 279 ATLALALAAGASLEEAAELANLAAGIVVG 307
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
71-362 |
1.10e-23 |
|
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: 98.64 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKEGE-TISAKTGQTLAGGkGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGiSHSSDSRESPGGG-GANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LdyvrSVNNEPTGHAVVMLQSDGQNSIIIVGGA--NMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINiqvakavkkag 227
Cdd:cd01947 81 V----AWRDKPTRKTLSFIDPNGERTITVPGERleDDLKWPILDEGDGVFITAAAVDKEAIRKCRETKL----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 228 vpVILDVG-GMDTPIPNELLDSIDILSPNETElsrltgMPTETFEQisqavaKCHKLGVKQVLVKLGSKGSALFIQGEkp 306
Cdd:cd01947 146 --VILQVTpRVRVDELNQALIPLDILIGSRLD------PGELVVAE------KIAGPFPRYLIVTEGELGAILYPGGR-- 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220039 307 iqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAI 362
Cdd:cd01947 210 --YNHVPAkkAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
70-360 |
3.05e-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: 98.26 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGkGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LDyvrSVNNEPTGHAVVMLQSDGQNSIIIVGGA------NMKAWPEIMSDDDLEIVR------NAGIVLL---QREIPds 214
Cdd:cd01944 80 LP---PRGGDDGGCLVALVEPDGERSFISISGAeqdwstEWFATLTVAPYDYVYLSGytlaseNASKVILlewLEALP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 215 iniqvakavkkAGVPVILDVGGMDTPIPNELLDSI----DILSPNETELSRLTGmptetfEQISQAVAKCHKLGVKQ--- 287
Cdd:cd01944 155 -----------AGTTLVFDPGPRISDIPDTILQALmakrPIWSCNREEAAIFAE------RGDPAAEASALRIYAKTaap 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220039 288 VLVKLGSKGSALFIQGEKPIqqsIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKG 360
Cdd:cd01944 218 VVVRLGSNGAWIRLPDGNTH---IIPGfkVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
71-336 |
5.15e-23 |
|
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: 95.24 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLmyptyfvgrlgedahgkliaealgddgcgvhl 150
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 151 dyvrsvnneptGHAVVMLQSDGqnsiIIVGGANMKawPEIMSDddleivrnagivllqreipdsiniqVAKAVKKAGVPV 230
Cdd:cd00287 50 -----------GVSVTLVGADA----VVISGLSPA--PEAVLD-------------------------ALEEARRRGVPV 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 231 ILDVGGMDTPIPNE----LLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFiQGEKP 306
Cdd:cd00287 88 VLDPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVA-TRGGT 166
|
250 260 270
....*....|....*....|....*....|
gi 15220039 307 IQQSIIPAAQVVDTTGAGDTFTAAFAVAMV 336
Cdd:cd00287 167 EVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
105-376 |
1.02e-22 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 97.38 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 105 GGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIV--GGA 182
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNG--VNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 183 NMKAWPeimSDDDLEIVRNAGI-----VLLQREIPDSINIQVAKAVKKAGVPVILDvggmdtpiPNELL----------- 246
Cdd:PLN02323 121 DMLLRE---SELDLDLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAGALLSYD--------PNLRLplwpsaeaare 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 247 ------DSIDILSPNETELSRLTGMPTETFEqisqAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIipAAQVVDT 320
Cdd:PLN02323 190 gimsiwDEADIIKVSDEEVEFLTGGDDPDDD----TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGF--KVKAVDT 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220039 321 TGAGDTFTAAFAVAMVEGKS-------HEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLLK 376
