|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
3-286 |
1.67e-106 |
|
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: 311.15 E-value: 1.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMVDTKGERIIINYPSPDlLPDAEWLEEIDFSQWDVVLADVRWHDGAKKAFTLARQAGV--MTVLD 160
Cdd:cd01945 81 FIVVAPGARSPISSITDITGDRATISITAIDT-QAAPDSLPDAILGGADAVLVDGRQPEAALHLAQEARARGIpiPLDLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 161 GDITPQdISELVALSDHAAFSEPGLARLTGVKEMaSALKQAQTLTNGHVYVTQGSAGCDWLE-NGGRQHQPAFKVDVVDT 239
Cdd:cd01945 160 GGGLRV-LEELLPLADHAICSENFLRPNTGSADD-EALELLASLGIPFVAVTLGEAGCLWLErDGELFHVPAFPVEVVDT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1782747458 240 TGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPD 286
Cdd:cd01945 238 TGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-286 |
2.61e-70 |
|
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: 219.76 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMVDTKGERIIINYPSPDLLPDAEWLEEIDFSQWDVV------LADVRWHDGAKKAFTLARQAGVM 156
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILhlggitLASEPPREALLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 157 TVLDGDITP-------QDISELVALSDHAAFSEPGLARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQ 229
Cdd:COG0524 161 VSLDPNYRPalweparELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVVHV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1782747458 230 PAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPD 286
Cdd:COG0524 241 PAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-282 |
1.41e-63 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 202.19 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKyvARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVR--VSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMVDTKGERIIINYPSP-------DLLPDAEWLEEIDFSQWDVVLADVRWHDGAKKAFTLARQAG- 154
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAaadltpeELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 155 -VMTVLDGDI-TPQDISELVALSDHAAFSEPGLARLTGVK--EMASALKQAQTLTN---GHVYVTQGSAGCDWLENGGRQ 227
Cdd:pfam00294 159 fDPNLLDPLGaAREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHKLLAkgiKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1782747458 228 H-QPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRA 282
Cdd:pfam00294 239 HvPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-286 |
1.92e-54 |
|
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: 178.51 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTEsGKYV-ARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNT 81
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKP-GETVlGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 82 RYTKRYNQAKSSQSAIMVDTKGERIIINYP------SPDLLPDAEwlEEIDFSqwDVVLA--DVRwHDGAKKAFTLARQA 153
Cdd:cd01174 80 SYVEVVVGAPTGTAVITVDESGENRIVVVPgangelTPADVDAAL--ELIAAA--DVLLLqlEIP-LETVLAALRAARRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 154 GVMTVLDGDITPQDISELVALSDHAAFSEPGLARLTGVK-----EMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQH 228
Cdd:cd01174 155 GVTVILNPAPARPLPAELLALVDILVPNETEAALLTGIEvtdeeDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1782747458 229 QPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPD 286
Cdd:cd01174 235 VPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
8-285 |
5.24e-54 |
|
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: 177.41 E-value: 5.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 8 GITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRY 87
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 88 NQAKSSQSAIMVDTKGERIIINYP------SPDLLPDAEwlEEIDFSqwDVVLA--DVRwHDGAKKAFTLARQAGVMTVL 159
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAganaelTPEDIDAAE--ALIAES--DIVLLqlEIP-LETVLEAAKIAKKHGVKVIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 160 D----GDITPQdisELVALSDHAAFSEPGLARLTG--VKEMASALKQAQTLTN---GHVYVTQGSAGCDWLENGGRQHQP 230
Cdd:TIGR02152 156 NpapaIKDLDD---ELLSLVDIITPNETEAEILTGieVTDEEDAEKAAEKLLEkgvKNVIITLGSKGALLVSKDESKLIP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1782747458 231 AFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIP 285
Cdd:TIGR02152 233 AFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIP 287
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-279 |
2.39e-41 |
|
