|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-330 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 548.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 1 MNRLHVIESHEGSNGPTVVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGD 80
Cdd:PTZ00292 1 MHRAGEVASHGGEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 81 GDEYIANFKRNGVDTTNVYRERNGATGLAMIFVDTKTSNNEIVICPNATHALTTEFLRRQSDNYNRFlsqsCRFLICQNE 160
Cdd:PTZ00292 81 GSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNI----CKYLICQNE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 161 IPLETTLDVLREAHKRGIYTVFNSAPAPSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVR 240
Cdd:PTZ00292 157 IPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 241 NVVITLGAQGYVICEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPT 320
Cdd:PTZ00292 237 NVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPH 316
|
330
....*....|
gi 70886975 321 PDELPADARA 330
Cdd:PTZ00292 317 PSELPADVKE 326
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
18-320 |
6.73e-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: 346.84 E-value: 6.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATGLAMIFVDtKTSNNEIVICPNATHALTTEFLRRQSDnynrfLSQSCRFLICQNEIPLETTLDVLREAHKRG 177
Cdd:cd01174 82 VEVVVGAPTGTAVITVD-ESGENRIVVVPGANGELTPADVDAALE-----LIAAADVLLLQLEIPLETVLAALRAARRAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 178 IYTVFNSAPAPSLAEvgvikPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYVICEmG 257
Cdd:cd01174 156 VTVILNPAPARPLPA-----ELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS-G 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 258 SEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPT 320
Cdd:cd01174 230 GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
22-325 |
3.36e-110 |
|
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: 322.24 E-value: 3.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 22 GSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVYRE 101
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 102 RNGATGLAMIFVDtKTSNNEIVICPNATHALTTEFLRRQSDnynrFLSQScRFLICQNEIPLETTLDVLREAHKRGIYTV 181
Cdd:TIGR02152 81 KDTPTGTAFITVD-DTGENRIVVVAGANAELTPEDIDAAEA----LIAES-DIVLLQLEIPLETVLEAAKIAKKHGVKVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 182 FNSAPA-PSLAEvgvikPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYVICEmGSEP 260
Cdd:TIGR02152 155 LNPAPAiKDLDD-----ELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVS-KDES 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886975 261 MHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPTPDELP 325
Cdd:TIGR02152 229 KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
18-324 |
1.33e-87 |
|
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: 264.82 E-value: 1.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATGLAMIFVDtKTSNNEIVICPNATHALTTEFLRRQsdnynrfLSQSCRFLICQ-----NEIPLETTLDVLRE 172
Cdd:COG0524 82 VRRDPGAPTGLAFILVD-PDGERTIVFYRGANAELTPEDLDEA-------LLAGADILHLGgitlaSEPPREALLAALEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 173 AHKRGIYTVFNSAPAPSLAEVG--VIKPFLPYVSLFCPNEVEAAMITGMEvsdgaSAAKAAKALQALGVRNVVITLGAQG 250
Cdd:COG0524 154 ARAAGVPVSLDPNYRPALWEPAreLLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70886975 251 YVICEmGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPTPDEL 324
Cdd:COG0524 229 ALLYT-GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
19-326 |
9.28e-77 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 237.46 E-value: 9.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 19 VVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNV 98
Cdd:PRK11142 6 VVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 99 YRERNGATGLAMIFVDtKTSNNEIVICPNATHALTTEFLRRQSDnynrfLSQSCRFLICQNEIPLETTLDVLREAHKRGI 178
Cdd:PRK11142 86 SVIKGESTGVALIFVN-DEGENSIGIHAGANAALTPALVEAHRE-----LIANADALLMQLETPLETVLAAAKIAKQHGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 179 YTVFNSAPAPSLAEvgvikPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYVICEMGS 258
Cdd:PRK11142 160 KVILNPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70886975 259 EPMhAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPTPDELPA 326
Cdd:PRK11142 235 GQR-VPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDA 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
18-316 |
1.81e-63 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 202.96 E-value: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPriGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATGLAMIFVDtKTSNNEIVICPNATHALTTEflrrQSDNYNRFLSQSCRFLIC---QNEIPLETTLDVLREAH 174
Cdd:pfam00294 80 VVIDEDTRTGTALIEVD-GDGERTIVFNRGAAADLTPE----ELEENEDLLENADLLYISgslPLGLPEATLEELIEAAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 175 KRGIYTVFNSAPAPSLAEVgvIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYVIC 254