Cdd:PLN02323 264 TGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEAVLKLLK 326
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
75-367 |
2.21e-15 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 76.60 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 75 GSAnadIYVEIERLPKEGETISAKTGQTLAGGKGANQAACgAKLMYPTY-----FVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:PTZ00247 35 GSA---ILAEEKQLPIFEELESIPNVSYVPGGSALNTARV-AQWMLQAPkgfvcYVGCVGDDRFAEILKEAAEKDGVEML 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LDYVRSvnnEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREI----PDSInIQVAKAVKK 225
Cdd:PTZ00247 111 FEYTTK---APTGTCAVLVCGKERSLVANLGAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFltvsPNNV-LQVAKHARE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 226 AGVPVILdvgGMDTPIP--------NELLDSIDILSPNETE---LSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGS 294
Cdd:PTZ00247 187 SGKLFCL---NLSAPFIsqffferlLQVLPYVDILFGNEEEaktFAKAMKWDTEDLKEIAARIAMLPKYSGTRPRLVVFT 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220039 295 KGS--ALFIQGEKPIQQSIIPAAQ--VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGA-IPSMPD 367
Cdd:PTZ00247 264 QGPepTLIATKDGVTSVPVPPLDQekIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCtYPEKPP 341
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
229-357 |
6.34e-15 |
|
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: 74.03 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVGGM---DTPIP----NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK---------- 291
Cdd:COG2240 112 PVMGDNGKGyyvFPGIAefimRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpad 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220039 292 -----LGSKGSALFIQGEKpiqqsiIPaaqvVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQ 357
Cdd:COG2240 192 kignlAVTADGAWLVETPL------LP----FSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLE 252
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
105-361 |
2.56e-14 |
|
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: 72.39 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 105 GGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHLDYVRSVNNEpTGHAVVMLQsdgQNSIIIVG---G 181
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTL--KRLGVDISHCRVKEGE-NAVADVELV---DGDRIFGLsnkG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 182 ANMKAWPEimsDDDLEIVRNAGIV-LLQREIPDSINiQVAKAVKKAGVPVILDVGG-MDTPIPNELLDSIDILSPNETEL 259
Cdd:cd01940 96 GVAREHPF---EADLEYLSQFDLVhTGIYSHEGHLE-KALQALVGAGALISFDFSDrWDDDYLQLVCPYVDFAFFSASDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 260 SRltgmptetfEQISQAVAKCHKLGVKQVLVKLGSKGSALFiQGEKPIQQSIIPAAqVVDTTGAGDTFTAAFAVAMVEGK 339
Cdd:cd01940 172 SD---------EEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRPVE-VVDTLGAGDSFIAGFLLSLLAGG 240
|
250 260
....*....|....*....|...
gi 15220039 340 SH-EECLRFAAAAASLCVQVKGA 361
Cdd:cd01940 241 TAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
185-354 |
3.08e-14 |
|
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: 71.66 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 185 KAWPEIMSDDdleIVRNAGIVLLQrEIPDSINIQVAKAVKkagvPVILDVGGM------DTPIPNELLDSIDILSPNETE 258
Cdd:cd01937 94 AAIPDTESPL---STITAEIVILG-PVPEEISPSLFRKFA----FISLDAQGFlrranqEKLIKCVILKLHDVLKLSRVE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 259 LSRLTGmPTETFEQIsqavakcHKLGVKQVLVKLGSKGSALFIqGEKPIQqsiIPAA--QVVDTTGAGDTFTAAFAVAMV 336
Cdd:cd01937 166 AEVIST-PTELARLI-------KETGVKEIIVTDGEEGGYIFD-GNGKYT---IPASkkDVVDPTGAGDVFLAAFLYSRL 233
|
170
....*....|....*...
