|
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: 521.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 4 TAGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKI 83
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 84 DVAPVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTT 163
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 164 VVLNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPG 243
Cdd:PRK11142 161 VILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246818 244 FRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFLAQQ 309
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
7-298 |
6.89e-120 |
|
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: 346.07 E-value: 6.89e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVL 166
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 167 NPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRV 246
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490246818 247 QAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPW 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 |
3.57e-116 |
|
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: 336.50 E-value: 3.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 12 GSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAV 91
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 92 AGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAPA 171
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 172 RE-LPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAID 250
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490246818 251 TIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEID 303
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
7-302 |
2.13e-78 |
|
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: 240.94 E-value: 2.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAekERIASAQALLMQL-----ESPLESVIAAAKIAHHHH 161
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 162 TTVVLNPA-------PARELPDELLALVDIITPNETEAEKLTGIrvesdEDAAKAADVLHAKGIGTVMITLGSRGVWLSA 234
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246818 235 EGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 302
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-293 |
2.01e-61 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 197.18 E-value: 2.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPtpGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHT 162
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 163 T--VVLNPA-PARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESR 239
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490246818 240 RIPGFR-VQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 293
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-302 |
8.75e-61 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 196.50 E-value: 8.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 2 MKTAGK-LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLAS 80
Cdd:PTZ00292 11 GGEAEPdVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 81 DKIDVAPVRAVAGEATGVALIFVNAE-GENVIGIHAGANAALSVSQVEAEKERIAS-AQALLMQLESPLESVIAAAKIAH 158
Cdd:PTZ00292 91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 159 HHHTTVVLNPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRG-VWL 232
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGcLIV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 233 SAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 302
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
7-292 |
2.87e-35 |
|
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: 129.23 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHIlnldaFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01166 1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 PVRAVAGEATGVALIFVNAEGENVIgIHAGANAALSVSQVEAEKER-IASAQAL------LMQLESPLESVIAAAKIAHH 159
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRV-LYYRAGSAASRLTPEDLDEAaLAGADHLhlsgitLALSESAREALLEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 160 HHTTVVL---------NPAPARELPDELLALVDIITPNETEAEKLTGIrvESDEDAAKAADVLHAkGIGTVMITLGSRGV 230
Cdd:cd01166 155 RGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGD--EDPTDAAERALALAL-GVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490246818 231 WLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGA 292
Cdd:cd01166 232 LVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
8-293 |
1.31e-32 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 121.65 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 8 LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 87
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 88 VRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVsqvEAEKERIASAQALLMQLESPLEsviAAAKIAHHHHTTVVLN 167
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEP---NDEADPDGLADIVHLSSGPGLI---ELARELAAGGITVSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 168 PAPA-----RELPDELLALVDIITPNETEAE---KLTGIRVESDedaakaadvlhAKGIGTVMITLGSRGVWLSAEGESR 239
Cdd:cd01942 156 PGQElprlsGEELEEILERADILFVNDYEAEllkERTGLSEAEL-----------ASGVRVVVVTLGPKGAIVFEDGEEV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490246818 240 RIPGF-RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 293
Cdd:cd01942 225 EVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
11-274 |
7.76e-29 |
|
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: 111.62 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 11 LGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRA 90
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 91 VAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEkerIASAQALLMQLESPLESVIAAAKIAHHHHTTVV-LNPA 169
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIDTQAAPDSLPDAI---LGGADAVLVDGRQPEAALHLAQEARARGIPIPLdLDGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 170 PARELpDELLALVDIITPNETEAEKLTGIrveSDEDAAKAadvLHAKGIGTVMITLGSRGV-WLSAEGESRRIPGFRVQA 248
Cdd:cd01945 162 GLRVL-EELLPLADHAICSENFLRPNTGS---ADDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVEV 234
|
250 260
....*....|....*....|....*.