Cdd:pfam00294 155 NGGTFDPNLLDPLGAAREA--LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 255 EmGSEPMHAPGLR-VKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQS 316
Cdd:pfam00294 233 E-GDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
17-315 |
8.73e-46 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 156.70 E-value: 8.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 17 TVVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTT 96
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 97 NVYRERNGATGLAMIFVDTktSNNEIVicpnATHALTTEFLRRQSDNYNRFLSQSCRFLICQNEIPLEttldvlREAHKR 176
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDG--DDNQIA----YFYPGAMDELEPNDEADPDGLADIVHLSSGPGLIELA------RELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 177 GIYTVFNSAPAPSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDgasaakaaKALQALGVRNVVITLGAQGYVICEM 256
Cdd:cd01942 149 GITVSFDPGQELPRLSGEELEEILERADILFVNDYEAELLKERTGLS--------EAELASGVRVVVVTLGPKGAIVFED 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886975 257 GSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQ 315
Cdd:cd01942 221 GEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
18-313 |
2.07e-44 |
|
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: 153.50 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAyvdriPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:cd01166 2 VVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATGLAMIFVDtktsnneivicPNATHALTteFLRRQS-------DNYNRFLSQSCRFL------ICQNEIPLE 164
Cdd:cd01166 77 VRVDPGRPTGLYFLEIG-----------AGGERRVL--YYRAGSaasrltpEDLDEAALAGADHLhlsgitLALSESARE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 165 TTLDVLREAHKRGIYTVF--NSAPAPSLAEVG--VIKPFLPYVSLFCPNEVEAAMITGMEVSDgasAAKAAKALQALGVR 240
Cdd:cd01166 144 ALLEALEAAKARGVTVSFdlNYRPKLWSAEEAreALEELLPYVDIVLPSEEEAEALLGDEDPT---DAAERALALALGVK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 241 NVVITLGAQGYVICEmGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:cd01166 221 AVVVKLGAEGALVYT-GGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
21-320 |
1.02e-34 |
|
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: 127.80 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 21 VGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVYR 100
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 101 ERNGATGLAMIFVDTKTSNNEIVIC---PNATHALTTEFLrrqsdnynrflsQSCRFLICQNEIPlETTLDVLREAHKRG 177
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAidtQAAPDSLPDAIL------------GGADAVLVDGRQP-EAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 178 IytvfnsaPAPSLAEVGVIKPF---LPYVS-LFCPNEVEAAMitgmevsDGASAAKAAKALQALGVRNVVITLGAQGYVI 253
Cdd:cd01945 152 I-------PIPLDLDGGGLRVLeelLPLADhAICSENFLRPN-------TGSADDEALELLASLGIPFVAVTLGEAGCLW 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886975 254 CEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSYPT 320
Cdd:cd01945 218 LERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
18-310 |
8.95e-34 |
|
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: 125.50 E-value: 8.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKgFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPGHVKQS-PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRErNGATG--LAMIfvdtkTSNNEIVICPNATHA---LTTEFLRRQSDNYNRflsqsCRFLICQNEIPLETTLDVLRE 172
Cdd:cd01941 81 IVFE-GRSTAsyTAIL-----DKDGDLVVALADMDIyelLTPDFLRKIREALKE-----AKPIVVDANLPEEALEYLLAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 173 AHKRGIYTVFNSAPAPSLAEVGVIkpfLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYV 252
Cdd:cd01941 150 AAKHGVPVAFEPTSAPKLKKLFYL---LHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70886975 253 ICEM--GSEPMHAP-GLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQ 310
Cdd:cd01941 227 LSSRegGVETKLFPaPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
18-313 |
2.38e-32 |
|
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: 121.97 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGScfldyiAYVDRIPRigETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:cd01167 2 VVCFGE------ALIDFIPE--GSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATGLAMIFVDtktsnneivicpnATHALTTEFLRRQSdnYNRFLSQ--------SCRFLiCQNEIPL------ 163
Cdd:cd01167 74 IQFDPAAPTTLAFVTLD-------------ADGERSFEFYRGPA--ADLLLDTelnpdllsEADIL-HFGSIALasepsr 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 164 ETTLDVLREAHKRGIYTVF--NSAPA---PSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKalqalG 238
Cdd:cd01167 138 SALLELLEAAKKAGVLISFdpNLRPPlwrDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLF-----G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 239 VRNVVITLGAQG-YVICEMGSEpmHAPGLRVKAVDTTGAGDSFVGSMVY-YMSRGMS------LSEACRRANVCAAFSVQ 310
Cdd:cd01167 213 LKLVLVTRGADGaLLYTKGGVG--EVPGIPVEVVDTTGAGDAFVAGLLAqLLSRGLLaldedeLAEALRFANAVGALTCT 290
|
...
