|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-299 |
3.31e-100 |
|
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: 296.02 E-value: 3.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 6 IAVIGECMVELQKKEG-------QLKQSFGGDTLNTALYLSRLTKahdiKTSYVTALGNDPFSQEMLSAWQEEGIDTSLV 78
Cdd:cd01166 2 VVTIGEVMVDLSPPGGgrleqadSFRKFFGGAEANVAVGLARLGH----RVALVTAVGDDPFGRFILAELRREGVDTSHV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 79 LSVKEKQPGIYYIETDETGERYFHYWRNEAAAKFLFeqnESPLLVDKLYSYDAVYLSGITLAILTEEGKTqLFGFLERFK 158
Cdd:cd01166 78 RVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLT---PEDLDEAALAGADHLHLSGITLALSESAREA-LLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 159 AQGGKVIFDNNYRPKLWeSRENAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIERTSA--LGVDEIIIKRGSKDCL 236
Cdd:cd01166 154 ARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKLGAEGAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491579583 237 VVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAI 299
Cdd:cd01166 233 VYTGGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-308 |
2.02e-75 |
|
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: 233.24 E-value: 2.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 5 NIAVIGECMVEL------------QKKEGQLKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEG 72
Cdd:COG0524 1 DVLVIGEALVDLvarvdrlpkggeTVLAGSFRRSPGGAAANVAVALARL----GARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 73 IDTSLVLSVKEKQPGIYYIETDETGERYFHYWRNeAAAKFlfeqNESPLLVDKLYSYDAVYLSGITLAilTEEGKTQLFG 152
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRG-ANAEL----TPEDLDEALLAGADILHLGGITLA--SEPPREALLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 153 FLERFKAQGGKVIFDNNYRPKLWESrenAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIERTSALGVDEIIIKRGS 232
Cdd:COG0524 150 ALEAARAAGVPVSLDPNYRPALWEP---ARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491579583 233 KDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAiipREVMPDL 308
Cdd:COG0524 227 EGALLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGA---QPALPTR 298
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-300 |
5.05e-54 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 177.92 E-value: 5.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 5 NIAVIGECMVELQ----------KKEGQLKQSFGGDTLNTALYLSRLTkahdIKTSYVTALGNDPFSQEMLSAWQEEGID 74
Cdd:pfam00294 1 KVVVIGEANIDLIgnveglpgelVRVSTVEKGPGGKGANVAVALARLG----GDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 75 TSLVLSVKEKQPGIYYIETDETGERYFHYWRNEAAAkflFEQNESPLLVDKLYSYDAVYLSGITLAILTEEGKTQLFgfl 154
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAAD---LTPEELEENEDLLENADLLYISGSLPLGLPEATLEELI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 155 ERFKAQGgkvIFDNNYRPKLWESRENamswYLKILKHTDIALLTFEDEQMLYGDEH--LEQCIERTSAL---GVDEIIIK 229
Cdd:pfam00294 151 EAAKNGG---TFDPNLLDPLGAAREA----LLELLPLADLLKPNEEELEALTGAKLddIEEALAALHKLlakGIKTVIVT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491579583 230 RGSKDCLVVANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAII 300
Cdd:pfam00294 224 LGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-299 |
1.50e-47 |
|
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: 161.26 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 5 NIAVIGECMVELQKKEGQLKQSF----GGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLS 80
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALARL----GGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 81 VKEKQPGIYYIETDETGERYFHYWRNEAAAKFLFEQnespLLVDKLYSYDAVYLSGITLAilTEEGKTQLFGFLERFKAQ 160
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTE----LNPDLLSEADILHFGSIALA--SEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 161 GGKVIFDNNYRPKLWESRENAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIERTSALGVDEIIIKRGSKDCLVVAN 240
Cdd:cd01167 151 GVLISFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491579583 241 GEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAES--------AYSGHCmAGAVIQHKGAI 299
Cdd:cd01167 231 GGVGEVPGIPVE-VVDTTGAGDAFVAGLLAQLLSRGLLALDedelaealRFANAV-GALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
22-299 |
8.15e-30 |
|
