|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
14-307 |
2.20e-128 |
|
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: 367.70 E-value: 2.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 14 GSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVI 93
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 94 DDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGADIAKARITLLQREVPHEANLAVAKAVRAAGGTVLLDPAPV 173
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 174 GDASQmADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVV 253
Cdd:TIGR02152 161 IKDLD-DELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 552104401 254 DTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPTAREVE 307
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-302 |
7.81e-110 |
|
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: 320.65 E-value: 7.81e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGADIAKARITLLQREVPHEANLAVAKAVRAAGGTVLL 168
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 169 DPAPVgdASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPF 248
Cdd:cd01174 161 NPAPA--RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 552104401 249 KVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPT 302
Cdd:cd01174 239 KVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
9-310 |
5.39e-83 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 252.87 E-value: 5.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:PRK11142 4 KLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGADIAKARITLLQREVPHEANLAVAKAVRAAGGTVLL 168
Cdd:PRK11142 84 PVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 169 DPAPvgdASQMAD-LIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTP 247
Cdd:PRK11142 164 NPAP---ARELPDeLLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552104401 248 FKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPTAREVEELI 310
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-306 |
5.29e-80 |
|
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: 244.79 E-value: 5.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAygADIAKARITLLQ-----REVPHEANLAVAKAVRAAG 163
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGgitlaSEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 164 GTVLLDPAPVGD-----ASQMADLIALSDIISPNETEAAEITGIEptdlaSAEAAGRKLLERGPKIVILKLGSRGALLIT 238
Cdd:COG0524 159 VPVSLDPNYRPAlwepaRELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552104401 239 ADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPTAREV 306
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
4-306 |
2.95e-63 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 203.04 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 4 GEAPLKIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREF 83
Cdd:PTZ00292 12 GEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 84 GLDTGSVRVIDDVDTGMAIIQVE-ETGQNTIAVCAGANARWSSADIDAYGADIAK-ARITLLQREVPHEANLAVAKAVRA 161
Cdd:PTZ00292 92 GVNTSFVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 162 AGGTVLLDPAPV---GDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLIT 238
Cdd:PTZ00292 172 RGCYTVFNPAPApklAEVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVE 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552104401 239 AD-EVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPTAREV 306
Cdd:PTZ00292 252 KEnEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-298 |
1.64e-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: 194.87 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARmaALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:pfam00294 1 KVVVIGEANIDLIGN--VEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGADIAKARI----TLLQREVPHEANLAVAKAVRAAGG 164
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLlyisGSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 165 T--VLLDPAPvGDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEV 242
Cdd:pfam00294 159 FdpNLLDPLG-AAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 552104401 243 KHFTPF-KVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGA 298
Cdd:pfam00294 238 VHVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
10-296 |
3.34e-46 |
|
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: 157.47 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 10 IFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGS 89
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 90 VRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYgadIAKARITLLQREVPHEANlavAKAVRAAGGTVLLD 169
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADP---DGLADIVHLSSGPGLIEL---ARELAAGGITVSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 170 PAPV---GDASQMADLIALSDIISPNETEAAeitgieptdlASAEAAGRKLLER--GPKIVILKLGSRGALLITADEVKH 244
Cdd:cd01942 156 PGQElprLSGEELEEILERADILFVNDYEAE----------LLKERTGLSEAELasGVRVVVVTLGPKGAIVFEDGEEVE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 552104401 245 FTPFK-VKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGA 296
Cdd:cd01942 226 VPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-296 |
2.29e-45 |
|
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: 155.81 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSArmaalPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:cd01166 1 DVVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIA--VCAGANARWSSADIDAygADIAKAR------ITLLQREVPHEANLAVAKAVR 160
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRVLyyRAGSAASRLTPEDLDE--AALAGADhlhlsgITLALSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 161 AAGGTVLLDP------APVGDASQ-MADLIALSDIISPNETEAAEITGIEptDLASAEAAGRKLlERGPKIVILKLGSRG 233
Cdd:cd01166 154 ARGVTVSFDLnyrpklWSAEEAREaLEELLPYVDIVLPSEEEAEALLGDE--DPTDAAERALAL-ALGVKAVVVKLGAEG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552104401 234 ALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGA 296
Cdd:cd01166 231 ALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
48-296 |
9.13e-38 |
|
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: 135.84 E-value: 9.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIIQVEETGQNTIA----VCAGANARW 123
Cdd:cd01167 32 ANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEfyrgPAADLLLDT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 124 SSADIDAYGADIAKA-RITLLqREVPHEANLAVAKAVRAAGGTVLLDP--------APVGDASQMADLIALSDIISPNET 194
Cdd:cd01167 112 ELNPDLLSEADILHFgSIALA-SEPSRSALLELLEAAKKAGVLISFDPnlrpplwrDEEEARERIAELLELADIVKLSDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 195 EAAEITGIEPtdlasAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQA- 273
Cdd:cd01167 191 ELELLFGEED-----PEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRg 265
|
250 260
....*....|....*....|....*....
