|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
70-348 |
7.47e-104 |
|
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: 307.17 E-value: 7.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcGVH 149
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE--GID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEiMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVP 229
Cdd:cd01174 79 VSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPA-DVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 230 VILDVGGMDtPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEkpiqQ 309
Cdd:cd01174 158 VILNPAPAR-PLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGE----V 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 145323924 310 SIIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01174 233 EHVPAFKVkaVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
75-348 |
3.91e-84 |
|
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: 256.76 E-value: 3.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 75 GSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcGVHLDYVR 154
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSN--GIDTEYVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 155 SVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDV 234
Cdd:TIGR02152 79 TVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDI-DAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 235 GGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGEKpiqQSIIPA 314
Cdd:TIGR02152 158 APAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKG-ALLVSKDE---SKLIPA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 145323924 315 --AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:TIGR02152 234 fkVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFA 269
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
71-348 |
4.55e-72 |
|
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: 226.30 E-value: 4.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHL 150
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAEL--RAEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEimsDDDLEIVRNAGIVLLQ-----REIPDSINIQVAKAVKK 225
Cdd:COG0524 80 SGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPE---DLDEALLAGADILHLGgitlaSEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 226 AGVPVILDVGGMD------TPIPNELLDSIDILSPNETELSRLTGMPTetfeqISQAVAKCHKLGVKQVLVKLGSKGSAL 299
Cdd:COG0524 157 AGVPVSLDPNYRPalwepaRELLRELLALVDILFPNEEEAELLTGETD-----PEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 145323924 300 FIQGEkpiqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:COG0524 232 YTGGE----VVHVPAfpVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
71-348 |
1.45e-60 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 196.63 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcGVHL 150
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKD--GIDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPV 230
Cdd:PRK11142 83 APVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALV-EAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 231 ILDVGGMdTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGekpiQQS 310
Cdd:PRK11142 162 ILNPAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENG----EGQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 145323924 311 IIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK11142 237 RVPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
71-348 |
5.24e-59 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 192.56 E-value: 5.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPkeGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHL 150
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQEL--KKEGVDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMsDDDLEIVRNAGIV----LLQREIPDSINIQVAKAVKKA 226
Cdd:pfam00294 78 DYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEEL-EENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 227 G--VPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGE 304
Cdd:pfam00294 157 GtfDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADG-ALVVEGD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 145323924 305 KPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:pfam00294 236 GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFA 279
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
68-348 |
2.23e-53 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 178.78 E-value: 2.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 68 APPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDgcG 147
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRN--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 148 VHLDYVRSVNNEPTGHAVVML-QSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKA 226
Cdd:PTZ00292 93 VNTSFVSRTENSSTGLAMIFVdTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 227 GVPVILDVggmdTPIPN--------ELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSA 298
Cdd:PTZ00292 173 GCYTVFNP----APAPKlaeveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145323924 299 LFIQGEKPIQqsiIPAAQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PTZ00292 249 IVEKENEPVH---VPGKRVkaVDTTGAGDCFVGSMAYFMSRGKDLKESCKRA 297
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
70-348 |
1.49e-38 |
|
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: 138.60 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVH 149
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEG--VD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LDYVRSVNNEPTGHAVVMlqSDGQNSIIIVG--GANMKAWPEIMSDDDleivRNAGIVLLQREIPDsinIQVAKAVKKAG 227
Cdd:cd01942 79 TSHVRVVDEDSTGVAFIL--TDGDDNQIAYFypGAMDELEPNDEADPD----GLADIVHLSSGPGL---IELARELAAGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 228 VPVILDVGGMDTPIPNELLDSI----DILSPNETE---LSRLTGMPTEtfeqisqAVAKchklGVKQVLVKLGSKGSALF 300
Cdd:cd01942 150 ITVSFDPGQELPRLSGEELEEIleraDILFVNDYEaelLKERTGLSEA-------ELAS----GVRVVVVTLGPKGAIVF 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 145323924 301 IQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01942 219 EDGEE-VEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLG 265
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
105-348 |
8.61e-35 |
|
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: 128.85 E-value: 8.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 105 GGKGANqAACG-AKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHldYVRSVNNEPTGHAVVMLQSDGQNSIIIV--GG 181
Cdd:cd01166 31 GGAEAN-VAVGlARLGHRVALVTAVGDDPFGRFILAELRREGVDTS--HVRVDPGRPTGLYFLEIGAGGERRVLYYraGS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 182 ANMKAWPEimsDDDLEIVRNA------GIVLLQREIPDSINIQVAKAVKKAGVPVILDV------GGMDTPIP--NELLD 247
Cdd:cd01166 108 AASRLTPE---DLDEAALAGAdhlhlsGITLALSESAREALLEALEAAKARGVTVSFDLnyrpklWSAEEAREalEELLP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 248 SIDILSPNETELSRLTGMPTETfEQIsqAVAKCHKLGVKQVLVKLGSKGSALFIQGEKpiQQSIIPAAQVVDTTGAGDTF 327
Cdd:cd01166 185 YVDIVLPSEEEAEALLGDEDPT-DAA--ERALALALGVKAVVVKLGAEGALVYTGGGR--VFVPAYPVEVVDTTGAGDAF 259
|
250 260
....*....|....*....|.
