|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
4-308 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 551.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 4 AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID 83
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 84 ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV 163
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 164 ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF 243
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGF 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833948 244 RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDAFLDRQ 308
Cdd:PRK11142 242 RVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-297 |
5.57e-129 |
|
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: 369.19 E-value: 5.57e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDIT 85
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 PVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVAL 165
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 166 NPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRV 245
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15833948 246 QAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPW 297
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
11-302 |
2.22e-121 |
|
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: 349.59 E-value: 2.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 11 GSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVI 90
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 91 KGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVALNPAPA 170
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 171 RE-LPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVD 249
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15833948 250 TIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEID 302
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-301 |
1.38e-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: 264.05 E-value: 1.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDIT 85
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 PVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAqrERIANASALLMQL-----ESPLESVMAAAKIAHQNK 160
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 161 TIVALNPA-------PARELPDELLALVDIITPNETEAEKLTGIrvendEDAAKAAQVLHEKGIRTVLITLGSRGVWASV 233
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833948 234 NGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEI 301
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
7-303 |
1.32e-74 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 231.93 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 7 LVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITP 86
Cdd:PTZ00292 18 VVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 87 VSVIKGESTGVALIFVNGE-GENVIGIHAGANAALSPALVEAQRERIAN-ASALLMQLESPLESVMAAAKIAHQNKTIVA 164
Cdd:PTZ00292 98 VSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERGCYTV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 165 LNPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQR 239
Cdd:PTZ00292 178 FNPAPAPKLAEveiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPV 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833948 240 -VPGFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDA 303
Cdd:PTZ00292 258 hVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPA 322
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-292 |
4.59e-72 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 224.14 E-value: 4.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPtpGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDIT 85
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 PVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASAL----LMQLESPLESVMAAAKIAHQNKT 161
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 162 IVALNPAP---ARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQ 238
Cdd:pfam00294 159 FDPNLLDPlgaAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15833948 239 RVPGFR-VQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQ 292
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
23-273 |
1.49e-43 |
|
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: 150.80 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 23 SFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFV 102
Cdd:cd01166 13 SPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 103 NGEGENVIgIHAGANAALSPALVEAQ-RERIANASAL------LMQLESPLESVMAAAKIAHQNKTIVAL---------N 166
Cdd:cd01166 93 GAGGERRV-LYYRAGSAASRLTPEDLdEAALAGADHLhlsgitLALSESAREALLEALEAAKARGVTVSFdlnyrpklwS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 167 PAPARELPDELLALVDIITPNETEAEKLTGIrvENDEDAAKAAQvLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQ 246
Cdd:cd01166 172 AEEAREALEELLPYVDIVLPSEEEAEALLGD--EDPTDAAERAL-ALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVE 248
|
250 260
....*....|....*....|....*..
gi 15833948 247 AVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01166 249 VVDTTGAGDAFAAGFLAGLLEGWDLEE 275
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-292 |
4.19e-37 |
|
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: 133.59 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDIT 85
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 PVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEaqrERIANASALLMQLESPLEsvmAAAKIAHQNKTIVAL 165
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEA---DPDGLADIVHLSSGPGLI---ELARELAAGGITVSF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 166 NPApaRELPD-------ELLALVDIITPNETEAE---KLTGIRvendeDAAKAaqvlheKGIRTVLITLGSRGVWASVNG 235
Cdd:cd01942 155 DPG--QELPRlsgeeleEILERADILFVNDYEAEllkERTGLS-----EAELA------SGVRVVVVTLGPKGAIVFEDG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15833948 236 EGQRVPGF-RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQ 292
Cdd:cd01942 222 EEVEVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
41-267 |
3.84e-35 |
|
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: 128.91 E-value: 3.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 41 GGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAAL 120
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 121 SPAlVEAQRERIANASAL----LMQLESPL-ESVMAAAKIAHQNKTIVAL----------NPAPARELPDELLALVDIIT 185
Cdd:cd01167 108 LLD-TELNPDLLSEADILhfgsIALASEPSrSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERIAELLELADIVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 186 PNETEAEKLTGIrvendEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITAL 265
Cdd:cd01167 187 LSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261
|
..