gi 15220039 337 EGKSHEECLRFAAAAASL 354
Cdd:cd01937 234 SGKDIKEAAEFAAAAAAK 251
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
244-357 |
1.79e-13 |
|
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: 70.45 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 244 ELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKL--------GVKQVLVKLGSKGSALFIQGEKPIQQsiIPAA 315
Cdd:cd01943 176 QALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVLQALlfsgilqdPGGGVVLRCGKLGCYVGSADSGPELW--LPAY 253
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15220039 316 Q-----VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQ 357
Cdd:cd01943 254 HtkstkVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIE 300
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
72-354 |
3.74e-13 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 69.96 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 72 VVVGSANADIY-VEIERLPKEGEtiSAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHL 150
Cdd:PRK09954 61 VVVGAINMDIRgMADIRYPQAAS--HPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRR--AGVNV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREI-PDSINIQVAKAvkkAGVP 229
Cdd:PRK09954 137 SGCIRLHGQSTSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLtAEALEWVFTLA---DEIP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 230 VILD-VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKgsALFIQgEKPIQ 308
Cdd:PRK09954 214 VFVDtVSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDE--SVFCS-EKDGE 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15220039 309 QSII--PAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASL 354
Cdd:PRK09954 291 QFLLtaPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAI 338
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
71-354 |
4.70e-13 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 69.25 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGK-LIAEAlgdDGCGVH 149
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPGKIKFT-PGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQsLLTQT---NQSGVY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 150 LDYVRSVNNEPTGHAVVMLQSDGQnsiIIVGGANMKAWPEIMSD---DDLEIVRNAGIVLLQREIPDSiniQVAKAVKKA 226
Cdd:PRK09850 83 VDKCLIVPGENTSSYLSLLDNTGE---MLVAINDMNISNAITAEylaQHREFIQRAKVIVADCNISEE---ALAWILDNA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 227 G-VPVILD-VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALF-IQG 303
Cdd:PRK09850 157 AnVPVFVDpVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSdISG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15220039 304 EK----PIQqsiipaAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASL 354
Cdd:PRK09850 237 ESgwsaPIK------TNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSM 285
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
229-351 |
2.00e-12 |
|
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: 66.45 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVG-------GMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK-----LGSKG 296
Cdd:cd01173 110 PVMGDNGklyvvaeEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelaDDDRI 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15220039 297 SALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAA 351
Cdd:cd01173 190 EMLGSTATEAWLVQRPKIPFPAYFNGTGDLFAALLLARLLKGKSLAEALEKALNF 244
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
98-361 |
2.11e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 66.68 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 98 KTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHLDYVRsVNNEPTghAVVMLQSDGQNSII 177
Cdd:PRK09813 16 QLGKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDL--ARMGVDISHVH-TKHGVT--AQTQVELHDNDRVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 178 --IVGG--ANMKawpeiMSDDDLEIVRNAGIVL--LQREIPDSIniqvaKAVKKAGVPVILDVGG-MDTPIPNELLDSID 250
Cdd:PRK09813 91 gdYTEGvmADFA-----LSEEDYAWLAQYDIVHaaIWGHAEDAF-----PQLHAAGKLTAFDFSDkWDSPLWQTLVPHLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 251 IL---SPNETELSRLTgmptetfeqiSQAVAKChklGVKQVLVKLGSKGSaLFIQGEKPIQQSIIPAaQVVDTTGAGDTF 327
Cdd:PRK09813 161 YAfasAPQEDEFLRLK----------MKAIVAR---GAGVVIVTLGENGS-IAWDGAQFWRQAPEPV-TVVDTMGAGDSF 225
|
250 260 270
....*....|....*....|....*....|....
