|
Name |
Accession |
Description |
Interval |
E-value |
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-276 |
1.01e-48 |
|
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: 164.02 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 4 PIICVGAILVDELIHAGHSILPATTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVkIDA 83
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL-NVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 84 SITKEGIS-GRYTGVLNVDGSLYTAFLSNAAVEMVTPAHLEKQEELLLSAQYIMADANTSVESMNWLLQFSKRTGIPFII 162
Cdd:cd01941 80 GIVFEGRStASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 163 EPVSVPPASKLKDMdLAGLYMVTPNEDELPVM---CSEKSFLTQLQVEELLKRGIQNIWLHNGKQGSAFYNKDKA-ITLH 238
Cdd:cd01941 160 EPTSAPKLKKLFYL-LHAIDLLTPNRAELEALagaLIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGvETKL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2648340274 239 APDI---EVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAH 276
Cdd:cd01941 239 FPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQ 279
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-298 |
4.03e-44 |
|
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: 152.35 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHSILPATTVDAK-ITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDA 83
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGsFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 84 SITKEGI-SGRYTGVLNVDGSLYTAFLSNAAvEMVTPAHLEkqEELLLSAQY-----IMADANTSVESMNWLLQFSKRTG 157
Cdd:COG0524 82 VRRDPGApTGLAFILVDPDGERTIVFYRGAN-AELTPEDLD--EALLAGADIlhlggITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 158 IPFIIEPVSVP----PASKLKDMDLAGLYMVTPNEDELPVMCSEKSFLTQLqvEELLKRGIQNIWLHNGKQGSAFYNKDK 233
Cdd:COG0524 159 VPVSLDPNYRPalwePARELLRELLALVDILFPNEEEAELLTGETDPEEAA--AALLARGVKLVVVTLGAEGALLYTGGE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648340274 234 AITLHAPDIEVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAIVTHLSQAEL 298
Cdd:COG0524 237 VVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-289 |
3.80e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 125.92 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDeLIHAGHSILPATTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDAS 84
Cdd:pfam00294 2 VVVIGEANID-LIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 85 ITKEGIS-GRYTGVLNVDGSLYTAFLSNAAVEMvTPAHLEKQEELLLSAQYI----MADANTSVESMNwLLQFSKRTGIP 159
Cdd:pfam00294 81 VIDEDTRtGTALIEVDGDGERTIVFNRGAAADL-TPEELEENEDLLENADLLyisgSLPLGLPEATLE-ELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 160 FIiePVSVPPASKLKDMDLAGLYMVT---PNEDELPVMCSEKSFLTQL---QVEELLKRGIQNIWLHNGKQGSAFYNKDK 233
Cdd:pfam00294 159 FD--PNLLDPLGAAREALLELLPLADllkPNEEELEALTGAKLDDIEEalaALHKLLAKGIKTVIVTLGADGALVVEGDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648340274 234 AITLHA-PDIEVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAI 289
Cdd:pfam00294 237 EVHVPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
2-259 |
2.21e-23 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 98.46 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 2 QKPIICVGAILVDELIHAGHSILPATTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKI 81
Cdd:PRK09954 57 QEYCVVVGAINMDIRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 82 DASITKEGIS-GRYTGVLNVDGSLYTAFLSNAAVEMVTPAHLEKQEELLLSAQYIMADANTSVESMNWLlqFSKRTGIPF 160
Cdd:PRK09954 137 SGCIRLHGQStSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWV--FTLADEIPV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 161 IIEPVSVPPASKLKDMdLAGLYMVTPNEDELPVMCSE--KSFLTQLQ-VEELLKRGIQNIWLHNGKQGSAFYNKD-KAIT 236
Cdd:PRK09954 215 FVDTVSEFKAGKIKHW-LAHIHTLKPTQPELEILWGQaiTSDADRNAaVNALHQQGVQQIFVYLPDESVFCSEKDgEQFL 293
|
250 260
....*....|....*....|...
