|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
3-308 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 516.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 3 TAGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKI 82
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 83 DVAPVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTT 162
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 163 VVLNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILG 242
Cdd:PRK11142 161 VILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681171067 243 FRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFLAQQ 308
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-297 |
9.56e-118 |
|
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: 340.68 E-value: 9.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVL 165
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 166 NPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRV 245
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1681171067 246 QAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPW 297
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
11-302 |
2.68e-114 |
|
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: 331.87 E-value: 2.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 11 GSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAV 90
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 91 AGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAPA 170
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 171 RE-LPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAID 249
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1681171067 250 TIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEID 302
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-301 |
2.80e-76 |
|
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: 235.16 E-value: 2.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAekERIASAQALLMQL-----ESPLESVIAAAKIAHHHH 160
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 161 TTVVLNPA-------PARELPDELLALVDIITPNETEAEKLTGIrvesdEDAAKAADVLHAKGIGTVMITLGSRGVWLSA 233
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681171067 234 EGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 301
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-292 |
4.52e-60 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 193.71 E-value: 4.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPtpGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 PVRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHT 161
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 162 T--VVLNPA-PARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESR 238
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1681171067 239 RILGFR-VQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 292
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-301 |
1.86e-59 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 193.03 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 1 MKTAGK-LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLAS 79
Cdd:PTZ00292 11 GGEAEPdVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 80 DKIDVAPVRAVAGEATGVALIFVNAE-GENVIGIHAGANAALSVSQVEAEKERIAS-AQALLMQLESPLESVIAAAKIAH 157
Cdd:PTZ00292 91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 158 HHHTTVVLNPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRG-VWL 231
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGcLIV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 232 SAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVPWRTEI 301
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-291 |
2.59e-33 |
|
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: 123.84 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHIlnldaFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:cd01166 1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 PVRAVAGEATGVALIFVNAEGENVIgIHAGANAALSVSQVEAEKER-IASAQAL------LMQLESPLESVIAAAKIAHH 158
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRV-LYYRAGSAASRLTPEDLDEAaLAGADHLhlsgitLALSESAREALLEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 159 HHTTVVL---------NPAPARELPDELLALVDIITPNETEAEKLTGIrvESDEDAAKAADVLHAkGIGTVMITLGSRGV 229
Cdd:cd01166 155 RGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGD--EDPTDAAERALALAL-GVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681171067 230 WLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGA 291
Cdd:cd01166 232 LVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
7-292 |
2.21e-31 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 118.57 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 7 LVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 86
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 87 VRAVAGEATGVALIFVNAEGENVIGIHAGANAALSVsqvEAEKERIASAQALLMQLESPLEsviAAAKIAHHHHTTVVLN 166
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEP---NDEADPDGLADIVHLSSGPGLI---ELARELAAGGITVSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 167 PAPA-----RELPDELLALVDIITPNETEAE---KLTGIRVESDedaakaadvlhAKGIGTVMITLGSRGVWLSAEGESR 238
Cdd:cd01942 156 PGQElprlsGEELEEILERADILFVNDYEAEllkERTGLSEAEL-----------ASGVRVVVVTLGPKGAIVFEDGEEV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1681171067 239 RILGF-RVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQ 292
Cdd:cd01942 225 EVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-273 |
7.25e-29 |
|
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: 112.02 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQvAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 PVRaVAGEATGVALIFVNAEGENVIGI-HAGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVV 164
Cdd:cd01941 80 GIV-FEGRSTASYTAILDKDGDLVVALaDMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 165 LNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILG 242
Cdd:cd01941 159 FEPTSAPKLKKlfYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVETKL 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1681171067 243 FRVQAIDTIA----AGDTFNGALVTALLEGTALPE 273
Cdd:cd01941 239 FPAPQPETVVnvtgAGDAFVAGLVAGLLEGMSLDD 273
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
10-273 |
1.78e-27 |
|
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: 108.15 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 10 LGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRA 89
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 90 VAGEATGVALIFVNAEGENVIGIHAGANAALSVSQVEAEkerIASAQALLMQLESPLESVIAAAKIAHHHHTTVV-LNPA 168
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIDTQAAPDSLPDAI---LGGADAVLVDGRQPEAALHLAQEARARGIPIPLdLDGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 169 PARELpDELLALVDIITPNETEAEKLTGIrveSDEDAAKAadvLHAKGIGTVMITLGSRGV-WLSAEGESRRILGFRVQA 247
Cdd:cd01945 162 GLRVL-EELLPLADHAICSENFLRPNTGS---ADDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVEV 234
|
250 260
....*....|....*....|....*.
