|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
14-241 |
1.04e-86 |
|
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: 261.07 E-value: 1.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 14 IVLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTS 93
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 94 FCMSAKDGASHFNYvIVDNQTNTRTCIYTPGYPPLLPDDLTESLlldvLDGVRVLYVNGRSREAELLLAQKAHSKNIPIL 173
Cdd:cd01945 81 FIVVAPGARSPISS-ITDITGDRATISITAIDTQAAPDSLPDAI----LGGADAVLVDGRQPEAALHLAQEARARGIPIP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 174 INAE--KKRTgLDELIDLADYAICSTNFPQEWTGapsSPSALLSMLIRLPKLKFVIMTLGEHGCVMLERC 241
Cdd:cd01945 156 LDLDggGLRV-LEELLPLADHAICSENFLRPNTG---SADDEALELLASLGIPFVAVTLGEAGCLWLERD 221
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
15-240 |
2.36e-36 |
|
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: 131.93 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSF 94
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 95 CMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPLLPDDLTEslllDVLDGVRVLYVNG------RSREAELLLAQKAHSK 168
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE----ALLAGADILHLGGitlasePPREALLAALEAARAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063735929 169 NIPILINA-------EKKRTGLDELIDLADYAICSTNFPQEWTGAPsSPSALLSMLIRLPkLKFVIMTLGEHGCVMLER 240
Cdd:COG0524 158 GVPVSLDPnyrpalwEPARELLRELLALVDILFPNEEEAELLTGET-DPEEAAAALLARG-VKLVVVTLGAEGALLYTG 234
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
19-240 |
1.90e-19 |
|
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: 86.45 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 19 GQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSA 98
Cdd:cd01174 6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 99 KDGASHFNYVIVDNqTNTRTCIYTPG---YppLLPDDLTESllLDVLDGVRVLYV-NGRSREAELLLAQKAHSKNIPILI 174
Cdd:cd01174 86 VGAPTGTAVITVDE-SGENRIVVVPGangE--LTPADVDAA--LELIAAADVLLLqLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063735929 175 NAEKKRTGLDELIDLADYAICSTNFPQEWTGAPSSPS---ALLSMLIRLPKLKFVIMTLGEHGCVMLER 240
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEedaEKAARLLLAKGVKNVIVTLGAKGALLASG 229
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
41-235 |
1.12e-16 |
|
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: 78.39 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 41 GTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSfcmsakdgashfnYVIVDNQTNTRTCI 120
Cdd:cd01166 23 ADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS-------------HVRVDPGRPTGLYF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 121 YTPGYPP---------------LLPDDLTEslllDVLDGVRVLYVNG-------RSREAELLLAQKAHSKNIPI------ 172
Cdd:cd01166 90 LEIGAGGerrvlyyragsaasrLTPEDLDE----AALAGADHLHLSGitlalseSAREALLEALEAAKARGVTVsfdlny 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063735929 173 ---LINAEKKRTGLDELIDLADYAICSTNFPQEWTGAPSSPSALLSMLIRLPKLKFVIMTLGEHGC 235
Cdd:cd01166 166 rpkLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGA 231
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
34-236 |
1.37e-16 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 78.15 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 34 IPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSAKDGASHFNYVIVDNQ 113
Cdd:pfam00294 19 LPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 114 TNTRTCIYTPGYPPLLPDDLTESLLLdvLDGVRVLYVNGR----SREAELLLAQKA---HSKNIPILIN-AEKKRTGLDE 185
Cdd:pfam00294 99 GERTIVFNRGAAADLTPEELEENEDL--LENADLLYISGSlplgLPEATLEELIEAaknGGTFDPNLLDpLGAAREALLE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063735929 186 LIDLADYAICSTNFPQEWTGAPSSPSALLsmLIRLPKLKF-----VIMTLGEHGCV 236
Cdd:pfam00294 177 LLPLADLLKPNEEELEALTGAKLDDIEEA--LAALHKLLAkgiktVIVTLGADGAL 230
