|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
19-312 |
3.40e-106 |
|
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: 311.46 E-value: 3.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 19 GSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATS 98
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 99 AAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVLNPAPA 178
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 179 VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNaARHYPAPAVQAV 258
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE-SKLIPAFKVKAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981689685 259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
14-307 |
3.22e-105 |
|
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: 308.71 E-value: 3.22e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVL 173
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 NPAPAVAPLPAgWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADnAARHYPAP 253
Cdd:cd01174 161 NPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGG-EVEHVPAF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPT 307
Cdd:cd01174 239 KVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
8-311 |
1.10e-76 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 237.33 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 8 GAPRAGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEA 87
Cdd:PTZ00292 11 GGEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 88 EGIDCAGLATSAAASTGVALIVVDDA-SQNAIVIVAGGNGEVTP-DTIARHDAAIAAADVLICQLETPADAVFAALAAGR 165
Cdd:PTZ00292 91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPqMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 166 RLGRTVVLNPAPAVAPLPAG----WLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLAL 241
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 242 TADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
12-311 |
3.11e-76 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 235.53 E-value: 3.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 12 AGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGID 91
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 92 CAGLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTV 171
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 172 VLNPAPAVAPLPAgWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARhYP 251
Cdd:PRK11142 162 ILNPAPARELPDE-LLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQR-VP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 252 APAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:PRK11142 240 GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEI 299
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
14-311 |
3.01e-67 |
|
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: 212.44 E-value: 3.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL---ICQLETPADAVFAALAAGRRLGRT 170
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLggiTLASEPPREALLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLN------PAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPirdpaDAEAAARALQAGGARNVLVTLGARGVLALTAD 244
Cdd:COG0524 161 VSLDpnyrpaLWEPARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981689685 245 NAArHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:COG0524 236 EVV-HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
14-302 |
2.04e-57 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 186.78 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPlpGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL----ICQLETPADAVFAALAAGRRLGR 169
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 170 T--VVLNPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAA 247
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 248 RHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:pfam00294 239 HVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
14-307 |
2.35e-37 |
|
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: 134.34 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETpadaVFAALAAGRRLGRTVVL 173
Cdd:cd01945 81 FIVVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEA----ALHLAQEARARGIPIPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 NPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAAralqagGARNVLVTLGARGVLALTADNAARHYPAP 253
Cdd:cd01945 157 DLDGGGLRVLEELLPLADHAICSENFLRPNTGSADDEALELLASL------GIPFVAVTLGEAGCLWLERDGELFHVPAF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPT 307
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
14-302 |
5.70e-33 |
|
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: 122.80 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLP-LPGETLAGHAFaQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDC 92
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPgPFESVLVKDLR-REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 93 AGLATSAAASTGVALIVVDDaSQNAIVIVA-GGNGEVTPDTIARHDAAIAaadvlICQLETPADAVFAALAAGRRlGRTV 171