gi 552104401 274 ------RPLHDCVRYSSAAGAIAVTRVGA 296
Cdd:cd01167 266 llaldeDELAEALRFANAVGALTCTKAGA 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
48-296 |
1.64e-35 |
|
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: 130.43 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTgSVRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSAD 127
Cdd:cd01168 59 ANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 128 IDAygADIAKARITLL---QREVPHEANLAVAKAVRAAGGTVLLD-PAPVGD---ASQMADLIALSDIISPNETEAAEIT 200
Cdd:cd01168 138 LDW--SLLAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFIVqrfKEALLELLPYVDILFGNEEEAEALA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 201 GIEPTDlaSAEAAgRKLLERGPKIVILKLGSRGALLITADEVKHFTPFK-VKVVDTVAAGDSFNGGFAVAFSQARPLHDC 279
Cdd:cd01168 216 EAETTD--DLEAA-LKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEPLEEC 292
|
250
....*....|....*..
gi 552104401 280 VRYSSAAGAIAVTRVGA 296
Cdd:cd01168 293 IRLGSYAAAEVIQQLGP 309
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
49-312 |
2.83e-33 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 124.09 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAfGELALKQMREFGLDTGSVRVIDDVDTGMAIIqVEETGQNTIAVCAGAnaRWSSADI 128
Cdd:COG1105 40 NVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIKIV-DPSDGTETEINEPGP--EISEEEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 129 DA----YGADIAKARITL----LQREVPHEANLAVAKAVRAAGGTVLLDPApvGDAsqMADLI-ALSDIISPNETEAAEI 199
Cdd:COG1105 116 EAllerLEELLKEGDWVVlsgsLPPGVPPDFYAELIRLARARGAKVVLDTS--GEA--LKAALeAGPDLIKPNLEELEEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 200 TGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDC 279
Cdd:COG1105 192 LGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEA 271
|
250 260 270
....*....|....*....|....*....|...
gi 552104401 280 VRYSSAAGAIAVTRVGAGaaAPTAREVEELIGR 312
Cdd:COG1105 272 LRLAVAAGAAAALSPGTG--LPDREDVEELLAQ 302
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
13-302 |
4.56e-31 |
|
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: 117.78 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 13 FGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRV 92
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 93 IDDVDTGMAIIQVEETGQNTIAVcagaNARWSSADIDAYGADIAKARITLLQREVPHEANLAVAKAVRAAGGTVLLDpAP 172
Cdd:cd01945 85 APGARSPISSITDITGDRATISI----TAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQEARARGIPIPLD-LD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 173 VGDASQMADLIALSDIISPNETEAAEITGieptdlASAEAAGRKLLERGPKIVILKLGSRGALLITAD-EVKHFTPFKVK 251
Cdd:cd01945 160 GGGLRVLEELLPLADHAICSENFLRPNTG------SADDEALELLASLGIPFVAVTLGEAGCLWLERDgELFHVPAFPVE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 552104401 252 VVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPT 302
Cdd:cd01945 234 VVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
49-297 |
2.56e-29 |
|
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: 113.40 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGhDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIiqVEETGQNTIAVCAGAnaRWSSADI 128
Cdd:cd01164 41 NVARVLKDLGVEVTALGFLG-GFTGDFFEALLKEEGIPDDFVEVAGETRINVKI--KEEDGTETEINEPGP--EISEEEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 129 DAYGADIAKAR-----ITL---LQREVPHEANLAVAKAVRAAGGTVLLDpapVGDASQMADLIALSDIISPNETEAAEIT 200
Cdd:cd01164 116 EALLEKLKALLkkgdiVVLsgsLPPGVPADFYAELVRLAREKGARVILD---TSGEALLAALAAKPFLIKPNREELEELF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 201 GIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCV 280
Cdd:cd01164 193 GRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEAL 272
|
250
....*....|....*..
