|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
4-309 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 540.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 4 TAGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNI 83
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 84 DVAPVRAVAGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTS 163
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 164 VILNPAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPG 243
Cdd:PRK11142 161 VILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802715819 244 FKVQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQPSVPWRKEIDEFLRQQ 309
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
7-298 |
1.24e-129 |
|
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: 370.73 E-value: 1.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 PVRAVAGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVIL 166
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 167 NPAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKV 246
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1802715819 247 QAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQPSVPW 298
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
12-303 |
7.84e-124 |
|
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: 356.14 E-value: 7.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 12 GSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAV 91
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 92 AGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVILNPAPA 171
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 172 RE-LPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVD 250
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1802715819 251 TIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQPSVPWRKEID 303
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
7-302 |
3.54e-88 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 265.59 E-value: 3.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 PVRAVAGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAekERIAGAQALLMQL-----ESPLESVLAAAKIAHQNQ 161
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 162 TSVILNPA-------PARELPDELLTLVDIITPNETEAEKLTGvrvesDDDAAKAAKVLHDKGIGTVIITLGSRGVWASS 234
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802715819 235 EGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQPSVPWRKEI 302
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-302 |
4.31e-70 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 220.38 E-value: 4.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 2 MKTAGK-LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLES 80
Cdd:PTZ00292 11 GGEAEPdVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 81 DNIDVAPVRAVAGESTGVALIFVNAE-GENTIGIHAGANAALSVAQVDAEKERI-AGAQALLMQLESPLESVLAAAKIAH 158
Cdd:PTZ00292 91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 159 QNQTSVILNPAPARELPD-----ELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWAS 233
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 234 SEGEG-RRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQPSVPWRKEI 302
Cdd:PTZ00292 251 EKENEpVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-293 |
6.40e-70 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 218.75 E-value: 6.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPtpGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 PVRAVAGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAEKERIAGAQAL----LMQLESPLESVLAAAKIAHQNQT 162
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 163 S--VILNPA-PARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGR 239
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1802715819 240 RVPGF-KVQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQ 293
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
7-274 |
5.04e-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: 154.66 E-value: 5.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHIlnldaFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:cd01166 1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 PVRAVAGESTGVALIFVNAEGENTIgIHAGANAALSVAQVDAEKER-IAGAQAL------LMQLESPLESVLAAAKIAHQ 159
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRV-LYYRAGSAASRLTPEDLDEAaLAGADHLhlsgitLALSESAREALLEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 160 NQTSVIL---------NPAPARELPDELLTLVDIITPNETEAEKLTGVrvESDDDAAKAAKvLHDKGIGTVIITLGSRGV 230
Cdd:cd01166 155 RGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGD--EDPTDAAERAL-ALALGVKAVVVKLGAEGA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1802715819 231 WASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:cd01166 232 LVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEE 275
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
8-293 |
5.78e-38 |
|
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: 135.90 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 8 LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAP 87
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 88 VRAVAGESTGVALIFVNAEGENTIGIHAGANAALSVaqvDAEKERIAGAQALLMQLESPLEsvlAAAKIAHQNQTSVILN 167
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEP---NDEADPDGLADIVHLSSGPGLI---ELARELAAGGITVSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 168 PAPA-----RELPDELLTLVDIITPNETEAEKLtgVRVESDDDAAKAAKVlhdkgiGTVIITLGSRGVWASSEGEGRRVP 242
Cdd:cd01942 156 PGQElprlsGEELEEILERADILFVNDYEAELL--KERTGLSEAELASGV------RVVVVTLGPKGAIVFEDGEEVEVP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1802715819 243 GFK-VQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKGAQ 293
Cdd:cd01942 228 AVPaVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
42-273 |
3.74e-35 |
|
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: 128.91 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 42 GGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGESTGVALIFVNAEGENTIGIHAGAnAAL 121
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGP-AAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 122 SVAQVDAEKERIAGAQAL----LMQLESPL-ESVLAAAKIAHQNQTSVIL----------NPAPARELPDELLTLVDIIT 186
Cdd:cd01167 107 LLLDTELNPDLLSEADILhfgsIALASEPSrSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERIAELLELADIVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 187 PNETEAEKLTGvrvesDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTAL 266
Cdd:cd01167 187 LSDEELELLFG-----EEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261
|
....*..