gi 15220039 328 TAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGA 361
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
25-379 |
2.84e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 67.55 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 25 LQISTVNPNPAQSRF--------SRPRSLRVLSLSADPS-----------ANRNPKSAVDAHAPPLVVVGSAN--ADIYV 83
Cdd:PLN02341 8 GQLGAFSPHPGLSSPpsphghlvPRRVCSRCRASARASSraragarsrarRRLGDTEVGSAAGKEIDVATLGNlcVDIVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 84 EIERLPK----------EGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVhldyV 153
Cdd:PLN02341 88 PVPELPPpsreerkaymEELAASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV----V 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 154 RSVNNEPTGHAVVMLQ--------SDGQNSIIIVGGANMKAWPEI--MSDDDLEI---VRNAGIVLLQ----REIPDSIN 216
Cdd:PLN02341 164 GLIEGTDAGDSSSASYetllcwvlVDPLQRHGFCSRADFGPEPAFswISKLSAEAkmaIRQSKALFCNgyvfDELSPSAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 217 IQVAKAVKKAGVPVILDVG----GMDTPIPNE------LLDSIDILSPNETELSRLTGMPTETfeQISQAVAKcHKLGVK 286
Cdd:PLN02341 244 ASAVDYAIDVGTAVFFDPGprgkSLLVGTPDErralehLLRMSDVLLLTSEEAEALTGIRNPI--LAGQELLR-PGIRTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 287 QVLVKLGSKGSALFIQGEkpiqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPS 364
Cdd:PLN02341 321 WVVVKMGSKGSILVTRSS----VSCAPAfkVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGAGRN 396
|
410
....*....|....*
gi 15220039 365 MPDRKSVLKLLKFSI 379
Cdd:PLN02341 397 VATLEKVLELLRASN 411
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
104-368 |
3.41e-12 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 66.50 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 104 AGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPTGHAVVMLQSDGQNSI--IIVGG 181
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEG--VDTTYLRLDPAHRTSTVVVDLDDQGERSFtfMVRPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 182 ANMkawpeIMSDDDLEIVRnAG-------IVLLQrEIPDSINIQVAKAVKKAGVPVILDvggmdtpiPN----------E 244
Cdd:PRK09434 105 ADL-----FLQPQDLPPFR-QGewlhlcsIALSA-EPSRSTTFEAMRRIKAAGGFVSFD--------PNlredlwqdeaE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 245 LLDSI-------DILSPNETELSRLTGmpTETFEQISQAVAKCHklGVKQVLVKLGSKGSALFIQGekpiQQSIIPAAQV 317
Cdd:PRK09434 170 LRECLrqalalaDVVKLSEEELCFLSG--TSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRG----QVQHFPAPSV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220039 318 --VDTTGAGDTFTAA--FAVAMVEGKSHEECLRFAAAAASLC----VQVKGAIPSMPDR 368
Cdd:PRK09434 242 dpVDTTGAGDAFVAGllAGLSQAGLWTDEAELAEIIAQAQACgalaTTAKGAMTALPNR 300
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
78-367 |
5.98e-12 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 65.89 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 78 NADIYVEIERLPKEGETISAKTGQTLAGGKGANQA-ACGAKLMYP--TYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVR 154
Cdd:PLN02548 25 NNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIrVAQWMLQIPgaTSYMGCIGKDKFGEEMKKCATAAGVNVHYYEDE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 155 SVnnePTGHAVVMLQsDGQNSIIivggANMKAWPEIMSDDdLEIVRNAGIVLLQREI----------PDSINIqVAK-AV 223
Cdd:PLN02548 105 ST---PTGTCAVLVV-GGERSLV----ANLSAANCYKVEH-LKKPENWALVEKAKFYyiagffltvsPESIML-VAEhAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 224 KKAGV-------PVILDVGGMDTpipNELLDSIDILSPNETE---LSRLTGMPTETFEQISQAVAKCHKLGVKQvlvklg 293
Cdd:PLN02548 175 ANNKTfmmnlsaPFICEFFKDQL---MEALPYVDFLFGNETEartFAKVQGWETEDVEEIALKISALPKASGTH------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 294 sKGSALFIQGEKPIQQS-----------IIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKG-A 361
Cdd:PLN02548 246 -KRTVVITQGADPTVVAedgkvkefpviPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGcT 324
|
....*.
