|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
2-294 |
5.20e-138 |
|
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: 391.91 E-value: 5.20e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAADVLKTCQLIILQLEIPLETVYAAIDFARQNNIKVIL 161
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 162 NPAPAsKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVS 241
Cdd:cd01174 161 NPAPA-RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 817365314 242 VHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPD 294
Cdd:cd01174 240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
7-298 |
1.55e-135 |
|
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: 385.80 E-value: 1.55e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 7 GSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAV 86
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 87 AGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAADVLKTCQLIILQLEIPLETVYAAIDFARQNNIKVILNPAPA 166
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 167 SKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVSVHAID 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 817365314 247 TSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPDASQF 298
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-297 |
8.81e-105 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 308.97 E-value: 8.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:PTZ00292 17 DVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVD-KSSQNRILIIKGANNHLLPADVDAAAD-VLKTCQLIILQLEIPLETVYAAIDFARQNNIKV 159
Cdd:PTZ00292 97 FVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDnIQNICKYLICQNEIPLETTLDALKEAKERGCYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 160 ILNPAPASKALDIGYACQC----EFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMH-GEEI 234
Cdd:PTZ00292 177 VFNPAPAPKLAEVEIIKPFlkyvSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEkENEP 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817365314 235 HHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPDASQ 297
Cdd:PTZ00292 257 VHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSE 319
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-298 |
1.65e-88 |
|
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: 266.37 E-value: 1.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAA----ADVLkTCQLIILQLEIPLETVYAAIDFARQNNI 157
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAllagADIL-HLGGITLASEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 158 KVILNPA-------PASKALDIGYAcQCEFFMPNETELAILTGMpvdslDNIYRAGRSLLDKGLHNLIITLGHRGSLWMH 230
Cdd:COG0524 160 PVSLDPNyrpalwePARELLRELLA-LVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817365314 231 GEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPDASQF 298
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
3-302 |
1.34e-74 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 231.30 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQH 82
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAADVLKTCQLIILQLEIPLETVYAAIDFARQNNIKVILN 162
Cdd:PRK11142 85 VSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 163 PAPASKALDIGYACqCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVSV 242
Cdd:PRK11142 165 PAPARELPDELLAL-VDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 243 HAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPDASQFIDFL 302
Cdd:PRK11142 244 QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-289 |
1.07e-60 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 195.25 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDDMPqvGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAADVLKTCQLI----ILQLEIPLETVYAAIDFARQNN- 156
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 157 -IKVILNPAPASKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIH 235
Cdd:pfam00294 159 fDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 236 HVPPV-SVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQ 289
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-287 |
1.16e-42 |
|
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: 148.49 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITyiddmPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:cd01166 1 DVVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVDKSSQNRILI-IKG-ANNHLLPADVDAAAdvLKTCQLIIL------QLEIPLETVYAAIDFAR 153
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRVLYyRAGsAASRLTPEDLDEAA--LAGADHLHLsgitlaLSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 154 QNNIKVILNPAPASKALDIGYACQ--------CEFFMPNETELAILTGMPVDS-LDNIYRAgrslLDKGLHNLIITLGHR 224
Cdd:cd01166 154 ARGVTVSFDLNYRPKLWSAEEAREaleellpyVDIVLPSEEEAEALLGDEDPTdAAERALA----LALGVKAVVVKLGAE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817365314 225 GSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKG 287
Cdd:cd01166 230 GALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
2-289 |
1.27e-37 |
