|
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 ... |
14-353 |
1.33e-111 |
|
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: 326.94 E-value: 1.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 14 IVLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTS 93
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 94 FCMSAKDGASHFNYvIVDNQTNTRTCIYTPGYPPLLPDDLTESLlldvLDGVRVLYVNGRSREAELLLAQKAHSKNIPIL 173
Cdd:cd01945 81 FIVVAPGARSPISS-ITDITGDRATISITAIDTQAAPDSLPDAI----LGGADAVLVDGRQPEAALHLAQEARARGIPIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 174 INAEKKRTG-LDELIDLADYAICSTNFPQEWTGapsSPSALLSMLIRLPKLKFVIMTLGEHGCVMLERCssevsgseeet 252
Cdd:cd01945 156 LDLDGGGLRvLEELLPLADHAICSENFLRPNTG---SADDEALELLASLGIPFVAVTLGEAGCLWLERD----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 253 didelheslkqstdftsvlpvcnsslvtrltgnvtGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGLCTGMALEEMLT 332
Cdd:cd01945 222 -----------------------------------GELFHVPAFPV---EVVDTTGAGDVFHGAFAHALAEGMPLREALR 263
|
330 340
....*....|....*....|.
gi 42573561 333 FASRVAACCCRGLGARTSLPY 353
Cdd:cd01945 264 FASAAAALKCRGLGGRAGLPT 284
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
15-356 |
1.76e-54 |
|
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: 181.24 E-value: 1.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSF 94
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 95 CMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPLLPDDLTEslllDVLDGVRVLYVNG------RSREAELLLAQKAHSK 168
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDE----ALLAGADILHLGGitlasePPREALLAALEAARAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 169 NIPILINA-------EKKRTGLDELIDLADYAICSTNFPQEWTGAPsSPSALLSMLIRLPkLKFVIMTLGEHGCVMLERc 241
Cdd:COG0524 158 GVPVSLDPnyrpalwEPARELLRELLALVDILFPNEEEAELLTGET-DPEEAAAALLARG-VKLVVVTLGAEGALLYTG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 242 ssevsgseeetdidelheslkqstdftsvlpvcnsslvtrltgnvtGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGL 321
Cdd:COG0524 235 ----------------------------------------------GEVVHVPAFPV---EVVDTTGAGDAFAAGFLAGL 265
|
330 340 350
....*....|....*....|....*....|....*
gi 42573561 322 CTGMALEEMLTFASRVAACCCRGLGARTSLPYRTD 356
Cdd:COG0524 266 LEGLDLEEALRFANAAAALVVTRPGAQPALPTREE 300
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
19-353 |
1.56e-35 |
|
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: 131.13 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 19 GQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSA 98
Cdd:cd01174 6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 99 KDGASHFNYVIVDNqTNTRTCIYTPG---YppLLPDDLTESllLDVLDGVRVLYV-NGRSREAELLLAQKAHSKNIPILI 174
Cdd:cd01174 86 VGAPTGTAVITVDE-SGENRIVVVPGangE--LTPADVDAA--LELIAAADVLLLqLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 175 NAEKKRTGLDELIDLADYAICSTNFPQEWTGAPSSPS---ALLSMLIRLPKLKFVIMTLGEHGCVMLERcssevsgseee 251
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEedaEKAARLLLAKGVKNVIVTLGAKGALLASG----------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 252 tdidelheslkqstdftsvlpvcnsslvtrltgnvtGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGLCTGMALEEML 331
Cdd:cd01174 230 ------------------------------------GEVEHVPAFKV---KAVDTTGAGDTFIGALAAALARGLSLEEAI 270
|
330 340
....*....|....*....|..