gi 2648340274 237 LHAPDIEVVDCTGAGDGSLSGFL 259
Cdd:PRK09954 294 LTAPAHTTVDSFGADDGFMAGLV 316
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-280 |
1.28e-21 |
|
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: 92.23 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 4 PIICVGAILVDELIHAGHsiLPAT--TVDAK-ITKTAGG------VAhnIAKqlsiLGANVQLISVFGNDSDGDWLKQSC 74
Cdd:cd01174 1 KVVVVGSINVDLVTRVDR--LPKPgeTVLGSsFETGPGGkganqaVA--AAR----LGARVAMIGAVGDDAFGDELLENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 75 SAAGVKIDA-SITKEGISGryTGVLNVDGS-----LYTAfLSNAaveMVTPAHLEKQEELLLSAQYIMADANTSVESMNW 148
Cdd:cd01174 73 REEGIDVSYvEVVVGAPTG--TAVITVDESgenriVVVP-GANG---ELTPADVDAALELIAAADVLLLQLEIPLETVLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 149 LLQFSKRTGIPFIIEPVsvpPASKLKDMDLAGLYMVTPNEDELpvmcsekSFLTQLQVEE----------LLKRGIQNIW 218
Cdd:cd01174 147 ALRAARRAGVTVILNPA---PARPLPAELLALVDILVPNETEA-------ALLTGIEVTDeedaekaarlLLAKGVKNVI 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648340274 219 LHNGKQGSAFYNKDKAITLHAPDIEVVDCTGAGD---GSLSGFLLGktlGRTDEECIKLAHTLSA 280
Cdd:cd01174 217 VTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDtfiGALAAALAR---GLSLEEAIRFANAAAA 278
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
5-258 |
2.50e-21 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 91.97 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHSILPATTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDAS 84
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 85 ITKEGIS-GRYTGVLNVDGSLYTAFLSNAAVEMVTPAHLEKQEELLLSAQYIMADANTSVESMNWLLQFSKRTgiPFIIE 163
Cdd:PRK09850 87 LIVPGENtSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAANV--PVFVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 164 PVSVPPASKLKDmDLAGLYMVTPNEDELPVMcSEKSFLTQLQVEELL----KRGIQNIWLHNGKQGSAFYNKDKAITLHA 239
Cdd:PRK09850 165 PVSAWKCVKVRD-RLNQIHTLKPNRLEAETL-SGIALSGREDVAKVAawfhQHGLNRLVLSMGGDGVYYSDISGESGWSA 242
|
250 260
....*....|....*....|
gi 2648340274 240 P-DIEVVDCTGAGDGSLSGF 258
Cdd:PRK09850 243 PiKTNVINVTGAGDAMMAGL 262
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-289 |
8.67e-20 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 87.25 E-value: 8.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHSILPATTvdakITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDAS 84
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQADS----FRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 85 ITKEGisgRYTGV--LNVDGSLYTAFL---SNAAVEMVTPAHLEkqEELLLSAQYI------MADANTSVESMNWLLQFS 153
Cdd:cd01166 78 RVDPG---RPTGLyfLEIGAGGERRVLyyrAGSAASRLTPEDLD--EAALAGADHLhlsgitLALSESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 154 KRTGIPFIIEPVSVPPASKLKDM-----DLAGLY-MVTPNEDELPVMCSEKSFLTQLQVEELLKRGIQNIWLHNGKQGSA 227
Cdd:cd01166 153 KARGVTVSFDLNYRPKLWSAEEArealeELLPYVdIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2648340274 228 FYNKDKAITLHAPDIEVVDCTGAGD----GSLSGFLLGKTLgrtdEECIKLAHTLSAEILQVNGAI 289
Cdd:cd01166 233 VYTGGGRVFVPAYPVEVVDTTGAGDafaaGFLAGLLEGWDL----EEALRFANAAAALVVTRPGDI 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
4-289 |
1.53e-18 |
|
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: 83.51 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 4 PIICVGAILVDeLIHAGHSI--LPATTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKI 81
Cdd:cd01942 1 DVAVVGHLNYD-IILKVESFpgPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 82 DASITKEgisGRYTGVlnvdgSLYTAFLSNAAVEMVTPAHLEKQEE-----LLLSAQYIMADANTSVEsmnWLLQFSKRT 156