|
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: 134.75 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQ 81
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 82 HVKAVAGTSSGVAPIFVDKsSQNRILII-KGANNHLLPADVDAAADVLKtcqliilqlEIPLETVYAAIDFARQ---NNI 157
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDG-DDNQIAYFyPGAMDELEPNDEADPDGLAD---------IVHLSSGPGLIELARElaaGGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 158 KVILNPAPASKALDIGYA----CQCEFFMPNETELAILTGMpvdsldniyrAGRSLLD--KGLHNLIITLGHRGSLWMHG 231
Cdd:cd01942 151 TVSFDPGQELPRLSGEELeeilERADILFVNDYEAELLKER----------TGLSEAElaSGVRVVVVTLGPKGAIVFED 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 817365314 232 EEIHHVPPV-SVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQ 289
Cdd:cd01942 221 GEEVEVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
6-294 |
4.44e-37 |
|
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: 133.57 E-value: 4.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 6 IGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKA 85
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 86 VAGTSSGVAPIFVDKSSQNRILIIKG---ANNHLLPADVDAAADVLktcqlIILQLEIPLETVYAAIdfARQNNIKVILN 162
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIdtqAAPDSLPDAILGGADAV-----LVDGRQPEAALHLAQE--ARARGIPIPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 163 PAPASKALDIGYACQCEFFMPNETELAILTGmpvDSLDNIYRAGRSLldkGLHNLIITLGHRGSLWMHGE-EIHHVPPVS 241
Cdd:cd01945 158 LDGGGLRVLEELLPLADHAICSENFLRPNTG---SADDEALELLASL---GIPFVAVTLGEAGCLWLERDgELFHVPAFP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 817365314 242 VHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPD 294
Cdd:cd01945 232 VEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-287 |
2.69e-36 |
|
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: 131.99 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITyiDDMPQVGETLEAPdfeigcGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQH 82
Cdd:cd01167 2 VVCFGEALIDFIP--EGSGAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPaDVDAAADVLKTCQLI----ILQLEIPL-ETVYAAIDFARQNNI 157
Cdd:cd01167 74 IQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLL-DTELNPDLLSEADILhfgsIALASEPSrSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 158 KVILNP---------APASKALDIGYACQCEFFMPNETELAILTGMpvdslDNIYRAGRSLLDKGLHNLIITLGHRGSLW 228
Cdd:cd01167 153 LISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817365314 229 MHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDIL-------KAMEMASAFAAYSVTGKG 287
Cdd:cd01167 228 YTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedelaEALRFANAVGALTCTKAG 293
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
1-302 |
5.18e-31 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 118.08 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 1 MDIAVIGSNMVDLITYiddmpQVGETLE-APDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVN 79
Cdd:TIGR04382 2 LDVITIGRVGVDLYPQ-----QIGVPLEdVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 80 TQHVKAVAGTSSGVApiFVDKSSQNRILII----KGANNHLLPADVDAaaDVLKTCQLII-----LQLEIPLETVYAAID 150
Cdd:TIGR04382 77 TSHVVTDPGRRTSLV--FLEIKPPDEFPLLfyreNAADLALTPDDVDE--DYIASARALLvsgtaLSQEPSREAVLKALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 151 FARQNNIKVIL----------NPAPASKALDIgYACQCEFFMPNETELAILTGmpvdSLDNIyRAGRSLLDKGLHNLIIT 220
Cdd:TIGR04382 153 YARAAGVRVVLdidyrpylwkSPEEAGIYLRL-VLPLVDVIIGTREEFDIAGG----EGDDE-AAARALLDAGVEILVVK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 221 LGHRGSLWMHG-EEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPDASQFI 299
Cdd:TIGR04382 227 RGPEGSLVYTGdGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLEELE 306
|
...
gi 817365314 300 DFL 302
Cdd:TIGR04382 307 AFL 309
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-283 |
1.87e-29 |
|
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: 113.56 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMPQV-----GETLEAPdfeigcGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAG 77
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPgtsnpGHVKQSP------GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 78 VNTqHVKAVAGTSSGVAPIFVDKssqNRILIIKGAN----NHLLPADVDAAADVLKTCQLIILQLEIPLETVYAAIDFAR 153
Cdd:cd01941 76 LNV-RGIVFEGRSTASYTAILDK---DGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 154 QNNIKVILNPAPASKALDIGYAC-QCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLW---M 229
Cdd:cd01941 152 KHGVPVAFEPTSAPKLKKLFYLLhAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLssrE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 230 HGEEIHHVPPVSVHAI-DTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSV 283
Cdd:cd01941 232 GGVETKLFPAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
11-294 |
9.34e-29 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 111.77 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 11 VDLITYIDDMpQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDdlFAENTIRN-LQQAGVNTQHVKAVAGT 89
