|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
8-289 |
1.72e-144 |
|
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: 407.76 E-value: 1.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 8 GSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEPV 87
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 88 THTESGTAHIVLAE-GDNSIVVVKGANDDITPAYALNALEQIEKVDMVLIQQEIPEETVDEVCKYCHSHDIPIILNPAPA 166
Cdd:TIGR02152 81 KDTPTGTAFITVDDtGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 167 RP-LKQETIDHATYLTPNEHEASILFP-----ELTISEALALYPAK----LFITEGKQGVRYSAGSKEVLIPSFPVEPVD 236
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGievtdEEDAEKAAEKLLEKgvknVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1072804023 237 TTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPTRNEVE 289
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-284 |
2.05e-133 |
|
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: 379.59 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTD 82
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVTHTESGTAHIVLAE-GDNSIVVVKGANDDITPAYALNALEQIEKVDMVLIQQEIPEETVDEVCKYCHSHDIPIIL 161
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDEsGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 162 NPAPARPLKQETIDHATYLTPNEHEASILFPELTISEALALYPAKLF---------ITEGKQGVRYSAGSKEVLIPSFPV 232
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLlakgvknviVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 233 EPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPT 284
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-288 |
2.95e-95 |
|
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: 282.93 E-value: 2.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTD 82
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVTHTESGTAHIVL-AEGDNSIVVVKGANDDITPAYALNALeqIEKVDMVLIQ-----QEIPEETVDEVCKYCHSHD 156
Cdd:COG0524 81 GVRRDPGAPTGLAFILVdPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGgitlaSEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 157 IPIILNPA-------PARPLKQETIDHATYLTPNEHEASILFPELTISEA----LALYPAKLFITEGKQGVRYSAGSKEV 225
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGETDPEEAaaalLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072804023 226 LIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPTRNEV 288
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-293 |
2.54e-85 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 257.88 E-value: 2.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 1 MRNICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVR 80
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 81 TDYMEPVTHTESGTAHI-VLAEGDNSIVVVKGANDDITPAYALNALEQIEKVDMVLIQQEIPEETVDEVCKYCHSHDIPI 159
Cdd:PRK11142 82 TAPVSVIKGESTGVALIfVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 160 ILNPAPARPLKQETIDHATYLTPNEHEASILFPELTISEALALYPAKLF---------ITEGKQGVRYSAGSKEVLIPSF 230
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLhqkgietvlITLGSRGVWLSENGEGQRVPGF 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072804023 231 PVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPTRNEVEELLS 293
Cdd:PRK11142 242 RVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-279 |
6.18e-83 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 251.49 E-value: 6.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPkaGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTD 82
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVTHTESGTAHIVL-AEGDNSIVVVKGANDDITPAYALNALEQIEKVDMV----LIQQEIPEETVDEVCKYCHSHD- 156
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVdGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 157 -IPIILNPA-PARPLKQETIDHATYLTPNEHEASILFPEL--TISEALALYPA-------KLFITEGKQGVRYSAGSKEV 225
Cdd:pfam00294 159 fDPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHKllakgikTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1072804023 226 LIPSFP-VEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQ 279
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-288 |
4.28e-72 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 225.00 E-value: 4.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 1 MRNICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVR 80
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 81 TDYMEPVTHTESGTAHIVL--AEGDNSIVVVKGANDDITPAYALNALEQIEKV-DMVLIQQEIPEETVDEVCKYCHSHDI 157
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFVdtKTGNNEIVIIPGANNALTPQMVDAQTDNIQNIcKYLICQNEIPLETTLDALKEAKERGC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 158 PIILNPAPA-----RPLKQETIDHATYLTPNEHEASILF---------PELTISEALALYPAKLFITEGKQGVRYSA-GS 222
Cdd:PTZ00292 175 YTVFNPAPApklaeVEIIKPFLKYVSLFCVNEVEAALITgmevtdtesAFKASKELQQLGVENVIITLGANGCLIVEkEN 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072804023 223 KEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPTRNEV 288
Cdd:PTZ00292 255 EPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-279 |
1.18e-44 |
|
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: 152.85 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 6 VIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYME 85
Cdd:cd01942 4 VVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 86 PVTHTESGTAhIVLAEGDNSIVVV--KGANDDITPAYALNAleqIEKVDMVLIQQEIPEETVDEVCkycHSHDIPIILNP 163
Cdd:cd01942 84 VVDEDSTGVA-FILTDGDDNQIAYfyPGAMDELEPNDEADP---DGLADIVHLSSGPGLIELAREL---AAGGITVSFDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 164 APARPLK-----QETIDHATYLTPNEHEASiLFPELT--ISEALALYPAKLFITEGKQGVRYSAGSKEVLIPSFP-VEPV 235
Cdd:cd01942 157 GQELPRLsgeelEEILERADILFVNDYEAE-LLKERTglSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPaVKVV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1072804023 236 DTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQ 279