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: 144.70 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVarnytevGGGPAATAAVAAaRLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFTKAP-------GGAPANVAVALA-RLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMVDTKGER--IIINYPSPDLLPDAEwLEEIDFSQWDVV------LADVRWHDGAKKAFTLARQAG 154
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDADGERsfEFYRGPAADLLLDTE-LNPDLLSEADILhfgsiaLASEPSRSALLELLEAAKKAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 155 VMTVLD----------GDITPQDISELVALSDHAAFSEPGLARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENG 224
Cdd:cd01167 152 VLISFDpnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782747458 225 GRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGD-------LAESVRFASGVAALKCTRPG 279
Cdd:cd01167 232 GVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAG 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-289 |
2.00e-33 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 124.85 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 1 MIRVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVN 80
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 81 TRYTKRYNQAKSSQSAIMVDTK---GERIII----NYPSPDLLpDAEWlEEIdFSQWDVVLA------DVRWHdgakkAF 147
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFVDTKtgnNEIVIIpganNALTPQMV-DAQT-DNI-QNICKYLICqneiplETTLD-----AL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 148 TLARQAGVMTVLDGDITPQD-----ISELVALSDHAAFSEPGLARLTG--VKEMASALKQA---QTLTNGHVYVTQGSAG 217
Cdd:PTZ00292 167 KEAKERGCYTVFNPAPAPKLaeveiIKPFLKYVSLFCVNEVEAALITGmeVTDTESAFKASkelQQLGVENVIITLGANG 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782747458 218 CDWLENG-GRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPDCDQ 289
Cdd:PTZ00292 247 CLIVEKEnEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSE 319
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
50-279 |
3.24e-32 |
|
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: 120.76 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 50 RLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERIIINY--PSPDLLPDAEWLEEIDF 127
Cdd:cd01166 43 RLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIGAGGERRVLYYraGSAASRLTPEDLDEAAL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 128 SQWDVV---------LADVRwhDGAKKAFTLARQAGVMTVLDGDITP---------QDISELVALSDHAAFSEPGLARLT 189
Cdd:cd01166 123 AGADHLhlsgitlalSESAR--EALLEALEAAKARGVTVSFDLNYRPklwsaeearEALEELLPYVDIVLPSEEEAEALL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 190 GVKEMASALKQAQTLTNG--HVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFA 267
Cdd:cd01166 201 GDEDPTDAAERALALALGvkAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFA 280
|
250
....*....|..
gi 1782747458 268 SGVAALKCTRPG 279
Cdd:cd01166 281 NAAAALVVTRPG 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
3-281 |
9.61e-32 |
|
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: 118.95 E-value: 9.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMVDTKGERIIINYPSPdllpdAEWLEEIDFSQWDVVLADVrwH-DGAKKAFTLARQA---GVMTV 158
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPGA-----MDELEPNDEADPDGLADIV--HlSSGPGLIELARELaagGITVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 159 LDG-----DITPQDISELVALSDHAAFSEpglARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFK 233
Cdd:cd01942 154 FDPgqelpRLSGEELEEILERADILFVND---YEAELLKERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1782747458 234 -VDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGR 281
Cdd:cd01942 231 aVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
50-295 |
8.96e-31 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 117.28 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 50 RLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERIII------NYPSPD-------LL 116
Cdd:PRK11142 51 RLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGihaganAALTPAlveahreLI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 117 PDAEWLeeidFSQWDVVLADVrwhdgaKKAFTLARQAGVMTVLDgditP---QDIS-ELVALSDHAAFSEPGLARLTGVK 192
Cdd:PRK11142 131 ANADAL----LMQLETPLETV------LAAAKIAKQHGTKVILN----PapaRELPdELLALVDIITPNETEAEKLTGIR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 193 --EMASALKQAQTLTN---GHVYVTQGSAGCdWLENGGRQHQ-PAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRF 266
Cdd:PRK11142 197 veDDDDAAKAAQVLHQkgiETVLITLGSRGV-WLSENGEGQRvPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRF 275
|
250 260
....*....|....*....|....*....