Cdd:COG1105 10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGG--FTGEFIEElLDEEGIPTDFVPIEGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 90 SSGVApiFVDKSSqNRILIIKGANNHLLPADVDAA----ADVLKTCQLII----LQLEIPlETVYAA-IDFARQNNIKVI 160
Cdd:COG1105 87 RINIK--IVDPSD-GTETEINEPGPEISEEELEALlerlEELLKEGDWVVlsgsLPPGVP-PDFYAElIRLARARGAKVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 161 LNpapAS-KALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPP 239
Cdd:COG1105 163 LD---TSgEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 240 VSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQRSYPD 294
Cdd:COG1105 240 PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDRE 294
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
3-294 |
2.34e-28 |
|
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: 110.73 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMpqvGETLEAP-------DFEIGCGGkGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQ 75
Cdd:cd01172 2 VLVVGDVILDEYLYGDVE---RISPEAPvpvvkveREEIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 76 AGVNTQhvkavagtssgvapIFVDKS----SQNRILiikGANNHLLPAD---------------VDAAADVLKTCQLIIL 136
Cdd:cd01172 78 EGIDTD--------------GIVDEGrpttTKTRVI---ARNQQLLRVDreddsplsaeeeqrlIERIAERLPEADVVIL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 137 ----QLEIPLETVYAAIDFARQNNIKVILNPapasKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDK 212
Cdd:cd01172 141 sdygKGVLTPRVIEALIAAARELGIPVLVDP----KGRDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 213 -GLHNLIITLGHRGSLWMHG-EEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVtGK-GTQ 289
Cdd:cd01172 217 lNLEALLVTLGEEGMTLFERdGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVV-GKvGTA 295
|
....*
gi 817365314 290 RSYPD 294
Cdd:cd01172 296 PVTPK 300
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-284 |
1.17e-27 |
|
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: 109.24 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 1 MDIAVIGSNMVDLITYIDD-----------------MPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDD 63
Cdd:cd01168 2 YDVLGLGNALVDILAQVDDafleklglkkgdmiladMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 64 LFAENTIRNLQQAGVNTqHVKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAAdvLKTCQLIIL---QLEI 140
Cdd:cd01168 82 KLGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAKYLYLegyLLTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 141 PLETVYAAIDFARQNNIKVILNpapASkALDIgyacqCEFFMP--------------NETELAILTGMPVDSLDNIyraG 206
Cdd:cd01168 159 PPEAILLAAEHAKENGVKIALN---LS-APFI-----VQRFKEallellpyvdilfgNEEEAEALAEAETTDDLEA---A 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817365314 207 RSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPV-SVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVT 284
Cdd:cd01168 227 LKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIpVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQ 305
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
3-260 |
3.38e-25 |
|
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: 99.86 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTrvgddlfaentirnlqqagvntqh 82
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPifvdkssqnriliikgannhllpadvdaaadvlktcqliilqleiplETVYAAIDFARQNNIKVILN 162
Cdd:cd00287 58 ADAVVISGLSPAP-----------------------------------------------EAVLDALEEARRRGVPVVLD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 163 PAPASKALDIGYACQCE----FFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMH-GEEIHHV 237
Cdd:cd00287 91 PGPRAVRLDGEELEKLLpgvdILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATrGGTEVHV 170
|
250 260
....*....|....*....|...
gi 817365314 238 PPVSVHAIDTSGAGDAFIGCFAH 260
Cdd:cd00287 171 PAFPVKVVDTTGAGDAFLAALAA 193
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
3-288 |
6.68e-25 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 101.81 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDliTYIDdmpqvGETL----EAP-------DFEIGCGGkGANQAVAAARLGANVMMVTRVGDDLFAENTIR 71
Cdd:COG2870 18 VLVVGDVMLD--RYWY-----GDVErispEAPvpvvrveREEERPGG-AANVAANLAALGAQVTLVGVVGDDEAGRELRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 72 NLQQAGVNTQHVkavagtssgvapifvdKSSQNRILIIK----GANNHLLPAD---------------VDAAADVLKTCQ 132
Cdd:COG2870 90 LLEEAGIDTDGL----------------VVDPRRPTTTKtrviAGGQQLLRLDfedrfplsaelearlLAALEAALPEVD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 133 LIIL---------QLEIPletvyAAIDFARQNNIKVILNPapasKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIY 203
Cdd:COG2870 154 AVILsdygkgvltPELIQ-----ALIALARAAGKPVLVDP----KGRDFSRYRGATLLTPNLKEAEAAVGIPIADEEELV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 204 RAGRSLLDK-GLHNLIITLGHRG-SLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAY 281
Cdd:COG2870 225 AAAAELLERlGLEALLVTRGEEGmTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGI 304
|
....*..