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: 114.33 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 22 QLKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQPGIYYIETDETGER-- 99
Cdd:cd01942 30 DLRREFGGSAGNTAVALAKL----GLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQia 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 100 YFHywrnEAAAKFLfeQNESPLLVDKLYsyDAVYLSGIT-LAILTEEgktqlfgflerFKAQGGKVIFDnnyrPklweSR 178
Cdd:cd01942 106 YFY----PGAMDEL--EPNDEADPDGLA--DIVHLSSGPgLIELARE-----------LAAGGITVSFD----P----GQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 179 ENAMSW---YLKILKHTDIaLLTFEDEQMLygDEHLEQCIERTSALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDNVI 255
Cdd:cd01942 159 ELPRLSgeeLEEILERADI-LFVNDYEAEL--LKERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVKVV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 491579583 256 DTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAI 299
Cdd:cd01942 236 DTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-301 |
2.56e-25 |
|
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: 102.63 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 5 NIAVIGECMVEL------QKKEGQ------LKQSFGGDTLNTALYLSRLTkahdIKTSYVTALGNDPFSQEMLSAWQEEG 72
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrLPKPGEtvlgssFETGPGGKGANQAVAAARLG----ARVAMIGAVGDDAFGDELLENLREEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 73 IDTSLVLSVKEKQPGIYYIETDETGE----------RYFH------YWRNEAAAKFLFEQNESPLlvdklysyDAVYLsg 136
Cdd:cd01174 77 IDVSYVEVVVGAPTGTAVITVDESGEnrivvvpganGELTpadvdaALELIAAADVLLLQLEIPL--------ETVLA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 137 itlailteegktqlfgFLERFKAQGGKVIFdnNYRPklwesrenAMSWYLKILKHTDI--------ALLTfedeQMLYGD 208
Cdd:cd01174 147 ----------------ALRAARRAGVTVIL--NPAP--------ARPLPAELLALVDIlvpneteaALLT----GIEVTD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 209 EHLEQCIERT-SALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVdNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHC 287
Cdd:cd01174 197 EEDAEKAARLlLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV-KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANA 275
|
330
....*....|....*.
gi 491579583 288 MAGAVIQHKGAI--IP 301
Cdd:cd01174 276 AAALSVTRPGAQpsIP 291
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
23-298 |
7.19e-24 |
|
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: 98.44 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 23 LKQSFGGDTLNTALYLSRLTkahdIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQPGIYYIETDETGE---- 98
Cdd:TIGR02152 26 FQIGPGGKGANQAVAAARLG----AEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGEnriv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 99 ------RYF------HYWRNEAAAKFLFEQNESPLlvdklysyDAVYLSgitlailteegktqlfgfLERFKAQGGKVIF 166
Cdd:TIGR02152 102 vvaganAELtpedidAAEALIAESDIVLLQLEIPL--------ETVLEA------------------AKIAKKHGVKVIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 167 dnNYRPKLWESREnamswylKILKHTDIaLLTFEDE-QMLYGDE--HLEQCIERTSAL---GVDEIIIKRGSKDCLVVAN 240
Cdd:TIGR02152 156 --NPAPAIKDLDD-------ELLSLVDI-ITPNETEaEILTGIEvtDEEDAEKAAEKLlekGVKNVIITLGSKGALLVSK 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 491579583 241 GEAQYVAPNKVdNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGA 298
Cdd:TIGR02152 226 DESKLIPAFKV-KAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
6-270 |
2.72e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 97.31 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 6 IAVIGECMVEL-QKKEGQLKQSFGGDTLNTALYLSRLTKahdiKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEK 84
Cdd:PRK09434 5 VWVLGDAVVDLiPEGENRYLKCPGGAPANVAVGIARLGG----ESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 85 QPGIYYIETDETGERYFHYWRNEAAAKFL-------FEQNEspllvdklysydAVYLSGITLAilTEEGKTQLFGFLERF 157
Cdd:PRK09434 81 RTSTVVVDLDDQGERSFTFMVRPSADLFLqpqdlppFRQGE------------WLHLCSIALS--AEPSRSTTFEAMRRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 158 KAQGGKVIFDNNYRPKLWESRENAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIER-TSALGVDEIIIKRGSKDCL 236
Cdd:PRK09434 147 KAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLGAEGVL 226
|
250 260 270
....*....|....*....|....*....|....