gi 1802715819 267 LEGSELA 273
Cdd:cd01167 262 LSRGLLA 268
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
42-274 |
2.64e-34 |
|
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: 126.96 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 42 GGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRaVAGESTGVALIFVNAEGENTIGIHAGANAAL 121
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 122 SVAQVDAEKerIAGAQALLM---QLESPLESVLAAAKIAHQNQTSVILN------PAPARELPDELLTLVDIITPNETEA 192
Cdd:cd01168 134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 193 EKLTGVRVESDDDAAKAAKVLHDKgigTVIITLGSRGVWASSEGEGRRVPGFK-VQAVDTIAAGDTFNGALVTALLEGSE 271
Cdd:cd01168 212 EALAEAETTDDLEAALKLLALRCR---IVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP 288
|
...
gi 1802715819 272 LAQ 274
Cdd:cd01168 289 LEE 291
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
11-274 |
3.21e-33 |
|
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: 123.56 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 11 LGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRA 90
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 91 VAGESTGVALIFVNAEGENTIGIHAGANAALSVAQVDAEkerIAGAQALLMQLESPlESVLAAAKIAHQNQTSVILNPAP 170
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIDTQAAPDSLPDAI---LGGADAVLVDGRQP-EAALHLAQEARARGIPIPLDLDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 171 ARELP-DELLTLVDIITPNETEAEKLTGVrveSDDDAAKAakvLHDKGIGTVIITLGSRGV-WASSEGEGRRVPGFKVQA 248
Cdd:cd01945 161 GGLRVlEELLPLADHAICSENFLRPNTGS---ADDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVEV 234
|
250 260
....*....|....*....|....*.
gi 1802715819 249 VDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:cd01945 235 VDTTGAGDVFHGAFAHALAEGMPLRE 260
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
7-274 |
1.51e-32 |
|
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: 121.65 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQvAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 PVRaVAGESTGVALIFVNAEGENTIGI-HAGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVI 165
Cdd:cd01941 80 GIV-FEGRSTASYTAILDKDGDLVVALaDMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 166 LNPAPARELPD--ELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASS---EGEGRR 240
Cdd:cd01941 159 FEPTSAPKLKKlfYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSregGVETKL 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1802715819 241 VPGFKVQAV-DTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:cd01941 239 FPAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDD 273
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
7-267 |
2.94e-31 |
|
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: 115.66 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIactgdddigervrrqlesdnidva 86
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 pvravagestGVALIFVNAEGentigihaganaalsvaqvdaekeriagaqallmqleSPLESVLAAAKIAHQNQTSVIL 166
Cdd:cd00287 57 ----------GADAVVISGLS-------------------------------------PAPEAVLDALEEARRRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 167 NPAPARELPD-----ELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGR-R 240
Cdd:cd00287 90 DPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEvH 169
|
250 260
....*....|....*....|....*..
gi 1802715819 241 VPGFKVQAVDTIAAGDTFNGALVTALL 267
Cdd:cd00287 170 VPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
7-291 |
1.07e-25 |
|
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: 103.27 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGkGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVA 86
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 -PVRAvaGESTGVALIFVNAEGENTIGIHAGANAALS---VAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQT 162
Cdd:cd01944 80 lPPRG--GDDGGCLVALVEPDGERSFISISGAEQDWStewFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 163 SVILNPAPA-RELPDELLTLV----DIITPNETEAEKLTGvrvESDDDAAKAAKVLHDKGIGTVIITLGSRGVWA-SSEG 236
Cdd:cd01944 158 TLVFDPGPRiSDIPDTILQALmakrPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIrLPDG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1802715819 237 EGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQAIRFAHAAAAIAVTRKG 291
Cdd:cd01944 235 NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
17-274 |
4.18e-23 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 96.74 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGA-NIAFIACTGDDdiGERVRRQLESDNIDVAPVRaVAGEs 95
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVdVTALGFLGGFT--GEFIEELLDEEGIPTDFVP-IEGE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 96 TGVALIFVNAEGENTIGIHaGANAALSVAQVDAEKERIAgaqallmQLESPLESVLAA---------------AKIAHQN 160
Cdd:COG1105 86 TRINIKIVDPSDGTETEIN-EPGPEISEEELEALLERLE-------ELLKEGDWVVLSgslppgvppdfyaelIRLARAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 161 QTSVIL--NPAPARELPDELltlVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEG 238
Cdd:COG1105 158 GAKVVLdtSGEALKAALEAG---PDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGV 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1802715819 239 RRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:COG1105 235 YRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
40-309 |
2.35e-17 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 81.21 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 40 AFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGESTGVALIFVNAEGENTIGI--HAGA 117