gi 817365314 282 SVTGKGT 288
Cdd:COG2870 305 VVGKLGT 311
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
11-289 |
1.18e-24 |
|
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: 100.68 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 11 VDLITYIDDmPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGD---DLFAENtirnLQQAGVNTQHVKAVA 87
Cdd:cd01164 11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGftgDFFEAL----LKEEGIPDDFVEVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 88 GTSSGVApIfvdKSSQNRILIIKGANNHLLPADVDAAADVLKT----CQLIILQLEIPL---ETVYAAI-DFARQNNIKV 159
Cdd:cd01164 86 ETRINVK-I---KEEDGTETEINEPGPEISEEELEALLEKLKAllkkGDIVVLSGSLPPgvpADFYAELvRLAREKGARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 160 ILNpapAS-KALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVP 238
Cdd:cd01164 162 ILD---TSgEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 817365314 239 PVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKGTQ 289
Cdd:cd01164 239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-284 |
1.16e-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: 92.10 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVntQH 82
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVDAAADvlktcqLIILQLEIPLETvyaAIDFARqNNIKVILN 162
Cdd:cd01947 80 TVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGD------GVFITAAAVDKE---AIRKCR-ETKLVILQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 163 PAPASKALDIGYACQ-CEFFMPNETELAILTgmpvdsldniyrAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVS 241
Cdd:cd01947 150 VTPRVRVDELNQALIpLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 817365314 242 VHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVT 284
Cdd:cd01947 218 AKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVS 260
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
37-280 |
1.34e-16 |
|
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: 77.78 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 37 GGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAVAGtSSGVApiFVDKSSQNRILII--KGANN 114
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEG-ENAVA--DVELVDGDRIFGLsnKGGVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 115 HLLPADVDAAAdvlktcqliILQLEIPLETVYAAIDFARQNNIKVILNPAPAS-----KALDIGYACQCEFfmpneTELA 189
Cdd:cd01940 99 REHPFEADLEY---------LSQFDLVHTGIYSHEGHLEKALQALVGAGALISfdfsdRWDDDYLQLVCPY-----VDFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 190 ILTGmPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHeYVLHGD-- 267
Cdd:cd01940 165 FFSA-SDLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLL-SLLAGGta 242
|
250
....*....|...
gi 817365314 268 ILKAMEMASAFAA 280
Cdd:cd01940 243 IAEAMRQGAQFAA 255
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
3-297 |
5.28e-16 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 76.90 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLItyiddmPQvGET--LEAPdfeigcGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNT 80
Cdd:PRK09434 5 VWVLGDAVVDLI------PE-GENryLKCP------GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 81 QHVKA-VAGTSSGVApifVDKSSQNR----ILIIKGANNHLLPADVDA--AADVLKTCQlIILQLEIPLETVYAAIDFAR 153
Cdd:PRK09434 72 TYLRLdPAHRTSTVV---VDLDDQGErsftFMVRPSADLFLQPQDLPPfrQGEWLHLCS-IALSAEPSRSTTFEAMRRIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 154 QN--------NI--KVILNPAPASKALD--IGYACQCEFfmpNETELAILTGmpVDSLDNIYRAGRSLLDKGLhnLIITL 221
Cdd:PRK09434 148 AAggfvsfdpNLreDLWQDEAELRECLRqaLALADVVKL---SEEELCFLSG--TSQLEDAIYALADRYPIAL--LLVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 222 GHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGD------ILKAMEMASAFAAYSVTGKGTQRSYPDA 295
Cdd:PRK09434 221 GAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLwtdeaeLAEIIAQAQACGALATTAKGAMTALPNR 300
|
..
gi 817365314 296 SQ 297
Cdd:PRK09434 301 QE 302
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
1-303 |
2.17e-15 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 76.02 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 1 MDIAVIGSNMVDLITYIDDMP--------QVGETLEA--PDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTI 70
Cdd:PLN02341 73 IDVATLGNLCVDIVLPVPELPppsreerkAYMEELAAspPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 71 RNLQQAGVntQHVKAVAGTSSGvapifvDKSSQNRILII-----KGANNH------------LLP--ADVDAAAD-VLKT 130
Cdd:PLN02341 153 DVLAEEGI--SVVGLIEGTDAG------DSSSASYETLLcwvlvDPLQRHgfcsradfgpepAFSwiSKLSAEAKmAIRQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 131 CQLIILQ----LEIPLETVYAAIDFARQNNIKVILNPAPASKALDIGYACQ----------CEFFMPNETELAILTGM-- 194
Cdd:PLN02341 225 SKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGTPDErralehllrmSDVLLLTSEEAEALTGIrn 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 195 PVDsldniyrAGRSLLDKGLHN--LIITLGHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYvLHGDIL-KA 271
Cdd:PLN02341 305 PIL-------AGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGY-IHNLPLvNT 376
|
330 340 350
....*....|....*....|....*....|..