gi 15833948 266 LE 267
Cdd:cd01167 262 LS 263
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-266 |
3.35e-33 |
|
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: 121.05 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIactgddsigesvrqqlatdnidit 85
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 pvsvikgestGVALIFVNGEGenvigihaganaalspalveaqrerianasallmqleSPLESVMAAAKIAHQNKTIVAL 165
Cdd:cd00287 57 ----------GADAVVISGLS-------------------------------------PAPEAVLDALEEARRRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 166 NPAPARELPD-----ELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQ-R 239
Cdd:cd00287 90 DPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEvH 169
|
250 260
....*....|....*....|....*..
gi 15833948 240 VPGFRVQAVDTIAAGDTFNGALITALL 266
Cdd:cd00287 170 VPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
41-273 |
7.58e-33 |
|
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: 123.11 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 41 GGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVsVIKGESTGVALIFVNGEGENVIGIHAGANAAL 120
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQ-VQPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 121 SPALVEAqrERIANASALLM---QLESPLESVMAAAKIAHQNKTIVALN------PAPARELPDELLALVDIITPNETEA 191
Cdd:cd01168 134 SPDDLDW--SLLAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 192 EKLTGIRVENDEDAAKAAQvlhEKGIRTVLITLGSRGVWASVNGEGQRVPGFR-VQAVDTIAAGDTFNGALITALLEEKP 270
Cdd:cd01168 212 EALAEAETTDDLEAALKLL---ALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGLVQGEP 288
|
...
gi 15833948 271 LPE 273
Cdd:cd01168 289 LEE 291
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
10-273 |
8.20e-33 |
|
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: 122.40 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 10 LGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSV 89
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 90 IKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQrerIANASALLMQLESPlESVMAAAKIAHQNK--TIVALNP 167
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIDTQAAPDSLPDAI---LGGADAVLVDGRQP-EAALHLAQEARARGipIPLDLDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 168 APARELpDELLALVDIITPNETEAEKLTGIRvenDEDAAKAaqvLHEKGIRTVLITLGSRGV-WASVNGEGQRVPGFRVQ 246
Cdd:cd01945 161 GGLRVL-EELLPLADHAICSENFLRPNTGSA---DDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVE 233
|
250 260
....*....|....*....|....*..
gi 15833948 247 AVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01945 234 VVDTTGAGDVFHGAFAHALAEGMPLRE 260
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
7-273 |
1.10e-32 |
|
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: 122.04 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 7 LVVLGSINADHILNLQSFPTPGETVTGnHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITP 86
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPG-HVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 87 VsVIKGESTGVALIFVNGEGENVIGI-HAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVAL 165
Cdd:cd01941 81 I-VFEGRSTASYTAILDKDGDLVVALaDMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 166 NPAPARELPD--ELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWAS---VNGEGQRV 240
Cdd:cd01941 160 EPTSAPKLKKlfYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSsreGGVETKLF 239
|
250 260 270
....*....|....*....|....*....|....
gi 15833948 241 PGFRVQAV-DTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01941 240 PAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDD 273
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-290 |
2.08e-24 |
|
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: 99.80 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 6 SLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGkGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDIT 85
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 86 pVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSP---ALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTI 162
Cdd:cd01944 80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTewfATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 163 VALNPAPA-RELPD----ELLALVDIITPNETEAEKLTGirvENDEDAAKAAQVLHEKGIRTVLITLGSRGVWA-SVNGE 236
Cdd:cd01944 159 LVFDPGPRiSDIPDtilqALMAKRPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIrLPDGN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15833948 237 GQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKG 290
Cdd:cd01944 236 THIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
16-273 |
1.67e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 86.73 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 16 DHILNLQSFpTPGETVTGNHYQVAFGGKGANQAVAAGRSGA-NIAFIACTGDDsiGESVRQQLATDNIDITPVSvIKGEs 94
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVdVTALGFLGGFT--GEFIEELLDEEGIPTDFVP-IEGE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 95 TGVALIFVNGEGENVIGIHaGANAALSPALVEAQRERIAnasallmQLESPLESVMAA---------------AKIAHQN 159
Cdd:COG1105 86 TRINIKIVDPSDGTETEIN-EPGPEISEEELEALLERLE-------ELLKEGDWVVLSgslppgvppdfyaelIRLARAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 160 --KTIVALNPAPARELpdeLLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWAsVNGEG 237
