|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-301 |
9.46e-103 |
|
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: 302.57 E-value: 9.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 6 DVITIGEAMAMFVATETGELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLD 85
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 86 GRFPTGFQLKSKVENGtDPIVEYFRKGSAASHLSVADYHADYFASARHLHLSGVAAALSASSYELLDHAATTMKAQGKTL 165
Cdd:cd01166 81 PGRPTGLYFLEIGAGG-ERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 166 SFDPNLRPVLWkSEAEMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADFYL--NKGVKAVVLKTGADGAWFKTAnG 243
Cdd:cd01166 160 SFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKLGAEGALVYTG-G 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 635773354 244 EQGAVAAVKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDS 301
Cdd:cd01166 238 GRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-310 |
2.34e-84 |
|
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: 255.96 E-value: 2.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 6 DVITIGEAMAMFVAT-----ETGELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAA 80
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 81 GVTLDGRFPTGFQLKSKVENGtDPIVEYFRkgSAASHLSVADYHADYFASARHLHLSGVAAAlSASSYELLDHAATTMKA 160
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDG-ERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLA-SEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 161 QGKTLSFDPNLRPVLWkseAEMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKT 240
Cdd:COG0524 157 AGVPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 241 AnGEQGAVAAVKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPTRAQL 310
Cdd:COG0524 234 G-GEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-299 |
1.19e-54 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 179.85 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 6 DVITIGEAMAMFVATET---GELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGV 82
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEglpGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 83 TLDGRFPTGFQLKSkVENGTDPIVEYFRKGSAASHLSVADYHADYFASARHLHLSG-VAAALSASSYELLDHAAttmKAQ 161
Cdd:pfam00294 81 VIDEDTRTGTALIE-VDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGsLPLGLPEATLEELIEAA---KNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 162 GKtlsFDPNLRPVLWkseaEMVEKLNRLAFRADWVLPGLKEGMILTGES--TPEGIADFY---LNKGVKAVVLKTGADGA 236
Cdd:pfam00294 157 GT---FDPNLLDPLG----AAREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALhklLAKGIKTVIVTLGADGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635773354 237 WFKTANGEQGaVAAVKVENVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:pfam00294 230 LVVEGDGEVH-VPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
7-299 |
5.17e-54 |
|
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: 178.21 E-value: 5.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 7 VITIGEAMAMFVATETGelsAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDG 86
Cdd:cd01167 2 VVCFGEALIDFIPEGSG---APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 87 RFPTGfqlKSKVENGTDPIVEY-FRKGSAASHLSVADYHADYFASARHLHLsGVAAALSASSYELLDHAATTMKAQGKTL 165
Cdd:cd01167 79 AAPTT---LAFVTLDADGERSFeFYRGPAADLLLDTELNPDLLSEADILHF-GSIALASEPSRSALLELLEAAKKAGVLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 166 SFDPNLRPVLWKSEAEMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKTaNGEQ 245
Cdd:cd01167 155 SFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYT-KGGV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635773354 246 GAVAAVKVEnVVDTVGAGDGFAVGVISALLEGK-------TLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01167 234 GEVPGIPVE-VVDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
33-299 |
1.99e-37 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 134.36 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 33 KRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKskVENGTDPIVEYFRKG 112
Cdd:cd01942 33 REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFI--LTDGDDNQIAYFYPG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 113 sAASHLSVADYhADYFASARHLHLSGVaaalsassYELLDHAaTTMKAQGKTLSFDPNlrPVLWKSEAEMVEKLNRlafR 192