gi 70886975 311 RKG 313
Cdd:cd01167 291 KAG 293
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
18-313 |
7.61e-29 |
|
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: 112.52 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGkGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVD--T 95
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEilL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 96 TNVYRErNGATGLAMIFVDTKTSnneIVICPNATHALTTEFLRRQSdnynrfLSQSCRFLICQNEIPLETTLDV-LREAH 174
Cdd:cd01944 81 PPRGGD-DGGCLVALVEPDGERS---FISISGAEQDWSTEWFATLT------VAPYDYVYLSGYTLASENASKViLLEWL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 175 KR---GIYTVFNSAPAPSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVrnvVITLGAQGY 251
Cdd:cd01944 151 EAlpaGTTLVFDPGPRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAPV---VVRLGSNGA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886975 252 VICEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:cd01944 228 WIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
26-326 |
7.23e-28 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 110.22 E-value: 7.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 26 LDYIAYVDRIpRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDgDGDEYIANFKRNGVDTTNVYRErnGA 105
Cdd:COG1105 10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGF-TGEFIEELLDEEGIPTDFVPIE--GE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 106 TGLAMIFVDTKTsNNEIVIC---PNATHALTTEFLRRQSDnynrfLSQSCRFLIC----QNEIPLETTLDVLREAHKRGI 178
Cdd:COG1105 86 TRINIKIVDPSD-GTETEINepgPEISEEELEALLERLEE-----LLKEGDWVVLsgslPPGVPPDFYAELIRLARARGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 179 YTVFNSAPAPsLAEVGVIKPFLpyVSlfcPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGyVICEMGS 258
Cdd:COG1105 160 KVVLDTSGEA-LKAALEAGPDL--IK---PNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADG-ALLVTED 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70886975 259 EPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQssYPTPDELPA 326
Cdd:COG1105 233 GVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG--LPDREDVEE 298
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
18-314 |
8.80e-27 |
|
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: 107.31 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVD-----------------RIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGD 80
Cdd:cd01168 4 VLGLGNALVDILAQVDdafleklglkkgdmilaDMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 81 GDEYIANFKRNGVDTTNVYRErNGATGLAMIFVDtktsnneivicPNA-----THALTTEFLRRQSDNYNRF-LSQSCR- 153
Cdd:cd01168 84 GDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVT-----------PDAertmcTYLGAANELSPDDLDWSLLaKAKYLYl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 154 --FLIcqnEIPLETTLDVLREAHKRGIYTVFNsapapsLAEVGVIKPF-------LPYVS-LFCpNEVEAAMITGMEVSD 223
Cdd:cd01168 152 egYLL---TVPPEAILLAAEHAKENGVKIALN------LSAPFIVQRFkeallelLPYVDiLFG-NEEEAEALAEAETTD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 224 gasAAKAAKALQALGVRNVVITLGAQGYVICEmGSEPMHAPGLR-VKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRAN 302
Cdd:cd01168 222 ---DLEAALKLLALRCRIVVITQGAKGAVVVE-GGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGS 297
|
330
....*....|..
gi 70886975 303 VCAAFSVQRKGT 314
Cdd:cd01168 298 YAAAEVIQQLGP 309
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
18-288 |
1.97e-26 |
|
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: 103.71 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIvgsdgdgdeyianfkrngvdttn 97
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 vyrerngatglamifvdtktsnneivicpnathaltteflrrqsdnynrflsqscRFLICQNEIP-LETTLDVLREAHKR 176
Cdd:cd00287 59 -------------------------------------------------------DAVVISGLSPaPEAVLDALEEARRR 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 177 GIYTVFNSAPAPSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGYVICEM 256
Cdd:cd00287 84 GVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATR 163
|
250 260 270
....*....|....*....|....*....|..