gi 490246818 249 IDTIAAGDTFNGALVTALLEGTALPE 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 |
1.12e-28 |
|
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: 111.25 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQvAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 PVRaVAGEATGVALIFVNAEGENVIGI-HAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVV 165
Cdd:cd01941 80 GIV-FEGRSTASYTAILDKDGDLVVALaDMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 166 LNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLS---AEGESRR 240
Cdd:cd01941 159 FEPTSAPKLKKlfYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSsreGGVETKL 238
|
250 260 270
....*....|....*....|....*....|....*
gi 490246818 241 IPGFRVQAI-DTIAAGDTFNGALVTALLEGTALPE 274
Cdd:cd01941 239 FPAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDD 273
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
42-272 |
2.37e-28 |
|
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: 110.80 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGAnAAL 121
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGP-AAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 122 SVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLALVDIIT 186
Cdd:cd01167 107 LLLDTELNPDLLSEADILhfgsIALASEPSRSALLELLEAAKKAGVLISfdpnlrpplwrDEEEARERIAELLELADIVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 187 PNETEAEKLTGIrvesdEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTAL 266
Cdd:cd01167 187 LSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261
|
....*.
gi 490246818 267 LEGTAL 272
Cdd:cd01167 262 LSRGLL 267
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
7-267 |
1.13e-25 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 101.02 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIActgdddigerirrqlasdkidva 86
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 pvravageatgvalifvnaegenVIGIHAGANAALSVSQVEAEKERIasaqallmqlesplesviaaakiahHHHTTVVL 166
Cdd:cd00287 58 -----------------------ADAVVISGLSPAPEAVLDALEEAR-------------------------RRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 167 NPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESR-R 240
Cdd:cd00287 90 DPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEvH 169
|
250 260
....*....|....*....|....*..
gi 490246818 241 IPGFRVQAIDTIAAGDTFNGALVTALL 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 |
3.55e-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: 102.12 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGkGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 86
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 -PVRAvaGEATGVALIFVNAEGE----NVIGIHAGANAA-LSVSQVEAEKERIASAQallmQLESPLESVIA--AAKIAH 158
Cdd:cd01944 80 lPPRG--GDDGGCLVALVEPDGErsfiSISGAEQDWSTEwFATLTVAPYDYVYLSGY----TLASENASKVIllEWLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 159 HHHTTVVLNPAPA-RELPD----ELLALVDIITPNETEAEKLTGirvESDEDAAKAADVLHAKGIGTVMITLGSRGVWL- 232
Cdd:cd01944 154 PAGTTLVFDPGPRiSDIPDtilqALMAKRPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIr 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490246818 233 SAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKG 291
Cdd:cd01944 231 LPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
42-274 |
2.66e-22 |
|
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: 94.60 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRaVAGEATGVALIFVNAEGENVIGIHAGANAAL 121
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 122 SVSQVEAEKerIASAQALLM---QLESPLESVIAAAKIAHHHHTTVVLN------PAPARELPDELLALVDIITPNETEA 192
Cdd:cd01168 134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 193 EKLTGIRVESDEDAAKAadvLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFR-VQAIDTIAAGDTFNGALVTALLEGTA 271
Cdd:cd01168 212 EALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP 288
|
...