Cdd:COG1105 158 gaKVVLDTSGEALKAA---LEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALL-VTEDG 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 15833948 238 Q-RVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:COG1105 234 VyRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
39-309 |
4.80e-19 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 85.83 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 39 AFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTgvALIFV----NGEGENVIGIHA 114
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGART--ALAFVtlrsDGEREFMFYRNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 115 GANAALSPAlvEAQRERIANASAL----LMQLESPLESV-MAAAKIAHQNKTIV--------ALNPAP--ARELPDELLA 179
Cdd:PLN02323 119 SADMLLRES--ELDLDLIRKAKIFhygsISLITEPCRSAhLAAMKIAKEAGALLsydpnlrlPLWPSAeaAREGIMSIWD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 180 LVDIITPNETEAEKLTGIRVENDEDAAKaaqvLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNG 259
Cdd:PLN02323 197 EADIIKVSDEEVEFLTGGDDPDDDTVVK----LWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVG 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15833948 260 ALITALL-------EEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDAFLDRQR 309
Cdd:PLN02323 273 GLLSQLAkdlslleDEERLREALRFANACGAITTTERGAIPALPTKEAVLKLLKKAV 329
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
34-302 |
1.79e-18 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 83.83 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 34 NHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVNGEGEN--VIG 111
Cdd:PRK09434 21 NRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 112 IHAGANAALSPALVEA--QRERIANASALLMQLESPLESVMAAAKIAHQNKTI---------VALNPAPARELPDELLAL 180
Cdd:PRK09434 101 VRPSADLFLQPQDLPPfrQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVsfdpnlredLWQDEAELRECLRQALAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 181 VDIITPNETEAEKLTGIrvenDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGA 260
Cdd:PRK09434 181 ADVVKLSEEELCFLSGT----SQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15833948 261 LITAL------LEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEID 302
Cdd:PRK09434 257 LLAGLsqaglwTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
1-273 |
6.63e-18 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 82.34 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 1 MQNAGSLVVLGSINAD------HILNLQSfPTPGetvtgnhyQVAF--GGKGANQAVAAGRSGANIAFIACTGDDSIGES 72
Cdd:PRK09850 1 MREKDYVVIIGSANIDvagyshESLNYAD-SNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 73 VRQQLATDNIDITPVSVIKGESTGVALIFVNGEGENVIGIH-AGANAALSPALVEAQRERIANASALLMQL---ESPLES 148
Cdd:PRK09850 72 LLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 149 VMAAAkiahqNKTIVALNPAPARELPD--ELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGS 226
Cdd:PRK09850 152 ILDNA-----ANVPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15833948 227 RGVWAS-VNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PRK09850 227 DGVYYSdISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAE 274
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
175-273 |
8.42e-17 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 78.40 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLIT------LGSRGVWASVNGEGQRVPGFRVQAV 248
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFP 210
|
90 100
....*....|....*....|....*.
gi 15833948 249 DTIA-AGDTFNGALITALLEEKPLPE 273
Cdd:cd01173 211 AYFNgTGDLFAALLLARLLKGKSLAE 236
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
7-273 |
8.67e-16 |
|
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: 75.53 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 7 LVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIdiTP 86
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 87 VSVIKGESTGVALIFVNGEGENVIGIHAGANAAL--SPALVEAQrerianasalLMQLESPLESVMAAAKIAHQNKTIVA 164
Cdd:cd01947 80 TVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDlkWPILDEGD----------GVFITAAAVDKEAIRKCRETKLVILQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 165 LNPAPARELPDELLALVDIITPNETEAEKLTgirvendedaakAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFR 244
Cdd:cd01947 150 VTPRVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK 217
|
250 260
....*....|....*....|....*....
gi 15833948 245 VQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01947 218 AKVPDSTGAGDSFAAGFIYGLLKGWSIEE 246
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
42-271 |
1.33e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 73.71 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 42 GKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDItpVSVIKGESTGVAlifVNGEGENVI--------GIH 113
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGDS---SSASYETLLcwvlvdplQRH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 114 A-------GANAALS--PALVEAQRERIANASALLMQ----LESPLESVMAAAKIAHQNKTIVALNPAP-----ARELPD 175
Cdd:PLN02341 195 GfcsradfGPEPAFSwiSKLSAEAKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkslLVGTPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 176 E------LLALVDIITPNETEAEKLTGIRvendeDAAKAAQVLHEKGIRT--VLITLGSRGVWASVNGEGQRVPGFRVQA 247
Cdd:PLN02341 275 ErralehLLRMSDVLLLTSEEAEALTGIR-----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
|
250 260
....*....|....*....|....