Cdd:cd01942 111 -AMDELEPNDE-ADPDGLADIVHLSSG--------PGLIELA-RELAAGGITVSFDPG--QELPRLSGEELEEILE---R 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 193 ADWVLPGLKEGMIL---TGESTPEgiadfyLNKGVKAVVLKTGADGAWFKTaNGEQGAVAAVKVENVVDTVGAGDGFAVG 269
Cdd:cd01942 175 ADILFVNDYEAELLkerTGLSEAE------LASGVRVVVVTLGPKGAIVFE-DGEEVEVPAVPAVKVVDTTGAGDAFRAG 247
|
250 260 270
....*....|....*....|....*....|
gi 635773354 270 VISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01942 248 FLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
29-310 |
9.32e-37 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 133.52 E-value: 9.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 29 EHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDgrfptGFQLKSKVENGTDPIVE- 107
Cdd:PRK09434 21 NRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLD-----PAHRTSTVVVDLDDQGEr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 108 ---YFRKGSAASHLSVADYHAdyFASARHLHLSGVaaALSA-----SSYElldhAATTMKAQGKTLSFDPNLRPVLWKSE 179
Cdd:PRK09434 96 sftFMVRPSADLFLQPQDLPP--FRQGEWLHLCSI--ALSAepsrsTTFE----AMRRIKAAGGFVSFDPNLREDLWQDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 180 AEMVEKLNRLAFRADWVLPGLKEGMILTGESTPE-GIADFYLNKGVKAVVLKTGADGAWFKTaNGEQGAVAAVKVEnVVD 258
Cdd:PRK09434 168 AELRECLRQALALADVVKLSEEELCFLSGTSQLEdAIYALADRYPIALLLVTLGAEGVLVHT-RGQVQHFPAPSVD-PVD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 635773354 259 TVGAGDGFAVGVISALLEGK------TLPQAVARGNKIGSLAIQVQGDSEGLPTRAQL 310
Cdd:PRK09434 246 TTGAGDAFVAGLLAGLSQAGlwtdeaELAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
23-306 |
4.14e-32 |
|
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: 120.73 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 23 GELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKSKVENGT 102
Cdd:cd01174 23 GETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 103 DPIVEYfrkGSAASHLSVADY--HADYFASARHLHLSG---VAAALsassyelldHAATTMKAQGKTLSFDPnlrpvlwk 177
Cdd:cd01174 103 NRIVVV---PGANGELTPADVdaALELIAAADVLLLQLeipLETVL---------AALRAARRAGVTVILNP-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 178 seAEMVEKLNRLAFRADWVLPGLKEGMILTGESTP-----EGIADFYLNKGVKAVVLKTGADGAWFKTaNGEQGAVAAVK 252
Cdd:cd01174 163 --APARPLPAELLALVDILVPNETEAALLTGIEVTdeedaEKAARLLLAKGVKNVIVTLGAKGALLAS-GGEVEHVPAFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 635773354 253 VEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPT 306
Cdd:cd01174 240 VK-AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
37-310 |
9.60e-32 |
|
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: 119.63 E-value: 9.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAelNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKSKVENGTDPIVEYfrKGsAAS 116
Cdd:TIGR02152 34 GA--NQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVV--AG-ANA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 117 HLSVADYHADYfasarhlhlsgvaAALSASSYELL---------DHAATTMKAQGKTLSFDPnlRPVLWKSEAEMVEKln 187
Cdd:TIGR02152 109 ELTPEDIDAAE-------------ALIAESDIVLLqleipletvLEAAKIAKKHGVKVILNP--APAIKDLDDELLSL-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 188 rlafrADWVLPGLKEGMILTG-----ESTPEGIADFYLNKGVKAVVLKTGADGAWFKTANgEQGAVAAVKVeNVVDTVGA 262
Cdd:TIGR02152 172 -----VDIITPNETEAEILTGievtdEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKD-ESKLIPAFKV-KAVDTTAA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 635773354 263 GDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPTRAQL 310
Cdd:TIGR02152 245 GDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
7-309 |
3.11e-25 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 103.16 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 7 VITIGEAMAMFVATETG-ELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLD 85
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGvSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 86 GRFPTGFQLKSKVENGTDPIVeYFRKGSAASHLSVADYHADYFASARHLHLsGVAAALSASSYELLDHAATTMKAQGKTL 165
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFM-FYRNPSADMLLRESELDLDLIRKAKIFHY-GSISLITEPCRSAHLAAMKIAKEAGALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 166 SFDPNLRPVLWKSEAEMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADFYL-NKGVKAVVLKTGADGAWFKTANGe 244