gi 552104401 281 RYSSAAGAIAVTRVGAG 297
Cdd:cd01164 273 RLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
49-309 |
3.02e-28 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 110.74 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAfGELALKQMREFGLDTGSVRVIDDVDTGMAIiqVEETGQNTIAVCAGANArwSSADI 128
Cdd:TIGR03168 40 NVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKI--KESSGEETELNEPGPEI--SEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 129 DA----YGADIAKARITL----LQREVPHEANLAVAKAVRAAGGTVLLDpapVGDASQMADLIALSDIISPNETEAAEIT 200
Cdd:TIGR03168 115 EQllekLRELLASGDIVVisgsLPPGVPPDFYAQLIAIARKKGAKVILD---TSGEALREALAAKPFLIKPNHEELEELF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 201 GIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCV 280
Cdd:TIGR03168 192 GRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEAL 271
|
250 260
....*....|....*....|....*....
gi 552104401 281 RYSSAAGAIAVTRVGAGaaAPTAREVEEL 309
Cdd:TIGR03168 272 RFAVAAGSAAAFSPGTG--LPDPEDVEEL 298
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
9-295 |
2.89e-27 |
|
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: 107.89 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGaNQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTG 88
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGGGF-NVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDvDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGADIAK----ARITLLQREVPHEANLAVAKAVrAAGG 164
Cdd:cd01944 80 LPPRGGD-DGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDyvylSGYTLASENASKVILLEWLEAL-PAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 165 TVLLDPAP-VGDASQ--MADLIALSDIISPNETEAAEITGiepTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADE 241
Cdd:cd01944 158 TLVFDPGPrISDIPDtiLQALMAKRPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 552104401 242 VKHFTP-FKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVG 295
Cdd:cd01944 235 NTHIIPgFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
48-307 |
1.62e-25 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 103.48 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIIQVEETGQN--TIAVCAGANARWSS 125
Cdd:PRK09434 32 ANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADLFLQP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 126 ADIDAYGAD-------IAkaritlLQREVPHEANLAVAKAVRAAGGTVLLDP---APV-GDASQMADLI----ALSDIIS 190
Cdd:PRK09434 112 QDLPPFRQGewlhlcsIA------LSAEPSRSTTFEAMRRIKAAGGFVSFDPnlrEDLwQDEAELRECLrqalALADVVK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 191 PNETEAAEITGIepTDLASAEAAGRKLLerGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAF 270
Cdd:PRK09434 186 LSEEELCFLSGT--SQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGL 261
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 552104401 271 SQARPLHDC------VRYSSAAGAIAVTRVGAGAAAPTAREVE 307
Cdd:PRK09434 262 SQAGLWTDEaelaeiIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
9-291 |
5.16e-24 |
|
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: 98.93 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTvNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTg 88
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTS-NPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRVIDDVDTGMAIIQVEETGQNTIAVC-AGANARWSSADIDAYGADIAKARITLLQREVPHEANLAVAKAVRAAGGTVL 167
Cdd:cd01941 79 RGIVFEGRSTASYTAILDKDGDLVVALAdMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 168 LDPAPVGDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALL---ITADEVKH 244
Cdd:cd01941 159 FEPTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLssrEGGVETKL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 552104401 245 FTPFKV-KVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAV 291
Cdd:cd01941 239 FPAPQPeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
49-313 |
4.33e-23 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 98.75 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTgsVRVIDDVDTGMAIIQVEET--------GQNTIAVCAGAN 120
Cdd:PLN02341 124 NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDSSSASYETllcwvlvdPLQRHGFCSRAD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 121 A------RWSSADIDAYGADIAKARITLLQREVPHEANL-AVAKAVRAA---GGTVLLDPAPVG-------DASQMA--D 181
Cdd:PLN02341 202 FgpepafSWISKLSAEAKMAIRQSKALFCNGYVFDELSPsAIASAVDYAidvGTAVFFDPGPRGksllvgtPDERRAleH 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 182 LIALSDIISPNETEAAEITGIEPtdlasAEAAGRKLLERG--PKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAG 259
Cdd:PLN02341 282 LLRMSDVLLLTSEEAEALTGIRN-----PILAGQELLRPGirTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCG 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 552104401 260 DSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAGAAAPTAREVEELIGRA 313
Cdd:PLN02341 357 DSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGAGRNVATLEKVLELLRAS 410
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
9-297 |
5.29e-20 |
|