Cdd:cd01942 236 DTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
7-284 |
1.71e-44 |
|
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: 152.45 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 7 IGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEP 86
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 87 VTHTESGTAHIVLAEGDNSIVVVkgaNDDITPAYALN-ALEQIEKVDMVLIQQEIPEETVDeVCKYCHSHDIPIIL--NP 163
Cdd:cd01945 85 APGARSPISSITDITGDRATISI---TAIDTQAAPDSlPDAILGGADAVLVDGRQPEAALH-LAQEARARGIPIPLdlDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 164 APARPLkQETIDHATYLTPNEH--EASILFPELTISEALALYPAKLF-ITEGKQGVRYSAGSKEV-LIPSFPVEPVDTTG 239
Cdd:cd01945 161 GGLRVL-EELLPLADHAICSENflRPNTGSADDEALELLASLGIPFVaVTLGEAGCLWLERDGELfHVPAFPVEVVDTTG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1072804023 240 AGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAQGGMPT 284
Cdd:cd01945 240 AGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-278 |
8.07e-42 |
|
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: 145.86 E-value: 8.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVvtsdkrpkAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTD 82
Cdd:cd01167 1 KVVCFGEALIDFI--------PEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVTHTESGTAHIVL-AEGDNSIVVVKGANDDITPAYALNaLEQIEKVDMV------LIQQEIpEETVDEVCKYCHSH 155
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLdADGERSFEFYRGPAADLLLDTELN-PDLLSEADILhfgsiaLASEPS-RSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 156 DIPIIL----------NPAPARPLKQETIDHATYLTPNEHEASILFPEL---TISEALALYPAK-LFITEGKQGVRYSAG 221
Cdd:cd01167 151 GVLISFdpnlrpplwrDEEEARERIAELLELADIVKLSDEELELLFGEEdpeEIAALLLLFGLKlVLVTRGADGALLYTK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072804023 222 SKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKD-------IEAALRFANRAASLSVCSFGA 278
Cdd:cd01167 231 GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAGA 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-278 |
8.57e-42 |
|
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: 145.80 E-value: 8.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 4 ICVIGSCSMDLVVtsdkrPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDY 83
Cdd:cd01166 2 VVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 84 ME--PVTHTesGTAHIVL-AEGDNSIVVVKG--ANDDITP-AYALNALEQiekVDMVLI------QQEIPEETVDEVCKY 151
Cdd:cd01166 77 VRvdPGRPT--GLYFLEIgAGGERRVLYYRAgsAASRLTPeDLDEAALAG---ADHLHLsgitlaLSESAREALLEALEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 152 CHSHDIPIIL---------NPAPARPLKQETIDHATYLTPNEHEASILFPELTISEALALYPAKLF------ITEGKQGV 216
Cdd:cd01166 152 AKARGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALgvkavvVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 217 RYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGA 278
Cdd:cd01166 232 LVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-275 |
2.50e-38 |
|
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: 136.67 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTvPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVrtd 82
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQS-PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVTHTESGTAHIVLAEGDNSIVVVKGANDDI----TPAYALNALEQIEKVDMVLIQQEIPEETVDEVCKYCHSHDIP 158
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKDGDLVVALADMDIyellTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 159 IILNPAPARPLK--QETIDHATYLTPNEHEASILFPELTISEA---------LALYPAKLFITEGKQGVRYSAGSKEV-- 225
Cdd:cd01941 157 VAFEPTSAPKLKklFYLLHAIDLLTPNRAELEALAGALIENNEdenkaakilLLPGIKNVIVTLGAKGVLLSSREGGVet 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 226 --LIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCS 275
Cdd:cd01941 237 klFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
35-278 |
3.25e-31 |
|
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: 118.49 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 35 TVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMePVTHTESGTAHIVLAEGDN-SIVvvkgAN 113
Cdd:cd01168 52 YIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQ-VQPDGPTGTCAVLVTPDAErTMC----TY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 114 DDITPAYALNAL--EQIEKVDMVLI---QQEIPEETVDEVCKYCHSHDIPIILN---PAPARPLK---QETIDHATYLTP 182
Cdd:cd01168 127 LGAANELSPDDLdwSLLAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlsaPFIVQRFKealLELLPYVDILFG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 183 NEHEASILFPELTIS------EALALYPAKLFITEGKQGVRYSAGSKEVLIPSFPVE-PVDTTGAGDTFNAAFAVALAEG 255
Cdd:cd01168 207 NEEEAEALAEAETTDdleaalKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQG 286
|
250 260
....*....|....*....|...
gi 1072804023 256 KDIEAALRFANRAASLSVCSFGA 278
Cdd:cd01168 287 EPLEECIRLGSYAAAEVIQQLGP 309
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
36-273 |
1.71e-30 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 116.45 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 36 VPGGkGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMepVTHTESGTA---HIVlaeGDNSIVV---- 108
Cdd:COG2870 54 RPGG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGL--VVDPRRPTTtktRVI---AGGQQLLrldf 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 109 -VKGANDDITPAYALNALEQ-IEKVDMVLIQQ----EIPEETVDEVCKYCHSHDIPIILNPAPARPLKQEtidHATYLTP 182
Cdd:COG2870 128 eDRFPLSAELEARLLAALEAaLPEVDAVILSDygkgVLTPELIQALIALARAAGKPVLVDPKGRDFSRYR---GATLLTP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 183 NEHEASILF-----PELTISEA----LALYPAK-LFITEGKQGVR-YSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVA 251
Cdd:COG2870 205 NLKEAEAAVgipiaDEEELVAAaaelLERLGLEaLLVTRGEEGMTlFDADGPPHHLPAQAREVFDVTGAGDTVIATLALA 284
|
250 260
....*....|....*....|..