Cdd:PLN02323 171 SYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLwHPNLKLLLVTEGEEGCRYYTKDF- 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635773354 245 QGAVAAVKVeNVVDTVGAGDGFAVGVISALLEGKTLPQ-------AVARGNKIGSLAIQVQGDSEGLPTRAQ 309
Cdd:PLN02323 250 KGRVEGFKV-KAVDTTGAGDAFVGGLLSQLAKDLSLLEdeerlreALRFANACGAITTTERGAIPALPTKEA 320
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
37-299 |
2.24e-24 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 100.38 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRfPTGfQLKSKVENGTDPivEYFRKGSAAS 116
Cdd:cd01168 56 GSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDG-PTG-TCAVLVTPDAER--TMCTYLGAAN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 117 HLSVADYHADYFASARHLHLSGvaaALSASSYELLDHAATTMKAQGKTLSFdpNLrpvlwkSEAEMVEKlNRLAFR---- 192
Cdd:cd01168 132 ELSPDDLDWSLLAKAKYLYLEG---YLLTVPPEAILLAAEHAKENGVKIAL--NL------SAPFIVQR-FKEALLellp 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 193 -ADWVLPGLKEGMILTGESTPEG--IADFYLNKGVKAVVLKTGADGAWFKTaNGEQGAVAAVKVENVVDTVGAGDGFAVG 269
Cdd:cd01168 200 yVDILFGNEEEAEALAEAETTDDleAALKLLALRCRIVVITQGAKGAVVVE-GGEVYPVPAIPVEKIVDTNGAGDAFAGG 278
|
250 260 270
....*....|....*....|....*....|
gi 635773354 270 VISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01168 279 FLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
37-310 |
1.72e-20 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 89.54 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAelNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKSKVENGTDPIVEYfrkGSAAS 116
Cdd:PRK11142 42 GA--NQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIH---AGANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 117 HLSVADYHADY--FASARHL------HLSGVAaalsassyelldHAATTMKAQGKTLSFDPNLRPVLWKSEAEMVeklnr 188
Cdd:PRK11142 117 ALTPALVEAHRelIANADALlmqletPLETVL------------AAAKIAKQHGTKVILNPAPARELPDELLALV----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 189 lafraDWVLPGLKEGMILTG-----ESTPEGIADFYLNKGVKAVVLKTGADGAWFkTANGEQGAVAAVKVEnVVDTVGAG 263
Cdd:PRK11142 180 -----DIITPNETEAEKLTGirvedDDDAAKAAQVLHQKGIETVLITLGSRGVWL-SENGEGQRVPGFRVQ-AVDTIAAG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 635773354 264 DGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPTRAQL 310
Cdd:PRK11142 253 DTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEI 299
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
32-299 |
3.59e-18 |
|
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: 82.86 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 32 IKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDaagVTLDGRF-PTGFQLKSKVEngTDPIVEYFR 110
Cdd:cd01944 31 KSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE---ILLPPRGgDDGGCLVALVE--PDGERSFIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 111 KGSAASHLSVADYHADYFASARHLHLSGVAAALSASSYELLDHAATTMKAqGKTLSFDP-NLRPVLWKSEaemvekLNRL 189
Cdd:cd01944 106 ISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPA-GTTLVFDPgPRISDIPDTI------LQAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 190 AFRADWVLPGLKEGMILTGESTP--EGIADFYLNKGVKAVVLKTGADGAWFKTANGEQGAVAAVKVEnVVDTVGAGDGFA 267
Cdd:cd01944 179 MAKRPIWSCNREEAAIFAERGDPaaEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKVK-AVDTIGAGDTHA 257
|
250 260 270
....*....|....*....|....*....|..
gi 635773354 268 VGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01944 258 GGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
34-299 |
3.62e-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: 76.62 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 34 RVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGV-TLDGrfPTGFQLkSKVENGTDPIVEYFRKG 112
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCrVKEG--ENAVAD-VELVDGDRIFGLSNKGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 113 SAASHLSVADYhaDYFASARHLHLsgvaaalsaSSYELLDHAATTMKA---QGKTLSFDPNLRpvlwkSEAEMVEKlnrl 189
Cdd:cd01940 97 VAREHPFEADL--EYLSQFDLVHT---------GIYSHEGHLEKALQAlvgAGALISFDFSDR-----WDDDYLQL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 190 afradwVLPGLKEGMILTGESTPEGIADF---YLNKGVKAVVLKTGADGAWFktANGEQGAVAAVKVENVVDTVGAGDGF 266
Cdd:cd01940 157 ------VCPYVDFAFFSASDLSDEEVKAKlkeAVSRGAKLVIVTRGEDGAIA--YDGAVFYSVAPRPVEVVDTLGAGDSF 228
|
250 260 270
....*....|....*....|....*....|....