Cdd:cd01942 80 SHVRVVDEDSTGVAFILTDG-DDNQIAYFYpGAMDELEPNDEADPDGLAD-----IVHLSSGPGLIELARELAAG-GITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 172 VL----NPAPAVAPLPAGWLPLVDYLIPNEVEAAAL---TGLPirdpadaeaaaRALQAGGARNVLVTLGARGVLALTAD 244
Cdd:cd01942 153 SFdpgqELPRLSGEELEEILERADILFVNDYEAELLkerTGLS-----------EAELASGVRVVVVTLGPKGAIVFEDG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 245 NAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:cd01942 222 EEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
14-301 |
1.27e-28 |
|
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: 111.51 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETlaghaFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADS-----FRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 GLATSAAASTGVALIVVDDASQNAIVIVAGGN--GEVTPDtIARHDAAIAAADVLIC-----QLETPADAVFAALAAGRR 166
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSaaSRLTPE-DLDEAALAGADHLHLSgitlaLSESAREALLEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 167 LGRTVV--------LNPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALqagGARNVLVTLGARGV 238
Cdd:cd01166 155 RGVTVSfdlnyrpkLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALAL---GVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981689685 239 LALTADnAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01166 232 LVYTGG-GRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
34-301 |
7.33e-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: 106.95 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 34 LPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALIVVDDA 113
Cdd:cd01167 13 IPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 114 SQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQL----ETPADAVFAALAAGRRLGRTVVL---------NPAPAVA 180
Cdd:cd01167 93 GERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIalasEPSRSALLELLEAAKKAGVLISFdpnlrpplwRDEEEAR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 181 PLPAGWLPLVDYLIPNEVEAAALTGLpirdpADAEAAARALQAGGARNVLVTLGARGVLALTADNAArHYPAPAVQAVDT 260
Cdd:cd01167 173 ERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVG-EVPGIPVEVVDT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 981689685 261 TAAGDTFIGGFAAQLAAG-------ADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01167 247 TGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAGA 294
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
15-296 |
2.22e-26 |
|
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: 105.47 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 15 VTVVGSLNMDLVVRAPRLPLPGETLAGHAFaQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAG 94
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPGHVK-QSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 95 LATSAAaSTGVALIVVDdasQNAIVIVAGGN----GEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRT 170
Cdd:cd01941 81 IVFEGR-STASYTAILD---KDGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLNPAPAV-APLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLA--LTADNAA 247
Cdd:cd01941 157 VAFEPTSAPkLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLssREGGVET 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 981689685 248 RHYPAPAVQAV-DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSV 296
Cdd:cd01941 237 KLFPAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
48-313 |
9.17e-23 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 96.03 E-value: 9.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALIVVDDASQnaIVIVAGGNGE 127
Cdd:COG2870 55 PGG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGGQQ--LLRLDFEDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 128 VTPDTIARHDAAIAAAD-----VLICQ-----LETPADAVFAALAAgRRLGRTVVLNPAPAVAPLPAGwlplVDYLIPNE 197
Cdd:COG2870 132 PLSAELEARLLAALEAAlpevdAVILSdygkgVLTPELIQALIALA-RAAGKPVLVDPKGRDFSRYRG----ATLLTPNL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 198 VEAAALTGLPIRDPADAEAAARAL-QAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLA 276
Cdd:COG2870 207 KEAEAAVGIPIADEEELVAAAAELlERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALA 286
|
250 260 270
....*....|....*....|....*....|....*..
gi 981689685 277 AGADVDAAIRFAQRAAALSVTRAGAQPsiPTLAELAD 313
Cdd:COG2870 287 AGASLEEAAELANLAAGIVVGKLGTAT--VSPEELLA 321
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
36-304 |
3.94e-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: 91.52 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 36 GETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDcAGLATSAAASTGVALIVVDDASQ 115
Cdd:cd01168 42 EELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVD-TRYQVQPDGPTGTCAVLVTPDAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 116 NAIVIVAGGNGEVTPDTIARHDAAIAAadvlICQLE-----TPADAVFAALAAGRRLGRTVVLNPAPAVAP-----LPAG 185
Cdd:cd01168 121 RTMCTYLGAANELSPDDLDWSLLAKAK----YLYLEgylltVPPEAILLAAEHAKENGVKIALNLSAPFIVqrfkeALLE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 186 WLPLVDYLIPNEVEAAALTGLpirDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGD 265
Cdd:cd01168 197 LLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGD 273
|
250 260 270
....*....|....*....|....*....|....*....