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: 87.47 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 9 KIFVFGSVNVDVSARMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGlDTG 88
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGG-DKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 89 SVRvIDDVDTGMAIIQVEETGQNTIAVCAGAnarwssaDIDAYGADIAKARITLLqreVPHEANLAVAKAVRAAGGTVLL 168
Cdd:cd01947 80 TVA-WRDKPTRKTLSFIDPNGERTITVPGER-------LEDDLKWPILDEGDGVF---ITAAAVDKEAIRKCRETKLVIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 169 DPAPVGDASQMADLIALSDIISPNETEAAEITgieptdlasaeaAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPF 248
Cdd:cd01947 149 QVTPRVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552104401 249 KVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAG 297
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
48-313 |
2.68e-19 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 86.60 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIIQVEETGQNTIAVcaganARWSSAD 127
Cdd:PLN02323 47 ANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMF-----YRNPSAD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 128 I----DAYGAD-IAKARI-----TLLQREVPHEANLAVAKAVRAAGGTVLLDPA------PVGDAS--QMADLIALSDII 189
Cdd:PLN02323 122 MllreSELDLDlIRKAKIfhygsISLITEPCRSAHLAAMKIAKEAGALLSYDPNlrlplwPSAEAAreGIMSIWDEADII 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 190 SPNETEAAEITGIEPTDLASAeaagRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVA 269
Cdd:PLN02323 202 KVSDEEVEFLTGGDDPDDDTV----VKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQ 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 552104401 270 FSQARP-------LHDCVRYSSAAGAIAVTRVGAGAAAPTAREVEELIGRA 313
Cdd:PLN02323 278 LAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEAVLKLLKKA 328
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
48-308 |
6.31e-18 |
|
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: 82.22 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSV-----------RVIDD------VDTGMAIIQVEETGQ 110
Cdd:cd01172 43 ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIvdegrptttktRVIARnqqllrVDREDDSPLSAEEEQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 111 NTIAVCAGANArwssaDIDAY-GADIAKARITLLQREvpheanlAVAKAVRAAGGTVLLDPAPVgDASQMADlialSDII 189
Cdd:cd01172 123 RLIERIAERLP-----EADVViLSDYGKGVLTPRVIE-------ALIAAARELGIPVLVDPKGR-DYSKYRG----ATLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 190 SPNETEAAEITGIEPTDLASAEAAGRKLLER-GPKIVILKLGSRGALLITAD-EVKHFTPFKVKVVDTVAAGDSFNGGFA 267
Cdd:cd01172 186 TPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDgEVQHIPALAKEVYDVTGAGDTVIATLA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 552104401 268 VAFSQARPLHDCVRYSSAAGAIAVTRVgaGAAAPTAREVEE 308
Cdd:cd01172 266 LALAAGADLEEAAFLANAAAGVVVGKV--GTAPVTPKELLL 304
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
120-270 |
8.11e-18 |
|
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: 79.83 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 120 NARWSSADIDAYGADIAKARITLLQREVPheanLAVAKAVRAAGGTVLLDPAPVG---DASQMADLIALSDIISPNETEA 196
Cdd:cd00287 45 ALARLGVSVTLVGADAVVISGLSPAPEAV----LDALEEARRRGVPVVLDPGPRAvrlDGEELEKLLPGVDILTPNEEEA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552104401 197 AEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITAD-EVKHFTPFKVKVVDTVAAGDSFNGGFAVAF 270
Cdd:cd00287 121 EALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
49-296 |
9.06e-13 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 67.07 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVdtgMAIIQVEETGQNTI------AVCAGAnaR 122
Cdd:PRK09813 28 NVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGV---TAQTQVELHDNDRVfgdyteGVMADF--A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 123 WSSADID-AYGADIAKARITllqrevpHEANLAVAKaVRAAGGTVLLDPAPVGDASQMADLIALSDIIspneteaaeiTG 201
Cdd:PRK09813 103 LSEEDYAwLAQYDIVHAAIW-------GHAEDAFPQ-LHAAGKLTAFDFSDKWDSPLWQTLVPHLDYA----------FA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 202 IEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVR 281
Cdd:PRK09813 165 SAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMA 244
|
250
....*....|....*
gi 552104401 282 YSSAAGAIAVTRVGA 296
Cdd:PRK09813 245 QGTACAAKTIQYHGA 259
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
49-294 |
1.47e-11 |
|
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: 63.53 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDvDTGMAIIQVEETGQNTIAVCAGANARWSSADI 128
Cdd:cd01940 27 NVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEG-ENAVADVELVDGDRIFGLSNKGGVAREHPFEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 129 DAY---GADIAKARITLLQREVPheanlavaKAVRAAGGtvlldpapvgdasqmaDLIALSDIISPNETEAAEITGIEPT 205
Cdd:cd01940 106 DLEylsQFDLVHTGIYSHEGHLE--------KALQALVG----------------AGALISFDFSDRWDDDYLQLVCPYV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 206 DLASAEAAG----------RKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARp 275
Cdd:cd01940 162 DFAFFSASDlsdeevkaklKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGG- 240
|
250
....*....|....*....