gi 1782747458 267 ASGVAALKCTRPGGRAGIPDCDQTRSFLS 295
Cdd:PRK11142 276 AHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
50-289 |
8.39e-25 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 101.17 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 50 RLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGER---IIINyPSPDLLPDAEWLEEID 126
Cdd:PRK09434 40 RLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsftFMVR-PSADLFLQPQDLPPFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 127 FSQW----DVVLADVRWHDGAKKAFTLARQAGVMTVLDGDITP---QDISEL-------VALSDHAAFSEPGLARLTGVK 192
Cdd:PRK09434 119 QGEWlhlcSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREdlwQDEAELreclrqaLALADVVKLSEEELCFLSGTS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 193 EMASALKQ-AQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGD------LAESVR 265
Cdd:PRK09434 199 QLEDAIYAlADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLwtdeaeLAEIIA 278
|
250 260
....*....|....*....|....
gi 1782747458 266 FASGVAALKCTRPGGRAGIPDCDQ 289
Cdd:PRK09434 279 QAQACGALATTAKGAMTALPNRQE 302
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
51-279 |
6.06e-20 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 87.94 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 51 LGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYtkrynqakssqsaIMVD------TKgERII--------INYPSPDLL 116
Cdd:COG2870 68 LGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDG-------------LVVDprrpttTK-TRVIaggqqllrLDFEDRFPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 117 PDA------EWLEEIdFSQWDVV---------LADVRwhdgAKKAFTLARQAGVMTVLDGD------------ITPqDIS 169
Cdd:COG2870 134 SAElearllAALEAA-LPEVDAVilsdygkgvLTPEL----IQALIALARAAGKPVLVDPKgrdfsryrgatlLTP-NLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 170 ELVALSDHAAFSEPGLARLtgvkemasALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQ-PAFKVDVVDTTGAGDVFHG 248
Cdd:COG2870 208 EAEAAVGIPIADEEELVAA--------AAELLERLGLEALLVTRGEEGMTLFDADGPPHHlPAQAREVFDVTGAGDTVIA 279
|
250 260 270
....*....|....*....|....*....|.
gi 1782747458 249 ALAVALATSGDLAESVRFASGVAALKCTRPG 279
Cdd:COG2870 280 TLALALAAGASLEEAAELANLAAGIVVGKLG 310
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-279 |
3.28e-19 |
|
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: 85.55 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYT-EVGGGpaATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNT 81
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSyVIGGG--FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 82 RYTKRYNQaKSSQSAIMVDTKGERIIINYPSPDLLPDAEWLEEIDFSQWDVV------LADVRWHDGAKKAFTLARQAGV 155
Cdd:cd01944 79 LLPPRGGD-DGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVylsgytLASENASKVILLEWLEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 156 MTVLD-----GDITPQDISELVALS-------DHAA-FSEPGLArltgvkEMASALKQAQTLTNGHVYVTQGSAGCdW-- 220
Cdd:cd01944 158 TLVFDpgpriSDIPDTILQALMAKRpiwscnrEEAAiFAERGDP------AAEASALRIYAKTAAPVVVRLGSNGA-Wir 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1782747458 221 LENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPG 279
Cdd:cd01944 231 LPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
32-283 |
9.74e-19 |
|
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: 84.59 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 32 NYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYtKRYNQAKSSQSAIMVDTKGERIIINY- 110
Cdd:cd01168 49 PVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMCTYl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 111 -PSPDLLPDAEWLEEIDFSQWdVVLADVRWHDG---AKKAFTLARQAGVMTVL---DGDITPQDISELVALSDHAAF--- 180
Cdd:cd01168 128 gAANELSPDDLDWSLLAKAKY-LYLEGYLLTVPpeaILLAAEHAKENGVKIALnlsAPFIVQRFKEALLELLPYVDIlfg 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 181 --SEPG-LARLTGVKEMASALKQAQTLTNGhVYVTQGSAGCDWLENGGRQHQPAFKVD-VVDTTGAGDVFHGALAVALAT 256
Cdd:cd01168 207 neEEAEaLAEAETTDDLEAALKLLALRCRI-VVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQ 285
|
250 260
....*....|....*....|....*..