gi 1072804023 252 LAEGKDIEAALRFANRAASLSV 273
Cdd:COG2870 285 LAAGASLEEAAELANLAAGIVV 306
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-278 |
1.31e-28 |
|
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: 110.20 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVR-T 81
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKhT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 82 DYMEPVthtESGTAHIVLA-EGDNSIVVVKGANDDITPAYALnaleqiEKVDMVLIQQEIPEETVDEVCKychsHDIPII 160
Cdd:cd01947 81 VAWRDK---PTRKTLSFIDpNGERTITVPGERLEDDLKWPIL------DEGDGVFITAAAVDKEAIRKCR----ETKLVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 161 LNPAPARPLK--QETIDHATYLTPNEHEasilFPELTISEALALYPAKLFI-TEGKQGVRYSAGSKEVLIPSFPVEPVDT 237
Cdd:cd01947 148 LQVTPRVRVDelNQALIPLDILIGSRLD----PGELVVAEKIAGPFPRYLIvTEGELGAILYPGGRYNHVPAKKAKVPDS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1072804023 238 TGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGA 278
Cdd:cd01947 224 TGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
37-279 |
2.77e-28 |
|
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: 110.34 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 37 PGGkGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYM---EPVTHTE----SGTAHIV-LAEGDNSIVv 108
Cdd:cd01172 39 LGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIvdeGRPTTTKtrviARNQQLLrVDREDDSPL- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 109 vkgaNDDITPAYALNALEQIEKVDMVLIQQE----IPEETVDEVCKYCHSHDIPIILNPapaRPLKQETIDHATYLTPNE 184
Cdd:cd01172 117 ----SAEEEQRLIERIAERLPEADVVILSDYgkgvLTPRVIEALIAAARELGIPVLVDP---KGRDYSKYRGATLLTPNE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 185 HEA-----SILFPELTISEA----LALYPAK-LFITEGKQGVR-YSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALA 253
Cdd:cd01172 190 KEArealgDEINDDDELEAAgeklLELLNLEaLLVTLGEEGMTlFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALA 269
|
250 260
....*....|....*....|....*.
gi 1072804023 254 EGKDIEAALRFANRAASLSVCSFGAQ 279
Cdd:cd01172 270 AGADLEEAAFLANAAAGVVVGKVGTA 295
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
11-292 |
1.08e-26 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 105.99 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 11 SMDLVVTSDkRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHyGTAILNNLKANGVRTDYMEpvTHT 90
Cdd:COG1105 9 ALDRTYEVD-ELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVP--IEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 91 ESGTAHIVLAEGDNSIVVVKGANDDITPAyALNAL-----EQIEKVDMVLI----QQEIPEETVDEVCKYCHSHDIPIIL 161
Cdd:COG1105 85 ETRINIKIVDPSDGTETEINEPGPEISEE-ELEALlerleELLKEGDWVVLsgslPPGVPPDFYAELIRLARARGAKVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 162 NpAPARPLKqETIDHATYLT-PNEHEASILF--PELTISEALAlYPAKL--------FITEGKQGVRYSAGSKEVLIPSF 230
Cdd:COG1105 164 D-TSGEALK-AALEAGPDLIkPNLEELEELLgrPLETLEDIIA-AARELlergaenvVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 231 PVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFGAqgGMPTRNEVEELL 292
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGT--GLPDREDVEELL 300
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
9-277 |
1.04e-24 |
|
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: 100.30 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 9 SCSMDLVVTSDkRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHyGTAILNNLKANGVRTDYMEPVT 88
Cdd:cd01164 8 NPAIDLTIELD-QLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVEVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 89 HTESgtaHIVLAEGDNSIVVVKGANDDITPAYALNALEQIE----KVDMVLIQ----QEIPEETVDEVCKYCHSHDIPII 160
Cdd:cd01164 86 ETRI---NVKIKEEDGTETEINEPGPEISEEELEALLEKLKallkKGDIVVLSgslpPGVPADFYAELVRLAREKGARVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 161 LNPAPArPLkQETIDHATYLT-PNEHEASILF--PELTISEALALypAKLFITEGKQGVRYSAGSKEVL---------IP 228
Cdd:cd01164 163 LDTSGE-AL-LAALAAKPFLIkPNREELEELFgrPLGDEEDVIAA--ARKLIERGAENVLVSLGADGALlvtkdgvyrAS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1072804023 229 SFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCSFG 277
Cdd:cd01164 239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
4-273 |
9.33e-23 |
|
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: 95.18 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 4 ICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGkGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTdy 83
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 84 MEPVTHTESGTAHIVLAEGD--NSIVVVKGANDDITpAYALNALEQIEKvDMVLI---QQEIPEETVDEVCKYchSHDIP 158