gi 635773354 267 AVGVISALLEGKT-LPQAVARGNKIGSLAIQVQG 299
Cdd:cd01940 229 IAGFLLSLLAGGTaIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
37-306 |
3.95e-16 |
|
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: 76.95 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTL--DGRFPTGFQLKSKVENGTdpiVEYFRKGSA 114
Cdd:cd01945 37 GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVapGARSPISSITDITGDRAT---ISITAIDTQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 115 ASHLSVADyhaDYFASARHLHLSGVAAALSAssyelldHAATTMKAQGKtlsfdpnlrPVLWKSEAEMVEKLNRLAFRAD 194
Cdd:cd01945 114 AAPDSLPD---AILGGADAVLVDGRQPEAAL-------HLAQEARARGI---------PIPLDLDGGGLRVLEELLPLAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 195 WVLPGLKEGMILTGESTPEGIAdfYL-NKGVKAVVLKTGADGAWFKTANGEQGAVAAVKVEnVVDTVGAGDGFAVGVISA 273
Cdd:cd01945 175 HAICSENFLRPNTGSADDEALE--LLaSLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVE-VVDTTGAGDVFHGAFAHA 251
|
250 260 270
....*....|....*....|....*....|...
gi 635773354 274 LLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPT 306
Cdd:cd01945 252 LAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
41-296 |
3.00e-15 |
|
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: 74.66 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 41 NVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRfPTGFQLKSKVENGTdpiveyfrkgsaaSHLSV 120
Cdd:cd01941 40 NIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGR-STASYTAILDKDGD-------------LVVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 121 ADyhADYFASARHLHLSGVAAALSASSYELLDH--AATTMKAQGKtlSFDPNLRPVlWKSEAEMVeKLNRLAFRA---DW 195
Cdd:cd01941 106 AD--MDIYELLTPDFLRKIREALKEAKPIVVDAnlPEEALEYLLA--LAAKHGVPV-AFEPTSAP-KLKKLFYLLhaiDL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 196 VLPGLKEGMILTGESTPEG-----IADFYLNKGVKAVVLKTGADGAWFKTANGEQGA--VAAVKVENVVDTVGAGDGFAV 268
Cdd:cd01941 180 LTPNRAELEALAGALIENNedenkAAKILLLPGIKNVIVTLGAKGVLLSSREGGVETklFPAPQPETVVNVTGAGDAFVA 259
|
250 260
....*....|....*....|....*...
gi 635773354 269 GVISALLEGKTLPQAVARGNKIGSLAIQ 296
Cdd:cd01941 260 GLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
37-299 |
3.35e-15 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 74.00 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVtldgRFPTGFQLKSKVE-NGTDPIVEYFRKGSAA 115
Cdd:PRK09813 24 GNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV----HTKHGVTAQTQVElHDNDRVFGDYTEGVMA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 116 sHLSVADYHADYFASARHLHlsgvaAALSASSYELLdhaaTTMKAQGKTLSFDPNLRPvlwksEAEMVEKLnrlafradw 195
Cdd:PRK09813 100 -DFALSEEDYAWLAQYDIVH-----AAIWGHAEDAF----PQLHAAGKLTAFDFSDKW-----DSPLWQTL--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 196 vLPGLKEGMILTGESTPEgIADFYLNK---GVKAVVLKTGADG--AWFKTANGEQGAVAAvkveNVVDTVGAGDGFAVGV 270
Cdd:PRK09813 156 -VPHLDYAFASAPQEDEF-LRLKMKAIvarGAGVVIVTLGENGsiAWDGAQFWRQAPEPV----TVVDTMGAGDSFIAGF 229
|
250 260
....*....|....*....|....*....