gi 1782747458 257 SGDLAESVRFASGVAALKCTRPGGRAG 283
Cdd:cd01168 286 GEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
3-276 |
4.28e-18 |
|
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: 82.45 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNQAKSSQSAIMV-DTKGERIIINYPSpdlLPDaewLEEIDFSQwdVVLADVRW-HDGAKKAF-TL---------- 149
Cdd:cd01939 81 HCYRKDIDEPASSYIIRsRAGGRTTIVNDNN---LPE---VTYDDFSK--IDLTQYGWiHFEGRNPDeTLrmmqhieehn 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 150 ARQAGVMTVLDGDI--TPQDISELVALSDHAAFSEPgLARLTGVKEMASALKQAQTLTNG--HVYVTQGSAGCDWLE-NG 224
Cdd:cd01939 153 NRRPEIRITISVEVekPREELLELAAYCDVVFVSKD-WAQSRGYKSPEECLRGEGPRAKKaaLLVCTWGDQGAGALGpDG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1782747458 225 GRQHQPAFKVD-VVDTTGAGDVFHGALAVALATSGD-LAESVRFASGVAALKCT 276
Cdd:cd01939 232 EYVHSPAHKPIrVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCT 285
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-273 |
4.36e-18 |
|
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: 82.36 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 4 VACVGITVMDRIYYVEGLP----------TESGKYVARNYTEvgggpaataavAAARLGAQVDFIGRVGDDDAGNSLLAE 73
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLvpgtsnpghvKQSPGGVGRNIAE-----------NLARLGVSVALLSAVGDDSEGESILEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 74 LESWGVNTRYTKRYNQAKSSQSAIMvDTKGERI-------IINYPSPDLLPdaEWLEEIDFSQWdvVLADVRWHDGAKKA 146
Cdd:cd01941 71 SEKAGLNVRGIVFEGRSTASYTAIL-DKDGDLVvaladmdIYELLTPDFLR--KIREALKEAKP--IVVDANLPEEALEY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 147 -FTLARQAGVMTVLDGDITP--QDISELVALSDHAAFSEPGLARLTGV---KEMASALKQAQTLTNGH--VYVTQGSAG- 217
Cdd:cd01941 146 lLALAAKHGVPVAFEPTSAPklKKLFYLLHAIDLLTPNRAELEALAGAlieNNEDENKAAKILLLPGIknVIVTLGAKGv 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1782747458 218 --CDWLENGGRQHQPAFKVD-VVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAAL 273
Cdd:cd01941 226 llSSREGGVETKLFPAPQPEtVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-272 |
3.29e-17 |
|
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: 79.38 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 4 VACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVnTRY 83
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD-KHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 84 TKRYNQaKSSQSAIMVDTKGERIIINYPSPdLLPDAEWLEeidFSQWDVVLADVRWHDGAKKAFTLARQAGVMtvldgDI 163
Cdd:cd01947 81 VAWRDK-PTRKTLSFIDPNGERTITVPGER-LEDDLKWPI---LDEGDGVFITAAAVDKEAIRKCRETKLVIL-----QV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 164 TPQ-DISELVALSDHAAF-----SEPGLArltgVKEMASALKQAQTLTnghvyVTQGSAGCDWLENGGRQHQPAFKVDVV 237
Cdd:cd01947 151 TPRvRVDELNQALIPLDIligsrLDPGEL----VVAEKIAGPFPRYLI-----VTEGELGAILYPGGRYNHVPAKKAKVP 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1782747458 238 DTTGAGDVFHGALAVALATSGDLAESVRFASGVAA 272
Cdd:cd01947 222 DSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGA 256
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
51-279 |
4.64e-17 |
|
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: 79.53 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 51 LGAQVDFIGRVGDDDAGNSLLAELESWGVNT-------RYTKRYNQ-AKSSQSAIMVDTKGERIIiNYPSPDLLpdAEWL 122
Cdd:cd01172 52 LGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTdgivdegRPTTTKTRvIARNQQLLRVDREDDSPL-SAEEEQRL--IERI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 123 EEIdFSQWDVVLADvrwhDGAKKAFT---------LARQAGVMTVLDGD------------ITPQDiSELVALSDHAAFS 181
Cdd:cd01172 129 AER-LPEADVVILS----DYGKGVLTprviealiaAARELGIPVLVDPKgrdyskyrgatlLTPNE-KEAREALGDEIND 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 182 EPGLARLtgvkemASALKQAQTLTNghVYVTQGSAGCDWLE-NGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDL 260
Cdd:cd01172 203 DDELEAA------GEKLLELLNLEA--LLVTLGEEGMTLFErDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADL 274
|
250
....*....|....*....