Cdd:cd01942 80 SHVRVVD---EDSTGV-----AFILTDGDDNQIAYFYPGAMDELEPndeadPDGLADIVHLSSGPGLI---ELARELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 157 GIPFIIEP---VSVPPASKLKDMdLAGLYMVTPNEDELPVMCSeksfLTQLQVEELLKrGIQNIWLHNGKQGSAFYNKDK 233
Cdd:cd01942 149 GITVSFDPgqeLPRLSGEELEEI-LERADILFVNDYEAELLKE----RTGLSEAELAS-GVRVVVVTLGPKGAIVFEDGE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648340274 234 AITLHA-PDIEVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAI 289
Cdd:cd01942 223 EVEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
5-290 |
6.46e-18 |
|
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: 82.28 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHSILP--------ATTVDA----------KITKTAGGVAHNIAKQLSILGANVQLISVFGNDSD 66
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEklglkkgdMILADMeeqeellaklPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 67 GDWLKQSCSAAGVKIDASITKEGISGRYTGVLNVDG--SLYTaFLSnAAVEmVTPAHLEKqeELLLSAQYI-----MADA 139
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAerTMCT-YLG-AANE-LSPDDLDW--SLLAKAKYLylegyLLTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 140 ntSVESMNWLLQFSKRTGIPFIIEPVS--VPPASKLKDMDLAG-LYMVTPNEDELPVMCSEKSFLTQLQVEELLKRGIQN 216
Cdd:cd01168 159 --PPEAILLAAEHAKENGVKIALNLSApfIVQRFKEALLELLPyVDILFGNEEEAEALAEAETTDDLEAALKLLALRCRI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648340274 217 IWLHNGKQGSAFYNKDKAITLHAPDIE-VVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAIV 290
Cdd:cd01168 237 VVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
32-302 |
2.42e-16 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 77.87 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 32 KITKTAGGVAHNIAKQLSILGANVQLISVFGNDsDGDWLKQSCSAAGVKIDA---------SIT-KEGISGRYTgVLNVD 101
Cdd:COG1105 29 EVRLDPGGKGINVARVLKALGVDVTALGFLGGF-TGEFIEELLDEEGIPTDFvpiegetriNIKiVDPSDGTET-EINEP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 102 GslytAFLSNAAVEMVtpahLEKQEELLLSAQYIMA--------DANTSVEsmnwLLQFSKRTGIPFIIEpvsvppASK- 172
Cdd:COG1105 107 G----PEISEEELEAL----LERLEELLKEGDWVVLsgslppgvPPDFYAE----LIRLARARGAKVVLD------TSGe 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 173 -LKDMDLAGLYMVTPNEDELPVMC-----SEKSFLTQLQveELLKRGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVD 246
Cdd:COG1105 169 aLKAALEAGPDLIKPNLEELEELLgrpleTLEDIIAAAR--ELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVS 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2648340274 247 CTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAIVTHLSQAE-LLSRV 302
Cdd:COG1105 247 TVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEeLLAQV 303
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-289 |
6.94e-16 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 76.52 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDelihaghsILPA-TTVDAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDA 83
Cdd:cd01167 2 VVCFGEALID--------FIPEgSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 84 SITKEGISgryTGVLNV----DGSLYTAFLSNAAVEMVTPAHLekQEELLLSAQYI------MADAnTSVESMNWLLQFS 153
Cdd:cd01167 74 IQFDPAAP---TTLAFVtldaDGERSFEFYRGPAADLLLDTEL--NPDLLSEADILhfgsiaLASE-PSRSALLELLEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 154 KRTGIPFIIEPvSVPPA---------SKLKDM-DLAGLYMVtpNEDELpvmcsekSFLTQLQVEEllkRGIQNIWLHN-- 221
Cdd:cd01167 148 KKAGVLISFDP-NLRPPlwrdeeearERIAELlELADIVKL--SDEEL-------ELLFGEEDPE---EIAALLLLFGlk 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 222 ------GKQGSAFYNKDKAITLHAPDIEVVDCTGAGDGSLSGFLLGktLGRTD---------EECIKLAHTLSAEILQVN 286
Cdd:cd01167 215 lvlvtrGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQ--LLSRGllaldedelAEALRFANAVGALTCTKA 292
|
...