gi 635773354 271 ISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:PRK09813 230 LCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
36-292 |
3.88e-15 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 75.64 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 36 AGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDA--------AGVTLDGRFPT--------GFQ---LKS 96
Cdd:PLN02341 119 AGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVvgliegtdAGDSSSASYETllcwvlvdPLQrhgFCS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 97 KVENGTDPIVEYFRKGSAASHLSVAdyhadyfaSARHLHLSGVAaaLSASSYELLDHAATTMKAQGKTLSFDPNLR-PVL 175
Cdd:PLN02341 199 RADFGPEPAFSWISKLSAEAKMAIR--------QSKALFCNGYV--FDELSPSAIASAVDYAIDVGTAVFFDPGPRgKSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 176 WKSEAEMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADFYLNKGVKA--VVLKTGADGAWFKTANGeQGAVAAVKV 253
Cdd:PLN02341 269 LVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSS-VSCAPAFKV 347
|
250 260 270
....*....|....*....|....*....|....*....
gi 635773354 254 eNVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGS 292
Cdd:PLN02341 348 -NVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
23-310 |
1.95e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 23 GELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQL-KSKVENG 101
Cdd:PTZ00292 39 GETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMiFVDTKTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 102 TDPIVEYfrkGSAASHLS---VADYHADYFASARHLhLSGVAAALsASSYELLDHAattmKAQGKTLSFDPNLRPvlwks 178
Cdd:PTZ00292 119 NNEIVII---PGANNALTpqmVDAQTDNIQNICKYL-ICQNEIPL-ETTLDALKEA----KERGCYTVFNPAPAP----- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 179 EAEMVEKLNRLAFRADWVLPGLKEGMILTG-ESTPEGIAD----FYLNKGVKAVVLKTGADGAWFKTANGEQGAVAAVKV 253
Cdd:PTZ00292 185 KLAEVEIIKPFLKYVSLFCVNEVEAALITGmEVTDTESAFkaskELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRV 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 635773354 254 eNVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGDSEGLPTRAQL 310
Cdd:PTZ00292 265 -KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
21-310 |
7.33e-13 |
|
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: 67.60 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 21 ETGELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSfGHFVLDSLKKEGIDAAGVTLDGrfPTGFQLKSKVEN 100
Cdd:TIGR03168 20 TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKG--ETRINVKIKESS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 101 G--TDpIVEyfrKGSAASHLSVA---DYHADYFASARHLHLSG-VAAALSASSYELLDHAAttmKAQGKTLSFDPNlRPV 174
Cdd:TIGR03168 97 GeeTE-LNE---PGPEISEEELEqllEKLRELLASGDIVVISGsLPPGVPPDFYAQLIAIA---RKKGAKVILDTS-GEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 175 LWKSeaemveklnrLAFRADWVLPGLKE-----GMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKTANGEQGAVA 249
Cdd:TIGR03168 169 LREA----------LAAKPFLIKPNHEEleelfGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635773354 250 AvKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQGdsEGLPTRAQL 310
Cdd:TIGR03168 239 P-KVE-VVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDV 295
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-310 |
2.34e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 66.31 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 40 LNVATGLARLGLNVGWVSRVGDDSfGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKSKVENGTDPIVEyfrKGSAASHLS 119
Cdd:COG1105 39 INVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTETEINE---PGPEISEEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 120 VADYHADYFASARH---LHLSG-VAAALSASSYELLDHAAttmKAQGKTLSFD---PNLRPVLwKSEAEMVeKLNRlafr 192
Cdd:COG1105 115 LEALLERLEELLKEgdwVVLSGsLPPGVPPDFYAELIRLA---RARGAKVVLDtsgEALKAAL-EAGPDLI-KPNL---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 193 adwvlpglKEGMILTGES--TPEGIADF---YLNKGVKAVVLKTGADGAWFKTANGEQgAVAAVKVEnVVDTVGAGDGFA 267