Cdd:cd01944 79 LLPPRGGDDGGCLVALVEPDgeRSFISISGAEQDWS-TEWFATLTVAPY-DYVYLsgyTLASENASKVILLEW--LEALP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 159 ----IILNPAP-----ARPLKQETIDHATYLTPNEHEASILFPELTISEALAL------YPAKLFITEGKQGVRY-SAGS 222
Cdd:cd01944 155 agttLVFDPGPrisdiPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASAlriyakTAAPVVVRLGSNGAWIrLPDG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1072804023 223 KEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSV 273
Cdd:cd01944 235 NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVV 285
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
27-293 |
1.23e-22 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 95.46 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 27 TVLGTS------FQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEPVTHTESGTAHIVL- 99
Cdd:PLN02323 26 TVSGVSlaeapaFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 100 AEGDNSIVVVKGANDDItpayalnaLEQIEKVDMVLIQQ-------EIpeETVDEVCKYCH--------------SHD-- 156
Cdd:PLN02323 106 SDGEREFMFYRNPSADM--------LLRESELDLDLIRKakifhygSI--SLITEPCRSAHlaamkiakeagallSYDpn 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 157 --IPIILNPAPARplkqETI----DHATYLTPNEHEasILFpeLTISE------ALALYPAK---LFITEGKQGVRYSAG 221
Cdd:PLN02323 176 lrLPLWPSAEAAR----EGImsiwDEADIIKVSDEE--VEF--LTGGDdpdddtVVKLWHPNlklLLVTEGEEGCRYYTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 222 SKEVLIPSFPVEPVDTTGAGDTFNAAFAVALA--------EGKdIEAALRFANRAASLSVCSFGAQGGMPTRNEVEELLS 293
Cdd:PLN02323 248 DFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAkdlslledEER-LREALRFANACGAITTTERGAIPALPTKEAVLKLLK 326
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
37-278 |
5.67e-21 |
|
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: 89.72 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 37 PGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEpVTHTESGTAHIVLAEGDNSIV-----VVKG 111
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCR-VKEGENAVADVELVDGDRIFGlsnkgGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 112 ANDDITPAYALNaleqieKVDMVLIQQEIPEETVDEVCKYCHSHDIPIILNPAPAR--PLKQETIDHATYltpneheASI 189
Cdd:cd01940 100 EHPFEADLEYLS------QFDLVHTGIYSHEGHLEKALQALVGAGALISFDFSDRWddDYLQLVCPYVDF-------AFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 190 LFPELTISEALAL------YPAKLFI-TEGKQGVRYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKD-IEAA 261
Cdd:cd01940 167 SASDLSDEEVKAKlkeavsRGAKLVIvTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTaIAEA 246
|
250
....*....|....*..
gi 1072804023 262 LRFANRAASLSVCSFGA 278
Cdd:cd01940 247 MRQGAQFAAKTCGHEGA 263
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
4-253 |
6.57e-21 |
|
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: 87.92 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 4 ICVIGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGkvgddhygtailnnlkangvrtdy 83
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 84 mepvthtesgtAHIVLAEGDNSivvvkgandditpayalnaleqiekvdmvliqqeiPEETVDEVCKYCHSHDIPIILNP 163
Cdd:cd00287 58 -----------ADAVVISGLSP-----------------------------------APEAVLDALEEARRRGVPVVLDP 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 164 AP-----ARPLKQETIDHATYLTPNEHEASILFPELTISEALALYPAKLF---------ITEGKQGVRYSA-GSKEVLIP 228
Cdd:cd00287 92 GPravrlDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLlskgpkvviVTLGEKGAIVATrGGTEVHVP 171
|
250 260
....*....|....*....|....*
gi 1072804023 229 SFPVEPVDTTGAGDTFNAAFAVALA 253
Cdd:cd00287 172 AFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-289 |
2.46e-19 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 85.76 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 1 MRNICVIGSCSMDLVVTSDKRpkagetvlgtsFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVR 80
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGENR-----------YLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 81 TDYM--EPVTHTesgtahivlaegdnSIVVVkGANDD--------ITPAyalnaleqiekVDMVLIQQEIPEETVDE--- 147
Cdd:PRK09434 71 TTYLrlDPAHRT--------------STVVV-DLDDQgersftfmVRPS-----------ADLFLQPQDLPPFRQGEwlh 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 148 VCKychshdipIILNPAPAR-------------------------------PLKQETIDHATYLTP----NEHEASILFP 192
Cdd:PRK09434 125 LCS--------IALSAEPSRsttfeamrrikaaggfvsfdpnlredlwqdeAELRECLRQALALADvvklSEEELCFLSG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 193 ELTISEAL----ALYPAKL-FITEGKQGVRYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKD------IEAA 261
Cdd:PRK09434 197 TSQLEDAIyalaDRYPIALlLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLwtdeaeLAEI 276
|
330 340
....*....|....*....|....*...