gi 1681171067 248 IDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:cd01945 235 VDTTGAGDVFHGAFAHALAEGMPLRE 260
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
41-271 |
7.32e-27 |
|
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: 106.57 E-value: 7.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 41 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGAnAAL 120
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGP-AAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 121 SVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLALVDIIT 185
Cdd:cd01167 107 LLLDTELNPDLLSEADILhfgsIALASEPSRSALLELLEAAKKAGVLISfdpnlrpplwrDEEEARERIAELLELADIVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 186 PNETEAEKLTGIrvesdEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTAL 265
Cdd:cd01167 187 LSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261
|
....*.
gi 1681171067 266 LEGTAL 271
Cdd:cd01167 262 LSRGLL 267
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-266 |
8.88e-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: 98.71 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIActgdddigerirrqlasdkidva 85
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 pvravageatgvalifvnaegenVIGIHAGANAALSVSQVEAEKERIasaqallmqlesplesviaaakiahHHHTTVVL 165
Cdd:cd00287 58 -----------------------ADAVVISGLSPAPEAVLDALEEAR-------------------------RRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 166 NPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRI 240
Cdd:cd00287 90 DPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVH 169
|
250 260
....*....|....*....|....*..
gi 1681171067 241 LG-FRVQAIDTIAAGDTFNGALVTALL 266
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 ... |
6-290 |
1.20e-23 |
|
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: 97.88 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGkGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVA 85
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 -PVRAvaGEATGVALIFVNAEGE----NVIGIHAGANAA-LSVSQVEAEKERIASAQallmQLESPLESVIA--AAKIAH 157
Cdd:cd01944 80 lPPRG--GDDGGCLVALVEPDGErsfiSISGAEQDWSTEwFATLTVAPYDYVYLSGY----TLASENASKVIllEWLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 158 HHHTTVVLNPAPA-RELPD----ELLALVDIITPNETEAEKLTGirvESDEDAAKAADVLHAKGIGTVMITLGSRGVWL- 231
Cdd:cd01944 154 PAGTTLVFDPGPRiSDIPDtilqALMAKRPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIr 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681171067 232 SAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPEAIRFAHAAAAIAVTRKG 290
Cdd:cd01944 231 LPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
41-273 |
4.81e-21 |
|
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: 91.14 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 41 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRaVAGEATGVALIFVNAEGENVIGIHAGANAAL 120
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 121 SVSQVEAEKerIASAQALLM---QLESPLESVIAAAKIAHHHHTTVVLN------PAPARELPDELLALVDIITPNETEA 191
Cdd:cd01168 134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 192 EKLTGIRVESDEDAAKAadvLHAKGIGTVMITLGSRGVWLSAEGESRRILGFR-VQAIDTIAAGDTFNGALVTALLEGTA 270
Cdd:cd01168 212 EALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP 288
|
...
gi 1681171067 271 LPE 273
Cdd:cd01168 289 LEE 291
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
16-273 |
3.01e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 80.18 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 16 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGAD-IAFIACTGDDdiGERIRRQLASDKIDVAPVRaVAGEa 94
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDvTALGFLGGFT--GEFIEELLDEEGIPTDFVP-IEGE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 95 TGVALIFVNAEGENVIGIHaGANAALSVSQVEAEKERIASAqallmqlesplesviaaakiaHHHHTTVVLNPAPARELP 174
Cdd:COG1105 86 TRINIKIVDPSDGTETEIN-EPGPEISEEELEALLERLEEL---------------------LKEGDWVVLSGSLPPGVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 226
Cdd:COG1105 144 PDFYaelirlarargakvvldtsgealkaaleAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1681171067 227 RGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:COG1105 224 DGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
176-223 |
3.23e-14 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 71.65 E-value: 3.23e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1681171067 176 ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT 223
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
175-273 |
1.15e-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: 69.54 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT------LGSRGVWLSAEGESRRILGFRVQAI 248
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFP 210
|
90 100
....*....|....*....|....*.