gi 70886975 257 GSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYM 288
Cdd:cd00287 164 GGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
26-315 |
1.70e-23 |
|
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: 97.99 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 26 LDYIAYVDRIpRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDgDGDEYIANFKRNGVDTTNVYrernga 105
Cdd:cd01164 11 IDLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 106 tglamifVDTKTSNNEIVICPNAThalTTEF--------------LRRQSDNynrfLSQSCRFLICQNEIP----LETTL 167
Cdd:cd01164 83 -------VAGETRINVKIKEEDGT---ETEInepgpeiseeeleaLLEKLKA----LLKKGDIVVLSGSLPpgvpADFYA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 168 DVLREAHKRGIYTVFNSAPAPsLAEVGVIKPFLpyvslFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLG 247
Cdd:cd01164 149 ELVRLAREKGARVILDTSGEA-LLAALAAKPFL-----IKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70886975 248 AQGyVICEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQ 315
Cdd:cd01164 223 ADG-ALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
17-324 |
1.05e-20 |
|
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: 90.31 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 17 TVVVVGSCFLDYIAY--VDRI----PRIGETLTSKSFskgFGGKGANQA--VAAgrLGARVAMVGIVGSDGDGDEYIANF 88
Cdd:cd01172 1 KVLVVGDVILDEYLYgdVERIspeaPVPVVKVEREEI---RLGGAANVAnnLAS--LGAKVTLLGVVGDDEAGDLLRKLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 89 KRNGVDTTNVYRERNGATglamifvdTKTSnneiVICPNA---------THALTTEFLRRQSDNYNRFLsQSCRFLICQN 159
Cdd:cd01172 76 EKEGIDTDGIVDEGRPTT--------TKTR----VIARNQqllrvdredDSPLSAEEEQRLIERIAERL-PEADVVILSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 160 E----IPLETTLDVLREAHKRGIYTVFNSAPapslaevgviKPFLPY--VSLFCPNEVEAAMITGMEV-SDGASAAKAAK 232
Cdd:cd01172 143 YgkgvLTPRVIEALIAAARELGIPVLVDPKG----------RDYSKYrgATLLTPNEKEAREALGDEInDDDELEAAGEK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 233 ALQALGVRNVVITLGAQGYVICEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRK 312
Cdd:cd01172 213 LLELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKV 292
|
330
....*....|..
gi 70886975 313 GTQSSypTPDEL 324
Cdd:cd01172 293 GTAPV--TPKEL 302
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
17-313 |
2.50e-19 |
|
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: 85.93 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 17 TVVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFkRNGVDTT 96
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 97 NVYReRNGATGLAMIFVDtktSNNE--IVICPNATHALTTEFLRRQSDnynrflsqscrFLICQNEIPLETTLDVLREaH 174
Cdd:cd01947 80 TVAW-RDKPTRKTLSFID---PNGErtITVPGERLEDDLKWPILDEGD-----------GVFITAAAVDKEAIRKCRE-T 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 175 KRGIYtvfnsAPAPSlAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGAsaakaakalqalGVRNVVITLGAQGyVIC 254
Cdd:cd01947 144 KLVIL-----QVTPR-VRVDELNQALIPLDILIGSRLDPGELVVAEKIAGP------------FPRYLIVTEGELG-AIL 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886975 255 EMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:cd01947 205 YPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
52-306 |
3.55e-17 |
|
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: 79.71 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 52 GGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVyRERNGATGLAmifvDTKTSNNEIVicpnatha 131
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVA----DVELVDGDRI-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 132 ltteFLRrqsdnynrflsqsCRFLICQNEIPLETTLDVLRE---AHKrGIYTVFNSAPAPSLAEVGVIKPF--------- 199
Cdd:cd01940 89 ----FGL-------------SNKGGVAREHPFEADLEYLSQfdlVHT-GIYSHEGHLEKALQALVGAGALIsfdfsdrwd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 200 LPYVSLFCPNeVEAAMITGMEVSDgASAAKAAKALQALGVRNVVITLGAQGyVICEMGSEPMHAPGLRVKAVDTTGAGDS 279
Cdd:cd01940 151 DDYLQLVCPY-VDFAFFSASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDG-AIAYDGAVFYSVAPRPVEVVDTLGAGDS 227
|
250 260
....*....|....*....|....*...
gi 70886975 280 FV-GSMVYYMSRGMSLSEACRRANVCAA 306
Cdd:cd01940 228 FIaGFLLSLLAGGTAIAEAMRQGAQFAA 255
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
11-323 |
1.57e-16 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 78.89 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 11 EGSNGPTVVVVGSCFLDYIAYVDripriGETLT-SKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFK 89
Cdd:PLN02323 6 STAESSLVVCFGEMLIDFVPTVS-----GVSLAeAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 90 RNGVDTTNVYRERNGATGLAmiFVdTKTSNNE----IVICPNA-----THALTTEFLRRQSD-NYNR--FLSQSCRF--- 154
Cdd:PLN02323 81 KNGVNNEGVRFDPGARTALA--FV-TLRSDGErefmFYRNPSAdmllrESELDLDLIRKAKIfHYGSisLITEPCRSahl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 155 ----------LICQNEIPLETTLDVLREAHKRGIYTVFNSAPAPSLAEVGVIkpFL-----PY----VSLFCPNeveaam 215
Cdd:PLN02323 158 aamkiakeagALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVE--FLtggddPDddtvVKLWHPN------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 216 itgmevsdgasaakaakalqalgVRNVVITLGAQGyviCEMGSEPMHA--PGLRVKAVDTTGAGDSFVGSMVYYMSRGMS 293
Cdd:PLN02323 230 -----------------------LKLLLVTEGEEG---CRYYTKDFKGrvEGFKVKAVDTTGAGDAFVGGLLSQLAKDLS 283
|
330 340 350
....*....|....*....|....*....|....*..