gi 42573561 332 TFASRVAACCCRGLGARTSLPY 353
Cdd:cd01174 271 RFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
19-354 |
1.90e-30 |
|
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: 117.70 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 19 GQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSA 98
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 99 KDGASHFNYVIVDNQTNTRTCIYTPGYPPLLPDDLTESLllDVLDGVRVLYVNGRSR-EAELLLAQKAHSKNIPILINAE 177
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAE--ALIAESDIVLLQLEIPlETVLEAAKIAKKHGVKVILNPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 178 KKRTGLD-ELIDLADYaiCSTN-------FPQEWTGAPSSPSALLSMLIRLPKlkFVIMTLGEHGCVMLERcssevsgse 249
Cdd:TIGR02152 159 PAIKDLDdELLSLVDI--ITPNeteaeilTGIEVTDEEDAEKAAEKLLEKGVK--NVIITLGSKGALLVSK--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 250 eetdidelheslkqstdftsvlpvcnsslvtrltgnvtGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGLCTGMALEE 329
Cdd:TIGR02152 226 --------------------------------------DESKLIPAFKV---KAVDTTAAGDTFNGAFAVALAEGKSLED 264
|
330 340
....*....|....*....|....*
gi 42573561 330 MLTFASRVAACCCRGLGARTSLPYR 354
Cdd:TIGR02152 265 AIRFANAAAAISVTRKGAQSSIPYL 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
34-349 |
4.72e-30 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 116.67 E-value: 4.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 34 IPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSAKDGASHFNYVIVDNQ 113
Cdd:pfam00294 19 LPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 114 TNTRTCIYTPGYPPLLPDDLTESLLLdvLDGVRVLYVNGR----SREAELLLAQKA---HSKNIPILIN-AEKKRTGLDE 185
Cdd:pfam00294 99 GERTIVFNRGAAADLTPEELEENEDL--LENADLLYISGSlplgLPEATLEELIEAaknGGTFDPNLLDpLGAAREALLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 186 LIDLADYAICSTNFPQEWTGAPSSPSALLsmLIRLPKLKF-----VIMTLGEHGCVMLERcssevsgseeetdidelhes 260
Cdd:pfam00294 177 LLPLADLLKPNEEELEALTGAKLDDIEEA--LAALHKLLAkgiktVIVTLGADGALVVEG-------------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 261 lkqstdftsvlpvcnsslvtrltgnvtGRLVIVTAekIPSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAAC 340
Cdd:pfam00294 235 ---------------------------DGEVHVPA--VPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAAL 285
|
....*....
gi 42573561 341 CCRGLGART 349
Cdd:pfam00294 286 VVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
41-348 |
1.76e-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: 112.28 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 41 GTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSfcmsakdgashfnYVIVDNQTNTRTCI 120
Cdd:cd01166 23 ADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS-------------HVRVDPGRPTGLYF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 121 YTPGYPP---------------LLPDDLTEslllDVLDGVRVLYVNG-------RSREAELLLAQKAHSKNIPI------ 172
Cdd:cd01166 90 LEIGAGGerrvlyyragsaasrLTPEDLDE----AALAGADHLHLSGitlalseSAREALLEALEAAKARGVTVsfdlny 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 173 ---LINAEKKRTGLDELIDLADYAICSTNFPQEWTGAPSSPSALLSMLIRLPKLKFVIMTLGEHGCVmlercssevsgse 249
Cdd:cd01166 166 rpkLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGAL------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 250 eetdidelheslkqstdftsvlpvcnsslvtrLTGNVTGRLVIVTAEKIpsselIDTTGAGDAFTGALLYGLCTGMALEE 329
Cdd:cd01166 233 --------------------------------VYTGGGRVFVPAYPVEV-----VDTTGAGDAFAAGFLAGLLEGWDLEE 275
|
330
....*....|....*....