gi 145323924 328 TAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01166 260 AAGFLAGLLEGWDLEEALRFA 280
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
80-348 |
1.50e-33 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 126.02 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 80 DIYVEIERLpKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAhGKLIAEALgdDGCGVHLDYVRSvnNE 159
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELL--DEEGIPTDFVPI--EG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 160 PTGHAVVML-QSDGQNSIIIVGGanmkawPEImSDDDLE--------IVRNAGIVL----LQREIPDSINIQVAKAVKKA 226
Cdd:COG1105 85 ETRINIKIVdPSDGTETEINEPG------PEI-SEEELEallerleeLLKEGDWVVlsgsLPPGVPPDFYAELIRLARAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 227 GVPVILDVGGmdtpipnELLD-----SIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFI 301
Cdd:COG1105 158 GAKVVLDTSG-------EALKaaleaGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADG-ALLV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 145323924 302 QGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:COG1105 230 TEDG-VYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
80-348 |
3.05e-33 |
|
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: 124.57 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 80 DIYVEIERLpKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDaHGKLIAEALGDDGcgvhLDYVRSVNNE 159
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEG----IPDDFVEVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 160 PTGHAVVMLQSDGQNSIIivggaNMKAwPEImSDDDLE--------IVRNAGIVL----LQREIPDSINIQVAKAVKKAG 227
Cdd:cd01164 86 ETRINVKIKEEDGTETEI-----NEPG-PEI-SEEELEalleklkaLLKKGDIVVlsgsLPPGVPADFYAELVRLAREKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 228 VPVILDVGGmdtpipNELLDSI----DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQG 303
Cdd:cd01164 159 ARVILDTSG------EALLAALaakpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADG-ALLVTK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 145323924 304 EKPIQqSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01164 232 DGVYR-ASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
70-348 |
1.41e-32 |
|
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: 122.81 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 70 PLVVVGSANADI--YVEIERLPkeGETISAKTGQTlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEAL---GDD 144
Cdd:cd01941 1 EIVVIGAANIDLrgKVSGSLVP--GTSNPGHVKQS-PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESekaGLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 145 gcgvhlDYVRSVNNEPTGHAVVMLQSDGQnsiIIVGGANMKAWpEIMSDDDL----EIVRNAGIVLLQREIPDSINIQVA 220
Cdd:cd01941 78 ------VRGIVFEGRSTASYTAILDKDGD---LVVALADMDIY-ELLTPDFLrkirEALKEAKPIVVDANLPEEALEYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 221 KAVKKAGVPVILDVGGMD-TPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSAL 299
Cdd:cd01941 148 ALAAKHGVPVAFEPTSAPkLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145323924 300 FiQGEKPIQQSIIPAAQ---VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01941 228 S-SREGGVETKLFPAPQpetVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
72-348 |
8.20e-30 |
|
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: 115.81 E-value: 8.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 72 VVVGSANADIyveIERLPKEGETISAKtgqtlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHLD 151
Cdd:cd01167 3 VCFGEALIDF---IPEGSGAPETFTKA-----PGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKE--AGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 152 YVRSVNNEPTGHAVVMLQSDGQNSIIIVGG--ANMKAWPEIMSD--DDLEIVRNAGIVLLQREIPDSINiQVAKAVKKAG 227
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADLLLDTELNPDllSEADILHFGSIALASEPSRSALL-ELLEAAKKAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 228 VPVILDVGGMDTPIPN---------ELLDSIDILSPNETELSRLTGMptetfEQISQAVAKCHKLGVKQVLVKLGSKGSA 298
Cdd:cd01167 152 VLISFDPNLRPPLWRDeeeareriaELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGAL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 145323924 299 LFIQGEKPIQQSiiPAAQVVDTTGAGDTFTAAFAVAMVEGKSH-------EECLRFA 348
Cdd:cd01167 227 LYTKGGVGEVPG--IPVEVVDTTGAGDAFVAGLLAQLLSRGLLaldedelAEALRFA 281
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
74-348 |
4.92e-28 |
|
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: 110.85 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 74 VGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHldYV 153
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS--FI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 154 RSVNNEPTGHAVVMlQSDGQNSIIIVGGANMKAWPEIMSDDDLEivrNAGIVLLQREIPDSiNIQVAKAVKKAGVPVILD 233
Cdd:cd01945 83 VVAPGARSPISSIT-DITGDRATISITAIDTQAAPDSLPDAILG---GADAVLVDGRQPEA-ALHLAQEARARGIPIPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 234 VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTEtfeqisQAVAKCHKLGVKQVLVKLGSKGSaLFIQGEKPIQQSIIP 313
Cdd:cd01945 158 LDGGGLRVLEELLPLADHAICSENFLRPNTGSADD------EALELLASLGIPFVAVTLGEAGC-LWLERDGELFHVPAF 230
|
250 260 270
....*....|....*....|....*....|....*