gi 15833948 248 VDTIAAGDTFNGALITALLEEKPL 271
Cdd:PLN02341 350 VDTVGCGDSFAAAIALGYIHNLPL 373
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
29-266 |
4.04e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 72.15 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 29 ETVTGNHYQVAFGGKGANQAVAAGRSGA--------NIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGeSTGVALI 100
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDG-TTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 101 FVNGEGENVIGIHAGANA--ALSPALVEAQRE-RIANASALLMQLESPLESVMAAAKIAHQNKTIVALNPAP----AREL 173
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSStvNYDSCLASAISKsRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDvsciERHR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 174 PDELLAL---VDIITPNETEAEKLTGIrvENDEDAAKAAQVLHEKgIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDT 250
Cdd:PLN02813 273 DDFWDVMgnyADILFANSDEARALCGL--GSEESPESATRYLSHF-CPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDT 349
|
250
....*....|....*.
gi 15833948 251 IAAGDTFNGALITALL 266
Cdd:PLN02813 350 CGAGDAYAAGILYGLL 365
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
8-267 |
9.41e-14 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 70.73 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 8 VVLGSINADhILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPV 87
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 88 SVIKGESTGVALIFVNGEGENVIGIH-AGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVALN 166
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLADEIPVFVDTV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 167 PAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASV-NGEGQRVPGFRV 245
Cdd:PRK09954 220 SEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEkDGEQFLLTAPAH 299
|
250 260
....*....|....*....|..
gi 15833948 246 QAVDTIAAGDTFNGALITALLE 267
Cdd:PRK09954 300 TTVDSFGADDGFMAGLVYSFLE 321
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
175-273 |
1.58e-13 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 69.41 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITlgsrgvwaSVNGEGQRVPGFRVQAVDTIAA- 253
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT--------SVPLDDTPADKIGNLAVTADGAw 204
|
90 100 110
....*....|....*....|....*....|....
gi 15833948 254 --------------GDTFNGALITALLEEKPLPE 273
Cdd:COG2240 205 lvetpllpfspngtGDLFAALLLAHLLRGKSLEE 238
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
176-223 |
1.73e-13 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 69.34 E-value: 1.73e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15833948 176 ELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLIT 223
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
16-273 |
1.86e-13 |
|
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: 69.10 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 16 DHILNLQSFpTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSiGESVRQQLATDNIDITPVSViKGES- 94
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVEV-AGETr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 95 TGVALIfvngEGENVIGIHAGANAALSPALVEAQRERIAnasallmQLESPLESVMAA---------------AKIAHQN 159
Cdd:cd01164 89 INVKIK----EEDGTETEINEPGPEISEEELEALLEKLK-------ALLKKGDIVVLSgslppgvpadfyaelVRLAREK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 160 KTIVAL--NPAPARELpdeLLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWAsVNGEG 237
Cdd:cd01164 158 GARVILdtSGEALLAA---LAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALL-VTKDG 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 15833948 238 Q-RVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01164 234 VyRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
55-273 |
5.39e-13 |
|
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: 67.97 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 55 GANIAFIACTGDDSIGESVRQQLATDNIDITPVsVIKGESTGVALIFVnGEGENVIGI----HAGANAALSPALVEAQRE 130
Cdd:cd01172 53 GAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTTKTRVI-ARNQQLLRVdredDSPLSAEEEQRLIERIAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 131 RIANASALL-------MQLESPLESVMAAAKiaHQNKTIVAlNPapaRELPDELLALVDIITPNETEAEKLTGIRVENDE 203
Cdd:cd01172 131 RLPEADVVIlsdygkgVLTPRVIEALIAAAR--ELGIPVLV-DP---KGRDYSKYRGATLLTPNEKEAREALGDEINDDD 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833948 204 DAAKAAQVLHEK-GIRTVLITLGSRGV-WASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01172 205 ELEAAGEKLLELlNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEE 276
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
41-268 |
5.60e-13 |
|
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: 67.76 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 41 GGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGEsTGVALI-FVNGegeNVIGIHAGANAA 119
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGE-NAVADVeLVDG---DRIFGLSNKGGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 120 LSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVALNPAPARELPDELLAL--VDIITpneteaekLTGI 197
Cdd:cd01940 98 AREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFSDRWDDDYLQLVCpyVDFAF--------FSAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833948 198 RVENDEDAAKAAQVlHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEE 268
Cdd:cd01940 170 DLSDEEVKAKLKEA-VSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAG 239
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
175-266 |
1.21e-12 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 66.35 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASV-------NGEGQRVPGFRVQA 247
Cdd:pfam08543 114 EELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHLEGEEAVvtdvlydGGGFYTLEAPRIPT 193
|
90
....*....|....*....