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
14-239 |
6.72e-16 |
|
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: 76.20 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 14 IVLGCGQLCLDYLVTVASFP-------IPDQKIRGtsfkvqgGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELE 86
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPgpfesvlVKDLRREF-------GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 87 SSGVDTSFCMSAKDGASHFNYVIVDnQTNTRTCIYTPGYPPLlpddLTESLLLDVLDGVRVLYVNGRSREAEllLAQKAH 166
Cdd:cd01942 74 EEGVDTSHVRVVDEDSTGVAFILTD-GDDNQIAYFYPGAMDE----LEPNDEADPDGLADIVHLSSGPGLIE--LARELA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063735929 167 SKNIPILINA--EKKRTGLDELID---LADYAICSTNfpqEWtGAPSSPSALLSMLIRLpKLKFVIMTLGEHGCVMLE 239
Cdd:cd01942 147 AGGITVSFDPgqELPRLSGEELEEileRADILFVNDY---EA-ELLKERTGLSEAELAS-GVRVVVVTLGPKGAIVFE 219
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
15-234 |
1.81e-15 |
|
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: 75.14 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSF 94
Cdd:cd01939 2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 95 CMSaKDGASHFNYVIVDNQTNTRTCIYtpgYPPLLPDDLTESLLLDVLDGVRVLYVNGRSREAELLLAQKAHSKN----- 169
Cdd:cd01939 82 CYR-KDIDEPASSYIIRSRAGGRTTIV---NDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNnrrpe 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 170 IPILINAE--KKRTGLDELIDLADYAICSTNFPQE--WTgapsSPSALLSMLIRLPKLK-FVIMTLGEHG 234
Cdd:cd01939 158 IRITISVEveKPREELLELAAYCDVVFVSKDWAQSrgYK----SPEECLRGEGPRAKKAaLLVCTWGDQG 223
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
49-239 |
2.06e-14 |
|
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: 72.26 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPL 128
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 129 LPDDLTESLlldvLDGVRVLYVNG----RSREAELLLAQKAHSKNIPILINA------EKKRTGLDELIDLADYAICSTN 198
Cdd:cd01168 134 SPDDLDWSL----LAKAKYLYLEGylltVPPEAILLAAEHAKENGVKIALNLsapfivQRFKEALLELLPYVDILFGNEE 209
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063735929 199 FPQEWTGAP--SSPSALLSMLIRLPKLkfVIMTLGEHGCVMLE 239
Cdd:cd01168 210 EAEALAEAEttDDLEAALKLLALRCRI--VVITQGAKGAVVVE 250
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
34-235 |
1.64e-13 |
|
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: 69.59 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 34 IPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFC------------MSAKDG 101
Cdd:cd01167 13 IPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIqfdpaapttlafVTLDAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 102 ASHfNYVIVDNQTNTRTciytpgyppllpddLTESLLLDVLDGVRVLY------VNGRSREAELLLAQKAHSKNIPILI- 174
Cdd:cd01167 93 GER-SFEFYRGPAADLL--------------LDTELNPDLLSEADILHfgsialASEPSRSALLELLEAAKKAGVLISFd 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063735929 175 ---------NAEKKRTGLDELIDLADYAICSTnfpQEWTG-APSSPSALLSMLIRLPKLKFVIMTLGEHGC 235
Cdd:cd01167 158 pnlrpplwrDEEEARERIAELLELADIVKLSD---EELELlFGEEDPEEIAALLLLFGLKLVLVTRGADGA 225
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
5-239 |
3.72e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 5 SDEAIPGQPIVLgCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEE 84
Cdd:PTZ00292 9 SHGGEAEPDVVV-VGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 85 LESSGVDTSFCMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPLLPDDLTESLLLDVLDGVRVLYV-NGRSREAELLLAQ 163
Cdd:PTZ00292 88 FKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICqNEIPLETTLDALK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 164 KAHSKNIPILIN---AEKKRTG--LDELIDLADYAICSTNFPQEWTGAPSSPSALLSMLIR-LPKLKF--VIMTLGEHGC 235
Cdd:PTZ00292 168 EAKERGCYTVFNpapAPKLAEVeiIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKeLQQLGVenVIITLGANGC 247
|
....