gi 817365314 272 MEMASAFAAYSVTGKGTQRSYPDASQFIDFLK 303
Cdd:PLN02341 377 LTLANAVGAATAMGCGAGRNVATLEKVLELLR 408
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
16-306 |
5.41e-15 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 74.27 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 16 YIDDMPQV-GETL-EAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAVAGTSSGV 93
Cdd:PLN02323 20 LIDFVPTVsGVSLaEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 94 ApiFVD-KSSQNRILII---KGANNHLLPADVDAaaDVLKTCQL-----IILQLEIPLETVYAAIDFARQN--------N 156
Cdd:PLN02323 100 A--FVTlRSDGEREFMFyrnPSADMLLRESELDL--DLIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAgallsydpN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 157 IKVILNPAP-ASKALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYragrSLLDKGLHNLIITLGHRGSLWMHGEEIH 235
Cdd:PLN02323 176 LRLPLWPSAeAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVV----KLWHPNLKLLLVTEGEEGCRYYTKDFKG 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817365314 236 HVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILK-------AMEMASAFAAYSVTGKGTQRSYPDASQFIDFLKTLH 306
Cdd:PLN02323 252 RVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLEdeerlreALRFANACGAITTTERGAIPALPTKEAVLKLLKKAV 329
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
2-308 |
5.79e-15 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 74.85 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 2 DIAVIGSNMVDLITYIDD--------------------MPQVGETLEAPDFEIGCGGKGANQAVAAARLGA--------N 53
Cdd:PLN02813 71 DVLGLGQAMVDFSGMVDDeflerlglekgtrkvinheeRGKVLRALDGCSYKASAGGSLSNTLVALARLGSqsaagpalN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 54 VMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAVAGTSsGVAPIFVDKSSQNRILIIKGANNHLlpaDVDAA-ADVLKTCQ 132
Cdd:PLN02813 151 VAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTT-GTVIVLTTPDAQRTMLSYQGTSSTV---NYDSClASAISKSR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 133 LIILQ---LEIP--LETVYAAIDFARQNNIKVILNPAPAS-------KALDIgyACQC-EFFMPNETELAILTGMPVDsl 199
Cdd:PLN02813 227 VLVVEgylWELPqtIEAIAQACEEAHRAGALVAVTASDVScierhrdDFWDV--MGNYaDILFANSDEARALCGLGSE-- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 200 DNIYRAGRSLlDKGLHNLIITLGHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEyVLHG--DILKAMEMASA 277
Cdd:PLN02813 303 ESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYG-LLRGvsDLRGMGELAAR 380
|
330 340 350
....*....|....*....|....*....|.
gi 817365314 278 FAAYSVTGKGTQRSYPDASQFIDFLKTLHQG 308
Cdd:PLN02813 381 VAATVVGQQGTRLRVEDAVELAESFALHLDG 411
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
3-263 |
1.01e-13 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 70.40 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDL-------ITYIDDMPqvGETLEAPdfeigcGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQ 75
Cdd:PRK09850 7 VVIIGSANIDVagyshesLNYADSNP--GKIKFTP------GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 76 AGVNTQHVKAVAGTSSGVAPIFVDKSSQNRILIIK-GANNHLLPADVDAAADVLKTCQLIILQLEIPLETVYAAIDFArq 154
Cdd:PRK09850 79 SGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINDmNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNA-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 155 NNIKVILNPAPASKALDI-GYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLW--MHG 231
Cdd:PRK09850 157 ANVPVFVDPVSAWKCVKVrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYsdISG 236
|
250 260 270
....*....|....*....|....*....|..