gi 15833948 248 VDTIAAGDTFnGALITALL 266
Cdd:pfam08543 194 KNTHGTGCTL-SAAIAANL 211
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
175-266 |
8.58e-12 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 64.76 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLIT----------LGSrgvwaSVNGEGQRVPGFR 244
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITsididgklllVGS-----HRKEKGARPEQFK 218
|
90 100
....*....|....*....|..
gi 15833948 245 VqAVDTIAAGDTFNGALITALL 266
Cdd:PLN02978 219 I-VIPKIPAYFTGTGDLMAALL 239
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
175-266 |
2.05e-11 |
|
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: 62.75 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVN----GEGQRV-PGFRVQAVD 249
Cdd:COG0351 121 ELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGDEAVDvlydGDGVREfSAPRIDTGN 200
|
90
....*....|....*..
gi 15833948 250 TIAAGDTFNGAlITALL 266
Cdd:COG0351 201 THGTGCTLSSA-IAALL 216
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
182-273 |
1.11e-10 |
|
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273221 [Multi-domain] Cd Length: 287 Bit Score: 61.00 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 182 DIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLIT-LGSRGVWASVNGEGQRVPG------------FRVQAV 248
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQRDRSFEGLVATQegrwhisrplavFDPPPV 219
|
90 100
....*....|....*....|....*
gi 15833948 249 DTiaaGDTFNGALITALLEEKPLPE 273
Cdd:TIGR00687 220 GT---GDLIAALLLATLLHGNSLKE 241
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
173-266 |
1.53e-10 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 60.52 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 173 LPDELLALVDIITPNETEAEKLTGIRVENDEDAAK-AAQVLHEKGIRTVLITLG-SRGVWASVN----GEGQRVpgFRVQ 246
Cdd:PRK06427 126 LRERLLPLATLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhLLDGEESVDwlfdGEGEER--FSAP 203
|
90 100
....*....|....*....|...
gi 15833948 247 AVDTIA---AGDTFNGAlITALL 266
Cdd:PRK06427 204 RIPTKNthgTGCTLSAA-IAAEL 225
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
34-273 |
4.54e-10 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 59.73 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 34 NHYQVAFGGKGANQ---AVAA---GRSGANiAFIACTGDDSIGESVRQQLATDNIDitpVSVIKGES--TGVALIFVNGE 105
Cdd:PLN02548 43 SKYNVEYIAGGATQnsiRVAQwmlQIPGAT-SYMGCIGKDKFGEEMKKCATAAGVN---VHYYEDEStpTGTCAVLVVGG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 106 GENVIGIHAGAN--------AALSPALVEaqRERIANASALLMQLeSPlESVMAAAKIAHQNKTIVALN-PAP-----AR 171
Cdd:PLN02548 119 ERSLVANLSAANcykvehlkKPENWALVE--KAKFYYIAGFFLTV-SP-ESIMLVAEHAAANNKTFMMNlSAPficefFK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 172 ELPDELLALVDIITPNETEAE---KLTGIRVEN-DEDAAKAAQVLHEKGI--RTVLITLGSRGVWASVNGegqRVPGFRV 245
Cdd:PLN02548 195 DQLMEALPYVDFLFGNETEARtfaKVQGWETEDvEEIALKISALPKASGThkRTVVITQGADPTVVAEDG---KVKEFPV 271
|
250 260 270
....*....|....*....|....*....|....