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFyrNPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 118 NAALSVAQVDAEKERIA-----GAQALLmqlESPLESV-LAAAKIAhqNQTSVILNPAPARELP---------DELLTL- 181
Cdd:PLN02323 121 DMLLRESELDLDLIRKAkifhyGSISLI---TEPCRSAhLAAMKIA--KEAGALLSYDPNLRLPlwpsaeaarEGIMSIw 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 182 --VDIITPNETEAEKLTGVRVESDDDAAKaakVLHDKgIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFN 259
Cdd:PLN02323 196 deADIIKVSDEEVEFLTGGDDPDDDTVVK---LWHPN-LKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFV 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1802715819 260 GALVT------ALLEGSE-LAQAIRFAHAAAAIAVTRKGAQPSVPWRKEIDEFLRQQ 309
Cdd:PLN02323 272 GGLLSqlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLKLLKKA 328
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
7-269 |
6.41e-17 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 79.00 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVa 86
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 87 pVRAVAGESTGVALIFVNAEGENTIGIHAGANAAlsvaqvDAEKERIAGAQALLMQLESPLESVLAAAKiahqNQTSVIL 166
Cdd:cd01947 80 -TVAWRDKPTRKTLSFIDPNGERTITVPGERLED------DLKWPILDEGDGVFITAAAVDKEAIRKCR----ETKLVIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 167 NPAP--ARELPDELLTLVDIITPNETEAekltGVRVESDDDAAKAAKVLhdkgigtvIITLGSRGVWASSEGEGRRVPGF 244
Cdd:cd01947 149 QVTPrvRVDELNQALIPLDILIGSRLDP----GELVVAEKIAGPFPRYL--------IVTEGELGAILYPGGRYNHVPAK 216
|
250 260
....*....|....*....|....*
gi 1802715819 245 KVQAVDTIAAGDTFNGALVTALLEG 269
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKG 241
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
17-274 |
6.65e-17 |
|
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: 79.11 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDdIGERVRRQLESDNIDVAPVRaVAGES- 95
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-VAGETr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 96 TGVALIfvnaEGENTIGIHAGANAALSVAQVDAEKERIAgaqallmQLESPLESVLAA---------------AKIAHQN 160
Cdd:cd01164 89 INVKIK----EEDGTETEINEPGPEISEEELEALLEKLK-------ALLKKGDIVVLSgslppgvpadfyaelVRLAREK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 161 QTSVIL--NPAPARELpdeLLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEG 238
Cdd:cd01164 158 GARVILdtSGEALLAA---LAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGV 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1802715819 239 RRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:cd01164 235 YRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
42-303 |
8.94e-17 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 79.21 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 42 GGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGESTGVALIFVNAEGEN--TIGIHAGANA 119
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 120 ALSVAQVDAEKER-------IAgaqalLMQLESPLESVLAAAKIAHQN---------QTSVILNPAPARELPDELLTLVD 183
Cdd:PRK09434 108 FLQPQDLPPFRQGewlhlcsIA-----LSAEPSRSTTFEAMRRIKAAGgfvsfdpnlREDLWQDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 184 IITPNETEAEKLTGvrveSDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFNGALV 263
Cdd:PRK09434 183 VVKLSEEELCFLSG----TSQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1802715819 264 TALLEGS------ELAQAIRFAHAAAAIAVTRKGAQPSVPWRKEID 303
Cdd:PRK09434 259 AGLSQAGlwtdeaELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
2-269 |
1.61e-16 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 78.49 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 2 MKTAGKLVVLGSINAD------HILNLdAFPTPGetvtghhyQVAF--GGKGANQAVAAGRSGANIAFIACTGDDDIGER 73
Cdd:PRK09850 1 MREKDYVVIIGSANIDvagyshESLNY-ADSNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 74 VRRQLESDNIDVAPVRAVAGESTGVALIFVNAEGENTIGIH-AGANAALSVAQVDAEKERIAGAQALLMQL---ESPLES 149
Cdd:PRK09850 72 LLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 150 VLAAAkiahqNQTSVILNPAPARELPD--ELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGS 227
Cdd:PRK09850 152 ILDNA-----ANVPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1802715819 228 RGVWASS-EGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEG 269
Cdd:PRK09850 227 DGVYYSDiSGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
35-271 |
1.41e-14 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 72.39 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 35 HHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGEsTGVALIFVnaEGENTIGIH 114
Cdd:cd01940 15 HLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVEL--VDGDRIFGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 115 AGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVILNPApARELPDELLTLVDIITPNETEAEK 194
Cdd:cd01940 92 SNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFS-DRWDDDYLQLVCPYVDFAFFSASD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802715819 195 ltgvrvESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSE 271
Cdd:cd01940 171 ------LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGT 241
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
176-274 |
2.47e-14 |
|
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: 71.46 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 176 DELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIIT------LGSRGVWASSEGEGRRVPGFKVQAV 249
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFP 210
|
90 100
....*....|....*....|....*.