Cdd:COG1105 186 --------EELEELLGRPleTLEDIIAAareLLERGAENVVVSLGADGALLVTEDGVY-RAKPPKVE-VVSTVGAGDSMV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 635773354 268 VGVISALLEGKTLPQAVARGNKIGSLAIQVQGdsEGLPTRAQL 310
Cdd:COG1105 256 AGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDV 296
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
23-299 |
7.31e-12 |
|
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: 64.36 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 23 GELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGrfPTGFQLKSKVENGT 102
Cdd:cd01947 23 GGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDK--PTRKTLSFIDPNGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 103 DPIV---EYFRKGSAASHLSVADYhadYFASArhlhlsgvaaalSASSYELLDHAATtMKAqgKTLSFDPNLRpvlwkse 179
Cdd:cd01947 101 RTITvpgERLEDDLKWPILDEGDG---VFITA------------AAVDKEAIRKCRE-TKL--VILQVTPRVR------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 180 aemVEKLNRLAFRADwvlpglkeGMILTGESTPE-GIADFYLNKGVKAVVLKTGADGAWFKTAnGEQGAVAAVKVeNVVD 258
Cdd:cd01947 156 ---VDELNQALIPLD--------ILIGSRLDPGElVVAEKIAGPFPRYLIVTEGELGAILYPG-GRYNHVPAKKA-KVPD 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 635773354 259 TVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01947 223 STGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
2-299 |
2.15e-11 |
|
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: 63.19 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 2 HKTLDVITIGEAMAMfvatETGELSAVEHFIKRvAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAG 81
Cdd:cd01939 7 LTVLDFITTVDKYPF----EDSDQRTTNGRWQR-GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 82 VtldgrFPTGFQ-------LKSKveNGTDPIVEYFRkgsAASHLSVADYHADYFASARHLHLSGVAAALSASSYELLDHA 154
Cdd:cd01939 82 C-----YRKDIDepassyiIRSR--AGGRTTIVNDN---NLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 155 ATTMKAQGKTLSFDpNLRPVlwkseaemvEKLNRLAFRADWVLpGLKEGMILTGESTP-EGIADFYLNKGVKAVVLKT-G 232
Cdd:cd01939 152 NNRRPEIRITISVE-VEKPR---------EELLELAAYCDVVF-VSKDWAQSRGYKSPeECLRGEGPRAKKAALLVCTwG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635773354 233 ADGAWFKTANGEQGAVAAVKVENVVDTVGAGDGFAVGVISALLEGK-TLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01939 221 DQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPdDLSEALDFGNRVASQKCTGVG 288
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
21-299 |
6.61e-11 |
|
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: 61.78 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 21 ETGELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDsFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLKSKVEN 100
Cdd:cd01164 21 QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 101 GTDpIVEyfrkgsAASHLSVADYHA------DYFASARHLHLSG-VAAALSASSYELLdhaATTMKAQGKTLSFD---PN 170
Cdd:cd01164 100 ETE-INE------PGPEISEEELEAlleklkALLKKGDIVVLSGsLPPGVPADFYAEL---VRLAREKGARVILDtsgEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 171 LRPVLwKSEAEMVeKLNRLAFrADWVlpglkeGMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKTANGEQGAVAA 250
Cdd:cd01164 170 LLAAL-AAKPFLI-KPNREEL-EELF------GRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 635773354 251 vKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01164 241 -KVK-VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
104-275 |
7.58e-11 |
|
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: 60.57 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 104 PIVEYFRKGSAA--SHLSVADYHADYFASARHLHLSGVAAALSASSyELLDHAATtmkaQGKTLSFDPNLRPVLWKSEAe 181
Cdd:cd00287 29 GDTEERAGGGAAnvAVALARLGVSVTLVGADAVVISGLSPAPEAVL-DALEEARR----RGVPVVLDPGPRAVRLDGEE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 182 mvekLNRLAFRADWVLPGLKEGMILTGESTPE-----GIADFYLNKGVKAVVLKTGADGAWFKTANGEQGAVAAVKVEnV 256
Cdd:cd00287 103 ----LEKLLPGVDILTPNEEEAEALTGRRDLEvkeaaEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVK-V 177
|
170
....*....|....*....