gi 15220039 362 IPSMPD 367
Cdd:PLN02548 325 YPEKPD 330
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
101-360 |
1.78e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 64.81 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 101 QTLAGGKGANQA-ACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHLDYVRSVNNePTGHAVVMLQSDGQNSIIIV 179
Cdd:PLN02379 82 KTMAGGSVANTIrGLSAGFGVSTGIIGACGDDEQGKLFVSNMGF--SGVDLSRLRAKKG-PTAQCVCLVDALGNRTMRPC 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 180 GGANMKAWPEIMSDDDLE----IVRNAGIVLLQrEIPDSINIqvakaVKKAGVPVILDVGGMDT-----PIPNELLDS-- 248
Cdd:PLN02379 159 LSSAVKLQADELTKEDFKgskwLVLRYGFYNLE-VIEAAIRL-----AKQEGLSVSLDLASFEMvrnfrSPLLQLLESgk 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 249 IDILSPNETELSRLT-GMPTETFEQISQAVAK-ChklgvKQVLVKLGSKGsALFIQGEKPIQQSIIPAAQVVDTTGAGDT 326
Cdd:PLN02379 233 IDLCFANEDEARELLrGEQESDPEAALEFLAKyC-----NWAVVTLGSKG-CIARHGKEVVRVPAIGETNAVDATGAGDL 306
|
250 260 270
....*....|....*....|....*....|....
gi 15220039 327 FTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKG 360
Cdd:PLN02379 307 FASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
254-356 |
5.01e-10 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 60.09 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 254 PNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGE-----KPiqqsiiPAAQVVDTTGAGDTFT 328
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEG-ALWVNASgewiaKP------PACDVVSTVGAGDSMV 258
|
90 100
....*....|....*....|....*...
gi 15220039 329 AAFAVAMVEGKSHEECLRFAAAAASLCV 356
Cdd:PRK09513 259 GGLIYGLLMRESSEHTLRLATAVSALAV 286
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
198-350 |
1.18e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 58.44 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 198 IVRNAGIVLLQREIPDSINI--QVAKAVKKAGVP-VILD----VGGMDTPIPNE--------LLDSIDILSPNETELSRL 262
Cdd:PRK12412 67 TIEGVGVDALKTGMLGSVEIieMVAETIEKHNFKnVVVDpvmvCKGADEALHPEtndclrdvLVPKALVVTPNLFEAYQL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 263 TGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKgsalfIQGEKPI------QQSIIPAAQVVDTT---GAGDTFTAAFAV 333
Cdd:PRK12412 147 SGVKINSLEDMKEAAKKIHALGAKYVLIKGGSK-----LGTETAIdvlydgETFDLLESEKIDTTnthGAGCTYSAAITA 221
|
170
....*....|....*..
gi 15220039 334 AMVEGKSHEECLRFAAA 350
Cdd:PRK12412 222 ELAKGKPVKEAVKTAKE 238
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
218-348 |
1.92e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 57.77 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 218 QVAKAVK-KAGVPVILDvggmdtPI----------PNELLDSI-------DILSPNETELSRLTGMPTETFEQISQAVAK 279
Cdd:PRK12413 87 QALDFIKgHPGIPVVLD------PVlvckethdveVSELRQELiqffpyvTVITPNLVEAELLSGKEIKTLEDMKEAAKK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 280 CHKLGVKQVLVKLGSKGSA-----LFIQG------EKPIQQSiipaaqvvDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK12413 161 LYDLGAKAVVIKGGNRLSQkkaidLFYDGkefvilESPVLEK--------NNIGAGCTFASSIASQLVKGKSPLEAVKNS 232
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
218-353 |
9.10e-09 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 56.33 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 218 QVAKAVKKAGVPVILDVGGmDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV-KQVLVKLGSKG 296
Cdd:PRK10294 151 QLISAAQKQGIRCIIDSSG-DALSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKaKRVVVSLGPQG 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220039 297 sALFIQGEKPIqQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAAS 353
Cdd:PRK10294 230 -ALGVDSENCI-QVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGS 284