gi 491579583 237 VVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLA 270
Cdd:PRK09434 227 VHTRGQVQHFPAPSVD-PVDTTGAGDAFVAGLLA 259
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
22-298 |
1.22e-22 |
|
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: 94.73 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 22 QLKQSF-GGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLsVKEKQPGIYYIETDEtGERY 100
Cdd:cd01940 15 HLGKMYpGGNALNVAVYAKRL----GHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCR-VKEGENAVADVELVD-GDRI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 101 FHYWRNEAAAKFLFEQNEspllVDKLYSYDAVYLSGITLAILTEEGKTQLfgflerfKAQGGKVIFDNNYRpklWESREn 180
Cdd:cd01940 89 FGLSNKGGVAREHPFEAD----LEYLSQFDLVHTGIYSHEGHLEKALQAL-------VGAGALISFDFSDR---WDDDY- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 181 amswYLKILKHTDIALLTFEDEqmlyGDEHLEQCIERTSALGVDEIIIKRGSKDCLVvANGEAQYVAPNKVDNVIDTTAA 260
Cdd:cd01940 154 ----LQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGEDGAIA-YDGAVFYSVAPRPVEVVDTLGA 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 491579583 261 GDSFSAGFLAKRLTGGNA-AESAYSGHCMAGAVIQHKGA 298
Cdd:cd01940 225 GDSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
19-301 |
7.94e-20 |
|
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: 87.67 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 19 KEGQLKQSFGGDTLNTALYLSRLTKahdiKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVlsVKEKQP-GIYYIETDETG 97
Cdd:cd01168 46 AKLPVKYIAGGSAANTIRGAAALGG----SAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQ--VQPDGPtGTCAVLVTPDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 98 ERYFHywRNEAAAKFLfeqNESPLLVDKLYSYDAVYLSGITLailteEGKTQLFGFL-ERFKAQGGKVIFD-------NN 169
Cdd:cd01168 120 ERTMC--TYLGAANEL---SPDDLDWSLLAKAKYLYLEGYLL-----TVPPEAILLAaEHAKENGVKIALNlsapfivQR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 170 YRPKLWEsrenamswylkILKHTDIaLLTFEDEQMLYGD---EHLEQCIERTSALGVDEIIIKRGSKDCLVVANGEAQYV 246
Cdd:cd01168 190 FKEALLE-----------LLPYVDI-LFGNEEEAEALAEaetTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPV 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491579583 247 APNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAIIP 301
Cdd:cd01168 258 PAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
5-298 |
3.41e-18 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 83.25 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 5 NIAVIGECMVEL--------QKKEG----QLKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEG 72
Cdd:PTZ00292 17 DVVVVGSSNTDLigyvdrmpQVGETlhgtSFHKGFGGKGANQAVMASKL----GAKVAMVGMVGTDGFGSDTIKNFKRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 73 IDTSLVLSVKEKQPGIYYIETDE-------------TGERYFHYWRNEAA-----AKFLFEQNESPLLVdklySYDAvyl 134
Cdd:PTZ00292 93 VNTSFVSRTENSSTGLAMIFVDTktgnneiviipgaNNALTPQMVDAQTDniqniCKYLICQNEIPLET----TLDA--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 135 sgitlailteegktqlfgfLERFKAQGGKVIFDNNYRPKLWESRENAmswylKILKHTDIALLTFEDEQMLYG-----DE 209
Cdd:PTZ00292 166 -------------------LKEAKERGCYTVFNPAPAPKLAEVEIIK-----PFLKYVSLFCVNEVEAALITGmevtdTE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 210 HLEQCIERTSALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMA 289
Cdd:PTZ00292 222 SAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
|
....*....