gi 490246818 272 LPE 274
Cdd:cd01168 289 LEE 291
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
17-274 |
4.74e-18 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 82.49 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGAD-IAFIACTGDDdiGERIRRQLASDKIDVAPVRaVAGEa 95
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDvTALGFLGGFT--GEFIEELLDEEGIPTDFVP-IEGE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 96 TGVALIFVNAEGENVIGIHaGANAALSVSQVEAEKERIASAqallmqlesplesviaaakiaHHHHTTVVLNPAPARELP 175
Cdd:COG1105 86 TRINIKIVDPSDGTETEIN-EPGPEISEEELEALLERLEEL---------------------LKEGDWVVLSGSLPPGVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 227
Cdd:COG1105 144 PDFYaelirlarargakvvldtsgealkaaleAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490246818 228 RGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:COG1105 224 DGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
177-224 |
3.27e-14 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 71.65 E-value: 3.27e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490246818 177 ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT 224
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
2-269 |
1.41e-13 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 70.02 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 2 MKTAGKLVVLGSINAD------HILNLdAFPTPGetvtghhyQVAF--GGKGANQAVAAGRSGADIAFIACTGDDDIGER 73
Cdd:PRK09850 1 MREKDYVVIIGSANIDvagyshESLNY-ADSNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 74 IRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQL---ESPLES 149
Cdd:PRK09850 72 LLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 150 VIAAAKIahhhhTTVVLNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 227
Cdd:PRK09850 152 ILDNAAN-----VPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490246818 228 RGVWLS-AEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK09850 227 DGVYYSdISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
176-274 |
2.24e-13 |
|
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: 68.77 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITlgsrGVWLSAEGE-----SRRIPGFRVQ--A 248
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT----SVELADDDRiemlgSTATEAWLVQrpK 206
|
90 100 110
....*....|....*....|....*....|
gi 490246818 249 IDTIA----AGDTFNGALVTALLEGTALPE 274
Cdd:cd01173 207 IPFPAyfngTGDLFAALLLARLLKGKSLAE 236
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
42-303 |
3.76e-13 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 68.42 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGEN--VIGIHAGANA 119
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 120 ALSVSQVEAEKER-------IASAQallmqleSPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLAL 181
Cdd:PRK09434 108 FLQPQDLPPFRQGewlhlcsIALSA-------EPSRSTTFEAMRRIKAAGGFVSfdpnlredlwqDEAELRECLRQALAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 182 VDIITPNETEAEKLTGirvESDEDAAKAAdVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGA 261
Cdd:PRK09434 181 ADVVKLSEEELCFLSG---TSQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490246818 262 LVTALLEGTALPEAIRFAHAAAAI------AVTRKGAQPSVPWRTEID 303
Cdd:PRK09434 257 LLAGLSQAGLWTDEAELAEIIAQAqacgalATTAKGAMTALPNRQELE 304
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
176-269 |
7.63e-13 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 67.84 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQ----AIDT 251
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEqfkiVIPK 223
|
90
....*....|....*...
gi 490246818 252 IAAGDTFNGALVTALLEG 269
Cdd:PLN02978 224 IPAYFTGTGDLMAALLLG 241
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
7-269 |
7.96e-13 |
|
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: 67.06 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 7 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVa 86
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 87 pVRAVAGEATGVALIFVNAEGENVIGIHAGanaalsvsQVEAEKERIASAQALLMQLESplESVIAAAKIAHHHHTTVVL 166
Cdd:cd01947 80 -TVAWRDKPTRKTLSFIDPNGERTITVPGE--------RLEDDLKWPILDEGDGVFITA--AAVDKEAIRKCRETKLVIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 167 NPAP--ARELPDELLALVDIITPNETEAEKLTgirvesdedaakAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGF 244
Cdd:cd01947 149 QVTPrvRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
|
250 260
....*....|....*....|....*
gi 490246818 245 RVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKG 241
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
176-274 |
8.35e-13 |
|
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: 67.10 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----------------LGSRGVWLSaegESR 239
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpadkignlaVTADGAWLV---ETP 209
|
90 100 110
....*....|....*....|....*....|....*
gi 490246818 240 RIPGFRVqaidtiAAGDTFNGALVTALLEGTALPE 274
Cdd:COG2240 210 LLPFSPN------GTGDLFAALLLAHLLRGKSLEE 238
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
176-274 |
2.42e-12 |
|
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: 65.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGSRGV---WLSAEGESRRIPGFRVQA 248
Cdd:pfam08543 114 EELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVvtdVLYDGGGFYTLEAPRIPT 193
|
90 100
....*....|....*....|....*.