gi 635773354 257 VDTVGAGDGFAVGVISALL 275
Cdd:cd00287 178 VDTTGAGDAFLAALAAGLA 196
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
31-194 |
9.35e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 62.23 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 31 FIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTG-FQLKSKVENGTDPIVEYF 109
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTAcSRMKIKFRDGGKMVAETV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 110 rKGSAASHLSVADYHADYFASARHLHLSGvAAALSASSYELLDHAATTMKAQGKTLSFDPNLRPVLWKSEAEMVEKLNRL 189
Cdd:PLN02543 247 -KEAAEDSLLASELNLAVLKEARMFHFNS-EVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKA 324
|
....*
gi 635773354 190 AFRAD 194
Cdd:PLN02543 325 WNEAD 329
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
32-296 |
1.74e-10 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 60.98 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 32 IKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGfqLKSKVENGTDPIVEYFRK 111
Cdd:COG2870 51 EEERPGGAANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTT--TKTRVIAGGQQLLRLDFE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 112 GSAASHLSVADYHADYFASArhlhLSGVAA---------ALSAssyELLDHAATTMKAQGKTLSFDPNLRpvlwkseaem 182
Cdd:COG2870 129 DRFPLSAELEARLLAALEAA----LPEVDAvilsdygkgVLTP---ELIQALIALARAAGKPVLVDPKGR---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 183 veklNRLAFR-ADWVLPGLKE-----GMILTGESTPEGIADFYLNK-GVKAVVLKTGADGAWFKTANGEQGAVAAVKVEn 255
Cdd:COG2870 192 ----DFSRYRgATLLTPNLKEaeaavGIPIADEEELVAAAAELLERlGLEALLVTRGEEGMTLFDADGPPHHLPAQARE- 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 635773354 256 VVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQ 296
Cdd:COG2870 267 VFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVG 307
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
8-310 |
5.11e-10 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 59.52 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 8 ITIGEAMAMFVATE---TGELSAVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSfGHFVLDSLKKEGIDAAGVTL 84
Cdd:TIGR03828 4 VTLNPAIDLTIELDgltLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 85 DGrfPTGFQLKSKVENG--TDpIVEYFRKGSAASHLSVADYHADYFASARHLHLSG-VAAALSASSYELLDHAAttmKAQ 161
Cdd:TIGR03828 83 PG--ETRINVKIKEPSGteTK-LNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGsLPPGVPPDFYAELIALA---REK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 162 GKTLSFD---PNLRPVLwkseaemveklnrlAFRADWVLPGLKE-----GMILTGESTPEGIADFYLNKGVKAVVLKTGA 233
Cdd:TIGR03828 157 GAKVILDtsgEALRDGL--------------KAKPFLIKPNDEEleelfGRELKTLEEIIEAARELLDLGAENVLISLGA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 635773354 234 DGAWFKTANGEQGAVAAvKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAiqVQGDSEGLPTRAQL 310
Cdd:TIGR03828 223 DGALLVTKEGALFAQPP-KGE-VVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAA--AFSEGTGLPDPEDI 295
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
37-295 |
6.96e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 56.15 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 37 GAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGFQLkSKVENGTDPIVEyFRKGSAAS 116
Cdd:PRK09850 41 GVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYL-SLLDNTGEMLVA-INDMNISN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 117 HLSvADY---HADYFASARHLhlsgVA-AALSASSYE-LLDHAattmkaqGKTLSFdpnLRPV-LWKSeAEMVEKLNRL- 189
Cdd:PRK09850 119 AIT-AEYlaqHREFIQRAKVI----VAdCNISEEALAwILDNA-------ANVPVF---VDPVsAWKC-VKVRDRLNQIh 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 190 AFRADWVLPGLKEGMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKTANGEQGAVAAVKVeNVVDTVGAGDGFAVG 269
Cdd:PRK09850 183 TLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPIKT-NVINVTGAGDAMMAG 261
|
250 260
....*....|....*....|....*.
gi 635773354 270 VISALLEGKTLPQAVARGNKIGSLAI 295
Cdd:PRK09850 262 LASCWVDGMPFAESVRFAQGCSSMAL 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
33-299 |
5.46e-08 |
|
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: 53.33 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 33 KRVAGAeLNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRfPTGFqlKSKV-------------- 98
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGR-PTTT--KTRViarnqqllrvdred 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 99 -----ENGTDPIVEYFRKgsaashlSVADYHA----DY---FASARHLHlsgvaaalsassyELLDHAattmKAQGKTLS 166
Cdd:cd01172 113 dsplsAEEEQRLIERIAE-------RLPEADVvilsDYgkgVLTPRVIE-------------ALIAAA----RELGIPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 167 FDPN------------LRPvlwkSEAEMVEKLNRLAFRADWVLPGLKEGMILTgestpegiadfylnkGVKAVVLKTGAD 234
Cdd:cd01172 169 VDPKgrdyskyrgatlLTP----NEKEAREALGDEINDDDELEAAGEKLLELL---------------NLEALLVTLGEE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635773354 235 GAWFKTANGEQGAVAAVKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:cd01172 230 GMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
126-296 |
3.52e-07 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 50.54 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 126 DYFASARHLHLSGVAAALSASSYELLDH----AATTMKaqgktlsfdpnlrpvLWKSEAEmvEKLNRLAFRADWVLPGLK 201
Cdd:cd01946 110 EHYKDSEFVFLGNIAPELQREVLEQVKDpklvVMDTMN---------------FWISIKP--EKLKKVLAKVDVVIINDG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 202 EGMILTGESTPEGIADFYLNKGVKAVVLKTGADGAWFKTANGeQGAVAAVKVENVVDTVGAGDGFAVGVISALLEGKTLP 281
Cdd:cd01946 173 EARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDG-YFAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDTS 251
|
170 180
....*....|....*....|
gi 635773354 282 -----QAVARGNKIGSLAIQ 296
Cdd:cd01946 252 eanmrRAIIYGSAMASFCVE 271
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
227-306 |
4.63e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 47.49 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 227 VVLKTGADGAWFKTANGEQGAVAAVKVEnvVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAI-QVqgdseGLP 305
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQ--VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVeQV-----GIP 278
|
.