gi 817365314 232 EEiHHVPPVSVHAIDTSGAGDAFIGCFAHEYV 263
Cdd:PRK09850 237 ES-GWSAPIKTNVINVTGAGDAMMAGLASCWV 267
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
153-284 |
4.22e-13 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 68.57 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 153 RQNNIKVILNPAPAskALDIGYACQCEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGE 232
Cdd:PRK09513 158 RSQCPCIIFDSSRE--ALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNAS 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 817365314 233 EIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVT 284
Cdd:PRK09513 236 GEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVS 287
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
1-283 |
4.40e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 65.14 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 1 MDIAVIGSNMVDLityiddMPQVGETLEapdfeigcGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNT 80
Cdd:PRK09813 1 KKLATIGDNCVDI------YPQLGKAFS--------GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 81 QHVKAVAGTSsgvAPIFVDKSSQNRIL--IIKGANNHLLPADVDAaaDVLKTCQLIILQLEIPLETVYAAIdfaRQNNIK 158
Cdd:PRK09813 67 SHVHTKHGVT---AQTQVELHDNDRVFgdYTEGVMADFALSEEDY--AWLAQYDIVHAAIWGHAEDAFPQL---HAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 159 VILNPA-----PASKA----LDIGYAcqcefFMPNETELailtgmpvdsldnIYRAGRSLLDKGLHNLIITLGHRGSLWM 229
Cdd:PRK09813 139 TAFDFSdkwdsPLWQTlvphLDYAFA-----SAPQEDEF-------------LRLKMKAIVARGAGVVIVTLGENGSIAW 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 230 HGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEyVLHG-DILKAMEMASAFAAYSV 283
Cdd:PRK09813 201 DGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCG-WLAGmTLPQAMAQGTACAAKTI 254
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-287 |
5.92e-12 |
|
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: 64.75 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLITYIDDMPQVGETLEAPDFEIGCGGkGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQh 82
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPIFVDKSSQNRILIIKGANNHLLPADVD----AAADVL------------KTCQLIILQLEIPlETVY 146
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFAtltvAPYDYVylsgytlasenaSKVILLEWLEALP-AGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 147 AAIDFA-RQNNI-KVILNPAPASKALdigYACqceffmpNETELAILTGmPVDSLDNIyrAGRSLLDKGLHNLIITLGHR 224
Cdd:cd01944 159 LVFDPGpRISDIpDTILQALMAKRPI---WSC-------NREEAAIFAE-RGDPAAEA--SALRIYAKTAAPVVVRLGSN 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 225 GSlWMH--GEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKG 287
Cdd:cd01944 226 GA-WIRlpDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
37-282 |
3.16e-11 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 63.41 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 37 GGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAVAGTSSGVapiFVDKSSQNRILIIKGANNHL 116
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTST---YLAIANRQDETVLAINDTHI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 117 L----PADVDAAADVLKTCQLIILQLEI---PLETVYAAIDfarqnNIKVILNPAPASKALDI-GYACQCEFFMPNETEL 188
Cdd:PRK09954 170 LqqltPQLLNGSRDLIRHAGVVLADCNLtaeALEWVFTLAD-----EIPVFVDTVSEFKAGKIkHWLAHIHTLKPTQPEL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 189 AILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMH--GEEIHHVPPVSVhAIDTSGAGDAFIGCFAHEYVLHG 266
Cdd:PRK09954 245 EILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEkdGEQFLLTAPAHT-TVDSFGADDGFMAGLVYSFLEGY 323
|
250
....*....|....*.
gi 817365314 267 DILKAMEMASAFAAYS 282
Cdd:PRK09954 324 SFRDSARFAMACAAIS 339
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
182-278 |
2.38e-09 |
|
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: 57.08 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 182 MPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIIT--------LGHRGSLWMHGEEIHHVP----PVSVHaidtsG 249
Cdd:COG2240 143 TPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTADGAWLVEtpllPFSPN-----G 217
|
90 100
....*....|....*....|....*....
gi 817365314 250 AGDAFIGCFAHEYVLHGDILKAMEMASAF 278
Cdd:COG2240 218 TGDLFAALLLAHLLRGKSLEEALERAAAF 246
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
29-256 |
1.54e-08 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 54.79 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 29 APDFEIGcgGKGANQAVAAARLGANVMMVTRVGDDLfAENTIRNLQQAGVNTQHVKAVAGTSSGVApIFVDKSSQNRILI 108
Cdd:PRK10294 32 APVFEPG--GGGINVARAIAHLGGSATAIFPAGGAT-GEHLVSLLADENVPVATVEAKDWTRQNLH-VHVEASGEQYRFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 109 IKGANNH-----LLPADVDAaadvLKTCQLIILQLEIP----LETVYAAIDFARQNNIKVILNPA--PASKALDIGyacQ 177
Cdd:PRK10294 108 MPGAALNedefrQLEEQVLE----IESGAILVISGSLPpgvkLEKLTQLISAAQKQGIRCIIDSSgdALSAALAIG---N 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 178 CEFFMPNETELAILTGMPVDSLDNIYRAGRSLLDKG-LHNLIITLGHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIG 256
Cdd:PRK10294 181 IELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVG 260
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-280 |
5.10e-08 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 52.79 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 3 IAVIGSNMVDLItyiddmPQVGETLEAPdfeigcGGKGANQAVAAARLGANVMMVTRVGDDlfaentirnlqqagvntqH 82
Cdd:cd01937 2 IVIIGHVTIDEI------VTNGSGVVKP------GGPATYASLTLSRLGLTVKLVTKVGRD------------------Y 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 83 VKAVAGTSSGVAPIFVDKSSQN-RILIIKGANNHLLPADVDAAADVLKTCQLIILQLEIpletvyaaidfarqnnikVIL 161
Cdd:cd01937 52 PDKWSDLFDNGIEVISLLSTETtTFELNYTNEGRTRTLLAKCAAIPDTESPLSTITAEI------------------VIL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 162 NP-----------APASKALDI-GYACQCE--------------FFMPNETELAILTgmpvdSLDNIYRAGRSLLDKglh 215
Cdd:cd01937 114 GPvpeeispslfrKFAFISLDAqGFLRRANqeklikcvilklhdVLKLSRVEAEVIS-----TPTELARLIKETGVK--- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817365314 216 NLIITLGHRGSLWMHGEEIHHVPPVSVHAIDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAA 280
Cdd:cd01937 186 EIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAA 250
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
182-278 |
1.20e-07 |
|
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: 51.82 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 182 MPNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIIT------LGHRGSLWMHGEEIHHvppVSVHAIDT----SGAG 251
Cdd:cd01173 141 TPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWL---VQRPKIPFpayfNGTG 217
|
90 100
....*....|....*....|....*..