gi 981689685 266 TFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPS 304
Cdd:cd01168 274 AFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
24-313 |
2.94e-20 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 88.65 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 24 DLVVRAPRLpLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAhGAALRAGLEAEGIDCAGLATsaAAST 103
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPI--EGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 104 GVALIVVDDASQNAIVIVAGGNgEVTPDTIAR-----HDAAIAAADVLIC---QLETPADAVFAALAAGRRLGRTVVLNP 175
Cdd:COG1105 87 RINIKIVDPSDGTETEINEPGP-EISEEELEAllerlEELLKEGDWVVLSgslPPGVPPDFYAELIRLARARGAKVVLDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 176 APAVAPLPAGWLPlvdYLI-PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADnAARHYPAPA 254
Cdd:COG1105 166 SGEALKAALEAGP---DLIkPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTED-GVYRAKPPK 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 981689685 255 VQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQpsIPTLAELAD 313
Cdd:COG1105 242 VEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG--LPDREDVEE 298
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
14-300 |
1.20e-16 |
|
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: 78.62 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 gLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAAdVLIC--QLETPADAVFAALAAGRRL--GR 169
Cdd:cd01944 80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDY-VYLSgyTLASENASKVILLEWLEALpaGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 170 TVVLNPAPAVAPLPAGWLPLVDYLIP----NEVEAAALTGlpiRDPADAEAAARALQAGGARNVLVTLGARGVLALTADN 245
Cdd:cd01944 158 TLVFDPGPRISDIPDTILQALMAKRPiwscNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 246 AARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01944 235 NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
229-312 |
1.46e-15 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 75.74 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 229 VLVTLGARGVLALTADNAaRHYPAPAVQAVDTTAAGDTFIGGFAAQLAAG------ADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:PRK09434 216 LLVTLGAEGVLVHTRGQV-QHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQACGALATTAKGAM 294
|
90
....*....|
gi 981689685 303 PSIPTLAELA 312
Cdd:PRK09434 295 TALPNRQELE 304
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
48-306 |
2.33e-15 |
|
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: 74.90 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLaTSAAASTGVALIVVDDASQ------------ 115
Cdd:cd01172 39 LGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTTKTRVIARNQQllrvdreddspl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 116 -------------------NAIVIVAGGNGEVTPDTIArhdaaiaaadvLICQLetpadavfaalaaGRRLGRTVVLNPA 176
Cdd:cd01172 117 saeeeqrlieriaerlpeaDVVILSDYGKGVLTPRVIE-----------ALIAA-------------ARELGIPVLVDPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 177 PAVAPLPAGwlplVDYLIPNEVEAAALTGLPIRDPADAEAAARALQ-AGGARNVLVTLGARGVLALTADNAARHYPAPAV 255
Cdd:cd01172 173 GRDYSKYRG----ATLLTPNEKEAREALGDEINDDDELEAAGEKLLeLLNLEALLVTLGEEGMTLFERDGEVQHIPALAK 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 981689685 256 QAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIP 306
Cdd:cd01172 249 EVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
14-276 |
3.57e-15 |
|
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: 72.51 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGcvgadahgaalragleaegIDCA 93
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG-------------------ADAV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 94 gLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAiaaadvlicqletpadavfaalaagrrlgrtvvl 173
Cdd:cd00287 62 -VISGLSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKL---------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 npapavaplpagwLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAP 253
Cdd:cd00287 107 -------------LPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAF 173
|
250 260
....*....|....*....|...
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLA 276
Cdd:cd00287 174 PVKVVDTTGAGDAFLAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
23-300 |
2.06e-14 |
|
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: 72.18 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 23 MDLVVRAPRLpLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADaHGAALRAGLEAEGID----------- 91
Cdd:cd01164 11 IDLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPddfvevagetr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 92 ----------------CAGLATSAAASTGVALIVVDDASQNAIVIVAGgngEVTPDTiarhdaaiaaadvlicqletPAD 155
Cdd:cd01164 89 invkikeedgteteinEPGPEISEEELEALLEKLKALLKKGDIVVLSG---SLPPGV--------------------PAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 156 AVFAALAAGRRLGRTVVLNPAPAVAPLPAGWLPlvdYLI-PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLG 234
Cdd:cd01164 146 FYAELVRLAREKGARVILDTSGEALLAALAAKP---FLIkPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981689685 235 ARGVLALTADNAArHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01164 223 ADGALLVTKDGVY-RASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
49-301 |
7.78e-12 |
|
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: 64.30 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 49 GGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATsAAASTGVALIVVDDASQNAIVIVAGGNGEV 128
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV-KEGENAVADVELVDGDRIFGLSNKGGVARE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 129 TPDTIARHdaaiaaadvLICQLETPADAVFAALAAGRRLGRTVVLNPAPAVAPLPAGW-LPLVDYLIPNeVEAAALTGlP 207
Cdd:cd01940 101 HPFEADLE---------YLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFSDRWdDDYLQLVCPY-VDFAFFSA-S 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 208 IRDPADAEAAARALQAGGARNVLVTLGARGVLALtADNAARHYPAPAVQAVDTTAAGDTFIGGF-AAQLAAGADVDAAIR 286
Cdd:cd01940 170 DLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRPVEVVDTLGAGDSFIAGFlLSLLAGGTAIAEAMR 248
|
250
....*....|....*
gi 981689685 287 FAQRAAALSVTRAGA 301
Cdd:cd01940 249 QGAQFAAKTCGHEGA 263
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
230-310 |
2.85e-09 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 57.32 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 230 LVTLGARGVLALTADNAARhYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADV-------DAAIRFAQRAAALSVTRAGAQ 302
Cdd:PLN02323 234 LVTEGEEGCRYYTKDFKGR-VEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLledeerlREALRFANACGAITTTERGAI 312
|
....*...