gi 552104401 276 lhDCVRYSSAAGAIAVTRV 294
Cdd:cd01940 241 --TAIAEAMRQGAQFAAKT 257
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
179-293 |
2.17e-11 |
|
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: 63.24 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 179 MADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILK--------LGSRGALLITADEVKHFT---- 246
Cdd:COG2240 132 MRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTADGAWLVEtpll 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 552104401 247 PFKVkvvdtVAAGDSFNGGFAVAFSQARPLHDCVRYSSAA--GAIAVTR 293
Cdd:COG2240 212 PFSP-----NGTGDLFAALLLAHLLRGKSLEEALERAAAFvyEVLERTA 255
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
181-266 |
9.48e-11 |
|
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: 61.33 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 181 DLIALSDIISPNETEAAEITGieptdLASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVK-VVDTVAAG 259
Cdd:cd01946 159 KVLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLEsVFDPTGAG 233
|
....*..
gi 552104401 260 DSFNGGF 266
Cdd:cd01946 234 DTFAGGF 240
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
154-295 |
3.36e-10 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 59.80 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 154 AVAKAVRAAGGTVLLDPApvGDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERG-PKIVILKLGSR 232
Cdd:PRK10294 151 QLISAAQKQGIRCIIDSS--GDALSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQ 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552104401 233 GALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVG 295
Cdd:PRK10294 229 GALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQG 291
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
165-281 |
5.06e-10 |
|
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: 58.75 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 165 TVLLDPApVGDASQM------------ADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILK---- 228
Cdd:cd01173 105 LYVCDPV-MGDNGKLyvvaeeivpvyrDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvel 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 552104401 229 --LGSRGALLITADEVKHF-TPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVR 281
Cdd:cd01173 184 adDDRIEMLGSTATEAWLVqRPKIPFPAYFNGTGDLFAALLLARLLKGKSLAEALE 239
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
10-292 |
1.67e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 58.08 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 10 IFVFGSVNVDVSARMAAlPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGS 89
Cdd:PRK09850 7 VVIIGSANIDVAGYSHE-SLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 90 VRVIDDVDTGMAIIQVEETGQNTIAVCAGANARWSSADIDAYGAD-IAKARITLLQREVPHEANLAVAKavRAAGGTVLL 168
Cdd:PRK09850 86 CLIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREfIQRAKVIVADCNISEEALAWILD--NAANVPVFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 169 DPAPVGDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITAD-EVKHFTP 247
Cdd:PRK09850 164 DPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISgESGWSAP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 552104401 248 FKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVT 292
Cdd:PRK09850 244 IKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
59-295 |
2.18e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 57.80 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 59 GAIRFVGAVGHDAFGElalkQMREFGLDTGsVRVIDDVDtgmaiiqvEETGQNTIAVCAGANARWSSADIDA---YGAD- 134
Cdd:PLN02548 70 GATSYMGCIGKDKFGE----EMKKCATAAG-VNVHYYED--------ESTPTGTCAVLVVGGERSLVANLSAancYKVEh 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 135 ---------IAKAR---ITLLQREVPHEANLAVAKAVRAAGGTVLLD-PAP-----VGDasQMADLIALSDIISPNETEA 196
Cdd:PLN02548 137 lkkpenwalVEKAKfyyIAGFFLTVSPESIMLVAEHAAANNKTFMMNlSAPficefFKD--QLMEALPYVDFLFGNETEA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 197 ---AEITGIEPTDL---ASAEAAGRKLLERGPKIVILKLGSRGALLITADEVKHF--TPF-KVKVVDTVAAGDSFNGGFA 267
Cdd:PLN02548 215 rtfAKVQGWETEDVeeiALKISALPKASGTHKRTVVITQGADPTVVAEDGKVKEFpvIPLpKEKLVDTNGAGDAFVGGFL 294
|
250 260
....*....|....*....|....*...