gi 70886975 294 -------LSEACRRANVCAAFSVQRKGTQSSYPTPDE 323
Cdd:PLN02323 284 lledeerLREALRFANACGAITTTERGAIPALPTKEA 320
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
242-324 |
1.30e-14 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 73.05 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 242 VVITLGAQGYVICEMGSEpMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRG------MSLSEACRRANVCAAFSVQRKGTQ 315
Cdd:PRK09434 216 LLVTLGAEGVLVHTRGQV-QHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQACGALATTAKGAM 294
|
....*....
gi 70886975 316 SSYPTPDEL 324
Cdd:PRK09434 295 TALPNRQEL 303
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
17-314 |
5.23e-14 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 71.28 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 17 TVVVVGSCFLDYIAYVDRIPRIGETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVgSDGDGDEYIAN-FKRNGVDT 95
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVL-SRGPVFESLLDdFQSRGIDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 96 TNVYRERNGaTGLAMIFVDTKTSNNEIVICPNATHALTTEFLRRQSDNYNRFLSQSCRflicQNEIPLETTLDVlrEAHK 175
Cdd:cd01939 80 SHCYRKDID-EPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGR----NPDETLRMMQHI--EEHN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 176 RGiytvfnSAPAPSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVI--TLGAQGYVI 253
Cdd:cd01939 153 NR------RPEIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLvcTWGDQGAGA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886975 254 ceMGSEPMH-----APGLRVkaVDTTGAGDSFVGSMVYYMS-RGMSLSEACRRANVCAAFSVQRKGT 314
Cdd:cd01939 227 --LGPDGEYvhspaHKPIRV--VDTLGAGDTFNAAVIYALNkGPDDLSEALDFGNRVASQKCTGVGF 289
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
32-313 |
1.49e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 66.68 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 32 VDRIPRIGetltsKSFSkgfGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVyRERNGATglAMI 111
Cdd:PRK09813 11 VDIYPQLG-----KAFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-HTKHGVT--AQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 112 FVDTKTSNNeivICPNATHALTTEFlrrqsdnynRFLSQSCRFLiCQNEIpLETTL-----DVLREAHKRGIYTVFNSAP 186
Cdd:PRK09813 80 QVELHDNDR---VFGDYTEGVMADF---------ALSEEDYAWL-AQYDI-VHAAIwghaeDAFPQLHAAGKLTAFDFSD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 187 APSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDgasaakaakalqaLGVRNVVITLGAQGYVICEmGSEPMHAPGL 266
Cdd:PRK09813 146 KWDSPLWQTLVPHLDYAFASAPQEDEFLRLKMKAIVA-------------RGAGVVIVTLGENGSIAWD-GAQFWRQAPE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 70886975 267 RVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:PRK09813 212 PVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
37-324 |
1.83e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 67.53 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 37 RIGETLTSKSFSKGFGGKGANQAVAAGRLGA--------RVAMVGIVGSDGDGDEYIANFKRNGVDTTNVyRERNGATGL 108
Cdd:PLN02813 111 KVLRALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQ-PVKDGTTGT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 109 AMIFVdtktsnneiviCPNATHALTTEFLRRQSDNYNRFLSQS---CRFLICQN---EIP--LETTLDVLREAHKRGIYT 180
Cdd:PLN02813 190 VIVLT-----------TPDAQRTMLSYQGTSSTVNYDSCLASAiskSRVLVVEGylwELPqtIEAIAQACEEAHRAGALV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 181 vfnsapAPSLAEVGVIKPFLP--------YVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQalgVRNVVITLGAQGYV 252
Cdd:PLN02813 259 ------AVTASDVSCIERHRDdfwdvmgnYADILFANSDEARALCGLGSEESPESATRYLSHF---CPLVSVTDGARGSY 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 253 ICEMGsEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMS-LSEACRRANVCAAFSVQRKGTQSSYPTPDEL 324
Cdd:PLN02813 330 IGVKG-EAVYIPPSPCVPVDTCGAGDAYAAGILYGLLRGVSdLRGMGELAARVAATVVGQQGTRLRVEDAVEL 401
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
52-311 |
9.50e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 62.12 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 52 GGKGAN--QAVAAGrLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVyRERNGATGLAMIFVDTkTSNNEIVICpnat 129
Cdd:PLN02379 86 GGSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRL-RAKKGPTAQCVCLVDA-LGNRTMRPC---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 130 halTTEFLRRQSDNYNRFLSQSCRFLICQNEI-PLETTLDVLREAHKRGIYTVFNsapapsLAEVGVIKPFLPY------ 202
Cdd:PLN02379 159 ---LSSAVKLQADELTKEDFKGSKWLVLRYGFyNLEVIEAAIRLAKQEGLSVSLD------LASFEMVRNFRSPllqlle 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 203 ---VSLFCPNEVEAAMITGMEVSDGASAAKAAKALQalgVRNVVITLGAQGyVICEMGSEPMHAPGL-RVKAVDTTGAGD 278
Cdd:PLN02379 230 sgkIDLCFANEDEARELLRGEQESDPEAALEFLAKY---CNWAVVTLGSKG-CIARHGKEVVRVPAIgETNAVDATGAGD 305
|
250 260 270
....*....|....*....|....*....|...