gi 42573561 330 MLTFASRVAACCCRGLGAR 348
Cdd:cd01166 276 ALRFANAAAALVVTRPGDI 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
49-348 |
3.53e-26 |
|
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: 106.54 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPL 128
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 129 LPDDLTESLlldvLDGVRVLYVNG----RSREAELLLAQKAHSKNIPILINA------EKKRTGLDELIDLADYAICSTN 198
Cdd:cd01168 134 SPDDLDWSL----LAKAKYLYLEGylltVPPEAILLAAEHAKENGVKIALNLsapfivQRFKEALLELLPYVDILFGNEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 199 FPQEWTGAP--SSPSALLSMLIRLPKLkfVIMTLGEHGCVMLERcssevsgseeetdiDElheslkqstdftsvlpvcns 276
Cdd:cd01168 210 EAEALAEAEttDDLEAALKLLALRCRI--VVITQGAKGAVVVEG--------------GE-------------------- 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573561 277 slvtrltgnvtgrlvIVTAEKIPSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAACCCRGLGAR 348
Cdd:cd01168 254 ---------------VYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPR 310
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
14-348 |
3.90e-26 |
|
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: 105.47 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 14 IVLGCGQLCLDYLVTVASFP-------IPDQKIRGtsfkvqgGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELE 86
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPgpfesvlVKDLRREF-------GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 87 SSGVDTSFCMSAKDGASHFNYVIVDnQTNTRTCIYTPGYPPLlpddLTESLLLDVLDGVRVLYVNGRSREAEllLAQKAH 166
Cdd:cd01942 74 EEGVDTSHVRVVDEDSTGVAFILTD-GDDNQIAYFYPGAMDE----LEPNDEADPDGLADIVHLSSGPGLIE--LARELA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 167 SKNIPILINA--EKKRTGLDELID---LADYAICSTNfpqEWtGAPSSPSALLSMLIRLpKLKFVIMTLGEHGCVMLErc 241
Cdd:cd01942 147 AGGITVSFDPgqELPRLSGEELEEileRADILFVNDY---EA-ELLKERTGLSEAELAS-GVRVVVVTLGPKGAIVFE-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 242 ssevsgseeetdidelheslkqsTDFTSVLPVcnsslvtrltgnvtgrlvivtaekIPSSELIDTTGAGDAFTGALLYGL 321
Cdd:cd01942 220 -----------------------DGEEVEVPA------------------------VPAVKVVDTTGAGDAFRAGFLYGL 252
|
330 340
....*....|....*....|....*..
gi 42573561 322 CTGMALEEMLTFASRVAACCCRGLGAR 348
Cdd:cd01942 253 LRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
34-348 |
1.87e-25 |
|
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: 104.26 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 34 IPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCmsAKDGASHFNYVIVDNQ 113
Cdd:cd01167 13 IPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGI--QFDPAAPTTLAFVTLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 114 TN-TRTCIYTPGYPplLPDDLTESLLLDVLDGVRVLY------VNGRSREAELLLAQKAHSKNIPILI----------NA 176
Cdd:cd01167 91 ADgERSFEFYRGPA--ADLLLDTELNPDLLSEADILHfgsialASEPSRSALLELLEAAKKAGVLISFdpnlrpplwrDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 177 EKKRTGLDELIDLADYAICSTnfpQEWTG-APSSPSALLSMLIRLPKLKFVIMTLGEHGCvmlercssevsgseeetdid 255
Cdd:cd01167 169 EEARERIAELLELADIVKLSD---EELELlFGEEDPEEIAALLLLFGLKLVLVTRGADGA-------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 256 elheslkqstdftsvlpvcnsslvTRLTGNVTGRLvivtaeKIPSSELIDTTGAGDAFTGALLYGLCTGMA-------LE 328
Cdd:cd01167 226 ------------------------LLYTKGGVGEV------PGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLA 275
|
330 340
....*....|....*....|
gi 42573561 329 EMLTFASRVAACCCRGLGAR 348
Cdd:cd01167 276 EALRFANAVGALTCTKAGAI 295