gi 981689685 303 PSIPTLAE 310
Cdd:PLN02323 313 PALPTKEA 320
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
224-297 |
3.41e-09 |
|
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: 56.64 E-value: 3.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981689685 224 GGARNVLVTLGARGVLALTaDNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVT 297
Cdd:cd01937 182 TGVKEIIVTDGEEGGYIFD-GNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
187-313 |
9.81e-09 |
|
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: 55.81 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIR-------DPADAEAAARALQAGGARNVLVT-LGARGVLALTADNA-ARHYPA---PA 254
Cdd:cd01943 178 LPRVDVFSPNLEEAARLLGLPTSepssdeeKEAVLQALLFSGILQDPGGGVVLrCGKLGCYVGSADSGpELWLPAyhtKS 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 981689685 255 VQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGaqpsIPTLAELAD 313
Cdd:cd01943 258 TKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG----LPRLTKVEG 312
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
187-300 |
1.25e-08 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 55.49 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALT------GLPIRDPADAEAAARALQAGGARNVLVTLGARGVLaLTADNAARHYPA---PAVQA 257
Cdd:PLN02548 201 LPYVDFLFGNETEARTFAkvqgweTEDVEEIALKISALPKASGTHKRTVVITQGADPTV-VAEDGKVKEFPViplPKEKL 279
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 981689685 258 VDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:PLN02548 280 VDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSG 322
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
15-301 |
1.63e-08 |
|
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: 54.73 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 15 VTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIdcAG 94
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 95 LATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTP-------DTIARHDAAIAAADVLICqletpadavfaalaagrRL 167
Cdd:cd01947 80 TVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKwpildegDGVFITAAAVDKEAIRKC-----------------RE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 168 GRTVVLNPAPAVAPLPAGW-LPLVDYLIPNEVEAAALTglpirdpadaeaAARALQAGGARNVLVTLGARGVLALTAdNA 246
Cdd:cd01947 143 TKLVILQVTPRVRVDELNQaLIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPG-GR 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 247 ARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01947 210 YNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
229-300 |
1.95e-08 |
|
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: 54.72 E-value: 1.95e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981689685 229 VLVTLGARGVLALTADNAARHYPA-PAVQAVDTTAAGDTFIGGFAAQLA-AGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01939 215 LVCTWGDQGAGALGPDGEYVHSPAhKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
187-284 |
2.06e-08 |
|
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: 54.39 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPirdpaDAEAAARALQAGGARNVLVTLGARGVLALTADN--AARHYPAPAVqaVDTTAAG 264
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDDGyfAAPAYPLESV--FDPTGAG 233
|
90 100
....*....|....*....|
gi 981689685 265 DTFIGGFAAQLAAGADVDAA 284
Cdd:cd01946 234 DTFAGGFIGYLASQKDTSEA 253
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
187-301 |
5.48e-08 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 53.49 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALT---GLP---IRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAaRHYPAPAVQA--- 257
Cdd:PTZ00247 212 LPYVDILFGNEEEAKTFAkamKWDtedLKEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGV-TSVPVPPLDQeki 290
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 981689685 258 VDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PTZ00247 291 VDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGC 334
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
225-301 |
6.88e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 52.82 E-value: 6.88e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981689685 225 GARNVLVTLGARGVLALTADNAARHYPAPaVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PRK09813 184 GAGVVIVTLGENGSIAWDGAQFWRQAPEP-VTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
6-272 |
1.36e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 52.53 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 6 TGGAPRAGR---VTVVGSLNMDLVVRAPRLPLPG--------ETLAGHAFAQAAGGKGGN--QAVAAARLGAQVAMIGCV 72
Cdd:PLN02341 63 TEVGSAAGKeidVATLGNLCVDIVLPVPELPPPSreerkaymEELAASPPDKKSWEAGGNcnFAIAAARLGLRCSTIGHV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 73 GADAHGAALRAGLEAEGIDCAGLA--------TSAAASTGVALIVVDDASQNAIVIVAGGNGEVT----PDTIARHDAAI 140