gi 1063735929 236 VMLE 239
Cdd:PTZ00292 248 LIVE 251
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
24-234 |
1.21e-06 |
|
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: 48.95 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 24 DYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSakDGAS 103
Cdd:cd01947 11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWR--DKPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 104 HFNYVIVDNqtNTRTCIYTPGYPpllpddLTESLLLDVLDGVRVLYVNGRSREAELLlaQKAHSKNIPILINAEKKR-TG 182
Cdd:cd01947 89 RKTLSFIDP--NGERTITVPGER------LEDDLKWPILDEGDGVFITAAAVDKEAI--RKCRETKLVILQVTPRVRvDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063735929 183 LDELIDLADYAICSTNFPQEWTGAPSspsallsmlIRLPKLKFVIMTLGEHG 234
Cdd:cd01947 159 LNQALIPLDILIGSRLDPGELVVAEK---------IAGPFPRYLIVTEGELG 201
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
15-184 |
2.37e-06 |
|
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: 47.47 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAkvADDSHgrymveeLESSGVDTSF 94
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG--ADAVV-------ISGLSPAPEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 95 CMSAKDGASHFNyVIVdnqtntrtcIYTPGYPPLLPDdltESLLLDVLDGVRVLYVNgrSREAELLLAQKAHSKNIPILI 174
Cdd:cd00287 73 VLDALEEARRRG-VPV---------VLDPGPRAVRLD---GEELEKLLPGVDILTPN--EEEAEALTGRRDLEVKEAAEA 137
|
170
....*....|
gi 1063735929 175 NAEKKRTGLD 184
Cdd:cd00287 138 AALLLSKGPK 147
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
15-152 |
3.31e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 48.29 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 15 VLGCGQLCLDYLVTVASFPIPDQKIR-------------GTSFKVqgGGNTgNALTCVARLGLPCRILAKVADDSHGRYM 81
Cdd:PLN02341 75 VATLGNLCVDIVLPVPELPPPSREERkaymeelaasppdKKSWEA--GGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 82 VEELESSGVDTSFCMSAKDGASHFN--------YVIVDNQTNTRTCI-YTPGYPPLLPD--DLTESLLLdVLDGVRVLYV 150
Cdd:PLN02341 152 LDVLAEEGISVVGLIEGTDAGDSSSasyetllcWVLVDPLQRHGFCSrADFGPEPAFSWisKLSAEAKM-AIRQSKALFC 230
|
..
gi 1063735929 151 NG 152
Cdd:PLN02341 231 NG 232
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
49-111 |
2.21e-05 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 45.31 E-value: 2.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063735929 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSaKDGASHFNYVIVD 111
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTY-LR-LDPAHRTSTVVVD 88
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
41-122 |
1.97e-04 |
|
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: 42.30 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 41 GTSFKVQGGGntG-NALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSakdgashfnyvivdnqTNTRTC 119
Cdd:cd01941 28 GHVKQSPGGV--GrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVF----------------EGRSTA 89
|
...
gi 1063735929 120 IYT 122
Cdd:cd01941 90 SYT 92
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
24-93 |
2.05e-04 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 42.16 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 24 DYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTS 93
Cdd:PRK11142 14 DHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTA 83
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
49-112 |
8.44e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 40.11 E-value: 8.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063735929 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSAKDGASHFNYV-IVDN 112
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISH-VHTKHGVTAQTQVeLHDN 86
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
13-93 |
1.43e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 39.60 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735929 13 PIVLGCGQLCLDYLVTVASFPIPDqkirGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDT 92
Cdd:PLN02323 11 SLVVCFGEMLIDFVPTVSGVSLAE----APAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNN 86
|
.
gi 1063735929 93 S 93
Cdd:PLN02323 87 E 87
|
|
| |