gi 817365314 252 DAFIGCFAHEYVLHGDILKAMEMASAF 278
Cdd:cd01173 218 DLFAALLLARLLKGKSLAEALEKALNF 244
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
37-258 |
1.36e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 49.40 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 37 GGKGANQAVA-AARLGANVMMVTRVGDD----LFAENtirnLQQAGVNTQHVKAVAGTSSGVApIFVDKSSqNRILiikg 111
Cdd:PLN02379 86 GGSVANTIRGlSAGFGVSTGIIGACGDDeqgkLFVSN----MGFSGVDLSRLRAKKGPTAQCV-CLVDALG-NRTM---- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 112 anNHLLPADVDAAADVL-----KTCQLIILQLEI-PLETVYAAIDFARQNNIKVILNPAP-------ASKALDIGYACQC 178
Cdd:PLN02379 156 --RPCLSSAVKLQADELtkedfKGSKWLVLRYGFyNLEVIEAAIRLAKQEGLSVSLDLASfemvrnfRSPLLQLLESGKI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 179 EFFMPNETELAILTGmpvDSLDNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPV-SVHAIDTSGAGDAFIGC 257
Cdd:PLN02379 234 DLCFANEDEARELLR---GEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIgETNAVDATGAGDLFASG 310
|
.
gi 817365314 258 F 258
Cdd:PLN02379 311 F 311
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
181-290 |
1.61e-06 |
|
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: 48.62 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 181 FMPNETELAILTGMPvdsldNIYRAGRSLLDKGLHNLIITLGHRGSLWMHGEEIHHVPPVSVHAI-DTSGAGDAFIGCFA 259
Cdd:cd01946 167 VIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTFAGGFI 241
|
90 100 110
....*....|....*....|....*....|....*.
gi 817365314 260 HEYVLHGDI-----LKAMEMASAFAAYSVTGKGTQR 290
Cdd:cd01946 242 GYLASQKDTseanmRRAIIYGSAMASFCVEDFGTKR 277
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
183-278 |
5.74e-06 |
|
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: 46.71 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 183 PNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHRGS-------LWMHGEEIHHVPPVSVHAIDTSGAGDAFI 255
Cdd:pfam08543 125 PNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHLEGeeavvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTLS 204
|
90 100
....*....|....*....|...
gi 817365314 256 GCFAHEYVLHGDILKAMEMASAF 278
Cdd:pfam08543 205 AAIAANLAKGLSLPEAVREAKEY 227
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
20-298 |
1.20e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 46.17 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 20 MPQVGETLEAPDFEIGCGGKGANQA-VAAARLGANVMMVTRVG---DDLFAENTIRNLQQAGVNT---QHVKAVAGTssg 92
Cdd:PTZ00247 45 LPIFEELESIPNVSYVPGGSALNTArVAQWMLQAPKGFVCYVGcvgDDRFAEILKEAAEKDGVEMlfeYTTKAPTGT--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 93 VAPIFVDKssqNRILIIK-GANNHLLPADVDAAADV--LKTCQLIILQ---LEIPLETVYAAIDFARQNNIKVILN-PAP 165
Cdd:PTZ00247 122 CAVLVCGK---ERSLVANlGAANHLSAEHMQSHAVQeaIKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 166 ---------ASKAL---DIGYACQCEFFmpnetELAILTGMPVDSLDNIYRAGRSLLDK-GLHN--LIITLGHRGSLWMH 230
Cdd:PTZ00247 199 fisqffferLLQVLpyvDILFGNEEEAK-----TFAKAMKWDTEDLKEIAARIAMLPKYsGTRPrlVVFTQGPEPTLIAT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817365314 231 GEEIHHVPPVSVHA---IDTSGAGDAFIGCFAHEYVLHGDILKAMEMASAFAAYSVTGKG-TQRSYPDASQF 298
Cdd:PTZ00247 274 KDGVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGcTYPEKPPFLPW 345
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
183-278 |
4.32e-05 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 44.35 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 183 PNETELAILTGMPVDSLDNIYR-AGRSLLDKGLHNLIITLGHRGS------LWMHGEEIHHVPPVSVHAIDTSGAGDAFI 255
Cdd:PRK06427 139 PNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGHLLDgeesvdWLFDGEGEERFSAPRIPTKNTHGTGCTLS 218
|
90 100
....*....|....*....|...