gi 1072804023 262 LRFANRAASLSVCSFGAQGGMPTRNEVE 289
Cdd:PRK09434 277 IAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-271 |
5.96e-18 |
|
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: 81.29 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVIGSCSMDLVVTSDKRPKAgetvlgtsfqtvPGGKGANQAVAAARLGAQVFMVGKVGDDhygtailnNLKANGVRTD 82
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSGVVK------------PGGPATYASLTLSRLGLTVKLVTKVGRD--------YPDKWSDLFD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 YMEPVT---HTESGTAHIVLA-EGDNSIVVVKGAN--DDITPAYALNAleqiEKVDMVLIQQEIPEETVDEVckychshd 156
Cdd:cd01937 61 NGIEVIsllSTETTTFELNYTnEGRTRTLLAKCAAipDTESPLSTITA----EIVILGPVPEEISPSLFRKF-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 157 IPIIL-------NPAPARPLKQETIDHATYLTPNEHEASILFPELTISEALALYPAKLFI-TEGKQGVRYSAGSKEVLIP 228
Cdd:cd01937 129 AFISLdaqgflrRANQEKLIKCVILKLHDVLKLSRVEAEVISTPTELARLIKETGVKEIIvTDGEEGGYIFDGNGKYTIP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1072804023 229 SFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASL 271
Cdd:cd01937 209 ASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
37-278 |
2.37e-17 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 79.78 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 37 PGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVrtdymepvthtesGTAHIVLAEGDNSIVVVK-GANDD 115
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGV-------------DISHVHTKHGVTAQTQVElHDNDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 116 ITPAYALNALEqiekvDMVLiqqeiPEETVDEVCKY-----------------CHSHDIPIILNPA--PARPLKQETIDH 176
Cdd:PRK09813 89 VFGDYTEGVMA-----DFAL-----SEEDYAWLAQYdivhaaiwghaedafpqLHAAGKLTAFDFSdkWDSPLWQTLVPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 177 ATYLTPNEHEASIlFPELTISEALALYPAKLFITEGKQGVRYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGK 256
Cdd:PRK09813 159 LDYAFASAPQEDE-FLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGM 237
|
250 260
....*....|....*....|..
gi 1072804023 257 DIEAALRFANRAASLSVCSFGA 278
Cdd:PRK09813 238 TLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
15-291 |
1.18e-15 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 76.39 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 15 VVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQ--------VFMVGKVGDDHYGTAILNNLKANGVRTdYMEP 86
Cdd:PLN02813 103 VINHEERGKVLRALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHF-LSQP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 87 VTHTESGTAhIVLAEGD--NSIVVVKGANDDITPAYALNALeqIEKVDMVLIQQ---EIP--EETVDEVCKYCHSHDIPI 159
Cdd:PLN02813 182 VKDGTTGTV-IVLTTPDaqRTMLSYQGTSSTVNYDSCLASA--ISKSRVLVVEGylwELPqtIEAIAQACEEAHRAGALV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 160 ILNPAPA------RPLKQETIDH-ATYLTPNEHEASIL--FPELTISEALALYPAKLF----ITEGKQGVRYSAGSKEVL 226
Cdd:PLN02813 259 AVTASDVscierhRDDFWDVMGNyADILFANSDEARALcgLGSEESPESATRYLSHFCplvsVTDGARGSYIGVKGEAVY 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072804023 227 IPSFPVEPVDTTGAGDTFNAAFAVALAEG-KDIEAALRFANRAASLSVcsfGAQGGMPTRNEVEEL 291
Cdd:PLN02813 339 IPPSPCVPVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVV---GQQGTRLRVEDAVEL 401
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-275 |
1.71e-14 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 72.33 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 4 ICVIGSCSMDLVVTSDKRPKAGETVLGtSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTD- 82
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPG-KIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 83 -YMEPVTHTES------GTAHIVLAEGDNSIvvvkgaNDDITPAYALNALEQIEKVDMVLIQQEIPEETVDEVCKycHSH 155
Cdd:PRK09850 86 cLIVPGENTSSylslldNTGEMLVAINDMNI------SNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILD--NAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 156 DIPIILNPAPA-RPLK-QETIDHATYLTPNEHEASILFP-ELTISEALALYPA--------KLFITEGKQGVRYSAGSKE 224
Cdd:PRK09850 158 NVPVFVDPVSAwKCVKvRDRLNQIHTLKPNRLEAETLSGiALSGREDVAKVAAwfhqhglnRLVLSMGGDGVYYSDISGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 225 V-LIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCS 275
Cdd:PRK09850 238 SgWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALSC 289
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
7-277 |
6.14e-13 |
|
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: 67.43 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 7 IGSCSMDLVVTSDKRPKAGETVLGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEP 86
Cdd:cd01939 5 VGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 87 VTHTESGTAHIV-LAEGDNSIVVVKGANDDITpayalnaLEQIEKVDM-----VLIQQEIPEETVDEV----CKYCHSHD 156
Cdd:cd01939 85 KDIDEPASSYIIrSRAGGRTTIVNDNNLPEVT-------YDDFSKIDLtqygwIHFEGRNPDETLRMMqhieEHNNRRPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 157 IPI-----ILNPAPA-RPLKQE---------TIDHATYLTPNEHEASILFpeltiseaLALYPAKLFITEGKQGVRYSAG 221
Cdd:cd01939 158 IRItisveVEKPREElLELAAYcdvvfvskdWAQSRGYKSPEECLRGEGP--------RAKKAALLVCTWGDQGAGALGP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072804023 222 SKEVL-IPSFPVEP-VDTTGAGDTFNAAFAVALAEGKD-IEAALRFANRAASLSVCSFG 277
Cdd:cd01939 230 DGEYVhSPAHKPIRvVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVG 288