gi 145323924 314 AAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFA 265
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
71-348 |
2.71e-24 |
|
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: 101.15 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKE-----------------GETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAH 133
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEklglkkgdmiladmeeqEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 134 GKLIAEALGDdgCGVHLDYVrSVNNEPTGHAVVMLQSDGQNSIIIVGGAnmkAWPEIMSDDDLEIVRNAGIVLL---QRE 210
Cdd:cd01168 84 GDFLLKDLRA--AGVDTRYQ-VQPDGPTGTCAVLVTPDAERTMCTYLGA---ANELSPDDLDWSLLAKAKYLYLegyLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 211 IPDSINIQVAKAVKKAGVPVILDVGgmDTPIPN-------ELLDSIDILSPNETELSRLTGM-PTETFEQisqAVAKCHk 282
Cdd:cd01168 158 VPPEAILLAAEHAKENGVKIALNLS--APFIVQrfkeallELLPYVDILFGNEEEAEALAEAeTTDDLEA---ALKLLA- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145323924 283 LGVKQVLVKLGSKGSALFIQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01168 232 LRCRIVVITQGAKGAVVVEGGEV-YPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLG 296
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
71-336 |
1.90e-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: 96.01 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLmyptyfvgrlgedahgkliaealgddgcgvhl 150
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 151 dyvrsvnneptGHAVVMLQSDGqnsiIIVGGANMKawPEIMSDddleivrnagivllqreipdsiniqVAKAVKKAGVPV 230
Cdd:cd00287 50 -----------GVSVTLVGADA----VVISGLSPA--PEAVLD-------------------------ALEEARRRGVPV 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 231 ILDVGGMDTPIPNE----LLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFiQGEKP 306
Cdd:cd00287 88 VLDPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVA-TRGGT 166
|
250 260 270
....*....|....*....|....*....|
gi 145323924 307 IQQSIIPAAQVVDTTGAGDTFTAAFAVAMV 336
Cdd:cd00287 167 EVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
72-348 |
4.08e-22 |
|
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: 94.93 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 72 VVVGSANADIYV--EIERLPKEGETISA--KTGQTLAGGKGA---NQAACGAKlmypTYFVGRLGEDAHGKLIAEALGDD 144
Cdd:cd01172 3 LVVGDVILDEYLygDVERISPEAPVPVVkvEREEIRLGGAANvanNLASLGAK----VTLLGVVGDDEAGDLLRKLLEKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 145 GcgVHLDYVRSvNNEPT---------GHAVVMLQSDGQNSIIIVGGANMKAW-PEIMSDDDLEIVRNAGIVLLQREIPDS 214
Cdd:cd01172 79 G--IDTDGIVD-EGRPTttktrviarNQQLLRVDREDDSPLSAEEEQRLIERiAERLPEADVVILSDYGKGVLTPRVIEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 215 InIQVAKavkKAGVPVILDVGGMDTpipnELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKC-HKLGVKQVLVKLG 293
Cdd:cd01172 156 L-IAAAR---ELGIPVLVDPKGRDY----SKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLlELLNLEALLVTLG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 145323924 294 SKGSALFiQGEKPIQqsIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01172 228 EEGMTLF-ERDGEVQ--HIPAlaKEVYDVTGAGDTVIATLALALAAGADLEEAAFLA 281
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
104-348 |
1.07e-21 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 94.11 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 104 AGGKG---ANQAACGAKlmypTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPT-------GHAVVMLQSDGQ 173
Cdd:COG2870 55 PGGAAnvaANLAALGAQ----VTLVGVVGDDEAGRELRRLLEEAG--IDTDGLVVDPRRPTttktrviAGGQQLLRLDFE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 174 NSIIIVGGAnmkawPEIMSDDDLEIVRNAGIVLLQR----EIPDSINIQVAKAVKKAGVPVILDVGGMDtpipNELLDSI 249
Cdd:COG2870 129 DRFPLSAEL-----EARLLAALEAALPEVDAVILSDygkgVLTPELIQALIALARAAGKPVLVDPKGRD----FSRYRGA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 250 DILSPNETELSRLTGMPTETFEQISQAVAK-CHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIiPAAQVVDTTGAGDTFT 328
Cdd:COG2870 200 TLLTPNLKEAEAAVGIPIADEEELVAAAAElLERLGLEALLVTRGEEGMTLFDADGPPHHLPA-QAREVFDVTGAGDTVI 278
|
250 260
....*....|....*....|
gi 145323924 329 AAFAVAMVEGKSHEECLRFA 348
Cdd:COG2870 279 ATLALALAAGASLEEAAELA 298
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
71-348 |
1.76e-21 |
|
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: 92.48 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKEGE-TISAKTGQTLAGGkGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGiSHSSDSRESPGGG-GANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LdyvrSVNNEPTGHAVVMLQSDGQNSIIIVGGA--NMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINiqvakavkkag 227
Cdd:cd01947 81 V----AWRDKPTRKTLSFIDPNGERTITVPGERleDDLKWPILDEGDGVFITAAAVDKEAIRKCRETKL----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 228 vpVILDVG-GMDTPIPNELLDSIDILSPNETElsrltgMPTETFEQisqavaKCHKLGVKQVLVKLGSKGSALFIQGEkp 306
Cdd:cd01947 146 --VILQVTpRVRVDELNQALIPLDILIGSRLD------PGELVVAE------KIAGPFPRYLIVTEGELGAILYPGGR-- 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 145323924 307 iqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01947 210 --YNHVPAkkAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELG 251
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
70-348 |