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
15-346 |
6.09e-22 |
|
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: 94.40 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSF 94
Cdd:cd01939 2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 95 CMSaKDGASHFNYVIVDNQTNTRTCIYtpgYPPLLPDDLTESLLLDVLDGVRVLYVNGRSREAELLLAQKAHSKN----- 169
Cdd:cd01939 82 CYR-KDIDEPASSYIIRSRAGGRTTIV---NDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNnrrpe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 170 IPILINAE--KKRTGLDELIDLADYAICSTNFPQE--WTgapsSPSALLSMLIRLPKLK-FVIMTLGEHG--CVMLErcs 242
Cdd:cd01939 158 IRITISVEveKPREELLELAAYCDVVFVSKDWAQSrgYK----SPEECLRGEGPRAKKAaLLVCTWGDQGagALGPD--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 243 sevsgseeetdiDELHESlkqstdftsvlpvcnsslvtrltgnvtgrlvivTAEKIPSseLIDTTGAGDAFTGALLYGL- 321
Cdd:cd01939 231 ------------GEYVHS---------------------------------PAHKPIR--VVDTLGAGDTFNAAVIYALn 263
|
330 340
....*....|....*....|....*
gi 42573561 322 CTGMALEEMLTFASRVAACCCRGLG 346
Cdd:cd01939 264 KGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
5-356 |
3.55e-21 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 92.88 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 5 SDEAIPGQPIVLgCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEE 84
Cdd:PTZ00292 9 SHGGEAEPDVVV-VGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 85 LESSGVDTSFCMSAKDGASHFNYVIVDNQTNTRTCIYTPGYPPLLPDDLTESLLLDVLDGVRVLYV-NGRSREAELLLAQ 163
Cdd:PTZ00292 88 FKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICqNEIPLETTLDALK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 164 KAHSKNIPILIN---AEKKRTG--LDELIDLADYAICSTNFPQEWTGAPSSPSALLSMLIR-LPKLKF--VIMTLGEHGC 235
Cdd:PTZ00292 168 EAKERGCYTVFNpapAPKLAEVeiIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKeLQQLGVenVIITLGANGC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 236 VMLErcssevsgseeeTDIDELHeslkqstdftsvlpvcnsslvtrltgnvtgrlviVTAEKIpssELIDTTGAGDAFTG 315
Cdd:PTZ00292 248 LIVE------------KENEPVH----------------------------------VPGKRV---KAVDTTGAGDCFVG 278
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 42573561 316 ALLYGLCTGMALEEMLTFASRVAACCCRGLGARTSLPYRTD 356
Cdd:PTZ00292 279 SMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSE 319
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
42-353 |
2.61e-15 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 75.71 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 42 TSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSAKDgashfnyvivdnqtnTRTC-- 119
Cdd:TIGR04382 27 TSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPG---------------RRTSlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 120 ---IYTPGYPPLL------------PDDLTESLLLDVldgvRVLYVNG------RSREAELLLAQKAHSKNIpilinaek 178
Cdd:TIGR04382 92 fleIKPPDEFPLLfyrenaadlaltPDDVDEDYIASA----RALLVSGtalsqePSREAVLKALEYARAAGV-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 179 kRTGLDelidlADYAicstnfPQEWtGAPSSPSALLSMLirLPKLKFVIMTLGEhgCVMLErcssevsgseeetDIDELH 258
Cdd:TIGR04382 160 -RVVLD-----IDYR------PYLW-KSPEEAGIYLRLV--LPLVDVIIGTREE--FDIAG-------------GEGDDE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 259 ESLKQSTDFTSVLPVCN----SSLVtrLTGNVTGrlviVTAEKIPSsELIDTTGAGDAFTGALLYGLCTGMALEEMLTFA 334
Cdd:TIGR04382 210 AAARALLDAGVEILVVKrgpeGSLV--YTGDGEG----VEVPGFPV-EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYG 282
|
330
....*....|....*....