gi 552104401 268 VAFSQARPLHDCVRYSSAAGAIAVTRVG 295
Cdd:PLN02548 295 SQLVQGKDIEECVRAGNYAANVIIQRSG 322
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
160-297 |
3.00e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 57.01 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 160 RAAGGTVLLDPApvgDASQMADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILKLGSRGALLITA 239
Cdd:PRK09513 158 RSQCPCIIFDSS---REALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNA 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 552104401 240 DEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVGAG 297
Cdd:PRK09513 235 SGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVG 292
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
154-281 |
3.41e-09 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 56.34 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 154 AVAKAVRAAGGTVLLDP-------APVGDASQMA----DLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGP 222
Cdd:pfam08543 77 AVAEKLDKYGVPVVLDPvmvaksgDSLLDDEAIEalkeELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552104401 223 KIVILK---LGSRGA----LLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVR 281
Cdd:pfam08543 157 KAVLIKgghLEGEEAvvtdVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVR 222
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
55-305 |
2.37e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 54.80 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 55 AKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVdTGMAIIQVEETGQNTIAVCAGANARWSSADI---DAY 131
Cdd:PLN02379 98 AGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGNRTMRPCLSSAVKLQADELtkeDFK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 132 GADIAKARITLLQREVPHEAnLAVAKAVraaGGTVLLDPAP---VGDA-SQMADLIALSDI--ISPNETEAAEITGIEPT 205
Cdd:PLN02379 177 GSKWLVLRYGFYNLEVIEAA-IRLAKQE---GLSVSLDLASfemVRNFrSPLLQLLESGKIdlCFANEDEARELLRGEQE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 206 dlASAEAAgRKLLERGPKIVILKLGSRGALLITADEVKHFTPFK-VKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSS 284
Cdd:PLN02379 253 --SDPEAA-LEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
250 260
....*....|....*....|.
gi 552104401 285 AAGAiAVTRVGAGAAAPTARE 305
Cdd:PLN02379 330 CSGG-SVVRALGGEVTPENWQ 349
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
59-296 |
2.49e-08 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 54.65 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 59 GAIRFVGAVGHDAFGElalkQMREfGLDTGSVRVIDDVDTGmaiiqvEETGqnTIAVCA-----------GANARWSSAD 127
Cdd:PTZ00247 81 GFVCYVGCVGDDRFAE----ILKE-AAEKDGVEMLFEYTTK------APTG--TCAVLVcgkerslvanlGAANHLSAEH 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 128 ID--AYGADIAKARITLLQ---REVPHEANLAVAKAVRAAGGTVLLD-PAP-VGDA--SQMADLIALSDIISPNETEA-- 196
Cdd:PTZ00247 148 MQshAVQEAIKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFffERLLQVLPYVDILFGNEEEAkt 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 197 -AEITGIEPTDLAS--AEAAG-RKLLERGPKIVILKLGSRGALLITADEVKHFTPFKV---KVVDTVAAGDSFNGGFAVA 269
Cdd:PTZ00247 228 fAKAMKWDTEDLKEiaARIAMlPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLdqeKIVDTNGAGDAFVGGFLAQ 307
|
250 260
....*....|....*....|....*..