gi 1782747458 261 AESVRFASGVAALKCTRPG 279
Cdd:cd01172 275 EEAAFLANAAAGVVVGKVG 293
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
3-280 |
4.86e-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: 76.24 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDriyyveglptesgKYVARNYTEVGGGPAATAAVAAaRLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:cd01940 1 RLAAIGDNVVD-------------KYLHLGKMYPGGNALNVAVYAK-RLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTKRYNqaKSSQSAIMVDTKGERIIINYPS---PDLLPDAEWLEEIdfSQWDVVLADVRWHDG-AKKAFTLARQAGVMTV 158
Cdd:cd01940 67 HCRVKE--GENAVADVELVDGDRIFGLSNKggvAREHPFEADLEYL--SQFDLVHTGIYSHEGhLEKALQALVGAGALIS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 159 LD--GDITPQDISELVALSDHAAFSEPGLARltgvKEMASALKQAQTLTNGHVYVTQGSAGCdWLENGGR-QHQPAFKVD 235
Cdd:cd01940 143 FDfsDRWDDDYLQLVCPYVDFAFFSASDLSD----EEVKAKLKEAVSRGAKLVIVTRGEDGA-IAYDGAVfYSVAPRPVE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1782747458 236 VVDTTGAGDVF-HGALAVALATSGDLAESVRFASGVAALKCTRPGG 280
Cdd:cd01940 218 VVDTLGAGDSFiAGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
50-295 |
4.01e-15 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 74.27 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 50 RLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERIIINY--PSPDLLpdaewLEEidf 127
Cdd:PLN02323 55 RLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADML-----LRE--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 128 SQWDVVL---ADVrWHDGA------------KKAFTLARQAGVMTVLDGDI------TPQDISE-LVALSDHAAF---SE 182
Cdd:PLN02323 127 SELDLDLirkAKI-FHYGSislitepcrsahLAAMKIAKEAGALLSYDPNLrlplwpSAEAAREgIMSIWDEADIikvSD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 183 PGLARLTG---------VKEMASALKQaqtltnghVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVA 253
Cdd:PLN02323 206 EEVEFLTGgddpdddtvVKLWHPNLKL--------LLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQ 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1782747458 254 LATS-------GDLAESVRFASGVAALKCTRPGGRAGIPDCDQTRSFLS 295
Cdd:PLN02323 278 LAKDlslledeERLREALRFANACGAITTTERGAIPALPTKEAVLKLLK 326
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
3-255 |
9.54e-15 |
|
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: 71.36 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGrvgdddagnsllaeleswgvntr 82
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 ytkrynqakssqsaimvdtkGERIIINYPSPDLLPDAEWLEEidfsqwdvvladvrwhdgakkaftlARQAGVMTVLD-- 160
Cdd:cd00287 58 --------------------ADAVVISGLSPAPEAVLDALEE-------------------------ARRRGVPVVLDpg 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 161 ---GDITPQDISELVALSDHAAFSEPGLARLTG-----VKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGG-RQHQPA 231
Cdd:cd00287 93 praVRLDGEELEKLLPGVDILTPNEEEAEALTGrrdleVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGtEVHVPA 172
|
250 260
....*....|....*....|....