gi 42573561 335 SRVAACCCRGLGARTSLPY 353
Cdd:TIGR04382 283 NACGAIVVSRHSCSPAMPT 301
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
24-341 |
1.30e-13 |
|
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: 70.14 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 24 DYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSakDGAS 103
Cdd:cd01947 11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWR--DKPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 104 HFNYVIVDNqtNTRTCIYTPGYPpllpddLTESLLLDVLDGVRVLYVNGRSREAELLlaQKAHSKNIPILINAEKKR-TG 182
Cdd:cd01947 89 RKTLSFIDP--NGERTITVPGER------LEDDLKWPILDEGDGVFITAAAVDKEAI--RKCRETKLVILQVTPRVRvDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 183 LDELIDLADYAICSTNFPQEWTGAPSspsallsmlIRLPKLKFVIMTLGEHGcvmlercssevsgseeetdidelheslk 262
Cdd:cd01947 159 LNQALIPLDILIGSRLDPGELVVAEK---------IAGPFPRYLIVTEGELG---------------------------- 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573561 263 qstdftsvlpvcnSSLVTrltgnvTGRLVIVTAEKipsSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAACC 341
Cdd:cd01947 202 -------------AILYP------GGRYNHVPAKK---AKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAIC 258
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
22-356 |
3.23e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 66.31 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 22 CLDYLVTVASFpIPDQKIRGTSFKVQGGGNtG-NALTCVARLGLPCRILAKVADDShGRYMVEELESSGVDTSFCMSakD 100
Cdd:COG1105 9 ALDRTYEVDEL-EPGEVNRASEVRLDPGGK-GiNVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPI--E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 101 GASHFNYVIVDNQTNTRTCIYTPGyPPLLPDDLTE--SLLLDVLDGVRVLYVNG---RSREAELL--LAQKAHSKNIPIL 173
Cdd:COG1105 84 GETRINIKIVDPSDGTETEINEPG-PEISEEELEAllERLEELLKEGDWVVLSGslpPGVPPDFYaeLIRLARARGAKVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 174 INAEKK--RTGLDELIDLADyaicstnfP-----QEWTGAP-SSPSALLSMLIRLPKL--KFVIMTLGEHGCVmlercss 243
Cdd:COG1105 163 LDTSGEalKAALEAGPDLIK--------PnleelEELLGRPlETLEDIIAAARELLERgaENVVVSLGADGAL------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 244 evsgseeetdidelheslkqstdftsvlpvcnssLVTRltgnvtGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGLCT 323
Cdd:COG1105 228 ----------------------------------LVTE------DGVYRAKPPKV---EVVSTVGAGDSMVAGFLAGLAR 264
|
330 340 350
....*....|....*....|....*....|...
gi 42573561 324 GMALEEMLTFASRVAACCCRGLGarTSLPYRTD 356
Cdd:COG1105 265 GLDLEEALRLAVAAGAAAALSPG--TGLPDRED 295
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
41-340 |
1.84e-10 |
|
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: 61.18 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 41 GTSFKVQGGGntG-NALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSakdgashfnyvivdnqTNTRTC 119
Cdd:cd01941 28 GHVKQSPGGV--GrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVF----------------EGRSTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 120 IYTpgyppllpddltesLLLDvldgvrvlyvngrsREAELL--LAQKAHSKNIPilinaEKKRTGLDELIDLADYAICST 197
Cdd:cd01941 90 SYT--------------AILD--------------KDGDLVvaLADMDIYELLT-----PDFLRKIREALKEAKPIVVDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 198 NFPQE----WTGA-----------PSSPSALLSMLIRLPKLKFVIMTLGEhGCVMLERCSSevsgseeeTDIDELHESLK 262
Cdd:cd01941 137 NLPEEaleyLLALaakhgvpvafePTSAPKLKKLFYLLHAIDLLTPNRAE-LEALAGALIE--------NNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 263 QSTDFTSVLPV---CNSSLVTRLTGNVTGRLVIVTAekipSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASrVAA 339
Cdd:cd01941 208 LLLPGIKNVIVtlgAKGVLLSSREGGVETKLFPAPQ----PETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQ-AAA 282
|
.