gi 70886975 279 SFVGSMVYYMSRGMSLSEACrRANVCAAFSVQR 311
Cdd:PLN02379 306 LFASGFLYGLIKGLSLEECC-KVGACSGGSVVR 337
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
53-306 |
1.12e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 62.16 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 53 GKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVYRERNGatglamifVDTKTSNNEIVIC-----PN 127
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEGTDA--------GDSSSASYETLLCwvlvdPL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 128 ATHALTTEF----------LRRQSDNYNRFLSQsCRFLICQ----NEIPLETTLDVLREAHKRGIYTVFNSAP-APSL-- 190
Cdd:PLN02341 192 QRHGFCSRAdfgpepafswISKLSAEAKMAIRQ-SKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrGKSLlv 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 191 ---AEVGVIKPFLPYVSLFCPNEVEAAMITGMevsdgASAAKAAKALQALGVRN--VVITLGAQGYVICEMGSEpMHAPG 265
Cdd:PLN02341 271 gtpDERRALEHLLRMSDVLLLTSEEAEALTGI-----RNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSV-SCAPA 344
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 70886975 266 LRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRAN-VCAA 306
Cdd:PLN02341 345 FKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANaVGAA 386
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
186-313 |
4.00e-10 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 60.05 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 186 PAPSLAEVGVIKPF---LPYVSLFCPNEVEAAMITGMEVS-----DGASAAKAAKALQALGVRN---VVITLGAQGYVIC 254
Cdd:cd01943 161 PLPDSCDPENLEDLlqaLPRVDVFSPNLEEAARLLGLPTSepssdEEKEAVLQALLFSGILQDPgggVVLRCGKLGCYVG 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 255 EMGS-EPMHAP---GLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:cd01943 241 SADSgPELWLPayhTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
19-327 |
4.45e-10 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 59.94 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 19 VVVGSCFLDYIAYVD-RIPRIGETLTSKSFSKGfgGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTN 97
Cdd:PRK09954 61 VVVGAINMDIRGMADiRYPQAASHPGTIHCSAG--GVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYR--ERNGATGLAMifvdtKTSNNEIVICPNATHALttEFLRRQSDNYNRFLSQSCRFLICQNEIPLETTldvlreahk 175
Cdd:PRK09954 139 CIRlhGQSTSTYLAI-----ANRQDETVLAINDTHIL--QQLTPQLLNGSRDLIRHAGVVLADCNLTAEAL--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 176 RGIYTVFNSAP----APSLAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGY 251
Cdd:PRK09954 203 EWVFTLADEIPvfvdTVSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 252 VICEMGSE------PMHApglrvkAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSvqRKGTQSSYPTpdeLP 325
Cdd:PRK09954 283 FCSEKDGEqflltaPAHT------TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAIS--RASGSLNNPT---LS 351
|
..