gi 15833948 246 ------QAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PLN02548 272 iplpkeKLVDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
162-223 |
2.53e-09 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 57.19 E-value: 2.53e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833948 162 IVAlnPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLIT 223
Cdd:PRK05756 122 IVA--PGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
172-273 |
9.84e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 55.07 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 172 ELPDELLAL---VDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSR-----GVWASVNGEGQRVPGF 243
Cdd:PRK12413 118 ELRQELIQFfpyVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNRlsqkkAIDLFYDGKEFVILES 197
|
90 100 110
....*....|....*....|....*....|
gi 15833948 244 RVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PRK12413 198 PVLEKNNIGAGCTFASSIASQLVKGKSPLE 227
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
9-273 |
1.50e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 55.18 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 9 VLGSINAdHILNLQSFPTPGETVTGnhyqvafgGKGAN--QAVAAGrSGANIAFIACTGDDSIGESVRQQLATDNIDITP 86
Cdd:PLN02379 63 ILREVNA-HILPSPDDLSPIKTMAG--------GSVANtiRGLSAG-FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 87 VSVIKGeSTGVALIFVNGEGenvigihagaNAALSPALVEA--------QRERIANASALLMQLE-SPLESVMAAAKIAH 157
Cdd:PLN02379 133 LRAKKG-PTAQCVCLVDALG----------NRTMRPCLSSAvklqadelTKEDFKGSKWLVLRYGfYNLEVIEAAIRLAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 158 QNKTIVALNPAP---ARELPDELLAL-----VDIITPNETEAEKLtgIRVENDEDAAKAAQVLhEKGIRTVLITLGSRGV 229
Cdd:PLN02379 202 QEGLSVSLDLASfemVRNFRSPLLQLlesgkIDLCFANEDEAREL--LRGEQESDPEAALEFL-AKYCNWAVVTLGSKGC 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15833948 230 WASVNGEGQRVPGF-RVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PLN02379 279 IARHGKEVVRVPAIgETNAVDATGAGDLFASGFLYGLIKGLSLEE 323
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
34-271 |
2.48e-08 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 54.65 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 34 NHYQVAF--GGKGANQA-VA---AGRSGANIAFIACTGDDSIGESVRQQLATDNIDiTPVSVIKGESTGVALIFVNGEgE 107
Cdd:PTZ00247 53 SIPNVSYvpGGSALNTArVAqwmLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVE-MLFEYTTKAPTGTCAVLVCGK-E 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 108 NVIGIHAGANAALSPALVEAQRERIANASALLMQLE------SPlESVMAAAKIAHQNKTIVALN-PAP----ARElpDE 176
Cdd:PTZ00247 131 RSLVANLGAANHLSAEHMQSHAVQEAIKTAQLYYLEgffltvSP-NNVLQVAKHARESGKLFCLNlSAPfisqFFF--ER 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 177 LLAL---VDIITPNETEAEKLTGIRVENDED----AAKAAQVLHEKGI--RTVLITLGSRGVWASVNGEGQRVPgfrVQA 247
Cdd:PTZ00247 208 LLQVlpyVDILFGNEEEAKTFAKAMKWDTEDlkeiAARIAMLPKYSGTrpRLVVFTQGPEPTLIATKDGVTSVP---VPP 284
|
250 260 270
....*....|....*....|....*....|
gi 15833948 248 ------VDTIAAGDTFNGALITALLEEKPL 271
Cdd:PTZ00247 285 ldqekiVDTNGAGDAFVGGFLAQYANGKDI 314
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
110-214 |
4.55e-08 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 53.96 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 110 IGIHAGANAALSpalveaQRERIANASALLMQLESPL--ESVMAAAKIAHqnktivALNPAPARELPDELLALVDIITPN 187
Cdd:PRK08573 70 MGIDAAKTGMLS------NREIIEAVAKTVSKYGFPLvvDPVMIAKSGAP------LLREDAVDALIKRLLPLATVVTPN 137
|
90 100
....*....|....*....|....*..
gi 15833948 188 ETEAEKLTGIRVENDEDAAKAAQVLHE 214
Cdd:PRK08573 138 RPEAEKLTGMKIRSVEDARKAAKYIVE 164
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
174-273 |
8.84e-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: 52.47 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 174 PDEL---LALVDIITPNETEAEKLTGirvenDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAV-D 249
Cdd:cd01946 154 PEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfD 228
|
90 100
....*....|....*....|....