gi 42573561 340 C 340
Cdd:cd01941 283 A 283
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
15-347 |
2.22e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 58.69 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 15 VLGCGQLCLDYLVTVASFPIPDQKIR-------------GTSFKVqgGGNTgNALTCVARLGLPCRILAKVADDSHGRYM 81
Cdd:PLN02341 75 VATLGNLCVDIVLPVPELPPPSREERkaymeelaasppdKKSWEA--GGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 82 VEELESSGVDTSFCMSAKDGASHFN--------YVIVDNQTNTRTCI-YTPGYPPLLPD--DLTESLLLdVLDGVRVLYV 150
Cdd:PLN02341 152 LDVLAEEGISVVGLIEGTDAGDSSSasyetllcWVLVDPLQRHGFCSrADFGPEPAFSWisKLSAEAKM-AIRQSKALFC 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 151 NG--------RSREAELLLAQKAHS--------KNIPILINAEKKRTGLDELIDLADYAICSTNFPQEWTGAPSSPSALL 214
Cdd:PLN02341 231 NGyvfdelspSAIASAVDYAIDVGTavffdpgpRGKSLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 215 SMLIRLPKLKFVIMTLGEHGcvmlercssevsgseeetdidelheslkqstdftsvlpvcnSSLVTRLTGNVTGRlvivt 294
Cdd:PLN02341 311 ELLRPGIRTKWVVVKMGSKG-----------------------------------------SILVTRSSVSCAPA----- 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 42573561 295 aekiPSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAACCCRGLGA 347
Cdd:PLN02341 345 ----FKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGA 393
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
304-363 |
3.22e-09 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 57.57 E-value: 3.22e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 304 IDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAACCCRGLGARTSLPYRTDpnLATFL 363
Cdd:PRK11142 246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREE--IDAFL 303
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
15-322 |
7.00e-09 |
|
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: 55.18 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 15 VLGCGQLCLDYLVTVASFPIPDQKIRGTSFKVQGGGNTGNALTCVARLGLPCRILAkvaddshGRYMVeeLESSGVDTSF 94
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG-------ADAVV--ISGLSPAPEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 95 CMSAKDGASHFNyVIVdnqtntrtcIYTPGYPPLLPDdltESLLLDVLDGVRVLYVNgrSREAELLlaqkahsknipili 174
Cdd:cd00287 73 VLDALEEARRRG-VPV---------VLDPGPRAVRLD---GEELEKLLPGVDILTPN--EEEAEAL-------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 175 naekkrTGLDELIDLADYAICStnfpqewtgapsspsallsmLIRLPKLKFVIMTLGEHGCVMLERcssevsgseeetdi 254
Cdd:cd00287 124 ------TGRRDLEVKEAAEAAA--------------------LLLSKGPKVVIVTLGEKGAIVATR-------------- 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573561 255 delheslkqstdftsvlpvcnsslvtrltgnvTGRLVIVTAEKIpssELIDTTGAGDAFTGALLYGLC 322
Cdd:cd00287 164 --------------------------------GGTEVHVPAFPV---KVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
49-356 |
1.37e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 55.33 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSaKDGASHFNYVIVD-NQTNTRTciYTPGYPP 127
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTY-LR-LDPAHRTSTVVVDlDDQGERS--FTFMVRP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 128 -----LLPDDLTESLLLDVLDGVRVLYVNGRSREAELLLAQKAHSK--------NI--PILINAEKKRTGLDELIDLADY 192
Cdd:PRK09434 104 sadlfLQPQDLPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAggfvsfdpNLreDLWQDEAELRECLRQALALADV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 193 AICSTnfpQEW---TGAPSSPSALLSMLIRLPkLKFVIMTLGEHGCVMLERcssevsgseeetdidelheslKQSTDFTS 269
Cdd:PRK09434 184 VKLSE---EELcflSGTSQLEDAIYALADRYP-IALLLVTLGAEGVLVHTR---------------------GQVQHFPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 270 vlpvcnsslvtrltgnvtgrlvivtaekiPSSELIDTTGAGDAFTGALLYGLC------TGMALEEMLTFASRVAACCCR 343
Cdd:PRK09434 239 -----------------------------PSVDPVDTTGAGDAFVAGLLAGLSqaglwtDEAELAEIIAQAQACGALATT 289
|
330
....*....|...