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
180-291 |
1.17e-10 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 61.20 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 180 LTPNEHEASILF-----PELTISEALALYPAKLF------------ITEGKQG-VRYSAGSKEVL-IPSF--PVEPV-DT 237
Cdd:cd01943 184 FSPNLEEAARLLglptsEPSSDEEKEAVLQALLFsgilqdpgggvvLRCGKLGcYVGSADSGPELwLPAYhtKSTKVvDP 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072804023 238 TGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVcsfgAQGGMP--TRNEVEEL 291
Cdd:cd01943 264 TGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAI----EQVGLPrlTKVEGEEL 315
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
3-293 |
4.83e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 59.84 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 3 NICVigscsmDLVVTSDKRPKAG----ETVLGTSFQTVPGGK------GANQAVAAARLGAQVFMVGKVGDDHYGTAILN 72
Cdd:PLN02341 80 NLCV------DIVLPVPELPPPSreerKAYMEELAASPPDKKsweaggNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 73 NLKANGVRTDYMEPVTHTE---SGTAHIVLAegdnsIVVVKGAND-------DITPAYALNALEQI-EKVDMVLIQ---- 137
Cdd:PLN02341 154 VLAEEGISVVGLIEGTDAGdssSASYETLLC-----WVLVDPLQRhgfcsraDFGPEPAFSWISKLsAEAKMAIRQskal 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 138 -------QEIPEETVDEVCKYCHSHDIPIILNPAParplKQETIDHATyltPNEHEASILFPE------LTISEALALYP 204
Cdd:PLN02341 229 fcngyvfDELSPSAIASAVDYAIDVGTAVFFDPGP----RGKSLLVGT---PDERRALEHLLRmsdvllLTSEEAEALTG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 205 AKLFITEGKQGVRYSAGSKEVLI------------------PSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFAN 266
Cdd:PLN02341 302 IRNPILAGQELLRPGIRTKWVVVkmgskgsilvtrssvscaPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLAN 381
|
330 340
....*....|....*....|....*..
gi 1072804023 267 RAASLSVCSFGAQGGMPTRNEVEELLS 293
Cdd:PLN02341 382 AVGAATAMGCGAGRNVATLEKVLELLR 408
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
34-278 |
1.65e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 57.80 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 34 QTVPGGKGANQA-VAAARL---GAQVFMvGKVGDDHYGTAILNNLKANGVRTDYMEPVThTESGTAHIVLAEGDNSIVvv 109
Cdd:PLN02548 48 EYIAGGATQNSIrVAQWMLqipGATSYM-GCIGKDKFGEEMKKCATAAGVNVHYYEDES-TPTGTCAVLVVGGERSLV-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 110 kgANDDITPAYALNALEQ------IEKVDMVLIQQ---EIPEETVDEVCKYCHSHDIPIILN-PAP-----ARPLKQETI 174
Cdd:PLN02548 124 --ANLSAANCYKVEHLKKpenwalVEKAKFYYIAGfflTVSPESIMLVAEHAAANNKTFMMNlSAPficefFKDQLMEAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 175 DHATYLTPNEHEASILFP----ELTISEALALYPAKLFITEGKQG--VRYSAGSKEVLIP------SFPVEP------VD 236
Cdd:PLN02548 202 PYVDFLFGNETEARTFAKvqgwETEDVEEIALKISALPKASGTHKrtVVITQGADPTVVAedgkvkEFPVIPlpkeklVD 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1072804023 237 TTGAGDTFNAAFAVALAEGKDIEAALRFANRAASL----SVCSFGA 278
Cdd:PLN02548 282 TNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANViiqrSGCTYPE 327
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
207-284 |
1.76e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 57.89 E-value: 1.76e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072804023 207 LFITEGKQGVRYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVcsfgAQGGMPT 284
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAV----EQVGIPK 279
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
6-275 |
4.21e-09 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 56.86 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 6 VIGSCSMDLVVTSDKR-PKAGETvlGTSFQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYM 84
Cdd:PRK09954 62 VVGAINMDIRGMADIRyPQAASH--PGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 85 EPVtHTESGTAHIVLAEGDNSIVVvkGAND-----DITPAYALNALEQIEKVDMVLIQQEIPEETVDEVckYCHSHDIPI 159
Cdd:PRK09954 140 IRL-HGQSTSTYLAIANRQDETVL--AINDthilqQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWV--FTLADEIPV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 160 ILNPAPArpLKQETI----DHATYLTPNEHEASILFPELTISEA------LALYP---AKLFITEGKQGVRYSAGSKEVL 226
Cdd:PRK09954 215 FVDTVSE--FKAGKIkhwlAHIHTLKPTQPELEILWGQAITSDAdrnaavNALHQqgvQQIFVYLPDESVFCSEKDGEQF 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1072804023 227 IPSFPVEP-VDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSVCS 275
Cdd:PRK09954 293 LLTAPAHTtVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRAS 342
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
36-270 |
5.77e-09 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 56.19 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 36 VPGGKGANQA-VAAARLGA---QVFMVGKVGDDHYGTAILNNLKANGVRTDYMEpVTHTESGTAHIVLAEGDNSIVVVKG 111
Cdd:PTZ00247 60 VPGGSALNTArVAQWMLQApkgFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTCAVLVCGKERSLVANLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 112 ANDDITPAYalnaleqiekvdmvlIQQEIPEETVDE--------------------VCKYCHSHDIPIILN-PAP----- 165
Cdd:PTZ00247 139 AANHLSAEH---------------MQSHAVQEAIKTaqlyylegffltvspnnvlqVAKHARESGKLFCLNlSAPfisqf 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 166 -ARPLKQeTIDHATYLTPNEHEASIL-----FPELTISEaLALYPAKLFITEGKQG--VRYSAGSKEVLIP------SFP 231
Cdd:PTZ00247 204 fFERLLQ-VLPYVDILFGNEEEAKTFakamkWDTEDLKE-IAARIAMLPKYSGTRPrlVVFTQGPEPTLIAtkdgvtSVP 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1072804023 232 VEP------VDTTGAGDTFNAAFAVALAEGKDIEAALRFANRAAS 270