5.03e-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: 88.63 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 70 PLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGkGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LDyvrSVNNEPTGHAVVMLQSDGQNSIIIVGGA------NMKAWPEIMSDDDLEIVR------NAGIVLL---QREIPds 214
Cdd:cd01944 80 LP---PRGGDDGGCLVALVEPDGERSFISISGAeqdwstEWFATLTVAPYDYVYLSGytlaseNASKVILlewLEALP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 215 iniqvakavkkAGVPVILDVGGMDTPIPNELLDSI----DILSPNETELSRLTGmptetfEQISQAVAKCHKLGVKQ--- 287
Cdd:cd01944 155 -----------AGTTLVFDPGPRISDIPDTILQALmakrPIWSCNREEAAIFAE------RGDPAAEASALRIYAKTaap 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145323924 288 VLVKLGSKGSALFIQGEKPIqqsIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01944 218 VVVRLGSNGAWIRLPDGNTH---IIPGfkVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLA 277
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
229-349 |
1.64e-13 |
|
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: 69.79 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVGGM---DTPIP----NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK---------- 291
Cdd:COG2240 112 PVMGDNGKGyyvFPGIAefimRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpad 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145323924 292 -----LGSKGSALFIQGEKpiqqsiIPaaqvVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAG 349
Cdd:COG2240 192 kignlAVTADGAWLVETPL------LP----FSPNGTGDLFAALLLAHLLRGKSLEEALERAA 244
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
71-352 |
3.57e-13 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 69.25 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 71 LVVVGSANADIYVEIERLPKEGETISAKTGQTlAGGKGANQAACGAKLMYPTYFVGRLGEDAHGK-LIAEAlgdDGCGVH 149
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPGKIKFT-PGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQsLLTQT---NQSGVY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LDYVRSVNNEPTGHAVVMLQSDGQnsiIIVGGANMKAWPEIMSD---DDLEIVRNAGIVLLQREIPDSiniQVAKAVKKA 226
Cdd:PRK09850 83 VDKCLIVPGENTSSYLSLLDNTGE---MLVAINDMNISNAITAEylaQHREFIQRAKVIVADCNISEE---ALAWILDNA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 227 G-VPVILD-VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALF-IQG 303
Cdd:PRK09850 157 AnVPVFVDpVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSdISG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 145323924 304 EK----PIQqsiipaAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA-GCNT 352
Cdd:PRK09850 237 ESgwsaPIK------TNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAqGCSS 284
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
185-349 |
2.04e-12 |
|
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: 66.27 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 185 KAWPEIMSDDdleIVRNAGIVLLQrEIPDSINIQVAKAVKkagvPVILDVGGM------DTPIPNELLDSIDILSPNETE 258
Cdd:cd01937 94 AAIPDTESPL---STITAEIVILG-PVPEEISPSLFRKFA----FISLDAQGFlrranqEKLIKCVILKLHDVLKLSRVE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 259 LSRLTGmPTETFEQIsqavakcHKLGVKQVLVKLGSKGSALFIqGEKPIQqsiIPAA--QVVDTTGAGDTFTAAFAVAMV 336
Cdd:cd01937 166 AEVIST-PTELARLI-------KETGVKEIIVTDGEEGGYIFD-GNGKYT---IPASkkDVVDPTGAGDVFLAAFLYSRL 233
|
170
....*....|...
gi 145323924 337 EGKSHEECLRFAG 349
Cdd:cd01937 234 SGKDIKEAAEFAA 246
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
105-338 |
2.19e-12 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 66.22 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 105 GGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHLDYVRSVNNEpTGHAVVMLQsdgQNSIIIVG---G 181
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTL--KRLGVDISHCRVKEGE-NAVADVELV---DGDRIFGLsnkG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 182 ANMKAWPEimsDDDLEIVRNAGIV-LLQREIPDSINiQVAKAVKKAGVPVILDVGG-MDTPIPNELLDSIDILSPNETEL 259
Cdd:cd01940 96 GVAREHPF---EADLEYLSQFDLVhTGIYSHEGHLE-KALQALVGAGALISFDFSDrWDDDYLQLVCPYVDFAFFSASDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145323924 260 SRltgmptetfEQISQAVAKCHKLGVKQVLVKLGSKGSALFiQGEKPIQQSIIPAAqVVDTTGAGDTFTAAFAVAMVEG 338
Cdd:cd01940 172 SD---------EEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRPVE-VVDTLGAGDSFIAGFLLSLLAG 239
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
101-350 |
4.22e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 66.35 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 101 QTLAGGKGANQA-ACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHLDYVRSVNNePTGHAVVMLQSDGQNSIIIV 179
Cdd:PLN02379 82 KTMAGGSVANTIrGLSAGFGVSTGIIGACGDDEQGKLFVSNMGF--SGVDLSRLRAKKG-PTAQCVCLVDALGNRTMRPC 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 180 GGANMKAWPEIMSDDDLE----IVRNAGIVLLQrEIPDSINIqvakaVKKAGVPVILDVGGMDT-----PIPNELLDS-- 248
Cdd:PLN02379 159 LSSAVKLQADELTKEDFKgskwLVLRYGFYNLE-VIEAAIRL-----AKQEGLSVSLDLASFEMvrnfrSPLLQLLESgk 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 249 IDILSPNETELSRLT-GMPTETFEQISQAVAK-ChklgvKQVLVKLGSKGsALFIQGEKPIQQSIIPAAQVVDTTGAGDT 326
Cdd:PLN02379 233 IDLCFANEDEARELLrGEQESDPEAALEFLAKyC-----NWAVVTLGSKG-CIARHGKEVVRVPAIGETNAVDATGAGDL 306
|
250 260
....*....|....*....|....