gi 70886975 326 AD 327
Cdd:PRK09954 352 AD 353
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
70-322 |
1.04e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 58.96 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 70 AMVGIVGSDGDGDEYIANFKRNGVdTTNVYRERNGATGL-AMIFVDTKTSnneIVICPNATHALTTEFLRRQSdnyNRFL 148
Cdd:PLN02548 73 SYMGCIGKDKFGEEMKKCATAAGV-NVHYYEDESTPTGTcAVLVVGGERS---LVANLSAANCYKVEHLKKPE---NWAL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 149 SQSCRFLICQN---EIPLETTLDVLREAHKRGIYTVFNSApAPSLAEV--GVIKPFLPYVS-LFCpNEVEA---AMITGM 219
Cdd:PLN02548 146 VEKAKFYYIAGfflTVSPESIMLVAEHAAANNKTFMMNLS-APFICEFfkDQLMEALPYVDfLFG-NETEArtfAKVQGW 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 220 EVSD-GASAAKAAKALQALGV--RNVVITLGAQGYVICEMGSEPMHA--PGLRVKAVDTTGAGDSFVGSMVYYMSRGMSL 294
Cdd:PLN02548 224 ETEDvEEIALKISALPKASGThkRTVVITQGADPTVVAEDGKVKEFPviPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDI 303
|
250 260
....*....|....*....|....*....
gi 70886975 295 SEACRRANVCAAFSVQRKGTqsSYP-TPD 322
Cdd:PLN02548 304 EECVRAGNYAANVIIQRSGC--TYPeKPD 330
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
18-309 |
3.49e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 57.31 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIAYVDRIPRIGETLTSK-SFSKGfgGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGV--D 94
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPGKiKFTPG--GVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVyvD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 95 TTNVYRERNGATGLAMIfvdtkTSNNEIVICPN---ATHALTTEFLRRQSDnynrFLsQSCRFLICQNEIPLETTLDVLR 171
Cdd:PRK09850 85 KCLIVPGENTSSYLSLL-----DNTGEMLVAINdmnISNAITAEYLAQHRE----FI-QRAKVIVADCNISEEALAWILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 172 EAHKRGIYTVFNSApapslAEVGVIKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGY 251
Cdd:PRK09850 155 NAANVPVFVDPVSA-----WKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886975 252 VICEMGSEPMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSV 309
Cdd:PRK09850 230 YYSDISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMAL 287
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
52-326 |
5.87e-09 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 56.57 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 52 GGKGANQA-VAAGRLGA---RVAMVGIVGSDGDGDEYIANFKRNGVDTTNVYRERNGaTGLAMIFVdtktSNNEIVICPN 127
Cdd:PTZ00247 62 GGSALNTArVAQWMLQApkgFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAP-TGTCAVLV----CGKERSLVAN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 128 --ATHALTTEFLrrQSDNYNRFLSQsCRFLICQN---EIPLETTLDVLREAHKRGIYTVFN-SAPAPSLAEVGVIKPFLP 201
Cdd:PTZ00247 137 lgAANHLSAEHM--QSHAVQEAIKT-AQLYYLEGfflTVSPNNVLQVAKHARESGKLFCLNlSAPFISQFFFERLLQVLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 202 YVSLFCPNEVEA-----AMITGME-VSDGASAAKAAKALQALGVRNVVITLGAQG-YVICEMGSEPMHAPGLRV-KAVDT 273
Cdd:PTZ00247 214 YVDILFGNEEEAktfakAMKWDTEdLKEIAARIAMLPKYSGTRPRLVVFTQGPEPtLIATKDGVTSVPVPPLDQeKIVDT 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 70886975 274 TGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGtqSSYP-TPDELPA 326
Cdd:PTZ00247 294 NGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNG--CTYPeKPPFLPW 345
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
30-309 |
9.59e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 55.86 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 30 AY--VDRIPRI--GETLTSKSFSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDeYIANFKRNGVdtTNVYRERNGA 105
Cdd:PRK09513 13 AYdlVGFCPEIerGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDG-FQQLFSELGI--ANRFQVVQGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 106 TglaMIFVDTKTSNNEIvicpnathaltTEF----LRRQSDNYNRFLSQSCRFL-------ICQN---EIPLETTLDVLR 171
Cdd:PRK09513 90 T---RINVKLTEKDGEV-----------TDFnfsgFEVTPADWERFVTDSLSWLgqfdmvaVSGSlprGVSPEAFTDWMT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 172 EAHKRGIYTVFNSAPApslAEVGVIKPfLPYvsLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLGAQGY 251
Cdd:PRK09513 156 RLRSQCPCIIFDSSRE---ALVAGLKA-APW--LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886975 252 V-ICEMGSepMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSV 309
Cdd:PRK09513 230 LwVNASGE--WIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAV 286
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
18-314 |