gi 1802715819 250 DTIA-AGDTFNGALVTALLEGSELAQ 274
Cdd:cd01173 211 AYFNgTGDLFAALLLARLLKGKSLAE 236
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
43-263 |
2.89e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 72.94 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 43 GKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVapVRAVAGESTGVA--------LIFVNAEGentIGIH 114
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDSssasyetlLCWVLVDP---LQRH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 115 A-------GANAALS-VAQVDAE-KERIAGAQALLMQL----ESPLESVLAAAKIAHQNQTSVILNPAP-----ARELPD 176
Cdd:PLN02341 195 GfcsradfGPEPAFSwISKLSAEaKMAIRQSKALFCNGyvfdELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 177 E------LLTLVDIITPNETEAEKLTGVRvesddDAAKAAKVLHDKGIGT--VIITLGSRGVWASSEGEGRRVPGFKVQA 248
Cdd:PLN02341 275 ErralehLLRMSDVLLLTSEEAEALTGIR-----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
|
250
....*....|....*
gi 1802715819 249 VDTIAAGDTFNGALV 263
Cdd:PLN02341 350 VDTVGCGDSFAAAIA 364
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
177-224 |
4.88e-13 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 68.18 E-value: 4.88e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1802715819 177 ELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIIT 224
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
30-269 |
4.92e-13 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 69.07 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 30 ETVTGHHYQVAFGGKGANQAVAAGRSGA--------NIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGeSTGVALI 101
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDG-TTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 102 FVNAEGENTIGIHAGANAALSVAQVDAE---KERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVILNPAP----AREL 174
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASaisKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDvsciERHR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 175 PDELLTL---VDIITPNETEAEKLTGVrvESDDDAAKAAKVLhDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDT 251
Cdd:PLN02813 273 DDFWDVMgnyADILFANSDEARALCGL--GSEESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDT 349
|
250
....*....|....*...
gi 1802715819 252 IAAGDTFNGALVTALLEG 269
Cdd:PLN02813 350 CGAGDAYAAGILYGLLRG 367
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
56-274 |
1.85e-12 |
|
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: 66.43 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 56 GANIAFIACTGDDDIGERVRRQLESDNIDVAPVRaVAGESTGVALIFVnAEGENTIGI----HAGANAALSVAQVDAEKE 131
Cdd:cd01172 53 GAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTTTKTRVI-ARNQQLLRVdredDSPLSAEEEQRLIERIAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 132 RIAGAQALL-------MQLESPLESVLAAAKIAHQNqtsVILNPapaRELPDELLTLVDIITPNETEAEKLTGVRVESDD 204
Cdd:cd01172 131 RLPEADVVIlsdygkgVLTPRVIEALIAAARELGIP---VLVDP---KGRDYSKYRGATLLTPNEKEAREALGDEINDDD 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802715819 205 DAAKAA-KVLHDKGIGTVIITLGSRGV-WASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:cd01172 205 ELEAAGeKLLELLNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEE 276
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
10-272 |
3.31e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 66.35 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 10 VLGSINAdHILNLDAFPTPGETVTGhhyqvafgGKGAN--QAVAAGrSGANIAFIACTGDDDIGERVRRQLESDNIDVAP 87
Cdd:PLN02379 63 ILREVNA-HILPSPDDLSPIKTMAG--------GSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 88 VRAVAGeSTGVALIFVNAEGENTIgihagANAALSVAQVDAE---KERIAGAQALLMQLE-SPLESVLAAAKIAHQNQTS 163
Cdd:PLN02379 133 LRAKKG-PTAQCVCLVDALGNRTM-----RPCLSSAVKLQADeltKEDFKGSKWLVLRYGfYNLEVIEAAIRLAKQEGLS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 164 VILNPAP---ARELPDELLTL-----VDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKgigTVIITLGSRGVWASSE 235
Cdd:PLN02379 207 VSLDLASfemVRNFRSPLLQLlesgkIDLCFANEDEARELLRGEQESDPEAALEFLAKYCN---WAVVTLGSKGCIARHG 283
|
250 260 270
....*....|....*....|....*....|....*...