gi 1681171067 249 DTIA-AGDTFNGALVTALLEGTALPE 273
Cdd:cd01173 211 AYFNgTGDLFAALLLARLLKGKSLAE 236
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
1-268 |
6.78e-13 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 68.09 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 1 MKTAGKLVVLGSINAD------HILNLdAFPTPGetvtghhyQVAF--GGKGANQAVAAGRSGADIAFIACTGDDDIGER 72
Cdd:PRK09850 1 MREKDYVVIIGSANIDvagyshESLNY-ADSNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 73 IRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQL---ESPLES 148
Cdd:PRK09850 72 LLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 149 VIAAAKIahhhhTTVVLNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 226
Cdd:PRK09850 152 ILDNAAN-----VPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1681171067 227 RGVWLS-AEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEG 268
Cdd:PRK09850 227 DGVYYSdISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
175-268 |
1.14e-12 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 67.07 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQ----AIDT 250
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEqfkiVIPK 223
|
90
....*....|....*...
gi 1681171067 251 IAAGDTFNGALVTALLEG 268
Cdd:PLN02978 224 IPAYFTGTGDLMAALLLG 241
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
41-302 |
4.32e-12 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 65.34 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 41 GGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGEN--VIGIHAGANA 118
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 119 ALSVSQVEAEKER-------IASAQallmqleSPLESVIAAAKIAHHHHTTVVL-----------NPAPARELPDELLAL 180
Cdd:PRK09434 108 FLQPQDLPPFRQGewlhlcsIALSA-------EPSRSTTFEAMRRIKAAGGFVSfdpnlredlwqDEAELRECLRQALAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 181 VDIITPNETEAEKLTGirvESDEDAAKAAdVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGA 260
Cdd:PRK09434 181 ADVVKLSEEELCFLSG---TSQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1681171067 261 LVTALLEGTALPEAIRFAHAAAAI------AVTRKGAQPSVPWRTEID 302
Cdd:PRK09434 257 LLAGLSQAGLWTDEAELAEIIAQAqacgalATTAKGAMTALPNRQELE 304
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
175-273 |
8.93e-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: 63.65 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGSRGV---WLSAEGESRRILGFRVQA 247
Cdd:pfam08543 114 EELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVvtdVLYDGGGFYTLEAPRIPT 193
|
90 100
....*....|....*....|....*.
gi 1681171067 248 IDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:pfam08543 194 KNTHGTGCTLSAAIAANLAKGLSLPE 219
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-268 |
1.54e-11 |
|
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: 63.59 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 6 KLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVa 85
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 86 pVRAVAGEATGVALIFVNAEGENVIGIHAGanaalsvsQVEAEKERIASAQALLMQLESplESVIAAAKIAHHHHTTVVL 165
Cdd:cd01947 80 -TVAWRDKPTRKTLSFIDPNGERTITVPGE--------RLEDDLKWPILDEGDGVFITA--AAVDKEAIRKCRETKLVIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 166 NPAP--ARELPDELLALVDIITPNETEAEKLTgirvesdedaakAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 243
Cdd:cd01947 149 QVTPrvRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
|
250 260
....*....|....*....|....*
gi 1681171067 244 RVQAIDTIAAGDTFNGALVTALLEG 268
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKG 241
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
175-273 |
1.92e-11 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 63.24 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----------------LGSRGVWLSaegESR 238
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpadkignlaVTADGAWLV---ETP 209
|
90 100 110
....*....|....*....|....*....|....*
gi 1681171067 239 RIlgfrvqAIDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:COG2240 210 LL------PFSPNGTGDLFAALLLAHLLRGKSLEE 238
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
16-273 |
4.63e-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: 62.16 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 16 DHILNLDAFpTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDdIGERIRRQLASDKIDVAPVRaVAGEA- 94
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE-VAGETr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 95 TGVALIfvnaEGENVIGIHAGANAALSVSQVEAEKERIASAQAllmqlesplesviaaakiahhHHTTVVLNPAPARELP 174
Cdd:cd01164 89 INVKIK----EEDGTETEINEPGPEISEEELEALLEKLKALLK---------------------KGDIVVLSGSLPPGVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELL----------------------------ALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGS 226
Cdd:cd01164 144 ADFYaelvrlarekgarvildtsgeallaalaAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1681171067 227 RGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:cd01164 224 DGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
182-273 |
2.09e-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: 60.23 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 182 DIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGS-------------RGVWLSaegeSRRILGFR 244
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThlirAGSqrdrsfeglvatqEGRWHI----SRPLAVFD 215
|
90 100
....*....|....*....|....*....