gi 42573561 344 GLGARTSLPYRTD 356
Cdd:PRK09434 290 AKGAMTALPNRQE 302
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
13-356 |
1.38e-06 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 49.62 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 13 PIVLGCGQLCLDYLVTVASFPIPDqkirGTSFKVQGGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDT 92
Cdd:PLN02323 11 SLVVCFGEMLIDFVPTVSGVSLAE----APAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 93 S-------------FCMSAKDGASHFNYvivdnqtntrtciY-TPGYPPLL-PDDLTesllLDVLDGVRVLYVNGRS--- 154
Cdd:PLN02323 87 EgvrfdpgartalaFVTLRSDGEREFMF-------------YrNPSADMLLrESELD----LDLIRKAKIFHYGSISlit 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 155 ---REAELL---LAQKA-----HSKNI--PILINAEKKRTGLDELIDLADYAICSTNFPQEWTGA-PSSPSALLSMLirL 220
Cdd:PLN02323 150 epcRSAHLAamkIAKEAgallsYDPNLrlPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGdDPDDDTVVKLW--H 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 221 PKLKFVIMTLGEHGCVMLERcssevsgseeetdidelheslkqstDFTsvlpvcnsslvtrltGNVTGRLVivtaekips 300
Cdd:PLN02323 228 PNLKLLLVTEGEEGCRYYTK-------------------------DFK---------------GRVEGFKV--------- 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573561 301 sELIDTTGAGDAFTGALLYGLCTGMA-------LEEMLTFASRVAACCCRGLGARTSLPYRTD 356
Cdd:PLN02323 259 -KAVDTTGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEA 320
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
33-349 |
2.72e-06 |
|
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: 48.33 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 33 PIPDQKIRGTSFKVQGGGNTGNALtcvARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCMSAKDGASHFNYVIVDN 112
Cdd:cd01172 26 PVPVVKVEREEIRLGGAANVANNL---ASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTTTKTRVIARN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 113 QTNTRtcIYTPGYPPLLPDDLTE--SLLLDVLDGVRVL----YVNG----RSREAellLAQKAHSKNIPILINAEKKrtg 182
Cdd:cd01172 103 QQLLR--VDREDDSPLSAEEEQRliERIAERLPEADVVilsdYGKGvltpRVIEA---LIAAARELGIPVLVDPKGR--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 183 ldeliDLADYAICSTNFPQE---------WTGAPSSPSALLSMLIRLPKLKFVIMTLGEHGCVMLERcssevsgseeetd 253
Cdd:cd01172 175 -----DYSKYRGATLLTPNEkearealgdEINDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFER------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 254 idelheslkqstdftsvlpvcnsslvtrltgnvTGRLVIVTAEkipSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTF 333
Cdd:cd01172 237 ---------------------------------DGEVQHIPAL---AKEVYDVTGAGDTVIATLALALAAGADLEEAAFL 280
|
330
....*....|....*.