gi 1802715819 236 GEGRRVPGFK-VQAVDTIAAGDTFNGALVTALLEGSEL 272
Cdd:PLN02379 284 KEVVRVPAIGeTNAVDATGAGDLFASGFLYGLIKGLSL 321
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
176-269 |
9.34e-12 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 64.38 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 176 DELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIIT----------LGSrgvwaSSEGEGRRVPGFK 245
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITsididgklllVGS-----HRKEKGARPEQFK 218
|
90 100
....*....|....*....|....
gi 1802715819 246 VqAVDTIAAGDTFNGALVTALLEG 269
Cdd:PLN02978 219 I-VIPKIPAYFTGTGDLMAALLLG 241
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
176-274 |
2.45e-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: 62.86 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 176 DELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITlgsrGVWASSEGEGR--------------RV 241
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT----SVPLDDTPADKignlavtadgawlvET 208
|
90 100 110
....*....|....*....|....*....|...
gi 1802715819 242 PGFKVQAVDTiaaGDTFNGALVTALLEGSELAQ 274
Cdd:COG2240 209 PLLPFSPNGT---GDLFAALLLAHLLRGKSLEE 238
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
163-272 |
4.23e-10 |
|
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: 59.03 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 163 SVILNPAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITlGSRGVWASS-------- 234
Cdd:pfam08543 101 DSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK-GGHLEGEEAvvtdvlyd 179
|
90 100 110
....*....|....*....|....*....|....*...
gi 1802715819 235 EGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSEL 272
Cdd:pfam08543 180 GGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSL 217
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
59-273 |
6.17e-10 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 59.27 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 59 IAFIACTGDDDIGERVRRQLESDNIDV-------APVRAVAG-----ESTGVALIfvnaegentigihaGANAALSVAQV 126
Cdd:PTZ00247 83 VCYVGCVGDDRFAEILKEAAEKDGVEMlfeyttkAPTGTCAVlvcgkERSLVANL--------------GAANHLSAEHM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 127 DAEKERIAGAQALLMQLE------SPlESVLAAAKIAHQN--QTSVILNpAP----ARELP-DELLTLVDIITPNETEAE 193
Cdd:PTZ00247 149 QSHAVQEAIKTAQLYYLEgffltvSP-NNVLQVAKHARESgkLFCLNLS-APfisqFFFERlLQVLPYVDILFGNEEEAK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 194 KL-TGVRVESDD---DAAKAAKVLhdKGIGT----VIITLGSRGVWASSEGEGRRVPGFKVQA---VDTIAAGDTFNGAL 262
Cdd:PTZ00247 227 TFaKAMKWDTEDlkeIAARIAMLP--KYSGTrprlVVFTQGPEPTLIATKDGVTSVPVPPLDQekiVDTNGAGDAFVGGF 304
|
250
....*....|.
gi 1802715819 263 VTALLEGSELA 273
Cdd:PTZ00247 305 LAQYANGKDID 315
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
183-274 |
6.44e-10 |
|
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: 59.07 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 183 DIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIIT-LGSRGVWASSEGEGRRVPG------------FKVQAV 249
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQRDRSFEGLVATQegrwhisrplavFDPPPV 219
|
90 100
....*....|....*....|....*
gi 1802715819 250 DTiaaGDTFNGALVTALLEGSELAQ 274
Cdd:TIGR00687 220 GT---GDLIAALLLATLLHGNSLKE 241
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
176-274 |
2.97e-09 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 56.59 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 176 DELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRG------VWASSEGEgRRVPGFKVQAV 249
Cdd:COG0351 121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPgdeavdVLYDGDGV-REFSAPRIDTG 199
|
90 100
....*....|....*....|....*
gi 1802715819 250 DTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:COG0351 200 NTHGTGCTLSSAIAALLAKGLDLEE 224
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
173-228 |
7.99e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 55.45 E-value: 7.99e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1802715819 173 ELPDELLTL---VDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSR 228
Cdd:PRK12413 118 ELRQELIQFfpyVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR 176
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
9-280 |
2.33e-08 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 54.55 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 9 VVLGSINADhILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPV 88
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 89 RAVAGESTGVALIFVNAEGENTIGIH-AGANAALSVAQVDAEKERIAGAQALLMQLESPLESVLAAAKIAHQNQTSVILN 167
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLADEIPVFVDTV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 168 PAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASS-EGEGRRVPGFKV 246
Cdd:PRK09954 220 SEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEkDGEQFLLTAPAH 299
|
250 260 270
....*....|....*....|....*....|....