gi 1681171067 245 VQAIDTiaaGDTFNGALVTALLEGTALPE 273
Cdd:TIGR00687 216 PPPVGT---GDLIAALLLATLLHGNSLKE 241
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
34-273 |
6.51e-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: 58.52 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 34 HHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEaTGVALIFVnaEGENVIGIH 113
Cdd:cd01940 15 HLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVEL--VDGDRIFGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 114 AGANAALSVSQVEAEKERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPApARELPDELLALVDIITPNETEAEK 193
Cdd:cd01940 92 SNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFS-DRWDDDYLQLVCPYVDFAFFSASD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 194 ltgirvESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVTALLEG-TALP 272
Cdd:cd01940 171 ------LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGgTAIA 244
|
.
gi 1681171067 273 E 273
Cdd:cd01940 245 E 245
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
175-273 |
1.27e-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: 57.74 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 175 DELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----LGSRGV-WLSAEGESRRILGFRVQAID 249
Cdd:COG0351 121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlPGDEAVdVLYDGDGVREFSAPRIDTGN 200
|
90 100
....*....|....*....|....
gi 1681171067 250 TIAAGDTFNGALVTALLEGTALPE 273
Cdd:COG0351 201 THGTGCTLSSAIAALLAKGLDLEE 224
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
42-271 |
1.33e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 58.69 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 42 GKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVapVRAVAGEATGVAlifVNAEGENVI--------GIH 113
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwvlvdplQRH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 114 A-------GANAALS-VSQVEAE-KERIASAQALLMQ----LESPLESVIAAAKIAHHHHTTVVLNPAP-----ARELPD 175
Cdd:PLN02341 195 GfcsradfGPEPAFSwISKLSAEaKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 176 E------LLALVDIITPNETEAEKLTGIRvesdeDAAKAADVLHAKGIGT--VMITLGSRGVWLSAEGESRRILGFRVQA 247
Cdd:PLN02341 275 ErralehLLRMSDVLLLTSEEAEALTGIR-----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
|
250 260
....*....|....*....|....
gi 1681171067 248 IDTIAAGDTFNGALVTALLEGTAL 271
Cdd:PLN02341 350 VDTVGCGDSFAAAIALGYIHNLPL 373
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
172-268 |
2.33e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 57.00 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 172 ELPDELLAL---VDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRgvwLSAE--------GESRRI 240
Cdd:PRK12413 118 ELRQELIQFfpyVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR---LSQKkaidlfydGKEFVI 194
|
90 100
....*....|....*....|....*...
gi 1681171067 241 LGFRVQAIDTIAAGDTFNGALVTALLEG 268
Cdd:PRK12413 195 LESPVLEKNNIGAGCTFASSIASQLVKG 222
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
181-296 |
4.07e-09 |
|
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: 56.80 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 181 VDIITPNETEAEKLTGIRVESDEDAAKAADVLHAK-GIGTVMITLGSRGV-WLSAEGESRRILGFRVQAIDTIAAGDTFN 258
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTVI 261
|
90 100 110
....*....|....*....|....*....|....*...