gi 491579583 290 GAVIQHKGA 298
Cdd:PTZ00292 302 AISVTRHGT 310
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
28-309 |
1.18e-17 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 82.00 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 28 GGDTLNTALYLSRLTKAHDIKTSYVTALGNDPFSQEMLSAWQEEGIDTslVLSVKEKQPgiyyietdeTGERYFHYWRNE 107
Cdd:PTZ00247 62 GGSALNTARVAQWMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEM--LFEYTTKAP---------TGTCAVLVCGKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 108 --------AAAKFLFEQNESPLLVDKLYSYDAVYLSGITLAILTEEGKtQLFGflerfKAQGGKVIFDNNYR-PKLWESR 178
Cdd:PTZ00247 131 rslvanlgAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFLTVSPNNVL-QVAK-----HARESGKLFCLNLSaPFISQFF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 179 ENAMswyLKILKHTDI------ALLTFEDeQMLYGDEHLEQCIERTSAL----GVDE--IIIKRGSKDCLVVANGEAQYV 246
Cdd:PTZ00247 205 FERL---LQVLPYVDIlfgneeEAKTFAK-AMKWDTEDLKEIAARIAMLpkysGTRPrlVVFTQGPEPTLIATKDGVTSV 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491579583 247 APNKVD--NVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAIIPrEVMPDLP 309
Cdd:PTZ00247 281 PVPPLDqeKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP-EKPPFLP 344
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
6-298 |
1.82e-15 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 74.77 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 6 IAVIGECMVELQKKEGqlKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLvLSVKEKQ 85
Cdd:PRK09813 3 LATIGDNCVDIYPQLG--KAFSGGNAVNVAVYCTRY----GIQPGCITWVGDDDYGTKLKQDLARMGVDISH-VHTKHGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 86 PGIYYIETDEtGERYFHYWRNEAAAKFLFEQNEspllVDKLYSYDAVYlsgitlailteegkTQLFGFLE----RFKAQG 161
Cdd:PRK09813 76 TAQTQVELHD-NDRVFGDYTEGVMADFALSEED----YAWLAQYDIVH--------------AAIWGHAEdafpQLHAAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 162 GKVIFDNNYRPK--LWESrenamswylkILKHTDIALLTFEDEqmlygDEHLEQCIERTSALGVDEIIIKRGSKDCLVVa 239
Cdd:PRK09813 137 KLTAFDFSDKWDspLWQT----------LVPHLDYAFASAPQE-----DEFLRLKMKAIVARGAGVVIVTLGENGSIAW- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491579583 240 NGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGA 298
Cdd:PRK09813 201 DGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
10-281 |
1.86e-12 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 66.86 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 10 GECMVELQKKEG-------QLKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVK 82
Cdd:NF041332 8 GETMLRLSPPGGerletadELDVRAGGAESNVAVAAARL----GADATWLSKLPDSPLGRRVVGELRSHGVDTDVVWDDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 83 EKQpGIYYIET-DETGERYFHYWRNEAAAkflfeQNESP--LLVDKLYSYDAVYLSGITLAI--LTEEGKTQLfgfLERF 157
Cdd:NF041332 84 GRQ-GTYYLEHgGEPRGTNVIYDRADAAV-----TTATPeeLPLDRIRDAEVFYTSGITPALseTLAETTAAL---LEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 158 KAQGGKVIFDNNYRPKLWeSRENAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIERTSA--LGVDEIIIKRGSKDC 235
Cdd:NF041332 155 QEAGTTTAFDLNYRSKLW-SPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHGLAseYDFETVVVTRGEEGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 491579583 236 LVVANG--------EAQYVAPnkvdnvIDTtaaGDSFSAGFLAKRLTGGNAAES 281
Cdd:NF041332 234 LALHDGevheqpayEADTVDP------IGT---GDAFVGGFLARRLAGGDVPTA 278
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
128-270 |
3.56e-12 |
|
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: 64.04 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 128 SYDAVYLSGITLAI-LTEEgktqlfgFLERFKAQGGKVIFDNNYRPKLWESREnamswYLKILKHTDIALLTFEDEQMLY 206
Cdd:cd00287 57 GADAVVISGLSPAPeAVLD-------ALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEALT 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491579583 207 G--DEHLEQCIERTSAL---GVDEIIIKRGSKDCLVVANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLA 270
Cdd:cd00287 125 GrrDLEVKEAAEAAALLlskGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAA 193
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
21-295 |
3.36e-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: 59.63 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 21 GQLKQSFGGDTLNTALYLSRLTkahdIKTSYVTALGNDPFSQEMLSAWQEEGID----------TSLVLSVKEK------ 84
Cdd:cd01941 28 GHVKQSPGGVGRNIAENLARLG----VSVALLSAVGDDSEGESILEESEKAGLNvrgivfegrsTASYTAILDKdgdlvv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 85 ---QPGIYyietDETGERYFHYWRNeaaakfLFEqNESPLLVDklysydaVYLSGITLAILTEEGKTQLFG-FLERFKAQ 160