gi 490246818 249 IDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:pfam08543 194 KNTHGTGCTLSAAIAANLAKGLSLPE 219
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
17-274 |
1.18e-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: 64.09 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 17 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDdIGERIRRQLASDKIDVAPVRaVAGEA- 95
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-VAGETr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 96 TGVALIfvnaEGENVIGIHAGANAALSVSQVEAEKERIASAQAllmqlesplesviaaakiahhHHTTVVLNPAPARELP 175
Cdd:cd01164 89 INVKIK----EEDGTETEINEPGPEISEEELEALLEKLKALLK---------------------KGDIVVLSGSLPPGVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 227
Cdd:cd01164 144 ADFYaelvrlarekgarvildtsgeallaalaAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490246818 228 RGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:cd01164 224 DGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
43-272 |
6.47e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 62.54 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 43 GKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVapVRAVAGEATGVAlifVNAEGENVI--------GIH 114
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwvlvdplQRH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 115 A-------GANAALS-VSQVEAE-KERIASAQALLMQ----LESPLESVIAAAKIAHHHHTTVVLNPAP-----ARELPD 176
Cdd:PLN02341 195 GfcsradfGPEPAFSwISKLSAEaKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 177 E------LLALVDIITPNETEAEKLTGIRvesdeDAAKAADVLHAKGIGT--VMITLGSRGVWLSAEGESRRIPGFRVQA 248
Cdd:PLN02341 275 ErralehLLRMSDVLLLTSEEAEALTGIR-----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
|
250 260
....*....|....*....|....
gi 490246818 249 IDTIAAGDTFNGALVTALLEGTAL 272
Cdd:PLN02341 350 VDTVGCGDSFAAAIALGYIHNLPL 373
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
182-297 |
8.59e-11 |
|
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: 61.81 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 182 VDIITPNETEAEKLTGIRVESDEDAAKAADVLHAK-GIGTVMITLGSRGV-WLSAEGESRRIPGFRVQAIDTIAAGDTFN 259
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTVI 261
|
90 100 110
....*....|....*....|....*....|....*...
gi 490246818 260 GALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVP 297
Cdd:cd01172 262 ATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
176-274 |
1.23e-10 |
|
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: 60.82 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 176 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGSRGV-WLSAEGESRRIPGFRVQAID 250
Cdd:COG0351 121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlPGDEAVdVLYDGDGVREFSAPRIDTGN 200
|
90 100
....*....|....*....|....
gi 490246818 251 TIAAGDTFNGALVTALLEGTALPE 274
Cdd:COG0351 201 THGTGCTLSSAIAALLAKGLDLEE 224
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
35-274 |
3.27e-10 |
|
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: 59.68 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 35 HHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEaTGVALIFVnaEGENVIGIH 114
Cdd:cd01940 15 HLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVEL--VDGDRIFGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 115 AGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPApARELPDELLALVDIITPNETEAEK 194
Cdd:cd01940 92 SNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFS-DRWDDDYLQLVCPYVDFAFFSASD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 195 ltgirvESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEG-TALP 273
Cdd:cd01940 171 ------LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGgTAIA 244
|
.
gi 490246818 274 E 274
Cdd:cd01940 245 E 245
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
40-306 |
7.47e-10 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 58.86 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 40 AFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGANA 119
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 120 ALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVV---------LNPAP--ARELPDELLALVDI 184
Cdd:PLN02323 121 DMLLRESELDLDLIRKAKIFhygsISLITEPCRSAHLAAMKIAKEAGALLsydpnlrlpLWPSAeaAREGIMSIWDEADI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 185 ITPNETEAEKLTGIRVESDEDAAKaadvLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVT 264
Cdd:PLN02323 201 IKVSDEEVEFLTGGDDPDDDTVVK----LWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLS 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490246818 265 ------ALLEGTA-LPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFL 306
Cdd:PLN02323 277 qlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
183-274 |
8.92e-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: 58.69 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 183 DIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGS-------------RGVWLSaegeSRRIPGFR 245
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThlirAGSqrdrsfeglvatqEGRWHI----SRPLAVFD 215
|
90 100
....*....|....*....|....*....
gi 490246818 246 VQAIDTiaaGDTFNGALVTALLEGTALPE 274
Cdd:TIGR00687 216 PPPVGT---GDLIAALLLATLLHGNSLKE 241
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
174-267 |
6.63e-09 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 55.52 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 174 LPDELLALVDIITPNETEAEKLTGIRVESDEDAAK-AADVLHAKGIGTVMITLG-------SRGVWLSAEGESRripgFR 245
Cdd:PRK06427 126 LRERLLPLATLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhlldgeeSVDWLFDGEGEER----FS 201
|
90 100
....*....|....*....|....*
gi 490246818 246 VQAIDTIA---AGDTFNGALvTALL 267
Cdd:PRK06427 202 APRIPTKNthgTGCTLSAAI-AAEL 225
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
173-269 |
3.15e-08 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 53.53 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 173 ELPDELLAL---VDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRgvwLSAE--------GESRRI 241
Cdd:PRK12413 118 ELRQELIQFfpyVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR---LSQKkaidlfydGKEFVI 194
|
90 100
....*....|....*....|....*...