gi 552104401 270 FSQARPLHDCVRYSSAAGAIAVTRVGA 296
Cdd:PTZ00247 308 YANGKDIDRCVEAGHYSAQVIIQHNGC 334
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
48-266 |
2.74e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.81 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 48 ANQAVAVAKLGGA--------IRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVdTGMAIIQVEETGQNTIAVCAGA 119
Cdd:PLN02813 130 SNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGT-TGTVIVLTTPDAQRTMLSYQGT 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 120 NarwSSADIDAYGAD-IAKARITLLQR---EVPH--EANLAVAKAVRAAGGTVLLDPAPVGDAS----QMADLIALS-DI 188
Cdd:PLN02813 209 S---STVNYDSCLASaISKSRVLVVEGylwELPQtiEAIAQACEEAHRAGALVAVTASDVSCIErhrdDFWDVMGNYaDI 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552104401 189 ISPNETEAAEITGIEPTDlaSAEAAGRKLLERGPkIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGF 266
Cdd:PLN02813 286 LFANSDEARALCGLGSEE--SPESATRYLSHFCP-LVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGI 360
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
183-286 |
1.02e-07 |
|
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: 52.52 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 183 IALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILK-LGSRGA--------LLITADEVKHF-TPFKVKV 252
Cdd:TIGR00687 136 IPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSqrdrsfegLVATQEGRWHIsRPLAVFD 215
|
90 100 110
....*....|....*....|....*....|....
gi 552104401 253 VDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAA 286
Cdd:TIGR00687 216 PPPVGTGDLIAALLLATLLHGNSLKEALEKTVSA 249
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
209-295 |
1.03e-07 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 52.41 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 209 SAEAAGRKLLERG--PKIVILKLGSRGALLITAD-EVKHFTPFK-VKVVDTVAAGDSFNGGFAVAFSQA-RPLHDCVRYS 283
Cdd:cd01939 197 SPEECLRGEGPRAkkAALLVCTWGDQGAGALGPDgEYVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFG 276
|
90
....*....|..
gi 552104401 284 SAAGAIAVTRVG 295
Cdd:cd01939 277 NRVASQKCTGVG 288
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
160-281 |
4.12e-07 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 50.51 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 160 RAAGGTVLLDPApvGDASQMADLIALSDIISPNETEAAEITGIEPTDLASA-EAAGRKLLERGPKIVILKLGSRGA---- 234
Cdd:PRK06427 110 IAKSGDPLLADD--AVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmKAAARALHALGCKAVLIKGGHLLDgees 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 552104401 235 --LLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVR 281
Cdd:PRK06427 188 vdWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQ 236
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
187-295 |
4.69e-07 |
|
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: 50.42 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 187 DIISPNETEAAEITGI---EPTDLASAEAAGRKLLE-----RGPKIVILKLGSRGALLITAD--EVKHFTPF---KVKVV 253
Cdd:cd01943 182 DVFSPNLEEAARLLGLptsEPSSDEEKEAVLQALLFsgilqDPGGGVVLRCGKLGCYVGSADsgPELWLPAYhtkSTKVV 261
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 552104401 254 DTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVG 295
Cdd:cd01943 262 DPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
182-266 |
4.92e-07 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 50.25 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 182 LIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILK--------LGSRGALLITADEVKHF-TPFKVKV 252
Cdd:PRK05756 135 ALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypADRFEMLLVTADGAWHIsRPLVDFM 214
|
90
....*....|....
gi 552104401 253 VDTVAAGDSFNGGF 266
Cdd:PRK05756 215 RQPVGVGDLTSALF 228
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
185-300 |
3.34e-06 |
|
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: 47.40 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 185 LSDIISPNETEAAEITgiEPTDLAsaeaagRKLLERGPKIVILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNG 264
Cdd:cd01937 155 LHDVLKLSRVEAEVIS--TPTELA------RLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLA 226
|
90 100 110
....*....|....*....|....*....|....*.