gi 145323924 327 FTAAFAVAMVEGKSHEECLRFAGC 350
Cdd:PLN02379 307 FASGFLYGLIKGLSLEECCKVGAC 330
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
229-346 |
5.56e-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: 64.91 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVG-------GMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK-----LGSKG 296
Cdd:cd01173 110 PVMGDNGklyvvaeEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelaDDDRI 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145323924 297 SALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLR 346
Cdd:cd01173 190 EMLGSTATEAWLVQRPKIPFPAYFNGTGDLFAALLLARLLKGKSLAEALE 239
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
75-346 |
7.70e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 65.43 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 75 GSAnadIYVEIERLPKEGETISAKTGQTLAGGKGANQAACgAKLMYPTY-----FVGRLGEDAHGKLIAEALGDDGCGVH 149
Cdd:PTZ00247 35 GSA---ILAEEKQLPIFEELESIPNVSYVPGGSALNTARV-AQWMLQAPkgfvcYVGCVGDDRFAEILKEAAEKDGVEML 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 150 LDYVRSvnnEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREI----PDSInIQVAKAVKK 225
Cdd:PTZ00247 111 FEYTTK---APTGTCAVLVCGKERSLVANLGAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFltvsPNNV-LQVAKHARE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 226 AGVPVILdvgGMDTPIP--------NELLDSIDILSPNETE---LSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGS 294
Cdd:PTZ00247 187 SGKLFCL---NLSAPFIsqffferlLQVLPYVDILFGNEEEaktFAKAMKWDTEDLKEIAARIAMLPKYSGTRPRLVVFT 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145323924 295 KGS--ALFIQGEKPIQQSIIPAAQ--VVDTTGAGDTFTAAFAVAMVEGKSHEECLR 346
Cdd:PTZ00247 264 QGPepTLIATKDGVTSVPVPPLDQekIVDTNGAGDAFVGGFLAQYANGKDIDRCVE 319
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
105-348 |
1.01e-11 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 65.03 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 105 GGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIV--GGA 182
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNG--VNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 183 NMKAWPeimSDDDLEIVRNAGI-----VLLQREIPDSINIQVAKAVKKAGVPVILDvggmdtpiPN-------------E 244
Cdd:PLN02323 121 DMLLRE---SELDLDLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAGALLSYD--------PNlrlplwpsaeaarE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 245 LLDSI----DILSPNETELSRLTGMPTETFEqisqAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIipAAQVVDT 320
Cdd:PLN02323 190 GIMSIwdeaDIIKVSDEEVEFLTGGDDPDDD----TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGF--KVKAVDT 263
|
250 260 270
....*....|....*....|....*....|....*
gi 145323924 321 TGAGDTFTAAFAVAMVEGKS-------HEECLRFA 348
Cdd:PLN02323 264 TGAGDAFVGGLLSQLAKDLSlledeerLREALRFA 298
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
72-348 |
1.63e-11 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 64.57 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 72 VVVGSANADIY-VEIERLPKEGEtiSAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDdgCGVHL 150
Cdd:PRK09954 61 VVVGAINMDIRgMADIRYPQAAS--HPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRR--AGVNV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 151 DYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREI-PDSINIQVAKAvkkAGVP 229
Cdd:PRK09954 137 SGCIRLHGQSTSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLtAEALEWVFTLA---DEIP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 230 VILD-VGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKgsALFIQgEKPIQ 308
Cdd:PRK09954 214 VFVDtVSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDE--SVFCS-EKDGE 290
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145323924 309 QSII--PAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK09954 291 QFLLtaPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFA 332
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
244-348 |
5.56e-11 |
|
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: 62.74 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 244 ELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKL--------GVKQVLVKLGSKGSALFIQGEKPIQQsiIPAA 315
Cdd:cd01943 176 QALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVLQALlfsgilqdPGGGVVLRCGKLGCYVGSADSGPELW--LPAY 253
|
90 100 110
....*....|....*....|....*....|....*...
gi 145323924 316 Q-----VVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:cd01943 254 HtkstkVVDPTGGGNSFLGGFAAGLALTKSIDEACIYG 291
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
78-350 |
7.02e-11 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 62.42 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 78 NADIYVEIERLPKEGETISAKTGQTLAGGKGANQA-ACGAKLMYP--TYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVR 154
Cdd:PLN02548 25 NNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIrVAQWMLQIPgaTSYMGCIGKDKFGEEMKKCATAAGVNVHYYEDE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 155 SVnnePTGHAVVMLQsDGQNSIIivggANMKAWPEIMSDDdLEIVRNAGIVLLQREI----------PDSINIqVAK-AV 223
Cdd:PLN02548 105 ST---PTGTCAVLVV-GGERSLV----ANLSAANCYKVEH-LKKPENWALVEKAKFYyiagffltvsPESIML-VAEhAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 224 KKAGV-------PVILDVGGMDTpipNELLDSIDILSPNETE---LSRLTGMPTETFEQISQAVAKCHKLGVKQvlvklg 293
Cdd:PLN02548 175 ANNKTfmmnlsaPFICEFFKDQL---MEALPYVDFLFGNETEartFAKVQGWETEDVEEIALKISALPKASGTH------ 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323924 294 sKGSALFIQGEKPIQQS-----------IIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRfAGC 350
Cdd:PLN02548 246 -KRTVVITQGADPTVVAedgkvkefpviPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVR-AGN 311
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
104-329 |
2.13e-10 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 60.72 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 104 AGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYVRSVNNEPTGHAVVMLQSDGQNSI--IIVGG 181
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEG--VDTTYLRLDPAHRTSTVVVDLDDQGERSFtfMVRPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 182 ANMkawpeIMSDDDLEIVRnAG-------IVLLQrEIPDSINIQVAKAVKKAGVPVILDvggmdtpiPN----------E 244
Cdd:PRK09434 105 ADL-----FLQPQDLPPFR-QGewlhlcsIALSA-EPSRSTTFEAMRRIKAAGGFVSFD--------PNlredlwqdeaE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 245 LLDSI-------DILSPNETELSRLTGmpTETFEQISQAVAKCHklGVKQVLVKLGSKGSALFIQGekpiQQSIIPAAQV 317
Cdd:PRK09434 170 LRECLrqalalaDVVKLSEEELCFLSG--TSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRG----QVQHFPAPSV 241
|
250
....*....|....