gi 1782747458 232 FKVDVVDTTGAGDVFHGALAVALA 255
Cdd:cd00287 173 FPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
185-294 |
7.77e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 64.39 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 185 LARLTGVK--EMASALKQAQTLTN---GHVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGD 259
Cdd:COG1105 188 LEELLGRPleTLEDIIAAARELLErgaENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLD 267
|
90 100 110
....*....|....*....|....*....|....*
gi 1782747458 260 LAESVRFASGVAALKCTRPGgrAGIPDCDQTRSFL 294
Cdd:COG1105 268 LEEALRLAVAAGAAAALSPG--TGLPDREDVEELL 300
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
149-279 |
7.59e-09 |
|
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: 55.62 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 149 LARQAGVMTVLDGD--------------ITPqDISELVALSDHAafsepglarLTGVKEMASALKQAQTLTNGHVYVTQG 214
Cdd:cd01164 153 LAREKGARVILDTSgeallaalaakpflIKP-NREELEELFGRP---------LGDEEDVIAAARKLIERGAENVLVSLG 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1782747458 215 SAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPG 279
Cdd:cd01164 223 ADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
209-274 |
4.41e-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: 53.17 E-value: 4.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782747458 209 VYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALK 274
Cdd:cd01937 187 IIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
51-272 |
2.78e-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: 51.37 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 51 LGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQA--------KSSQSAIMVDTkgERIIINYPSPDLLPDAE-W 121
Cdd:PRK11316 63 LGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVPTHPtitklrvlSRNQQLIRLDF--EEGFEGVDPQPLLERIEqA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 122 LEEIDFsqwdVVLADVrwhdgAKKAFT-------LARQAGVMTVLD---GD---------ITPqDISELVALSDHAAfSE 182
Cdd:PRK11316 141 LPSIGA----LVLSDY-----AKGALAsvqamiqLARKAGVPVLIDpkgTDferyrgatlLTP-NLSEFEAVVGKCK-DE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 183 PGLArltgvkemASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQ-HQPAFKVDVVDTTGAGDVFHGALAVALATSGDLA 261
Cdd:PRK11316 210 AELV--------EKGMKLIADYDLSALLVTRSEQGMTLLQPGKAPlHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLE 281
|
250
....*....|.
gi 1782747458 262 ESVRFASgVAA 272
Cdd:PRK11316 282 EACALAN-AAA 291
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
173-272 |
2.82e-06 |
|
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: 48.11 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 173 ALSDHAAFSePG---LARLTGVKEMA-SALKQAQT------------LTNGHVYVTQGSAGC-----DWlenGGRQHQPA 231
Cdd:cd01943 177 ALPRVDVFS-PNleeAARLLGLPTSEpSSDEEKEAvlqallfsgilqDPGGGVVLRCGKLGCyvgsaDS---GPELWLPA 252
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1782747458 232 FKVD---VVDTTGAGDVFHGALAVALATSGDLAESVRFASgVAA 272
Cdd:cd01943 253 YHTKstkVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGS-VAA 295
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
51-275 |
2.98e-06 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 48.06 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 51 LGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERII-INYPSPDLLPDAEWL-EEIDFS 128
Cdd:PRK09850 53 LGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVaINDMNISNAITAEYLaQHREFI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 129 QW-DVVLADVRWHDGAKkAFTLARQAGVMTVLDgditPQDISELVALSDH------------AAFSEPGLArLTGVKEMA 195
Cdd:PRK09850 133 QRaKVIVADCNISEEAL-AWILDNAANVPVFVD----PVSAWKCVKVRDRlnqihtlkpnrlEAETLSGIA-LSGREDVA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 196 SALKQAQTLTNGHVYVTQGSAGCDWLE-NGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVA--A 272
Cdd:PRK09850 207 KVAAWFHQHGLNRLVLSMGGDGVYYSDiSGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSsmA 286
|
...
gi 1782747458 273 LKC 275
Cdd:PRK09850 287 LSC 289
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
185-286 |
3.26e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 47.77 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 185 LARLTGVKEMASALKqAQTLTngHVYVTQGSAGCDWL-ENGGRQHQPAfKVDVVDTTGAGDVFHGALAVALATSGDLAES 263
Cdd:PRK09513 199 LPELKDVIEAAHALR-EQGIA--HVVISLGAEGALWVnASGEWIAKPP-ACDVVSTVGAGDSMVGGLIYGLLMRESSEHT 274
|
90 100
....*....|....*....|...