Cdd:cd01941 104 alaDMDIY----ELLTPDFLRKIRE------ALK-EAKPIVVD-------ANLPEEALEYLLALAAKHGVPvAFEPTSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 161 GGKVIFDNNyrpklwesreNAMSWyLKILKHTDIALLTFEDEQMLygDEHLEQCIERTSalGVDEIIIKRGSKDCLVV-- 238
Cdd:cd01941 166 KLKKLFYLL----------HAIDL-LTPNRAELEALAGALIENNE--DENKAAKILLLP--GIKNVIVTLGAKGVLLSsr 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 491579583 239 -ANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQH 295
Cdd:cd01941 231 eGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
27-298 |
7.50e-10 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 58.73 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 27 FGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQPGIYYIETDETGE-------- 98
Cdd:PRK11142 38 FGGKGANQAVAAARL----GADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGEnsigihag 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 99 -------RYFHYWRNE-AAAKFLFEQNESPLlvdklysydavylSGITLAilteegktqlfgfLERFKAQGGKVIFdnNY 170
Cdd:PRK11142 114 anaaltpALVEAHRELiANADALLMQLETPL-------------ETVLAA-------------AKIAKQHGTKVIL--NP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 171 RPklwesrenAMSWYLKILKHTDI--------ALLT---FEDE-------QMLYgdehleqciertsALGVDEIIIKRGS 232
Cdd:PRK11142 166 AP--------ARELPDELLALVDIitpneteaEKLTgirVEDDddaakaaQVLH-------------QKGIETVLITLGS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491579583 233 KDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGA 298
Cdd:PRK11142 225 RGVWLSENGEGQRVPGFRVQ-AVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
24-271 |
2.45e-08 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 54.24 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 24 KQSFGGDTLNTALYLSRLTKahdiKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQPGIYYIETDETGERYFHY 103
Cdd:PLN02323 39 KKAPGGAPANVAVGISRLGG----SSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 104 WRNeAAAKFLFEQNEspLLVDKLYSYDAVYLSGITLaiLTEEGKTQLFGFLERFKAQGGKVIFDNNYRPKLWESRENAMS 183
Cdd:PLN02323 115 YRN-PSADMLLRESE--LDLDLIRKAKIFHYGSISL--ITEPCRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAARE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 184 WYLKILKHTDIALLTFEDEQMLYGDEHLEqciertsalgvDEIIIKRGSKDC--LVVANGE--AQYVAPN--------KV 251
Cdd:PLN02323 190 GIMSIWDEADIIKVSDEEVEFLTGGDDPD-----------DDTVVKLWHPNLklLLVTEGEegCRYYTKDfkgrvegfKV 258
|
250 260
....*....|....*....|
gi 491579583 252 DnVIDTTAAGDSFSAGFLAK 271
Cdd:PLN02323 259 K-AVDTTGAGDAFVGGLLSQ 277
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
22-297 |
2.91e-08 |
|
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: 53.97 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 22 QLKQSFGGdTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQPGIY-YIETDetGERY 100
Cdd:cd01944 30 SKSYVIGG-GFNVMVAASRL----GIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVaLVEPD--GERS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 101 FHYW---RNEAAAKFLFEQNESPllvdklysYDAVYLSGITLA-------ILTE------EGKTQLFGFLERFKAQGGKV 164
Cdd:cd01944 103 FISIsgaEQDWSTEWFATLTVAP--------YDYVYLSGYTLAsenaskvILLEwlealpAGTTLVFDPGPRISDIPDTI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 165 IFDNNYRPKLWES-RENAMswylkilkhtdiallTFEDEQMLYGDEHLEQCIERTSALgvdeIIIKRGSKDCLV-VANGE 242
Cdd:cd01944 175 LQALMAKRPIWSCnREEAA---------------IFAERGDPAAEASALRIYAKTAAP----VVVRLGSNGAWIrLPDGN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491579583 243 AQYVAPNKVdNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKG 297
Cdd:cd01944 236 THIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
22-281 |
7.42e-08 |
|
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: 52.68 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 22 QLKQSFGGDTLNTALYLSRLtkahDIKTSYVTALGNDPFSQEMLSAWQEEGIDTSLVLSVKEKQP---GIYYIETDETGE 98
Cdd:cd01945 30 DYAVIGGGNAANAAVAVARL----GGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSpisSITDITGDRATI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 99 RYFHYWRNEAAAKFLFE--QNESPLLVDKlYSYDAVYL-------SGITLAILTEEGKTqlfGFLERFKAQGGKVIFDNN 169
Cdd:cd01945 106 SITAIDTQAAPDSLPDAilGGADAVLVDG-RQPEAALHlaqearaRGIPIPLDLDGGGL---RVLEELLPLADHAICSEN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 170 YRPKLWESRENAMSWYLKILKHTDIAlltfedeqmlygdehleqciertsalgvdeiiIKRGSKDCLVV-ANGEAQYVAP 248
Cdd:cd01945 182 FLRPNTGSADDEALELLASLGIPFVA--------------------------------VTLGEAGCLWLeRDGELFHVPA 229
|
250 260 270
....*....|....*....|....*....|...