gi 1802715819 247 QAVDTIAAGDTFNGALVTALLEGSELAQAIRFAH 280
Cdd:PRK09954 300 TTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAM 333
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
174-267 |
6.75e-08 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 52.82 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 174 LPDELLTLVDIITPNETEAEKLTGVRVESDDDAAK-AAKVLHDKGIGTVIITLG-------SRGVWASSEGEGRrvpgFK 245
Cdd:PRK06427 126 LRERLLPLATLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhlldgeeSVDWLFDGEGEER----FS 201
|
90 100
....*....|....*....|....*
gi 1802715819 246 VQAVDTIA---AGDTFNGALvTALL 267
Cdd:PRK06427 202 APRIPTKNthgTGCTLSAAI-AAEL 225
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
42-274 |
1.92e-07 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 51.28 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 42 GGKGANQAVAAGRSGANIAFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGESTGVALIFVNAE---GENTIGIHAGan 118
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELHDNDrvfGDYTEGVMAD-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 119 aalsVAQVDAEKERIAGAQALLMQLESPLESVLAAAKiAHQNQTSVILNPAPARELPDELLTLVDIitpneteaekltGV 198
Cdd:PRK09813 101 ----FALSEEDYAWLAQYDIVHAAIWGHAEDAFPQLH-AAGKLTAFDFSDKWDSPLWQTLVPHLDY------------AF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802715819 199 RVESDDDA--AKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:PRK09813 164 ASAPQEDEflRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQ 241
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
165-226 |
7.58e-07 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 50.11 E-value: 7.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802715819 165 ILNPAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLG 226
Cdd:PRK08573 114 LLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEELGAEAVVVKG 175
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
164-224 |
7.89e-07 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 49.48 E-value: 7.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802715819 164 VILNPAPARELPDELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIIT 224
Cdd:PRK05756 121 CIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
184-296 |
1.88e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 48.54 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 184 IITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRG-VWASSEGEGRRVPGfKVQAVDTIAAGDTFNGAL 262
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGaLWVNASGEWIAKPP-ACDVVSTVGAGDSMVGGL 261
|
90 100 110
....*....|....*....|....*....|....
gi 1802715819 263 VTALLEGSELAQAIRFAHAAAAIAVTrkgaQPSV 296
Cdd:PRK09513 262 IYGLLMRESSEHTLRLATAVSALAVS----QSNV 291
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
123-274 |
2.01e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 48.43 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 123 VAQVDAEKERI---AGAQALLMQLESPLESV-LAAAKIAHQNQTSVILNPAPARELPDELL----------TLVD---II 185
Cdd:PRK12412 57 ASTLKPQLETTiegVGVDALKTGMLGSVEIIeMVAETIEKHNFKNVVVDPVMVCKGADEALhpetndclrdVLVPkalVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 186 TPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSR-----GVWASSEGEGRRV-PGFKVQAVDTIAAGDTFN 259
Cdd:PRK12412 137 TPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetAIDVLYDGETFDLlESEKIDTTNTHGAGCTYS 216
|
170
....*....|....*
gi 1802715819 260 GALVTALLEGSELAQ 274
Cdd:PRK12412 217 AAITAELAKGKPVKE 231
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
177-272 |
2.31e-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: 48.17 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 177 ELLTLVDIITPNETEAEKLTgvrvesddDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGD 256
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGD 222
|
90
....*....|....*.