Cdd:PTZ00247 282 VPPldqekiVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQ 326
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
37-273 |
2.39e-08 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 54.45 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 37 PGGkGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGV--------------------------RTDYMEPVTHT 90
Cdd:PRK11316 50 PGG-AANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVkcdfvsvpthptitklrvlsrnqqliRLDFEEGFEGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 91 ESGTAHIVLAEGDNSIVVVkganddITPAYALNALEQIEKvdmvLIQQeipeetvdevckyCHSHDIPIILNPaparplK 170
Cdd:PRK11316 129 DPQPLLERIEQALPSIGAL------VLSDYAKGALASVQA----MIQL-------------ARKAGVPVLIDP------K 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 171 QETIDH---ATYLTPNEHE-----------ASILFPELTISEALALypAKLFITEGKQGVRY-SAGSKEVLIPSFPVEPV 235
Cdd:PRK11316 180 GTDFERyrgATLLTPNLSEfeavvgkckdeAELVEKGMKLIADYDL--SALLVTRSEQGMTLlQPGKAPLHLPTQAREVY 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 1072804023 236 DTTGAGDTFNAAFAVALAEGKDIEAALRFANRAASLSV 273
Cdd:PRK11316 258 DVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVV 295
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
121-266 |
2.11e-07 |
|
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: 51.05 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 121 ALNALEQIEKVDMVLI-------QQEIPEETVDEVCKycHSHDIPIILNP-----------AP--ARPLKQETIDHATYL 180
Cdd:cd01173 63 GLEALGLLLEYDAVLTgylgsaeQVEAVAEIVKRLKE--KNPNLLYVCDPvmgdngklyvvAEeiVPVYRDLLVPLADII 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 181 TPNEHEASIL--FPELTISEA-------LALYPAKLFIT---EGKQGVRYSAGS--KEVLIPSFPVEPVDT--TGAGDTF 244
Cdd:cd01173 141 TPNQFELELLtgKKINDLEDAkaaaralHAKGPKTVVVTsveLADDDRIEMLGStaTEAWLVQRPKIPFPAyfNGTGDLF 220
|
170 180
....*....|....*....|..
gi 1072804023 245 NAAFAVALAEGKDIEAALRFAN 266
Cdd:cd01173 221 AALLLARLLKGKSLAEALEKAL 242
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
183-277 |
2.99e-07 |
|
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: 50.54 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 183 NEHEASILFPELTISEA----LALYPAKLFITEGKQGVRYSAGSKEVLIPSFPVEPV-DTTGAGDTFNAAFAVALAEGKD 257
Cdd:cd01946 170 NDGEARQLTGAANLVKAarliLAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDTFAGGFIGYLASQKD 249
|
90 100
....*....|....*....|....*
gi 1072804023 258 I-EAALR----FANRAASLSVCSFG 277
Cdd:cd01946 250 TsEANMRraiiYGSAMASFCVEDFG 274
|
|
| PLN02967 |
PLN02967 |
kinase |
33-97 |
5.64e-07 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 50.43 E-value: 5.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072804023 33 FQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGV--RTDYMEPVTHTESGTAHI 97
Cdd:PLN02967 238 FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVqtRSVCIDGKRATAVSTMKI 304
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
143-265 |
6.15e-06 |
|
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: 46.57 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 143 ETVDEVCKYCHSHD-IPIILNP-----APARPLKQETID--------HATYLTPNEHEASIL--FPELTISEA------- 199
Cdd:COG0351 79 EIIEAVAEILADYPlVPVVLDPvmvakSGDRLLDEDAVEalrelllpLATVVTPNLPEAEALlgIEITTLDDMreaakal 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072804023 200 LALYPAKLFIT----EGKQGV-RYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFA 265
Cdd:COG0351 159 LELGAKAVLVKgghlPGDEAVdVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREA 229
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
143-265 |
6.52e-05 |
|
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: 43.24 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 143 ETVDEVCKYCHSHDIPIILNP-----APARPLKQETID--------HATYLTPNEHEASIL--FPELTISEA-------L 200
Cdd:pfam08543 73 EIIEAVAEKLDKYGVPVVLDPvmvakSGDSLLDDEAIEalkeellpLATLITPNLPEAEALtgRKIKTLEDMkeaakklL 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072804023 201 ALYPAKLFITEGKQGVRYS-------AGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFA 265
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEAvvtdvlyDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
33-291 |
9.23e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 43.74 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 33 FQTVPGGKGANQAVAAARLGAQVFMVGKVGDDHYGTAILNNLKANGVRTDYMEPVTHTESGTAHIVLAEGDNSIVV---V 109
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKFRDGGKMVaetV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 110 KGANDDITPAYALNaLEQIEKVDMVLIQQEI---P--EETVDEVCKYCHSHDIPIILNPAPARPL---KQET-------- 173
Cdd:PLN02543 247 KEAAEDSLLASELN-LAVLKEARMFHFNSEVltsPsmQSTLFRAIELSKKFGGLIFFDLNLPLPLwrsRDETrelikkaw 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 174 ----------------IDHATY----------------LTPNEHEASILFPElTIS----EALALypakLFITEGKQGVR 217
Cdd:PLN02543 326 neadiievsrqeleflLDEDYYerkrnyppqyyaesfeQTKNWRDYYHYTPE-EIAplwhDGLKL----LLVTDGTLRIH 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 218 YSA--------GSKEVLIPSFpvePVDTTGAGDTFNAAFAVALA------EGKDI-EAALRFANRAASLSVCSFGAQGGM 282
Cdd:PLN02543 401 YYTpkfdgvvvGTEDVLITPF---TCDRTGSGDAVVAAIMRKLTtcpemfEDQDVlERQLRFAVAAGIISQWTIGAVRGF 477
|
....*....