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
219-348 |
1.24e-08 |
|
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: 55.18 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 219 VAKAVKKAGVPVILD-V----GGmDTPIPNELLDSI--------DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV 285
Cdd:pfam08543 78 VAEKLDKYGVPVVLDpVmvakSG-DSLLDDEAIEALkeellplaTLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGA 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220039 286 KQVLVK---LGSKGSA---LFIQGEKPIQQSiipaAQVVDTT---GAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:pfam08543 157 KAVLIKgghLEGEEAVvtdVLYDGGGFYTLE----APRIPTKnthGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
242-357 |
1.34e-08 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 55.55 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 242 PNELLDS---IDILSPNETELSRLTGMPTetfeqISQAVAKCHKLGVKQVLVKLGSKGSALFIQGekpiQQSIIPA---A 315
Cdd:cd01946 154 PEKLKKVlakVDVVIINDGEARQLTGAAN-----LVKAARLILAMGPKALIIKRGEYGALLFTDD----GYFAAPAyplE 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15220039 316 QVVDTTGAGDTFTAAFAVAMV-EGKSHEECLR----FAAAAASLCVQ 357
Cdd:cd01946 225 SVFDPTGAGDTFAGGFIGYLAsQKDTSEANMRraiiYGSAMASFCVE 271
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
97-359 |
2.13e-08 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 55.11 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 97 AKTGQTlAGGKGANQaacgaklmypTYFVGRLGED--AHGkLIAEALGDdgcgvhldYVRSVNNEPTGHAVVMLQSDGQN 174
Cdd:PRK13508 29 VDVSKT-AGGKGLNV----------TRVLSEFGENvlATG-LIGGELGQ--------FIAEHLDDQIKHAFYKIKGETRN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 175 SIIIVGGAN----MKAWPEIMSD-------------DDLEIVRNAGIvlLQREIPDSINIQVAKAVKKAGVPVILDVGGm 237
Cdd:PRK13508 89 CIAILHEGQqteiLEKGPEISVQeadgflhhfkqllESVEVVAISGS--LPAGLPVDYYAQLIELANQAGKPVVLDCSG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 238 dtpipnELLDSI-------DILSPNETELSRLTGMP-TETFEQISQAVAKCHKLGVKQVLVKLGSKGSalFIQGEKPIQQ 309
Cdd:PRK13508 166 ------AALQAVlespykpTVIKPNIEELSQLLGKEvSEDLDELKEVLQQPLFEGIEWIIVSLGADGA--FAKHNDTFYK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15220039 310 SIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVK 359
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQEK 287
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
229-351 |
7.46e-08 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 53.33 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVG-GMDTP------IPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK---------- 291
Cdd:PRK05756 112 PVMGDPEkGCIVApgvaefLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypad 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220039 292 -----LGSKGSALFIqgEKPiqqsIIP-AAQVVdttGAGDTFTAAFAVAMVEGKSHEECLRFAAAA 351
Cdd:PRK05756 192 rfemlLVTADGAWHI--SRP----LVDfMRQPV---GVGDLTSALFLARLLQGGSLEEALEHTTAA 248
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
219-348 |
1.41e-07 |
|
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: 51.96 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 219 VAKAVKK-AGVPVILD-V---GGMDTPIPNELLDSI--------DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV 285
Cdd:COG0351 84 VAEILADyPLVPVVLDpVmvaKSGDRLLDEDAVEALrelllplaTVVTPNLPEAEALLGIEITTLDDMREAAKALLELGA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 286 KQVLVK----LGSKGSALFIQGEKPIQQSiipaAQVVDTT---GAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:COG0351 164 KAVLVKgghlPGDEAVDVLYDGDGVREFS----APRIDTGnthGTGCTLSSAIAALLAKGLDLEEAVREA 229
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
217-356 |
2.02e-07 |
|