1.17e-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: 49.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 18 VVVVGSCFLDYIayvdriprigETLTSKSfSKGFGGKGANQAVAAGrLGARVAMVGIVGSDGDgDEYIANFKRNGVDTTN 97
Cdd:cd01946 2 LLVVGSVAFDAI----------ETPFGKV-DKALGGSATYFSLSAS-YFTDVRLVGVVGEDFP-EEDYKLLNSHNIVTLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 98 VYRERNGATglamiFVDTKTSNNEIvicpNATHALTTE------FLRRQSDNYnrflsQSCRFLICQNEIPlettlDVLR 171
Cdd:cd01946 69 LLSKEDGKT-----FHWAGRYHYDL----NEADTLDTDlnvfadFDPQLPEHY-----KDSEFVFLGNIAP-----ELQR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 172 EahkrgiytVFNSAPAPSLAEVGV------IKP-----FLPYVSLFCPNEVEAAMITGMevsdgASAAKAAKALQALGVR 240
Cdd:cd01946 130 E--------VLEQVKDPKLVVMDTmnfwisIKPeklkkVLAKVDVVIINDGEARQLTGA-----ANLVKAARLILAMGPK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 241 NVVITLGAQGYVICEmGSEPMHAPGLRVKAV-DTTGAGDSFVGSMVYYMSRGMSLSEA-CRRA----NVCAAFSVQRKGT 314
Cdd:cd01946 197 ALIIKRGEYGALLFT-DDGYFAAPAYPLESVfDPTGAGDTFAGGFIGYLASQKDTSEAnMRRAiiygSAMASFCVEDFGT 275
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
161-315 |
2.98e-06 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 48.24 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 161 IPLETTLDVLREAHKRGIYTVFNS-----APAPSLAEVGVIKPflpyvslfcpNEVEAAMITGMEVSDGASAAKAAKALQ 235
Cdd:PRK10294 144 VKLEKLTQLISAAQKQGIRCIIDSsgdalSAALAIGNIELVKP----------NQKELSALVNRDLTQPDDVRKAAQELV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 236 ALGV-RNVVITLGAQGYV-ICEMGSEPMHAPglRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:PRK10294 214 NSGKaKRVVVSLGPQGALgVDSENCIQVVPP--PVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQG 291
|
..
gi 70886975 314 TQ 315
Cdd:PRK10294 292 TR 293
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
198-307 |
3.17e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 47.78 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 198 PFLPYVSLFCPNEVEAAMI-TGMEVSDGASAAkaakalqalGVRNVVITLGAQGYVICEMGSePMHAPGLRVKAVDTTGA 276
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVIsTPTELARLIKET---------GVKEIIVTDGEEGGYIFDGNG-KYTIPASKKDVVDPTGA 220
|
90 100 110
....*....|....*....|....*....|.
gi 70886975 277 GDSFVGSMVYYMSRGMSLSEACRRANVCAAF 307
Cdd:cd01937 221 GDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
244-324 |
8.03e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 44.05 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 244 ITLGAQGYVICEMGSEPMHAPGlRVKAV-DTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKGTQSSypTPD 322
Cdd:PRK11316 230 VTRSEQGMTLLQPGKAPLHLPT-QAREVyDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTV--SPI 306
|
..
gi 70886975 323 EL 324
Cdd:PRK11316 307 EL 308
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
47-109 |
2.60e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 42.59 E-value: 2.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886975 47 FSKGFGGKGANQAVAAGRLGARVAMVGIVGSDGDGDEYIANFKRNGVDTTNVYRERNGATGLA 109
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACS 229
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
242-313 |
1.07e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 40.18 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886975 242 VVITLGAQGYVICEMGSEpMHAPGLRVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRANVCAAFSVQRKG 313
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGE-MRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
196-301 |
1.38e-03 |
|
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: 39.77 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 196 IKPFLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVIT----LGAQGY---VICEmGSEPMHAPGLRV 268
Cdd:pfam08543 113 KEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVvtdVLYD-GGGFYTLEAPRI 191
|
90 100 110
....*....|....*....|....*....|...
gi 70886975 269 KAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRA 301
Cdd:pfam08543 192 PTKNTHGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
199-301 |
3.11e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 38.51 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886975 199 FLPYVSLFCPNEVEAAMITGMEVSDGASAAKAAKALQALGVRNVVITLG--------------AQGYVICEmgsepmhAP 264
Cdd:PRK12413 126 FFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGnrlsqkkaidlfydGKEFVILE-------SP 198
|
90 100 110
....*....|....*....|....*....|....*..
gi 70886975 265 glrVKAVDTTGAGDSFVGSMVYYMSRGMSLSEACRRA 301
Cdd:PRK12413 199 ---VLEKNNIGAGCTFASSIASQLVKGKSPLEAVKNS 232
|
|
| |