gi 145323924 318 --VDTTGAGDTFTA 329
Cdd:PRK09434 242 dpVDTTGAGDAFVA 255
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
25-348 |
2.64e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 61.39 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 25 LQISTVNPNPAQSRF--------SRPRSLRVLSLSADPS-----------ANRNPKSAVDAHAPPLVVVGSAN--ADIYV 83
Cdd:PLN02341 8 GQLGAFSPHPGLSSPpsphghlvPRRVCSRCRASARASSraragarsrarRRLGDTEVGSAAGKEIDVATLGNlcVDIVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 84 EIERLPK----------EGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVhldyV 153
Cdd:PLN02341 88 PVPELPPpsreerkaymEELAASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV----V 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 154 RSVNNEPTGHAVVMLQ--------SDGQNSIIIVGGANMKAWPEI--MSDDDLEI---VRNAGIVLLQ----REIPDSIN 216
Cdd:PLN02341 164 GLIEGTDAGDSSSASYetllcwvlVDPLQRHGFCSRADFGPEPAFswISKLSAEAkmaIRQSKALFCNgyvfDELSPSAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 217 IQVAKAVKKAGVPVILDVG----GMDTPIPNE------LLDSIDILSPNETELSRLTGMPTETfeQISQAVAKcHKLGVK 286
Cdd:PLN02341 244 ASAVDYAIDVGTAVFFDPGprgkSLLVGTPDErralehLLRMSDVLLLTSEEAEALTGIRNPI--LAGQELLR-PGIRTK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145323924 287 QVLVKLGSKGSALFIQGEkpiqQSIIPA--AQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PLN02341 321 WVVVKMGSKGSILVTRSS----VSCAPAfkVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLA 380
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
218-348 |
1.05e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 58.15 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 218 QVAKAVK-KAGVPVILDvggmdtPI----------PNELLDSI-------DILSPNETELSRLTGMPTETFEQISQAVAK 279
Cdd:PRK12413 87 QALDFIKgHPGIPVVLD------PVlvckethdveVSELRQELiqffpyvTVITPNLVEAELLSGKEIKTLEDMKEAAKK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 280 CHKLGVKQVLVKLGSKGSA-----LFIQG------EKPIQQSiipaaqvvDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK12413 161 LYDLGAKAVVIKGGNRLSQkkaidLFYDGkefvilESPVLEK--------NNIGAGCTFASSIASQLVKGKSPLEAVKNS 232
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
198-348 |
1.32e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 58.06 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 198 IVRNAGIVLLQREIPDSINI--QVAKAVKKAGVP-VILD----VGGMDTPIPNE--------LLDSIDILSPNETELSRL 262
Cdd:PRK12412 67 TIEGVGVDALKTGMLGSVEIieMVAETIEKHNFKnVVVDpvmvCKGADEALHPEtndclrdvLVPKALVVTPNLFEAYQL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 263 TGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKgsalfIQGEKPI------QQSIIPAAQVVDTT---GAGDTFTAAFAV 333
Cdd:PRK12412 147 SGVKINSLEDMKEAAKKIHALGAKYVLIKGGSK-----LGTETAIdvlydgETFDLLESEKIDTTnthGAGCTYSAAITA 221
|
170
....*....|....*
gi 145323924 334 AMVEGKSHEECLRFA 348
Cdd:PRK12412 222 ELAKGKPVKEAVKTA 236
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
98-346 |
1.69e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 57.83 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 98 KTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALgdDGCGVHLDYVRsVNNEPTghAVVMLQSDGQNSII 177
Cdd:PRK09813 16 QLGKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDL--ARMGVDISHVH-TKHGVT--AQTQVELHDNDRVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 178 --IVGG--ANMKawpeiMSDDDLEIVRNAGIVL--LQREIPDSIniqvaKAVKKAGVPVILDVGG-MDTPIPNELLDSID 250
Cdd:PRK09813 91 gdYTEGvmADFA-----LSEEDYAWLAQYDIVHaaIWGHAEDAF-----PQLHAAGKLTAFDFSDkWDSPLWQTLVPHLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 251 IL---SPNETELSRLTgmptetfeqiSQAVAKChklGVKQVLVKLGSKGSaLFIQGEKPIQQSIIPAaQVVDTTGAGDTF 327
Cdd:PRK09813 161 YAfasAPQEDEFLRLK----------MKAIVAR---GAGVVIVTLGENGS-IAWDGAQFWRQAPEPV-TVVDTMGAGDSF 225
|
250
....*....|....*....