gi 1072804023 283 PTRNEVEEL 291
Cdd:PLN02543 478 PTESATQNL 486
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
139-265 |
1.83e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 41.97 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 139 EIPEETVDevckYCHSH-DIPIILNPA---------PARPLKQETID---HATYLTPNEHEASILfPELTISE------- 198
Cdd:PRK12413 83 EIAEQALD----FIKGHpGIPVVLDPVlvckethdvEVSELRQELIQffpYVTVITPNLVEAELL-SGKEIKTledmkea 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072804023 199 ALALYP--AKLFITEGkqGVRYSA--------GSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFA 265
Cdd:PRK12413 158 AKKLYDlgAKAVVIKG--GNRLSQkkaidlfyDGKEFVILESPVLEKNNIGAGCTFASSIASQLVKGKSPLEAVKNS 232
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
143-265 |
1.88e-04 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 42.04 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 143 ETVDEVCKYCHSHDI-PIILNP-----APARPLKQETIDH--------ATYLTPNEHEASIL--FPELTISEAL------ 200
Cdd:PRK06427 86 EIIETVAEALKRYPIpPVVLDPvmiakSGDPLLADDAVAAlrerllplATLITPNLPEAEALtgLPIADTEDEMkaaara 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072804023 201 --ALYPAKLFIT-----EGKQGV-RYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGKDIEAALRFA 265
Cdd:PRK06427 166 lhALGCKAVLIKgghllDGEESVdWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
108-265 |
5.63e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 40.72 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 108 VVKGANDDITPAYALNALEQIEKVDMVLIQQEIPEETVDEVcKYCHSHDIPiiLNPAPARPLKQETIDHATYLTPNEHEA 187
Cdd:PRK12412 67 TIEGVGVDALKTGMLGSVEIIEMVAETIEKHNFKNVVVDPV-MVCKGADEA--LHPETNDCLRDVLVPKALVVTPNLFEA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 188 SILfPELTISEALALYPAKLFITE-GKQGVRYSAGSK-------EVL--------IPSFPVEPVDTTGAGDTFNAAFAVA 251
Cdd:PRK12412 144 YQL-SGVKINSLEDMKEAAKKIHAlGAKYVLIKGGSKlgtetaiDVLydgetfdlLESEKIDTTNTHGAGCTYSAAITAE 222
|
170
....*....|....
gi 1072804023 252 LAEGKDIEAALRFA 265
Cdd:PRK12412 223 LAKGKPVKEAVKTA 236
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
37-271 |
7.25e-03 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 37.46 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 37 PGGKGANQAVAAARLGAQ---VFMVGKVGDDHYgTAILNnlkANGVRTDYMEPVTHTESGTAHIVLAEGDNSIVVVKGAn 113
Cdd:PRK10294 37 PGGGGINVARAIAHLGGSataIFPAGGATGEHL-VSLLA---DENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 114 dDITP---AYALNALEQIEKVDMVLIQQEIPE----ETVDEVCKYCHSHDIPIILNPAPARPLKQETIDHATYLTPNEHE 186
Cdd:PRK10294 112 -ALNEdefRQLEEQVLEIESGAILVISGSLPPgvklEKLTQLISAAQKQGIRCIIDSSGDALSAALAIGNIELVKPNQKE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072804023 187 ASILF------PELTISEALALYPA----KLFITEGKQGVRYSAGSKEVLIPSFPVEPVDTTGAGDTFNAAFAVALAEGK 256
Cdd:PRK10294 191 LSALVnrdltqPDDVRKAAQELVNSgkakRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENA 270
|
250
....*....|....*...
gi 1072804023 257 DIEAALRF---ANRAASL 271
Cdd:PRK10294 271 SLEEMVRFgvaAGSAATL 288
|
|
| |