gi 1681171067 259 GALVTALLEGTALPEAIRFAHAAAAIAVTRKGAQPSVP 296
Cdd:cd01172 262 ATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
39-305 |
5.95e-09 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 56.17 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 39 AFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPVRAVAGEATGVALIFVNAEGENVIGIHAGANA 118
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 119 ALSVSQVEAEKERIASAQAL----LMQLESPLESVIAAAKIAHHHHTTVV---------LNPAP--ARELPDELLALVDI 183
Cdd:PLN02323 121 DMLLRESELDLDLIRKAKIFhygsISLITEPCRSAHLAAMKIAKEAGALLsydpnlrlpLWPSAeaAREGIMSIWDEADI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 184 ITPNETEAEKLTGIRVESDEDAAKaadvLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGDTFNGALVT 263
Cdd:PLN02323 201 IKVSDEEVEFLTGGDDPDDDTVVK----LWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLS 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1681171067 264 ------ALLEGTA-LPEAIRFAHAAAAIAVTRKGAQPSVPWRTEIDEFL 305
Cdd:PLN02323 277 qlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
173-266 |
6.96e-09 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 55.52 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 173 LPDELLALVDIITPNETEAEKLTGIRVESDEDAAK-AADVLHAKGIGTVMITLG-------SRGVWLSAEGESRrilgFR 244
Cdd:PRK06427 126 LRERLLPLATLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhlldgeeSVDWLFDGEGEER----FS 201
|
90 100
....*....|....*....|....*
gi 1681171067 245 VQAIDTIA---AGDTFNGALvTALL 266
Cdd:PRK06427 202 APRIPTKNthgTGCTLSAAI-AAEL 225
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
8-278 |
2.46e-08 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 54.55 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 8 VVLGSINADhILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGADIAFIACTGDDDIGERIRRQLASDKIDVAPV 87
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 88 RAVAGEATGVALIFVNAEGENVIGIH-AGANAALSVSQVEAEKERIASAQALLMQLE---SPLESVIAAAKIAHHHHTTV 163
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNltaEALEWVFTLADEIPVFVDTV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 164 VLNPAparELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGF 243
Cdd:PRK09954 220 SEFKA---GKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTA 296
|
250 260 270
....*....|....*....|....*....|....*.
gi 1681171067 244 RVQA-IDTIAAGDTFNGALVTALLEGTALPEAIRFA 278
Cdd:PRK09954 297 PAHTtVDSFGADDGFMAGLVYSFLEGYSFRDSARFA 332
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
167-273 |
3.13e-08 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 53.72 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 167 PAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMIT----------------LGSRGVW 230
Cdd:PRK05756 125 PGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypadrfemllVTADGAW 204
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1681171067 231 LSaegeSRRILGFRVQaidTIAAGDTFNGALVTALLEGTALPE 273
Cdd:PRK05756 205 HI----SRPLVDFMRQ---PVGVGDLTSALFLARLLQGGSLEE 240
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
29-268 |
1.47e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 49.42 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 29 ETVTGHHYQVAFGGKGANQAVAAGRSGA--------DIAFIACTGDDDIGERIRRQLASdkidvAPVR----AVAGEATG 96
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRR-----ANVHflsqPVKDGTTG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 97 VALIFVNAEGENVIGIHAGANAALSVSQVEAE---KERIASAQALLMQLESPLESVIAAAKIAHHHHTTVVLNPAP---- 169
Cdd:PLN02813 189 TVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASaisKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDvsci 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 170 ARELPDELLAL---VDIITPNETEAEKLTGIrvESDEDAAKAADVLhAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQ 246
Cdd:PLN02813 269 ERHRDDFWDVMgnyADILFANSDEARALCGL--GSEESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCV 345
|
250 260
....*....|....*....|..