gi 552104401 265 GFavafsqarplhdCVRYSSAAGAIAVTRVGAGAAA 300
Cdd:cd01937 227 AF------------LYSRLSGKDIKEAAEFAAAAAA 250
|
|
| PLN02967 |
PLN02967 |
kinase |
49-225 |
1.06e-05 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 46.96 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 49 NQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIIQVEETGQ---NTIAVCAGANARWSS 125
Cdd:PLN02967 248 GVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRlktTCVKPCAEDSLSKSE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 126 ADIDAygadIAKARI------TLLQREVPHEANLAVaKAVRAAGGTVLLD---PAPVGDASQMADLIA-----LSDIISP 191
Cdd:PLN02967 328 INIDV----LKEAKMfyfnthSLLDPTMRSTTLRAI-KISKKLGGVIFYDlnlPLPLWSSSEETKSFIqeawnLADIIEV 402
|
170 180 190
....*....|....*....|....*....|....*
gi 552104401 192 NETEAAEITGIEPTD-LASAEAAGRKLLERGPKIV 225
Cdd:PLN02967 403 TKQELEFLCGIEPTEeFDTKDNDKSKFVHYSPEVV 437
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
179-228 |
1.94e-05 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 45.46 E-value: 1.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 552104401 179 MADLIALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVILK 228
Cdd:PTZ00344 133 YRELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
225-295 |
4.57e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 44.41 E-value: 4.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552104401 225 VILKLGSRGALLITADEVKHFTPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIAVTRVG 295
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
12-290 |
2.58e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 42.23 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 12 VFGSVNVDVSArMAALPRPGQTVNASGYGIGLGGKGANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLD-TGSV 90
Cdd:PRK09954 62 VVGAINMDIRG-MADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNvSGCI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 91 RViddvdtgmaiiqveeTGQNTIAVCAGANARWSSAdidaygadIAKARITLLQREVPHEANlAVAKAVRAAgGTVLLD- 169
Cdd:PRK09954 141 RL---------------HGQSTSTYLAIANRQDETV--------LAINDTHILQQLTPQLLN-GSRDLIRHA-GVVLADc 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 170 ---PAPVGDASQMADLIA-----------------LSDI--ISPNETEAAEITGIEPTDLASAEAAGRKLLERGPKIVIL 227
Cdd:PRK09954 196 nltAEALEWVFTLADEIPvfvdtvsefkagkikhwLAHIhtLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFV 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552104401 228 KLGSRgALLITADEVKHF--TPFKVKVVDTVAAGDSFNGGFAVAFSQARPLHDCVRYSSAAGAIA 290
Cdd:PRK09954 276 YLPDE-SVFCSEKDGEQFllTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAIS 339
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
178-227 |
6.83e-04 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 40.67 E-value: 6.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 552104401 178 QMADLIALSDIISPNETEAAEITGiEPTDLASA-----EAAGRKLLERGPKIVIL 227
Cdd:PRK07105 130 EMRKLIQKADVITPNLTEACLLLD-KPYLEKSYseeeiKQLLRKLADLGPKIVII 183
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
108-230 |
3.48e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 38.94 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 108 TGQNTIAVCA------GANARWSSADIDAYGADIAKARItLLQREVPHeanlAVAKAVRAAGGTVLLDP-------APVG 174
Cdd:PRK08573 41 TAQNTYEVRAihdlppEVVAAQIEAVWEDMGIDAAKTGM-LSNREIIE----AVAKTVSKYGFPLVVDPvmiaksgAPLL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552104401 175 DASQMADLI----ALSDIISPNETEAAEITGIEPTDLASAEAAGRKLLER-GPKIVILKLG 230
Cdd:PRK08573 116 REDAVDALIkrllPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKGG 176
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
188-271 |
4.21e-03 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 38.17 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 188 IISPNETEAAEITGIEPT-DLASAEAAGRKLLERGPKIVILKLGSRGALlitadeVKHFTPF------KVKVVDTVAAGD 260
Cdd:PRK13508 180 VIKPNIEELSQLLGKEVSeDLDELKEVLQQPLFEGIEWIIVSLGADGAF------AKHNDTFykvdipKIEVVNPVGSGD 253
|
90
....*....|.
gi 552104401 261 SFNGGFAVAFS 271
Cdd:PRK13508 254 STVAGIASGLL 264
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
48-105 |
6.39e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 37.96 E-value: 6.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 552104401 48 ANQAVAVAKLGGAIRFVGAVGHDAFGELALKQMREFGLDTGSVRVIDDVDTGMAIIQV 105
Cdd:PLN02543 176 SNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKI 233
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
152-230 |
7.72e-03 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 37.83 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552104401 152 NLAVAKAVRAAGGTVLLDPAPVGDASQmaDLIALSDIISPNETEAAEITGIEPTD-LASAEAAGRKLLERGPKIVILKLG 230
Cdd:PLN02898 107 ALVVDPVMVSTSGDVLAGPSILSALRE--ELLPLATIVTPNVKEASALLGGDPLEtVADMRSAAKELHKLGPRYVLVKGG 184
|
|
| |