gi 490246818 242 PGFRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK12413 195 LESPVLEKNNIGAGCTFASSIASQLVKG 222
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
30-269 |
4.43e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.04 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 30 ETVTGHHYQVAFGGKGANQAVAAGRSGA--------DIAFIACTGDDDIGERIRRQLASdkidvAPVR----AVAGEATG 97
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRR-----ANVHflsqPVKDGTTG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 98 VALIFVNAEGENVIGIHAGANAALSVSQVEAE---KERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAP---- 170
Cdd:PLN02813 189 TVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASaisKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDvsci 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 171 ARELPDELLAL---VDIITPNETEAEKLTGIrvESDEDAAKAADVLhAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQ 247
Cdd:PLN02813 269 ERHRDDFWDVMgnyADILFANSDEARALCGL--GSEESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCV 345
|
250 260
....*....|....*....|..
gi 490246818 248 AIDTIAAGDTFNGALVTALLEG 269
Cdd:PLN02813 346 PVDTCGAGDAYAAGILYGLLRG 367
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
9-279 |
4.72e-08 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 53.78 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 9 VVLGSINADhILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPV 88
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 89 RAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQLE---SPLESVIAAAKIAHHHHTTV 164
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNltaEALEWVFTLADEIPVFVDTV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 165 VLNPAparELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSA-EGESRRIPG 243
Cdd:PRK09954 220 SEFKA---GKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEkDGEQFLLTA 296
|
250 260 270
....*....|....*....|....*....|....*.
gi 490246818 244 FRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFA 279
Cdd:PRK09954 297 PAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFA 332
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
168-274 |
7.56e-08 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 52.56 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 168 PAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----------------LGSRGVW 231
Cdd:PRK05756 125 PGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypadrfemllVTADGAW 204
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490246818 232 LSaegESRRIPGFRvqaiDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PRK05756 205 HI---SRPLVDFMR----QPVGVGDLTSALFLARLLQGGSLEE 240
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
184-308 |
2.12e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 48.54 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 184 IITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRG-VWLSAEGESRRIPGfRVQAIDTIAAGDTFNGAL 262
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGaLWVNASGEWIAKPP-ACDVVSTVGAGDSMVGGL 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 490246818 263 VTALLEGTALPEAIRFAHAAAAIAVTrkgaQPSVPW--RTEIDEFLAQ 308
Cdd:PRK09513 262 IYGLLMRESSEHTLRLATAVSALAVS----QSNVGItdRPQLAAMMAR 305
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
178-214 |
3.12e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 48.19 E-value: 3.12e-06
10 20 30
....*....|....*....|....*....|....*..
gi 490246818 178 LLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLH 214
Cdd:PRK08573 127 LLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIV 163
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
175-260 |
5.39e-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: 47.07 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 175 PDEL---LALVDIITPNETEAEKLTGirvesDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAI-D 250
Cdd:cd01946 154 PEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
|
90
....*....|
gi 490246818 251 TIAAGDTFNG 260
Cdd:cd01946 229 PTGAGDTFAG 238
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
10-274 |
1.03e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 46.71 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 10 VLGSINAdHILNLDAFPTPGETVTGhhyqvafgGKGAN--QAVAAGrSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 87
Cdd:PLN02379 63 ILREVNA-HILPSPDDLSPIKTMAG--------GSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 88 VRAVAGEaTGVALIFVNAEGENVIgiHAGANAALSVSQVEAEKERIASAQALLMQLE-SPLESVIAAAKIAHHHHTTVVL 166
Cdd:PLN02379 133 LRAKKGP-TAQCVCLVDALGNRTM--RPCLSSAVKLQADELTKEDFKGSKWLVLRYGfYNLEVIEAAIRLAKQEGLSVSL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 167 NPAP---ARELPDELLAL-----VDIITPNETEAEKLTGIRVESDEDAAKAadvLHAKGIGTVMITLGSRGVWLSAEGES 238
Cdd:PLN02379 210 DLASfemVRNFRSPLLQLlesgkIDLCFANEDEARELLRGEQESDPEAALE---FLAKYCNWAVVTLGSKGCIARHGKEV 286
|
250 260 270
....*....|....*....|....*....|....*..