gi 145323924 328 TAAFAVAMVEGKSHEECLR 346
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAMA 244
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
219-348 |
9.91e-09 |
|
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: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 219 VAKAVKKAGVPVILD-V----GGmDTPIPNELLDSI--------DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV 285
Cdd:pfam08543 78 VAEKLDKYGVPVVLDpVmvakSG-DSLLDDEAIEALkeellplaTLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGA 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145323924 286 KQVLVK---LGSKGSA---LFIQGEKPIQQSiipaAQVVDTT---GAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:pfam08543 157 KAVLIKgghLEGEEAVvtdVLYDGGGFYTLE----APRIPTKnthGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
97-348 |
3.74e-08 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 54.34 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 97 AKTGQTlAGGKGANQaacgaklmypTYFVGRLGED--AHGkLIAEALGDdgcgvhldYVRSVNNEPTGHAVVMLQSDGQN 174
Cdd:PRK13508 29 VDVSKT-AGGKGLNV----------TRVLSEFGENvlATG-LIGGELGQ--------FIAEHLDDQIKHAFYKIKGETRN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 175 SIIIVGGAN----MKAWPEIMSD-------------DDLEIVRNAGIvlLQREIPDSINIQVAKAVKKAGVPVILDVGGm 237
Cdd:PRK13508 89 CIAILHEGQqteiLEKGPEISVQeadgflhhfkqllESVEVVAISGS--LPAGLPVDYYAQLIELANQAGKPVVLDCSG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 238 dtpipnELLDSI-------DILSPNETELSRLTGMP-TETFEQISQAVAKCHKLGVKQVLVKLGSKGSalFIQGEKPIQQ 309
Cdd:PRK13508 166 ------AALQAVlespykpTVIKPNIEELSQLLGKEvSEDLDELKEVLQQPLFEGIEWIIVSLGADGA--FAKHNDTFYK 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 145323924 310 SIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKA 276
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
254-348 |
5.61e-08 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 53.55 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 254 PNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGsALFIQGE-----KPiqqsiiPAAQVVDTTGAGDTFT 328
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEG-ALWVNASgewiaKP------PACDVVSTVGAGDSMV 258
|
90 100
....*....|....*....|
gi 145323924 329 AAFAVAMVEGKSHEECLRFA 348
Cdd:PRK09513 259 GGLIYGLLMRESSEHTLRLA 278
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
219-348 |
1.08e-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: 52.35 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 219 VAKAVKK-AGVPVILD-V---GGMDTPIPNELLDSI--------DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV 285
Cdd:COG0351 84 VAEILADyPLVPVVLDpVmvaKSGDRLLDEDAVEALrelllplaTVVTPNLPEAEALLGIEITTLDDMREAAKALLELGA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 286 KQVLVK----LGSKGSALFIQGEKPIQQSiipaAQVVDTT---GAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:COG0351 164 KAVLVKgghlPGDEAVDVLYDGDGVREFS----APRIDTGnthGTGCTLSSAIAALLAKGLDLEEAVREA 229
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
242-331 |
2.36e-07 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 51.31 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 242 PNELLDS---IDILSPNETELSRLTGMPTetfeqISQAVAKCHKLGVKQVLVKLGSKGSALFIQGekpiQQSIIPA---A 315
Cdd:cd01946 154 PEKLKKVlakVDVVIINDGEARQLTGAAN-----LVKAARLILAMGPKALIIKRGEYGALLFTDD----GYFAAPAyplE 224
|
90
....*....|....*.
gi 145323924 316 QVVDTTGAGDTFTAAF 331
Cdd:cd01946 225 SVFDPTGAGDTFAGGF 240
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
218-347 |
3.04e-07 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 51.32 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 218 QVAKAVKKAGVPVILDVGGmDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGV-KQVLVKLGSKG 296
Cdd:PRK10294 151 QLISAAQKQGIRCIIDSSG-DALSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKaKRVVVSLGPQG 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 145323924 297 sALFIQGEKPIqQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRF 347
Cdd:PRK10294 230 -ALGVDSENCI-QVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRF 278
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
22-340 |
3.56e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 51.73 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 22 RPQLQISTVNPNPAQSRFSRPRSLRVLSLS-ADPSANRNPKSAVDAHAPP----------LVVVGSANADI-------YV 83
Cdd:PLN02813 12 SLYVPKPNRRLRRVTSQRGAPGLFRIHSRAnNAALAIQQDEEQPEGFGPIpekavperwdVLGLGQAMVDFsgmvddeFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 84 EIERLPKEGETI-----SAKTGQTLAGGkgANQAACGAKLMYPTYFVGRLG-EDAHGK----LIAEALGDDGCGvhlDYV 153
Cdd:PLN02813 92 ERLGLEKGTRKVinheeRGKVLRALDGC--SYKASAGGSLSNTLVALARLGsQSAAGPalnvAMAGSVGSDPLG---DFY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 154 RS-------------VNNEPTGHAVVMLQSDGQNSIIIVGGANmkawpEIMS-DDDL-EIVRNAGIVLLQR---EIPDSI 215
Cdd:PLN02813 167 RTklrranvhflsqpVKDGTTGTVIVLTTPDAQRTMLSYQGTS-----STVNyDSCLaSAISKSRVLVVEGylwELPQTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 216 NI--QVAKAVKKAGVPVIL---DVGGMdTPIPNELLD----SIDILSPNETELSRLTGMP-TETFEQISQAVAKChklgV 285
Cdd:PLN02813 242 EAiaQACEEAHRAGALVAVtasDVSCI-ERHRDDFWDvmgnYADILFANSDEARALCGLGsEESPESATRYLSHF----C 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 145323924 286 KQVLVKLGSKGSALFIQGEKpiqQSIIPAAQV-VDTTGAGDTFTAAFAVAMVEGKS 340
Cdd:PLN02813 317 PLVSVTDGARGSYIGVKGEA---VYIPPSPCVpVDTCGAGDAYAAGILYGLLRGVS 369
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
219-348 |
1.56e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 49.73 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 219 VAKAVKKAGVPVILD---VGGMDTPIPNEllDSIDIL-----------SPNETELSRLTGMPTETFEQISQAVAKCHK-L 283
Cdd:PRK08573 89 VAKTVSKYGFPLVVDpvmIAKSGAPLLRE--DAVDALikrllplatvvTPNRPEAEKLTGMKIRSVEDARKAAKYIVEeL 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 284 GVKQVLVKLGSKGSA-----LFIQGEkpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK08573 167 GAEAVVVKGGHLEGEeavdvLYHNGT--FREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTA 234
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
250-345 |
2.34e-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: 48.67 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 250 DILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK-LGSKGSA-------LFIQGEKPIQQSIIPAAQVVDTT 321
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQrdrsfegLVATQEGRWHISRPLAVFDPPPV 219
|
90 100
....*....|....*....|....