Cdd:PLN02341 143 GDEIYGKFLLDVLAEEGISVVGLIegtdagdsSSASYETLLCWVLVDPLQRHGFCSRADFGPEPAfswiSKLSAEAKMAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 141 AAADVLICQ----LETPADAVFAALAAGRRLGRTVVLNPAPAVAPLPAG----------WLPLVDYLIPNEVEAAALTGL 206
Cdd:PLN02341 223 RQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGtpderralehLLRMSDVLLLTSEEAEALTGI 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 207 --PIRDPADAEAAARalqagGARNVLVTLGARGVLALTADNAARhYPAPAVQAVDTTAAGDTFIGGFA 272
Cdd:PLN02341 303 rnPILAGQELLRPGI-----RTKWVVVKMGSKGSILVTRSSVSC-APAFKVNVVDTVGCGDSFAAAIA 364
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
17-309 |
3.57e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 51.09 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 17 VVGSLNMDLVVRAPrLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLA 96
Cdd:PRK09954 62 VVGAINMDIRGMAD-IRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 97 TSAAASTGVALIVvddASQNAIVIVAGGNG----EVTPDTIARHDAAIAAADVLI--CQLeTPADAVFAALAAGrrlGRT 170
Cdd:PRK09954 141 RLHGQSTSTYLAI---ANRQDETVLAINDThilqQLTPQLLNGSRDLIRHAGVVLadCNL-TAEALEWVFTLAD---EIP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLNPAPA-VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARH 249
Cdd:PRK09954 214 VFVDTVSEfKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 250 YPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSvtRAGAQPSIPTLA 309
Cdd:PRK09954 294 LTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAIS--RASGSLNNPTLS 351
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
230-301 |
2.32e-06 |
|
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: 48.67 E-value: 2.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981689685 230 LVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PRK11316 229 LVTRSEQGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT 300
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
187-290 |
3.74e-06 |
|
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: 47.09 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLG------ARGVLALTADNAARHYPAPAVQAVDT 260
Cdd:pfam08543 117 LPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeAVVTDVLYDGGGFYTLEAPRIPTKNT 196
|
90 100 110
....*....|....*....|....*....|
gi 981689685 261 TAAGDTFIGGFAAQLAAGADVDAAIRFAQR 290
Cdd:pfam08543 197 HGTGCTLSAAIAANLAKGLSLPEAVREAKE 226
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
229-308 |
1.61e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 45.95 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 229 VLVTLGARGVLALTADNAARHYPAPAVQaVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGaqpsIPTL 308
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQ-VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG----IPKF 280
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
195-297 |
1.67e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.84 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 195 PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPaPAVQAVDTTAAGDTFIGGFAAQ 274
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP-PACDVVSTVGAGDSMVGGLIYG 264
|
90 100
....*....|....*....|...
gi 981689685 275 LAAGADVDAAIRFAQRAAALSVT 297
Cdd:PRK09513 265 LLMRESSEHTLRLATAVSALAVS 287
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
37-312 |
1.75e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 45.96 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 37 ETLAGHAFAQAAGGKGGNQAVAAARLGAQ--------VAMIGCVGADAHGAALRAGLEAEGIDCAGlATSAAASTGVALI 108
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFLS-QPVKDGTTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 109 VVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL---ICQLETPADAVFAALAAGRRLGRTVVLNPAPAVAPL--- 182
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLVVegyLWELPQTIEAIAQACEEAHRAGALVAVTASDVSCIErhr 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 183 PAGWLPL---VDYLIPNEVEAAALTGLPIRDPADAEAAARALQaggARNVLVTLGARGVLALTADNAARHYPAPAVqAVD 259
Cdd:PLN02813 273 DDFWDVMgnyADILFANSDEARALCGLGSEESPESATRYLSHF---CPLVSVTDGARGSYIGVKGEAVYIPPSPCV-PVD 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981689685 260 TTAAGDTFIGGFAAQLAAGA-DVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:PLN02813 349 TCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQGTRLRVEDAVELA 402
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
187-290 |
2.80e-05 |
|
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: 44.64 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT----LGARGVLALTADNAARHYPAPAVQAVDTTA 262
Cdd:COG0351 124 LPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlPGDEAVDVLYDGDGVREFSAPRIDTGNTHG 203
|
90 100
....*....|....*....|....*...