gi 2648340274 287 GAI 289
Cdd:cd01167 293 GAI 295
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
38-288 |
1.43e-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: 72.00 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 38 GGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDASITKEGISGrYTGVLNVDGSlyTAFL-SNAAVeM 116
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENA-VADVELVDGD--RIFGlSNKGG-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 117 VTPAHLEKQEELLLSAQYIMADANTSVESMNWLLQFSKRTGIPFIIEpVSVppasklkDMDLAGLYMVTPNEDELPVMCS 196
Cdd:cd01940 98 AREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFD-FSD-------RWDDDYLQLVCPYVDFAFFSAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 197 EksfLTQLQVEELLK----RGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVDCTGAGDGSLSGFLLGKTLGRTD-EEC 271
Cdd:cd01940 170 D---LSDEEVKAKLKeavsRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAiAEA 246
|
250
....*....|....*..
gi 2648340274 272 IKLAHTLSAEILQVNGA 288
Cdd:cd01940 247 MRQGAQFAAKTCGHEGA 263
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
5-275 |
1.37e-13 |
|
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: 69.90 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHaGHSI-------LPATTVDaKITKTAGGVAhNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAA 77
Cdd:cd01172 2 VLVVGDVILDEYLY-GDVErispeapVPVVKVE-REEIRLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 78 GVKIDA-------SITKEGISGRYTGVLNVD---GSLYTAFLSNAAVEMVtpahlekqEELLLSAQ-YIMADANTSV--- 143
Cdd:cd01172 79 GIDTDGivdegrpTTTKTRVIARNQQLLRVDredDSPLSAEEEQRLIERI--------AERLPEADvVILSDYGKGVltp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 144 ESMNWLLQFSKRTGIPFIIEPvSVPPASKLKDMDLaglymVTPNEDELPVMCSeKSFLTQLQVEELLKRGIQ-----NIW 218
Cdd:cd01172 151 RVIEALIAAARELGIPVLVDP-KGRDYSKYRGATL-----LTPNEKEAREALG-DEINDDDELEAAGEKLLEllnleALL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2648340274 219 LHNGKQGSAFYNKDKAITlHAPDI--EVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLA 275
Cdd:cd01172 224 VTLGEEGMTLFERDGEVQ-HIPALakEVYDVTGAGDTVIATLALALAAGADLEEAAFLA 281
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
34-275 |
1.19e-12 |
|
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: 66.79 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 34 TKTAGGVAHNIAKQLSILGANVQLISVFGNDSdGDWLKQSCSAAGVKID----ASITKEGI-----SGRYTGvLNVDGSL 104
Cdd:cd01164 32 RKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDfvevAGETRINVkikeeDGTETE-INEPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 105 ytafLSNAAVEMVtpahLEKQEELLLSAQYIMA----DANTSVESMNWLLQFSKRTGIPFIIEPVSVPPASKLKdmdlAG 180
Cdd:cd01164 110 ----ISEEELEAL----LEKLKALLKKGDIVVLsgslPPGVPADFYAELVRLAREKGARVILDTSGEALLAALA----AK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 181 LYMVTPNEDELPVMCSeKSFLTQLQVE----ELLKRGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVDCTGAGDGSLS 256
Cdd:cd01164 178 PFLIKPNREELEELFG-RPLGDEEDVIaaarKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVA 256
|
250
....*....|....*....