gi 491579583 249 NKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAES 281
Cdd:cd01945 230 FPVE-VVDTTGAGDVFHGAFAHALAEGMPLREA 261
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
24-299 |
7.58e-08 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 52.42 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 24 KQSFGGDTLNTALYLSRLTkaHDIKtsYVTALGNDPFSQEMLSAWQEEGIdtSLVLSVKEKQPGIYYIETDETGERYFHY 103
Cdd:cd01947 32 RESPGGGGANVAVQLAKLG--NDVR--FFSNLGRDEIGIQSLEELESGGD--KHTVAWRDKPTRKTLSFIDPNGERTITV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 104 WRNEaaakfLFEQNESPLLVdklySYDAVYLSGitLAILTEegktqlfgfLERFKAQGGKVIFDNNYRPKLWESREnams 183
Cdd:cd01947 106 PGER-----LEDDLKWPILD----EGDGVFITA--AAVDKE---------AIRKCRETKLVILQVTPRVRVDELNQ---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 184 wylkILKHTDIaLLTFEDEQMLYGDEhleqciERTSALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDnVIDTTAAGDS 263
Cdd:cd01947 162 ----ALIPLDI-LIGSRLDPGELVVA------EKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAK-VPDSTGAGDS 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 491579583 264 FSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAI 299
Cdd:cd01947 230 FAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
28-301 |
1.15e-07 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 52.41 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 28 GGDTLNT---ALYLSRLTKAhdikTSYVTALGNDPFSQEMLSAWQEEGIDtslvlsvkekqpgIYYIETDET-------- 96
Cdd:PLN02548 52 GGATQNSirvAQWMLQIPGA----TSYMGCIGKDKFGEEMKKCATAAGVN-------------VHYYEDESTptgtcavl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 97 ---GERYFhyWRNEAAAKFL----FEQNESPLLVDKLYSYdavYLSGITLAILTEEGKTqlfgfLERFKAQGGKVIFDNN 169
Cdd:PLN02548 115 vvgGERSL--VANLSAANCYkvehLKKPENWALVEKAKFY---YIAGFFLTVSPESIML-----VAEHAAANNKTFMMNL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 170 YRPKLWESRENAMswyLKILKHTDIaLLTFEDEQMLYGDEH------LEQCIERTSALGVDE------IIIKRGSKDCLV 237
Cdd:PLN02548 185 SAPFICEFFKDQL---MEALPYVDF-LFGNETEARTFAKVQgwetedVEEIALKISALPKASgthkrtVVITQGADPTVV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491579583 238 VANGEAQY--VAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAIIP 301
Cdd:PLN02548 261 AEDGKVKEfpVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYP 326
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
220-302 |
6.61e-07 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 49.75 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 220 ALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAI 299
Cdd:COG1105 211 ERGAENVVVSLGADGALLVTEDGVYRAKPPKVE-VVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG 289
|
...
gi 491579583 300 IPR 302
Cdd:COG1105 290 LPD 292
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
179-293 |
1.68e-06 |
|
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: 48.62 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 179 ENAMSWYLKILKHTDIALLTFEDEQMLYGDEHLEQCIERTSALGVDEIIIKRGSKDCLVVANgEAQYVAPN-KVDNVIDT 257
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTD-DGYFAAPAyPLESVFDP 229
|
90 100 110
....*....|....*....|....*....|....*.