gi 42573561 334 ASRVAACCCRGLGART 349
Cdd:cd01172 281 ANAAAGVVVGKVGTAP 296
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
304-350 |
6.00e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 47.88 E-value: 6.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 42573561 304 IDTTGAGDAFTGALLYGLCTGMA-LEEMLTFASRVAACCCRGLGARTS 350
Cdd:PLN02813 347 VDTCGAGDAYAAGILYGLLRGVSdLRGMGELAARVAATVVGQQGTRLR 394
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
292-346 |
3.52e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 45.17 E-value: 3.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 42573561 292 IVTAEKIPSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAACCCRGLG 346
Cdd:PLN02379 286 VVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
297-339 |
3.57e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.07 E-value: 3.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 42573561 297 KIPSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAA 339
Cdd:PRK09513 241 KPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSA 283
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
298-340 |
9.63e-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: 43.54 E-value: 9.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 42573561 298 IPSS--ELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAAC 340
Cdd:cd01937 207 IPASkkDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
253-340 |
1.70e-04 |
|
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: 42.90 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 253 DIDELHESL-KQSTDFTSVLPVCnSSLVTRLTGNV------TGRLViVTAEK-----IPSSELIDTTGAGDAFTGALLYG 320
Cdd:cd01164 184 NREELEELFgRPLGDEEDVIAAA-RKLIERGAENVlvslgaDGALL-VTKDGvyrasPPKVKVVSTVGAGDSMVAGFVAG 261
|
90 100
....*....|....*....|
gi 42573561 321 LCTGMALEEMLTFASRVAAC 340
Cdd:cd01164 262 LAQGLSLEEALRLAVAAGSA 281
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
294-339 |
2.28e-04 |
|
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: 42.41 E-value: 2.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 42573561 294 TAEKIPS--SELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAA 339
Cdd:cd01944 235 NTHIIPGfkVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
48-347 |
2.52e-04 |
|
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: 42.34 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 48 GGGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFCmSAKDGASHFNYVIVDNqtNTRTCI-YTPG-- 124
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD--GDRIFGlSNKGgv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 125 --YPPLLPDdltesllLDVLDGVRVLYVNGRSREAELL-LAQKAHSKNIPILINAEKKRTglDELIDLA----DYAICSt 197
Cdd:cd01940 98 arEHPFEAD-------LEYLSQFDLVHTGIYSHEGHLEkALQALVGAGALISFDFSDRWD--DDYLQLVcpyvDFAFFS- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 198 nfpqewtGAPSSPSALLSMLIRL----PKLkfVIMTLGEHGCVMLErcssevsgseeetdidelheslkqSTDFTSVLPV 273
Cdd:cd01940 168 -------ASDLSDEEVKAKLKEAvsrgAKL--VIVTRGEDGAIAYD------------------------GAVFYSVAPR 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42573561 274 cnsslvtrltgnvtgrlvivtaekipSSELIDTTGAGDAF-TGALLYGLCTGMALEEMLTFASRVAACCCRGLGA 347
Cdd:cd01940 215 --------------------------PVEVVDTLGAGDSFiAGFLLSLLAGGTAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
49-339 |
5.19e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 41.26 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 49 GGNTGNALTCVARLGLPCRILAKVADDSHGRYMVEELESSGVDTSFcMSAKDGASHFNYVIVDNqtNTRtciytpgyppl 128
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISH-VHTKHGVTAQTQVELHD--NDR----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 129 LPDDLTESLLLD-VLDGVRV-------LYVNGRSREAELLLAQkAHSKNIPILINAEKKRTglDELIDLA----DYAICS 196
Cdd:PRK09813 89 VFGDYTEGVMADfALSEEDYawlaqydIVHAAIWGHAEDAFPQ-LHAAGKLTAFDFSDKWD--SPLWQTLvphlDYAFAS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573561 197 TNFPQEWTgapssPSALLSMLIRLPKLkfVIMTLGEHGCVMLErcssevsgseeetdidelheslkqSTDFTSVLPVcns 276
Cdd:PRK09813 166 APQEDEFL-----RLKMKAIVARGAGV--VIVTLGENGSIAWD------------------------GAQFWRQAPE--- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573561 277 slvtrltgnvtgrlvivtaekipSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASRVAA 339
Cdd:PRK09813 212 -----------------------PVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAA 251
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
288-329 |
4.79e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 38.54 E-value: 4.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 42573561 288 GRLVIVTAEKIPSSELIDTTGAGDAFTGALLYGLCTGMALEE 329
Cdd:PLN02548 264 GKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
299-341 |
9.34e-03 |
|
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: 37.71 E-value: 9.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 42573561 299 PSSELIDTTGAGDAFTGALLYGLCTGMALEEMLTFASrVAACC 341
Cdd:cd01943 256 KSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGS-VAASF 297
|
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| |