gi 2648340274 257 GFLLGKTLGRTDEECIKLA 275
Cdd:cd01164 257 GFVAGLAQGLSLEEALRLA 275
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-304 |
1.38e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 1 MQKPIICVGAILVDELIHAGHSILPATTVDAKITKTA-GGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGV 79
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGfGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 80 KID-ASITKEGISGRYTGVLNVDGSLYTAFLSNAAVEMVTPAHLEKQEELLLS-AQYIMADANTSVESMNWLLQFSKRTG 157
Cdd:PTZ00292 94 NTSfVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 158 IPFIIEPVSVPPAS---KLKDMdLAGLYMVTPNEDELPVMCSEKSFLTQ---LQVEELLKRGIQNIWLHNGKQGSAFYNK 231
Cdd:PTZ00292 174 CYTVFNPAPAPKLAeveIIKPF-LKYVSLFCVNEVEAALITGMEVTDTEsafKASKELQQLGVENVIITLGANGCLIVEK 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2648340274 232 DKA-ITLHAPDIEVVDCTGAGD---GSLSGFLlgkTLGRTDEECIKLAHTLSAEILQVNGAIVTHLSQAELLSRVSK 304
Cdd:PTZ00292 253 ENEpVHVPGKRVKAVDTTGAGDcfvGSMAYFM---SRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPADVKE 326
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
51-280 |
1.69e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 66.82 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 51 LGANVQLISVFGNDSDGDWLKQSCSAAGVKIDAsITKegISGRYTGV----LNVDG--SLYTAFLSNAAVemvTPAHLEK 124
Cdd:PRK11142 52 LGADIAFIACVGDDSIGESMRQQLAKDGIDTAP-VSV--IKGESTGValifVNDEGenSIGIHAGANAAL---TPALVEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 125 QEELLLSAQYIMADANTSVESMNWLLQFSKRTGIPFIIEPVsvpPASKLKDMDLAGLYMVTPNEdelpvmcSEKSFLTQL 204
Cdd:PRK11142 126 HRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILNPA---PARELPDELLALVDIITPNE-------TEAEKLTGI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 205 QVEE----------LLKRGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVDCTGAGD---GSL-SGFLLGKTLgrtdEE 270
Cdd:PRK11142 196 RVEDdddaakaaqvLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDtfnGALvTALLEGKPL----PE 271
|
250
....*....|
gi 2648340274 271 CIKLAHTLSA 280
Cdd:PRK11142 272 AIRFAHAAAA 281
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-261 |
2.93e-12 |
|
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: 64.42 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHSILPATTVDAKITK-TAGGVAHNIAKQLSILGANVQLIsvfgndsdgdwlkqscsaagvkida 83
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEeRAGGGAANVAVALARLGVSVTLV------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 84 sitkeGISGRYTGVLNVDGslytaflsnaavemvtpahlekqeelllsaqyimadantsvESMNWLLQFSKRTGIPFIIE 163
Cdd:cd00287 57 -----GADAVVISGLSPAP-----------------------------------------EAVLDALEEARRRGVPVVLD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 164 PVSV---PPASKLKDMdLAGLYMVTPNEDELPVMCSEKSFLTQLQVE---ELLKRGIQNIWLHNGKQGSAFYNKDKAI-T 236
Cdd:cd00287 91 PGPRavrLDGEELEKL-LPGVDILTPNEEEAEALTGRRDLEVKEAAEaaaLLLSKGPKVVIVTLGEKGAIVATRGGTEvH 169
|
250 260
....*....|....*....|....*
gi 2648340274 237 LHAPDIEVVDCTGAGDGSLSGFLLG 261
Cdd:cd00287 170 VPAFPVKVVDTTGAGDAFLAALAAG 194
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
2-275 |
5.48e-12 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 65.22 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 2 QKPIICVGAILVDELIHaGHSI-------LPATTVDaKITKTAGG---VAHNIAKqlsiLGANVQLISVFGNDSDGDWLK 71
Cdd:COG2870 15 RARVLVVGDVMLDRYWY-GDVErispeapVPVVRVE-REEERPGGaanVAANLAA----LGAQVTLVGVVGDDEAGRELR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 72 QSCSAAGVKIDASITKegiSGRYTgvlnvdgSLYTAFLSNAA------VEMVTPAHLEKQEELLLSAQYIMADANT---- 141