gi 1802715819 257 TFNGALVTALLEGSEL 272
Cdd:cd01937 223 VFLAAFLYSRLSGKDI 238
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
175-260 |
6.83e-06 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 46.69 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 175 PDEL---LTLVDIITPNETEAEKLTGvrvesDDDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGEGRRVPGFKVQAV-D 250
Cdd:cd01946 154 PEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
|
90
....*....|
gi 1802715819 251 TIAAGDTFNG 260
Cdd:cd01946 229 PTGAGDTFAG 238
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
36-274 |
2.92e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 45.09 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 36 HYQVAFGGKGANQ---AVAA---GRSGANiAFIACTGDDDIGERVRRQLESDNIDV-------AP-----VRAVAGESTG 97
Cdd:PLN02548 44 KYNVEYIAGGATQnsiRVAQwmlQIPGAT-SYMGCIGKDKFGEEMKKCATAAGVNVhyyedesTPtgtcaVLVVGGERSL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 98 VAlifvNAEGENTIGIH---AGANAALsvaqvdAEKER---IAGaqalLMQLESPlESVLAAAKIAHQNQTSVILN-PAP 170
Cdd:PLN02548 123 VA----NLSAANCYKVEhlkKPENWAL------VEKAKfyyIAG----FFLTVSP-ESIMLVAEHAAANNKTFMMNlSAP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 171 -----ARELPDELLTLVDIITPNETEAEKLTGVRVESDDD----AAKAAKVlhDKGIGT----VIITLGSRGVWASSEGE 237
Cdd:PLN02548 188 ficefFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDveeiALKISAL--PKASGThkrtVVITQGADPTVVAEDGK 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1802715819 238 GRRVPGF---KVQAVDTIAAGDTFNGALVTALLEGSELAQ 274
Cdd:PLN02548 266 VKEFPVIplpKEKLVDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
182-273 |
5.89e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 40.92 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 182 VDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGT-VIITLGSRGVWASSEGEGRRVPGFKVQAVDTIAAGDTFNG 260
Cdd:PRK10294 181 IELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKrVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVG 260
|
90
....*....|...
gi 1802715819 261 ALVTALLEGSELA 273
Cdd:PRK10294 261 AMTLKLAENASLE 273
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
164-226 |
1.03e-03 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 40.52 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802715819 164 VILNPAPARELPDELLTLVDIITPNETEAEKLTG-VRVESDDDAAKAAKVLHDKGIGTVIITLG 226
Cdd:PLN02898 121 VLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMRSAAKELHKLGPRYVLVKGG 184
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
176-273 |
1.50e-03 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 39.64 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 176 DELLTLVDIITPNETEAEKLTGVRVESDDDAAKAAKVLHDKGIGTVIITLGSRGVWASS------EGEGRRVPGFKVQAV 249
Cdd:PRK08176 147 QHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmqvvvvTADSVNVISHPRVDT 226
|
90 100
....*....|....*....|....
gi 1802715819 250 DTIAAGDTFNGALVTALLEGSELA 273
Cdd:PRK08176 227 DLKGTGDLFCAELVSGLLKGKALT 250
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
155-267 |
1.55e-03 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 39.71 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 155 KIAHQNQTSVILNPAPArELPDELLTLVD--IITPNETEAEKLTGVRVESDDDAAKAakVLHD---KGIGTVIITLGSRG 229
Cdd:PRK13508 150 ELANQAGKPVVLDCSGA-ALQAVLESPYKptVIKPNIEELSQLLGKEVSEDLDELKE--VLQQplfEGIEWIIVSLGADG 226
|
90 100 110
....*....|....*....|....*....|....*...
gi 1802715819 230 VWASSEGEGRRVPGFKVQAVDTIAAGDTFNGALVTALL 267
Cdd:PRK13508 227 AFAKHNDTFYKVDIPKIEVVNPVGSGDSTVAGIASGLL 264
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
177-269 |
4.87e-03 |
|
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: 38.09 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802715819 177 ELLTLVDIITPNETEAEKLTGVRV---ESDDDAAKAAKVLHD-----KGIGTVIITLGSRGVWASSEGEG--RRVPGF-- 244
Cdd:cd01943 176 QALPRVDVFSPNLEEAARLLGLPTsepSSDEEKEAVLQALLFsgilqDPGGGVVLRCGKLGCYVGSADSGpeLWLPAYht 255
|
90 100
....*....|....*....|....*...
gi 1802715819 245 ---KVqaVDTIAAGDTFNGALVTALLEG 269
Cdd:cd01943 256 kstKV--VDPTGGGNSFLGGFAAGLALT 281
|
|
| |