gi 491579583 258 TAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVI 293
Cdd:cd01946 230 TGAGDTFAGGFIGYLASQKDTSEANMRRAIIYGSAM 265
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
158-290 |
3.35e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 48.29 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 158 KAQGGKVIFDNNYRPKLWESRENAMSWYLK-ILKHTDIALLTFEDEQMLYG---DEHLEQCIERTSAlGVDEIIIKRGSK 233
Cdd:PLN02341 251 IDVGTAVFFDPGPRGKSLLVGTPDERRALEhLLRMSDVLLLTSEEAEALTGirnPILAGQELLRPGI-RTKWVVVKMGSK 329
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491579583 234 DCLVVANGEAQYVAPNKVdNVIDTTAAGDSFSA----GFLAK-----RLTGGNAAESAYSGHCMAG 290
Cdd:PLN02341 330 GSILVTRSSVSCAPAFKV-NVVDTVGCGDSFAAaialGYIHNlplvnTLTLANAVGAATAMGCGAG 394
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
158-307 |
8.14e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 46.71 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 158 KAQGGKVIFD-------NNYRPKLwesrenamswyLKILKHTDIAL-LTFEDEQM-LYGDEhLEQCIErtSALG-----V 223
Cdd:PLN02379 201 KQEGLSVSLDlasfemvRNFRSPL-----------LQLLESGKIDLcFANEDEAReLLRGE-QESDPE--AALEflakyC 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 224 DEIIIKRGSKDCLVVANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAiiprE 303
Cdd:PLN02379 267 NWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGG----E 342
|
....
gi 491579583 304 VMPD 307
Cdd:PLN02379 343 VTPE 346
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
197-301 |
1.00e-05 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 46.41 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 197 LTFEDEQMLYGDEHLEQciertsalGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGG 276
Cdd:TIGR03168 195 LKTLEEIIEAARELLDR--------GAENVLVSLGADGALLVTKEGALKATPPKVE-VVNTVGAGDSMVAGFLAGLARGL 265
|
90 100
....*....|....*....|....*
gi 491579583 277 NAAESAYSGHCMAGAVIQHKGAIIP 301
Cdd:TIGR03168 266 SLEEALRFAVAAGSAAAFSPGTGLP 290
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
220-301 |
2.79e-05 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 44.89 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 220 ALGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGAI 299
Cdd:TIGR03828 210 DLGAENVLISLGADGALLVTKEGALFAQPPKGE-VVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTG 288
|
..
gi 491579583 300 IP 301
Cdd:TIGR03828 289 LP 290
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
209-294 |
4.72e-05 |
|
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: 44.09 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 209 EHLEQCIERTsaLGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCM 288
Cdd:cd01172 207 EAAGEKLLEL--LNLEALLVTLGEEGMTLFERDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAA 284
|
....*.
gi 491579583 289 AGAVIQ 294
Cdd:cd01172 285 AGVVVG 290
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
205-297 |
9.28e-05 |
|
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: 43.29 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 205 LYGDEHLEQCIERTSALGVDEIIIKRGSKDCLVVaNGEAQYVAPNKVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYS 284
Cdd:cd01164 196 LGDEEDVIAAARKLIERGAENVLVSLGADGALLV-TKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRL 274
|
90
....*....|...
gi 491579583 285 GHCMAGAVIQHKG 297
Cdd:cd01164 275 AVAAGSATAFSPG 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
184-302 |
1.76e-04 |
|
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: 42.71 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579583 184 WYLKILKHTDIALLTFEDEQMLYGDEH-----LEQCIERTSAL--------GVDEIIIKRGSKDCLVVAN---GEAQYVA 247
Cdd:cd01943 173 DLLQALPRVDVFSPNLEEAARLLGLPTsepssDEEKEAVLQALlfsgilqdPGGGVVLRCGKLGCYVGSAdsgPELWLPA 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491579583 248 PN-KVDNVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVIQHKGaiIPR 302
Cdd:cd01943 253 YHtKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG--LPR 306
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
221-293 |
3.11e-04 |
|
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: 41.62 E-value: 3.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491579583 221 LGVDEIIIKRGSKDCLVVANGEAQYVAPNKVDnVIDTTAAGDSFSAGFLAKRLTGGNAAESAYSGHCMAGAVI 293
Cdd:cd01937 182 TGVKEIIVTDGEEGGYIFDGNGKYTIPASKKD-VVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| |