Cdd:COG2870 89 RLLEEAGIDTDGLVVD---PRRPT-------TTKTRVIAGGQqllrldFEDRFPLSAELEARLLAALEAALPEVDAvils 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 142 -------SVESMNWLLQFSKRTGIPFIIEPvsvppasKLKD-MDLAGLYMVTPNEDEL----PVMCSEKSFLTQLQVEEL 209
Cdd:COG2870 159 dygkgvlTPELIQALIALARAAGKPVLVDP-------KGRDfSRYRGATLLTPNLKEAeaavGIPIADEEELVAAAAELL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2648340274 210 LKRGIQNIWLHNGKQGSAFYNKDKAIT-LHAPDIEVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLA 275
Cdd:COG2870 232 ERLGLEALLVTRGEEGMTLFDADGPPHhLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELA 298
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-252 |
9.29e-11 |
|
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: 61.16 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 5 IICVGAILVDELIHAGHsiLPATtvDAKI-----TKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGV 79
Cdd:cd01945 2 VLGVGLAVLDLIYLVAS--FPGG--DGKIvatdyAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 80 KIDASITKEGISGRYTGVLNVDGS----LYTAFLSNAAVEMVTPAHLEKQEELLLSAQyiMADANTSVesmnwlLQFSKR 155
Cdd:cd01945 78 DTSFIVVAPGARSPISSITDITGDratiSITAIDTQAAPDSLPDAILGGADAVLVDGR--QPEAALHL------AQEARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 156 TGIPfiiEPVSVPPASKLKDMDLAGL--YMVTPnEDELPVMC--SEKSFLTQLQveellKRGIQNIWLHNGKQGSAFYNK 231
Cdd:cd01945 150 RGIP---IPLDLDGGGLRVLEELLPLadHAICS-ENFLRPNTgsADDEALELLA-----SLGIPFVAVTLGEAGCLWLER 220
|
250 260
....*....|....*....|..
gi 2648340274 232 DKA-ITLHAPDIEVVDCTGAGD 252
Cdd:cd01945 221 DGElFHVPAFPVEVVDTTGAGD 242
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-289 |
4.65e-10 |
|
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: 58.97 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 4 PIICVGAILVDELIHAG-HSILpattvdAKITKTAGGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKID 82
Cdd:cd01947 7 HVEWDIFLSLDAPPQPGgISHS------SDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 83 ASITKEGiSGRYTGVLNVDGSLYTAFLSNAAVEMVTPAHLEKQEELLLSAQYIMADA-NTSVESMNWLLQFSKRTGIPFI 161
Cdd:cd01947 81 VAWRDKP-TRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGDGVFITAAAVDKEAiRKCRETKLVILQVTPRVRVDEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 162 IEpvsvppASKLKDMdlaglymvtpnedelpVMCSEKSFLTQLQVEELLKRGIQNIWLHNGKQGSAFY--NKDKAITLHA 239
Cdd:cd01947 160 NQ------ALIPLDI----------------LIGSRLDPGELVVAEKIAGPFPRYLIVTEGELGAILYpgGRYNHVPAKK 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2648340274 240 PDieVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAI 289
Cdd:cd01947 218 AK--VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
38-288 |
1.06e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 57.83 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 38 GGVAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVKIDASITKEGisgrytgvlnvdgslytaflsNAAVEMV 117
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG---------------------VTAQTQV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 118 TPAHLEKqeellLSAQY---IMADANTSVESMNWLLQFSK-RTGI--------PFIIE---PVSVPPASKLKDMDLAGLy 182
Cdd:PRK09813 82 ELHDNDR-----VFGDYtegVMADFALSEEDYAWLAQYDIvHAAIwghaedafPQLHAagkLTAFDFSDKWDSPLWQTL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 183 mvTPNEDELPVMCSEKSFLTQLQVEELLKRGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVDCTGAGDGSLSGFLLGK 262
Cdd:PRK09813 156 --VPHLDYAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGW 233
|
250 260
....*....|....*....|....*.