gi 981689685 263 AGDTFIGGFAAQLAAGADVDAAIRFAQR 290
Cdd:COG0351 204 TGCTLSSAIAALLAKGLDLEEAVREAKE 231
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
195-300 |
5.84e-05 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 44.00 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 195 PNEVEAAALTGLPIRD-PADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAPaVQAVDTTAAGDTFIGGFAA 273
Cdd:PRK10294 186 PNQKELSALVNRDLTQpDDVRKAAQELVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPP-VKSQSTVGAGDSMVGAMTL 264
|
90 100
....*....|....*....|....*..
gi 981689685 274 QLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:PRK10294 265 KLAENASLEEMVRFGVAAGSAATLNQG 291
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
187-311 |
7.58e-05 |
|
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: 43.60 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT--------LGARGVLALTADnAARHYPAPAVqAV 258
Cdd:COG2240 136 VPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTAD-GAWLVETPLL-PF 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRA--AALSVTRAGAQPSIPTLAEL 311
Cdd:COG2240 214 SPNGTGDLFAALLLAHLLRGKSLEEALERAAAFvyEVLERTAAAGSDELLLEAAL 268
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
43-108 |
8.57e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 43.46 E-value: 8.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981689685 43 AFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALI 108
Cdd:PLN02323 37 AFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFV 102
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
15-297 |
1.49e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 42.67 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 15 VTVVGSLNMDLVvraprlplpGETLAGHAFAQA--------AGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLE 86
Cdd:PRK09850 7 VVIIGSANIDVA---------GYSHESLNYADSnpgkikftPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 87 AEGI---DC---AGLATSAAAS----TGVALIVVDDAS-----------------QNAIVIVAGGNgeVTPDTIARHDAA 139
Cdd:PRK09850 78 QSGVyvdKClivPGENTSSYLSlldnTGEMLVAINDMNisnaitaeylaqhrefiQRAKVIVADCN--ISEEALAWILDN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 140 IAAADVLIcqleTPADAVFAALAAGRrlgrtvvlnpapavaplpagwLPLVDYLIPNEVEAAALTGLPIRDPADAEAAAR 219
Cdd:PRK09850 156 AANVPVFV----DPVSAWKCVKVRDR---------------------LNQIHTLKPNRLEAETLSGIALSGREDVAKVAA 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 220 ALQAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVT 297
Cdd:PRK09850 211 WFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
187-288 |
5.27e-04 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 40.88 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAG-GARNVLVTLGARGVLALTAD-----NAARHYPAPAVQAVDT 260
Cdd:PRK06427 131 LPLATLITPNLPEAEALTGLPIADTEDEMKAAARALHAlGCKAVLIKGGHLLDGEESVDwlfdgEGEERFSAPRIPTKNT 210
|
90 100
....*....|....*....|....*...
gi 981689685 261 TAAGDTFIGGFAAQLAAGADVDAAIRFA 288
Cdd:PRK06427 211 HGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
48-92 |
2.23e-03 |
|
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: 39.43 E-value: 2.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 981689685 48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDC 92
Cdd:PRK11316 50 PGG-AANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKC 93
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
44-81 |
3.02e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 39.12 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|....*...
gi 981689685 44 FAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAAL 81
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEEL 204
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
187-289 |
6.87e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 37.35 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT----LGARGVLALTADNAARHYPAPAVQAVDTTA 262
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKggnrLSQKKAIDLFYDGKEFVILESPVLEKNNIG 206
|
90 100
....*....|....*....|....*..
gi 981689685 263 AGDTFIGGFAAQLAAGADVDAAIRFAQ 289
Cdd:PRK12413 207 AGCTFASSIASQLVKGKSPLEAVKNSK 233
|
|
|