gi 145323924 322 GAGDTFTAAFAVAMVEGKSHEECL 345
Cdd:TIGR00687 220 GTGDLIAALLLATLLHGNSLKEAL 243
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
229-348 |
3.58e-06 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 47.94 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVG-GMDTP------IPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK---------- 291
Cdd:PRK05756 112 PVMGDPEkGCIVApgvaefLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypad 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145323924 292 -----LGSKGSALFIqgEKPiqqsIIP-AAQVVdttGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK05756 192 rfemlLVTADGAWHI--SRP----LVDfMRQPV---GVGDLTSALFLARLLQGGSLEEALEHT 245
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
243-348 |
7.30e-06 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 46.66 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 243 NELLDSIDILSPN--ETELsrLTGMPTETFEQISQAVAK-CHKLGVKQVLVK---LGSKGSA--LFIQGEkpiQQSIIPA 314
Cdd:PRK06427 128 ERLLPLATLITPNlpEAEA--LTGLPIADTEDEMKAAARaLHALGCKAVLIKgghLLDGEESvdWLFDGE---GEERFSA 202
|
90 100 110
....*....|....*....|....*....|....*.
gi 145323924 315 AQV--VDTTGAGDTFTAAFAVAMVEGKSHEECLRFA 348
Cdd:PRK06427 203 PRIptKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
217-343 |
9.63e-06 |
|
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: 47.13 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 217 IQVAKavkKAGVPVILDVGGMDTpipnELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKG 296
Cdd:PRK11316 164 IQLAR---KAGVPVLIDPKGTDF----ERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQG 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145323924 297 SALFIQGEKPIqqsIIPA-AQ-VVDTTGAGDTFTAAFAVAMVEGKSHEE 343
Cdd:PRK11316 237 MTLLQPGKAPL---HLPTqAReVYDVTGAGDTVISVLAAALAAGNSLEE 282
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
74-348 |
2.97e-05 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 45.09 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 74 VGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGcgVHLDYV 153
Cdd:cd01939 5 VGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRG--IDISHC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 154 RSVNNEPTGHAVVMLQSDGQNSIIIvggaNMKAWPEIMSDDDLEIVRN-AGIVLLQREIPDsiniQVAKAVKKagvpvIL 232
Cdd:cd01939 83 YRKDIDEPASSYIIRSRAGGRTTIV----NDNNLPEVTYDDFSKIDLTqYGWIHFEGRNPD----ETLRMMQH-----IE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 233 DVGGMDTPIPNELldSIDILSPNEtELSRLTGM------------------PTETFE-QISQAVAKCHklgvkqVLVKLG 293
Cdd:cd01939 150 EHNNRRPEIRITI--SVEVEKPRE-ELLELAAYcdvvfvskdwaqsrgyksPEECLRgEGPRAKKAAL------LVCTWG 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 145323924 294 SKG-SALFIQGEKpIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSH-EECLRFA 348
Cdd:cd01939 221 DQGaGALGPDGEY-VHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFG 276
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
229-331 |
3.69e-05 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 45.07 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVGGMDTP-----IPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVK----------LG 293
Cdd:PTZ00344 115 PVMGDDGKLYVKeevvdAYRELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITsfrededpthLR 194
|
90 100 110
....*....|....*....|....*....|....*...
gi 145323924 294 SKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAF 331
Cdd:PTZ00344 195 FLLSCRDKDTKNNKRFTGKVPYIEGRYTGTGDLFAALL 232
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
229-349 |
1.66e-04 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 42.72 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVG-GM--DTPIP----NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKlgskgSALFI 301
Cdd:PRK08176 126 PVIGDIDsGIyvKPDLPeayrQHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT-----SAAGN 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 145323924 302 QGEKPIQQSIIPAAQV-------VDTT--GAGDTFTAAFAVAMVEGKSHEECLRFAG 349
Cdd:PRK08176 201 EENQEMQVVVVTADSVnvishprVDTDlkGTGDLFCAELVSGLLKGKALTDAAHRAG 257
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
229-329 |
6.14e-04 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 41.26 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 229 PVILDVGGMDTPIP------NELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLV-------KLGSK 295
Cdd:PLN02978 124 PVLGDEGKLYVPPElvpvyrEKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVItsididgKLLLV 203
|
90 100 110
....*....|....*....|....*....|....*...
gi 145323924 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 |
4.37e-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: 38.36 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323924 186 AWPEIMSDDDLEIVRNAGIVLLQReiPDSINI-----------QVAKAVKKAGVPVILDVGGMdTPIPNELLDSI----D 250
Cdd:cd01171 54 YSPELMVHPLLETDIEELLELLER--ADAVVIgpglgrdeeaaEILEKALAKDKPLVLDADAL-NLLADEPSLIKrygpV 130
|
90 100
....*....|....*....|....*....
gi 145323924 251 ILSPNETELSRLTGMPTETFEQISQAVAK 279
Cdd:cd01171 131 VLTPHPGEFARLLGALVEEIQADRLAAAR 159
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
288-338 |
5.50e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.25 E-value: 5.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 145323924 288 VLVKLGSKGSALFIQgEKPIQQSIIPAAQVvDTTGAGDTFTAAFAVAMVEG 338
Cdd:PLN02630 206 VIVTNGKKGCRIYWK-DGEMRVPPFPAIQV-DPTGAGDSFLGGFVAGLVQG 254
|
|
| |