gi 817365314 256 GCFAHEYVLHGDILKAMEMASAF 278
Cdd:PRK06427 219 AAIAAELAKGASLLDAVQTAKDY 241
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
178-271 |
1.04e-04 |
|
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: 43.48 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 178 CEFFMPNETELAILTGMPVD----------SLDNIYRAGRSLLDKGLhnLIITLGHRGSL---WMHGEEIH----HVPPV 240
Cdd:cd01943 181 VDVFSPNLEEAARLLGLPTSepssdeekeaVLQALLFSGILQDPGGG--VVLRCGKLGCYvgsADSGPELWlpayHTKST 258
|
90 100 110
....*....|....*....|....*....|.
gi 817365314 241 SVhaIDTSGAGDAFIGCFAHEYVLHGDILKA 271
Cdd:cd01943 259 KV--VDPTGGGNSFLGGFAAGLALTKSIDEA 287
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
28-163 |
1.23e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 40.28 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 28 EAPDFEIGCGGKGANQAVAAARLGANVMMVTRVGDDLFAENTIRNLQQAGVNTQHVKAVAGTSSGVAPI---FVDKSSQN 104
Cdd:PLN02543 163 DPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMkikFRDGGKMV 242
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817365314 105 RILIIKGANNHLLPADVDaaADVLKTCQLIILQLEIPL-----ETVYAAIDFARQNNIKVILNP 163
Cdd:PLN02543 243 AETVKEAAEDSLLASELN--LAVLKEARMFHFNSEVLTspsmqSTLFRAIELSKKFGGLIFFDL 304
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
183-298 |
1.80e-03 |
|
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: 39.43 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 183 PNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIIT-LGHRGS--------LWMHGEEIHHV-PPVSVHAIDTSGAGD 252
Cdd:TIGR00687 144 PNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSqrdrsfegLVATQEGRWHIsRPLAVFDPPPVGTGD 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 817365314 253 AFIGCFAHEYvLHGDILK-AME-MASAFAAYSVTGK--GTQRSYPDASQF 298
Cdd:TIGR00687 224 LIAALLLATL-LHGNSLKeALEkTVSAVYHVLRTTIqlGKYELQPVAAQL 272
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
183-283 |
1.97e-03 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 39.08 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817365314 183 PNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIITLGHR--------GSLWMHGEEIHHV---------PPVsvhai 245
Cdd:PRK05756 144 PNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTSLARagypadrfEMLLVTADGAWHIsrplvdfmrQPV----- 218
|
90 100 110
....*....|....*....|....*....|....*...
gi 817365314 246 dtsGAGDAFIGCFAHEYVLHGDILKAMEMASAfAAYSV 283
Cdd:PRK05756 219 ---GVGDLTSALFLARLLQGGSLEEALEHTTA-AVYEV 252
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
217-288 |
3.10e-03 |
|
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: 38.54 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817365314 217 LIITLGHRGSLWMHGE-EIHHVP---PVSVhaIDTSGAGDAFIGCFAHEYVLHGDIL-KAMEMASAFAAYSVTGKGT 288
Cdd:cd01939 215 LVCTWGDQGAGALGPDgEYVHSPahkPIRV--VDTLGAGDTFNAAVIYALNKGPDDLsEALDFGNRVASQKCTGVGF 289
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
183-220 |
9.53e-03 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 36.94 E-value: 9.53e-03
10 20 30
....*....|....*....|....*....|....*...
gi 817365314 183 PNETELAILTGMPVDSLDNIYRAGRSLLDKGLHNLIIT 220
Cdd:PRK08176 158 PNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT 195
|
|
| |