gi 2648340274 263 TLGRTDEECIKLAHTLSAEILQVNGA 288
Cdd:PRK09813 234 LAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
37-277 |
1.73e-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: 52.14 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 37 AGGVAHNIAKqlsiLGANVQLISVFGNDSDGDWLKQSCSAAGVKID-------ASITKEGISGRYTGVLNVDgslytaFl 109
Cdd:PRK11316 53 AANVAMNIAS----LGAQARLVGLTGIDEAARALSKLLAAVGVKCDfvsvpthPTITKLRVLSRNQQLIRLD------F- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 110 sNAAVEMVTPAHLEKQEELLLsAQY---IMAD----ANTSVESMnwlLQFSKRTGIPFIIEPvsvppasKLKDMDL-AGL 181
Cdd:PRK11316 122 -EEGFEGVDPQPLLERIEQAL-PSIgalVLSDyakgALASVQAM---IQLARKAGVPVLIDP-------KGTDFERyRGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 182 YMVTPN--EDELPV--MCSEksfltqlqvEELLKRGIQNIWLHN--------GKQGSAFYNKDKAiTLHAPDI--EVVDC 247
Cdd:PRK11316 190 TLLTPNlsEFEAVVgkCKDE---------AELVEKGMKLIADYDlsallvtrSEQGMTLLQPGKA-PLHLPTQarEVYDV 259
|
250 260 270
....*....|....*....|....*....|..
gi 2648340274 248 TGAGDGSLSgfLLGKTL--GRTDEECIKLAHT 277
Cdd:PRK11316 260 TGAGDTVIS--VLAAALaaGNSLEEACALANA 289
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
179-302 |
3.46e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 50.85 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 179 AGL----YMVTPNEDELPVMCSEKsfLTQLQ-----VEELLKRGIQNIWLHNGKQGSAFYNKDKAITLHAPDIEVVDCTG 249
Cdd:PRK09513 175 AGLkaapWLVKPNRRELEIWAGRK--LPELKdvieaAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVG 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2648340274 250 AGDGSLSGFLLGKTLGRTDEECIKLAHTLSA-EILQVNGAIVTHLSQAELLSRV 302
Cdd:PRK09513 253 AGDSMVGGLIYGLLMRESSEHTLRLATAVSAlAVSQSNVGITDRPQLAAMMARV 306
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
4-280 |
6.67e-05 |
|
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: 43.56 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 4 PIICVGAILVDELIHAGHsiLPATTVDA---KITKTAGGvAHNIAKQLSILGANVQLISVFGNDSDGDWLKQSCSAAGVK 80
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDK--LPASGGDIeakSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 81 IdaSITKEGISGRYTGVLNVDGSLYTAFLSNAAVE----MVTPAHLEKQEE-LLLSAQYIMADANTSVESM-NWLLQFSK 154
Cdd:cd01944 78 I--LLPPRGGDDGGCLVALVEPDGERSFISISGAEqdwsTEWFATLTVAPYdYVYLSGYTLASENASKVILlEWLEALPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648340274 155 RTgiPFIIEP---VSVPPASKLKDMdLAGLYMVTPNEDELPVMCSEKSFLTQLQVEELLKRGIQNIWLHNGKQGSAFYNK 231
Cdd:cd01944 156 GT--TLVFDPgprISDIPDTILQAL-MAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2648340274 232 D-KAITLHAPDIEVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSA 280
Cdd:cd01944 233 DgNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
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| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
243-290 |
2.53e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 42.32 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2648340274 243 EVVDCTGAGDGSLSGFLLGKTLGRTDEECIKLAHTLSAEILQVNGAIV 290
Cdd:PTZ00247 289 KIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTY 336
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| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
221-261 |
2.22e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 39.02 E-value: 2.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2648340274 221 NGKQGSAFYNKDKAITLHA-PDIEVvDCTGAGDGSLSGFLLG 261
Cdd:PLN02630 210 NGKKGCRIYWKDGEMRVPPfPAIQV-DPTGAGDSFLGGFVAG 250
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