gi 15833948 250 TIAAGDTFNGALITALLEEKPLPE 273
Cdd:cd01946 229 PTGAGDTFAGGFIGYLASQKDTSE 252
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
41-273 |
9.93e-07 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 48.97 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 41 GGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVNGE---GENVIGIHAGAn 117
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELHDNDrvfGDYTEGVMADF- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 118 aalspALVEAQRERIANASALLMQLESPLESVMAAAkiaHQNKTIVALNPA--PARELPDELLALVDIitpneteaeklt 195
Cdd:PRK09813 102 -----ALSEEDYAWLAQYDIVHAAIWGHAEDAFPQL---HAAGKLTAFDFSdkWDSPLWQTLVPHLDY------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 196 GIRVENDEDA--AKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PRK09813 162 AFASAPQEDEflRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQ 241
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
164-273 |
1.34e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 48.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 164 ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSR-----GVWASVNGEG- 237
Cdd:PRK12412 116 ALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetAIDVLYDGETf 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 15833948 238 QRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPE 273
Cdd:PRK12412 196 DLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
176-269 |
2.63e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 44.70 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 176 ELLALVDIITPNETEAEKLTgirvendeDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGD 255
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGD 222
|
90
....*....|....
gi 15833948 256 TFNGALITALLEEK 269
Cdd:cd01937 223 VFLAAFLYSRLSGK 236
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
183-307 |
2.79e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.07 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 183 IITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRG-VWASVNGEGQRVPGfRVQAVDTIAAGDTFNGAL 261
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGaLWVNASGEWIAKPP-ACDVVSTVGAGDSMVGGL 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15833948 262 ITALLEEKPLPEAIRFAHAAAAIAVTrkgaQPSVPW--REEIDAFLDR 307
Cdd:PRK09513 262 IYGLLMRESSEHTLRLATAVSALAVS----QSNVGItdRPQLAAMMAR 305
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
175-225 |
1.14e-04 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 43.60 E-value: 1.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15833948 175 DELLALVDIITPNETEAEKLTG-IRVENDEDAAKAAQVLHEKGIRTVLITLG 225
Cdd:PLN02898 133 EELLPLATIVTPNVKEASALLGgDPLETVADMRSAAKELHKLGPRYVLVKGG 184
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
181-273 |
1.36e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 42.85 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 181 VDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKG-IRTVLITLGSRGVWAsVNGEG--QRVPGfRVQAVDTIAAGDTF 257
Cdd:PRK10294 181 IELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALG-VDSENciQVVPP-PVKSQSTVGAGDSM 258
|
90
....*....|....*.
gi 15833948 258 NGALITALLEEKPLPE 273
Cdd:PRK10294 259 VGAMTLKLAENASLEE 274
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
175-273 |
1.58e-03 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 39.64 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 175 DELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLgsrgvwASVNGEGQRVPGFRVQA------- 247
Cdd:PRK08176 147 QHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITS------AAGNEENQEMQVVVVTAdsvnvis 220
|
90 100 110
....*....|....*....|....*....|.
gi 15833948 248 ---VDTIA--AGDTFNGALITALLEEKPLPE 273
Cdd:PRK08176 221 hprVDTDLkgTGDLFCAELVSGLLKGKALTD 251
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
183-266 |
5.01e-03 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 38.17 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833948 183 IITPNETEAEKLTGIRVENDEDAAKAA--QVLHEkGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGA 260
Cdd:PRK13508 180 VIKPNIEELSQLLGKEVSEDLDELKEVlqQPLFE-GIEWIIVSLGADGAFAKHNDTFYKVDIPKIEVVNPVGSGDSTVAG 258
|
....*.
gi 15833948 261 LITALL 266
Cdd:PRK13508 259 IASGLL 264
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
171-225 |
5.74e-03 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 38.02 E-value: 5.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833948 171 RELPDELLALVDIITPNETEAEKLTGIR-VENDEDAAKAAQVLHEKGIRTVLITLG 225
Cdd:PTZ00347 351 AMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAAAQALAQYGSRYVLVKGG 406
|
|
| |