gi 635773354 306 T 306
Cdd:PLN02630 279 K 279
|
|
| PLN02967 |
PLN02967 |
kinase |
27-181 |
5.20e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 47.73 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 27 AVEHFIKRVAGAELNVATGLARLGLNVGWVSRVGDDSFGHFVLDSLKKEGIDAAGVTLDGRFPTGF-QLKSKVENGTDPI 105
Cdd:PLN02967 234 APEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVsTMKIAKRGRLKTT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 106 VEyfrKGSAASHLSVADYHADYFASARHLHLsgvaaalsaSSYELLDH--AATTMKA------QGKTLSFDPNLRPVLWK 177
Cdd:PLN02967 314 CV---KPCAEDSLSKSEINIDVLKEAKMFYF---------NTHSLLDPtmRSTTLRAikiskkLGGVIFYDLNLPLPLWS 381
|
....
gi 635773354 178 SEAE 181
Cdd:PLN02967 382 SSEE 385
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
247-299 |
4.60e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 44.32 E-value: 4.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 635773354 247 AVAAVKVENVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:PLN02548 270 PVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSG 322
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
248-299 |
3.63e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 41.55 E-value: 3.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 635773354 248 VAAVKVENVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQVQG 299
Cdd:PTZ00247 282 VPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNG 333
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
227-306 |
4.53e-04 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 41.17 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 227 VVLKTGADGAWFKTAN-GEQGAVAAV--KVENVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAI-QVqgdse 302
Cdd:cd01943 228 VVLRCGKLGCYVGSADsGPELWLPAYhtKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIeQV----- 302
|
....
gi 635773354 303 GLPT 306
Cdd:cd01943 303 GLPR 306
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
209-280 |
8.53e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 40.54 E-value: 8.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635773354 209 ESTPEGIADFyLNKGVKAVVLKTGADGAWFKTANgEQGAVAAVKVENVVDTVGAGDGFAVGVISALLEGKTL 280
Cdd:PLN02379 252 ESDPEAALEF-LAKYCNWAVVTLGSKGCIARHGK-EVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
221-310 |
2.38e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 38.91 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 221 NKGVKAVVLKTGADGAWFKTANGEQGAVAAvKVEnVVDTVGAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAiqVQGD 300
Cdd:PRK09513 214 EQGIAHVVISLGAEGALWVNASGEWIAKPP-ACD-VVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALA--VSQS 289
|
90
....*....|
gi 635773354 301 SEGLPTRAQL 310
Cdd:PRK09513 290 NVGITDRPQL 299
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
181-296 |
3.25e-03 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 38.36 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773354 181 EMVEKLNRLAFRADWVLPGLKEGMILTGESTPEGIADF-----YL----NKGVKAVVLkTGAdgawfkTANGEQGAVAAV 251
Cdd:PRK07105 126 EMVEEMRKLIQKADVITPNLTEACLLLDKPYLEKSYSEeeikqLLrklaDLGPKIVII-TSV------PFEDGKIGVAYY 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 635773354 252 -KVENVVDTV----------GAGDGFAVGVISALLEGKTLPQAVARGNKIGSLAIQ 296
Cdd:PRK07105 199 dRATDRFWKVfckyipahypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIR 254
|
|
| |