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: 52.52 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 217 IQVAKavkKAGVPVILDVGGMDTpipnELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKG 296
Cdd:PRK11316 164 IQLAR---KAGVPVLIDPKGTDF----ERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQG 236
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220039 297 SALFIQGEKPIqqsIIPA-AQ-VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCV 356
Cdd:PRK11316 237 MTLLQPGKAPL---HLPTqAReVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVV 295
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
22-361 |
2.04e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 52.50 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 22 RPQLQISTVNPNPAQSRFSRPRSLRVLSLS-ADPSANRNPKSAVDAHAPP----------LVVVGSANADI-------YV 83
Cdd:PLN02813 12 SLYVPKPNRRLRRVTSQRGAPGLFRIHSRAnNAALAIQQDEEQPEGFGPIpekavperwdVLGLGQAMVDFsgmvddeFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 84 EIERLPKEGETI-----SAKTGQTLAGGkgANQAACGAKLMYPTYFVGRLG-EDAHGK----LIAEALGDDGCGvhlDYV 153
Cdd:PLN02813 92 ERLGLEKGTRKVinheeRGKVLRALDGC--SYKASAGGSLSNTLVALARLGsQSAAGPalnvAMAGSVGSDPLG---DFY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 154 RS-------------VNNEPTGHAVVMLQSDGQNSIIIVGGANmkawpEIMS-DDDL-EIVRNAGIVLLQR---EIPDSI 215
Cdd:PLN02813 167 RTklrranvhflsqpVKDGTTGTVIVLTTPDAQRTMLSYQGTS-----STVNyDSCLaSAISKSRVLVVEGylwELPQTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 216 NI--QVAKAVKKAGVPVIL---DVGGMdTPIPNELLD----SIDILSPNETELSRLTGMP-TETFEQISQAVAKChklgV 285
Cdd:PLN02813 242 EAiaQACEEAHRAGALVAVtasDVSCI-ERHRDDFWDvmgnYADILFANSDEARALCGLGsEESPESATRYLSHF----C 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 286 KQVLVKLGSKGSALFIQGEKpiqQSIIPAAQV-VDTTGAGDTFTAAFAVAMVEGKSHeecLR----FAAAAASLCVQVKG 360
Cdd:PLN02813 317 PLVSVTDGARGSYIGVKGEA---VYIPPSPCVpVDTCGAGDAYAAGILYGLLRGVSD---LRgmgeLAARVAATVVGQQG 390
|
.
gi 15220039 361 A 361
Cdd:PLN02813 391 T 391
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
74-360 |
7.03e-07 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 50.48 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 74 VGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYV 153
Cdd:cd01939 5 VGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRG--IDISHC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 154 RSVNNEPTGHAVVMLQSDGQNSIIIvggaNMKAWPEIMSDDDLEIVRN-AGIVLLQREIPDsiniQVAKAVKKagvpvIL 232
Cdd:cd01939 83 YRKDIDEPASSYIIRSRAGGRTTIV----NDNNLPEVTYDDFSKIDLTqYGWIHFEGRNPD----ETLRMMQH-----IE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 233 DVGGMDTPIPNELldSIDILSPNEtELSRLTGM------------------PTETFE-QISQAVAKCHklgvkqVLVKLG 293
Cdd:cd01939 150 EHNNRRPEIRITI--SVEVEKPRE-ELLELAAYcdvvfvskdwaqsrgyksPEECLRgEGPRAKKAAL------LVCTWG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220039 294 SKG-SALFIQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSH-EECLRFAAAAASLCVQVKG 360
Cdd:cd01939 221 DQGaGALGPDGEY-VHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFGNRVASQKCTGVG 288
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
250-351 |
1.62e-06 |
|
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: 49.06 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 250 DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK-LGSKGSA-------LFIQGEKPIQQSIIPAAQVVDTT 321
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQrdrsfegLVATQEGRWHISRPLAVFDPPPV 219
|
90 100 110
....*....|....*....|....*....|
gi 15220039 322 GAGDTFTAAFAVAMVEGKSHEECLRFAAAA 351
Cdd:TIGR00687 220 GTGDLIAALLLATLLHGNSLKEALEKTVSA 249
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
219-348 |