gi 490246818 239 RRIPGF-RVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PLN02379 287 VRVPAIgETNAVDATGAGDLFASGFLYGLIKGLSLEE 323
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
166-274 |
1.37e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 45.73 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 166 LNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSR-----GVWLSAEGESRR 240
Cdd:PRK12412 117 LHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetAIDVLYDGETFD 196
|
90 100 110
....*....|....*....|....*....|....*
gi 490246818 241 I-PGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PRK12412 197 LlESEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
177-269 |
5.76e-05 |
|
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: 43.93 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 177 ELLALVDIITPNETEAEKLTgirvesdeDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGD 256
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGD 222
|
90
....*....|...
gi 490246818 257 TFNGALVTALLEG 269
Cdd:cd01937 223 VFLAAFLYSRLSG 235
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
42-274 |
1.06e-03 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 40.11 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 42 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEAtgvALIFVNAEG-ENVIGIHA-GANA 119
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT---AQTQVELHDnDRVFGDYTeGVMA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 120 ALSVSQveaEKERIASAQ-----ALLMQLESPLESVIAAAkiahhhhTTVVLNPA--PARELPDELLALVDIitpnetea 192
Cdd:PRK09813 100 DFALSE---EDYAWLAQYdivhaAIWGHAEDAFPQLHAAG-------KLTAFDFSdkWDSPLWQTLVPHLDY-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 193 ekltGIRVESDEDA--AKAADVLHAKGIGTVMITLGSRGVwLSAEGES-RRIPGFRVQAIDTIAAGDTFNGALVTALLEG 269
Cdd:PRK09813 162 ----AFASAPQEDEflRLKMKAIVARGAGVVIVTLGENGS-IAWDGAQfWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAG 236
|
....*
gi 490246818 270 TALPE 274
Cdd:PRK09813 237 MTLPQ 241
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
177-266 |
2.74e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 39.39 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 177 ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGSRGV---WLSAEGESRRIPGFRVQAI 249
Cdd:PRK14713 153 ELVPRADLITPNLPELAVLLGEPPATTWEEALAQARRLAAETGTTVLVkgghLDGQRApdaLVGPDGAVTEVPGPRVDTR 232
|
90
....*....|....*..
gi 490246818 250 DTIAAGDTFNGALVTAL 266
Cdd:PRK14713 233 NTHGTGCSLSSALATRL 249
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
164-226 |
3.32e-03 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 38.98 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490246818 164 VVLNPAPARELPDELLALVDIITPNETEAEKLTG-IRVESDEDAAKAADVLHAKGIGTVMITLG 226
Cdd:PLN02898 121 VLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMRSAAKELHKLGPRYVLVKGG 184
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
177-274 |
3.99e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 38.54 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246818 177 ELLALVDIITPNETEAEKLTGIRVESDED----AAKAADVLHAKGIG--TVMITLGSRGVWLSAEGESRRIPGFRV---Q 247
Cdd:PLN02548 199 EALPYVDFLFGNETEARTFAKVQGWETEDveeiALKISALPKASGTHkrTVVITQGADPTVVAEDGKVKEFPVIPLpkeK 278
|
90 100
....*....|....*....|....*..
gi 490246818 248 AIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PLN02548 279 LVDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
198-274 |
8.09e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 37.48 E-value: 8.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246818 198 IRVESDEdaAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRIPGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 274
Cdd:PLN02630 185 LKASSEE--ALFIDVEEVRQKCCVIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPD 259
|
|
| |