gi 1681171067 247 AIDTIAAGDTFNGALVTALLEG 268
Cdd:PLN02813 346 PVDTCGAGDAYAAGILYGLLRG 367
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
165-273 |
2.34e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 48.04 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 165 LNPAPARELPDELLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSR-----GVWLSAEGESRR 239
Cdd:PRK12412 117 LHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetAIDVLYDGETFD 196
|
90 100 110
....*....|....*....|....*....|....*
gi 1681171067 240 IL-GFRVQAIDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:PRK12412 197 LLeSEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
177-213 |
3.04e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 48.19 E-value: 3.04e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1681171067 177 LLALVDIITPNETEAEKLTGIRVESDEDAAKAADVLH 213
Cdd:PRK08573 127 LLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIV 163
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
183-307 |
6.39e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 43.92 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 183 IITPNETEAEKLTGIRVESDEDAAKAADVLHAKGIGTVMITLGSRG-VWLSAEGESRrILGFRVQAIDTIAAGDTFNGAL 261
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGaLWVNASGEWI-AKPPACDVVSTVGAGDSMVGGL 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1681171067 262 VTALLEGTALPEAIRFAHAAAAIAVTrkgaQPSVPW--RTEIDEFLAQ 307
Cdd:PRK09513 262 IYGLLMRESSEHTLRLATAVSALAVS----QSNVGItdRPQLAAMMAR 305
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
9-273 |
6.53e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 44.01 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 9 VLGSINAdHILNLDAFPTPGETVTGhhyqvafgGKGAN--QAVAAGrSGADIAFIACTGDDDIGERIRRQLASDKIDVAP 86
Cdd:PLN02379 63 ILREVNA-HILPSPDDLSPIKTMAG--------GSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 87 VRAVAGEaTGVALIFVNAEGENVIgiHAGANAALSVSQVEAEKERIASAQALLMQLE-SPLESVIAAAKIAHHHHTTVVL 165
Cdd:PLN02379 133 LRAKKGP-TAQCVCLVDALGNRTM--RPCLSSAVKLQADELTKEDFKGSKWLVLRYGfYNLEVIEAAIRLAKQEGLSVSL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 166 NPAP---ARELPDELLAL-----VDIITPNETEAEKLTGIRVESDEDAAKAadvLHAKGIGTVMITLGSRG--------- 228
Cdd:PLN02379 210 DLASfemVRNFRSPLLQLlesgkIDLCFANEDEARELLRGEQESDPEAALE---FLAKYCNWAVVTLGSKGciarhgkev 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1681171067 229 VWLSAEGESRrilgfrvqAIDTIAAGDTFNGALVTALLEGTALPE 273
Cdd:PLN02379 287 VRVPAIGETN--------AVDATGAGDLFASGFLYGLIKGLSLEE 323
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
174-259 |
1.83e-04 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 42.45 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 174 PDEL---LALVDIITPNETEAEKLTGirvesDEDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAI-D 249
Cdd:cd01946 154 PEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
|
90
....*....|
gi 1681171067 250 TIAAGDTFNG 259
Cdd:cd01946 229 PTGAGDTFAG 238
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
176-268 |
7.06e-04 |
|
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: 40.46 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 176 ELLALVDIITPNETEAEKLTgirvesdeDAAKAADVLHAKGIGTVMITLGSRGVWLSAEGESRRILGFRVQAIDTIAAGD 255
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGD 222
|
90
....*....|...
gi 1681171067 256 TFNGALVTALLEG 268
Cdd:cd01937 223 VFLAAFLYSRLSG 235
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
163-225 |
3.41e-03 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 38.98 E-value: 3.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681171067 163 VVLNPAPARELPDELLALVDIITPNETEAEKLTG-IRVESDEDAAKAADVLHAKGIGTVMITLG 225
Cdd:PLN02898 121 VLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMRSAAKELHKLGPRYVLVKGG 184
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
176-273 |
6.53e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 37.77 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681171067 176 ELLALVDIITPNETEAEKLTGIRVESDED----AAKAADVLHAKGIG--TVMITLGSRGVWLSAEGesrRILGFRVQAI- 248
Cdd:PLN02548 199 EALPYVDFLFGNETEARTFAKVQGWETEDveeiALKISALPKASGTHkrTVVITQGADPTVVAEDG---KVKEFPVIPLp 275
|
90 100 110
....*....|....*....|....*....|
gi 1681171067 249 -----DTIAAGDTFNGALVTALLEGTALPE 273
Cdd:PLN02548 276 keklvDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| |