2.10e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 49.34 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 219 VAKAVKKAGVPVILD---VGGMDTPIPNEllDSIDIL-----------SPNETELSRLTGMPTETFEQISQAVAKCHK-L 283
Cdd:PRK08573 89 VAKTVSKYGFPLVVDpvmIAKSGAPLLRE--DAVDALikrllplatvvTPNRPEAEKLTGMKIRSVEDARKAAKYIVEeL 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 284 GVKQVLVKLGSKGSA-----LFIQGEkpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK08573 167 GAEAVVVKGGHLEGEeavdvLYHNGT--FREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTA 234
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
243-348 |
8.28e-06 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 46.66 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 243 NELLDSIDILSPN--ETELsrLTGMPTETFEQISQAVAK-CHKLGVKQVLVK---LGSKGSA--LFIQGEkpiQQSIIPA 314
Cdd:PRK06427 128 ERLLPLATLITPNlpEAEA--LTGLPIADTEDEMKAAARaLHALGCKAVLIKgghLLDGEESvdWLFDGE---GEERFSA 202
|
90 100 110
....*....|....*....|....*....|....*.
gi 15220039 315 AQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK06427 203 PRIptKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
229-331 |
4.11e-05 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 45.07 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVGGMDTP-----IPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK----------LG 293
Cdd:PTZ00344 115 PVMGDDGKLYVKeevvdAYRELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITsfrededpthLR 194
|
90 100 110
....*....|....*....|....*....|....*...
gi 15220039 294 SKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAF 331
Cdd:PTZ00344 195 FLLSCRDKDTKNNKRFTGKVPYIEGRYTGTGDLFAALL 232
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
229-349 |
1.89e-04 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 42.72 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVG-GM--DTPIP----NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKlgskgSALFI 301
Cdd:PRK08176 126 PVIGDIDsGIyvKPDLPeayrQHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT-----SAAGN 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15220039 302 QGEKPIQQSIIPAAQV-------VDTT--GAGDTFTAAFAVAMVEGKSHEECLRFAA 349
Cdd:PRK08176 201 EENQEMQVVVVTADSVnvishprVDTDlkGTGDLFCAELVSGLLKGKALTDAAHRAG 257
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
229-329 |
7.31e-04 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 41.26 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 229 PVILDVGGMDTPIP------NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLV-------KLGSK 295
Cdd:PLN02978 124 PVLGDEGKLYVPPElvpvyrEKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVItsididgKLLLV 203
|
90 100 110
....*....|....*....|....*....|....*...
gi 15220039 296 GSALFIQGEKPIQQSI----IPAAqvvdTTGAGDTFTA 329
Cdd:PLN02978 204 GSHRKEKGARPEQFKIvipkIPAY----FTGTGDLMAA 237
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
186-279 |
5.92e-03 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 37.98 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220039 186 AWPEIMSDDDLEIVRNAGIVLLQReiPDSINI-----------QVAKAVKKAGVPVILDVGGMdTPIPNELLDSI----D 250
Cdd:cd01171 54 YSPELMVHPLLETDIEELLELLER--ADAVVIgpglgrdeeaaEILEKALAKDKPLVLDADAL-NLLADEPSLIKrygpV 130
|
90 100
....*....|....*....|....*....
gi 15220039 251 ILSPNETELSRLTGMPTETFEQISQAVAK 279
Cdd:cd01171 131 VLTPHPGEFARLLGALVEEIQADRLAAAR 159
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
288-338 |
6.53e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.25 E-value: 6.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15220039 288 VLVKLGSKGSALFIQgEKPIQQSIIPAAQVvDTTGAGDTFTAAFAVAMVEG 338
Cdd:PLN02630 206 VIVTNGKKGCRIYWK-DGEMRVPPFPAIQV-DPTGAGDSFLGGFVAGLVQG 254
|
|
| |