gi 1782747458 264 VRFASGVAALKCTRPGgrAGIPD 286
Cdd:PRK09513 275 LRLATAVSALAVSQSN--VGITD 295
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-272 |
2.13e-05 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 45.11 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 3 RVACVGITVMDrIYyveglPTESGKYVARNYTEVGggpaataaVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTR 82
Cdd:PRK09813 2 KLATIGDNCVD-IY-----PQLGKAFSGGNAVNVA--------VYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 83 YTkRYNQAKSSQSAIMVDTkGERIIINYPSPDLLPDAEWLEEIDF-SQWDVVLADVRWHdgAKKAFTLARQAGVMTVLDG 161
Cdd:PRK09813 68 HV-HTKHGVTAQTQVELHD-NDRVFGDYTEGVMADFALSEEDYAWlAQYDIVHAAIWGH--AEDAFPQLHAAGKLTAFDF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 162 DITPQD--ISELVALSDHAAFSEPGlarltGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFKVDVVDT 239
Cdd:PRK09813 144 SDKWDSplWQTLVPHLDYAFASAPQ-----EDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDT 218
|
250 260 270
....*....|....*....|....*....|...
gi 1782747458 240 TGAGDVFHGALAVALATSGDLAESVRFASGVAA 272
Cdd:PRK09813 219 MGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAA 251
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
51-248 |
2.43e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 42.09 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 51 LGAQVDFIGRVGDDDAGNSLLAELESWGVN-TRYtkRYNQAKSSQSAIMVDTKGERIIINYPSPDLLPDAEWLEEIDF-- 127
Cdd:PLN02379 100 FGVSTGIIGACGDDEQGKLFVSNMGFSGVDlSRL--RAKKGPTAQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFkg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 128 SQWDVVLADVRWHDGAKKAFTLARQAGVMTVLD-------GDITPQDISELVALSDHAAFSEPGLAR-LTGVKEMA---S 196
Cdd:PLN02379 178 SKWLVLRYGFYNLEVIEAAIRLAKQEGLSVSLDlasfemvRNFRSPLLQLLESGKIDLCFANEDEAReLLRGEQESdpeA 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1782747458 197 ALKQAQTLTNGHVyVTQGSAGCdwLENGGRQ--HQPAFK-VDVVDTTGAGDVFHG 248
Cdd:PLN02379 258 ALEFLAKYCNWAV-VTLGSKGC--IARHGKEvvRVPAIGeTNAVDATGAGDLFAS 309
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
206-264 |
4.64e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 41.36 E-value: 4.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1782747458 206 NGHVYVTQGSAGCdwlenggrqhQPAFKVDVVDTTGAGDVFHGALA------VALATSGDLAESV 264
Cdd:PLN02341 329 KGSILVTRSSVSC----------APAFKVNVVDTVGCGDSFAAAIAlgyihnLPLVNTLTLANAV 383
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
162-263 |
8.99e-04 |
|
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: 40.14 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 162 DITPQDISELVALSDHAAFSEPGLARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFKV-DVVDTT 240
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLeSVFDPT 230
|
90 100
....*....|....*....|...
gi 1782747458 241 GAGDVFHGALAVALATSGDLAES 263
Cdd:cd01946 231 GAGDTFAGGFIGYLASQKDTSEA 253
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
163-267 |
2.61e-03 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 38.48 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782747458 163 ITPqDISELVALSDHAAfsepglarlTGVKEMASALKQAQTLTNGHVYVT----QGSAGCDWLENGGRQHQ-PAFKVDVV 237
Cdd:COG0351 130 VTP-NLPEAEALLGIEI---------TTLDDMREAAKALLELGAKAVLVKgghlPGDEAVDVLYDGDGVREfSAPRIDTG 199
|
90 100 110
....*....|....*....|....*....|
gi 1782747458 238 DTTGAGDVFHGALAVALATSGDLAESVRFA 267
Cdd:COG0351 200 NTHGTGCTLSSAIAALLAKGLDLEEAVREA 229
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
38-99 |
2.72e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 39.12 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782747458 38 GGPAATAAVAAARLGAQVDFIGRVGDDDAGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMV 99
Cdd:PLN02543 172 GGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKI 233
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
209-254 |
4.28e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.25 E-value: 4.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1782747458 209 VYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVAL 254
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGL 251
|
|
| |
