|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-301 |
4.58e-107 |
|
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: 313.36 E-value: 4.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIGECMIELS-------EKGADVKRGFGGDTLNTSVYIARQvdpaALTVHYVTALGTDSFSQQMLDAWHGENVDTSL 76
Cdd:cd01166 1 DVVTIGEVMVDLSppgggrlEQADSFRKFFGGAEANVAVGLARL----GHRVALVTAVGDDPFGRFILAELRREGVDTSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 77 TQRMENRLPGLYYIETDSTGERTFYYWRNEAAAKFWLESEQSAAIceeLANFDYLYLSGISLAIlSPTSREKLLSLLREC 156
Cdd:cd01166 77 VRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAA---LAGADHLHLSGITLAL-SESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 157 RANGGKVIFDNNYRPRLWaSKEETQQVYQQMLECTDIAFLTLDDEDALWGQQPVEDVIART--HNAGVKEVVVKRGADSC 234
Cdd:cd01166 153 KARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERAlaLALGVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111606 235 LVSiAGEGLVDVPAvklPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01166 232 LVY-TGGGRVFVPA---YPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-308 |
2.92e-76 |
|
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: 235.16 E-value: 2.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIGECMIEL------------SEKGADVKRGFGGDTLNTSVYIARqvdpAALTVHYVTALGTDSFSQQMLDAWHGEN 71
Cdd:COG0524 1 DVLVIGEALVDLvarvdrlpkggeTVLAGSFRRSPGGAAANVAVALAR----LGARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 72 VDTSLTQRMENRLPGLYYIETDSTGERTFYYWRneAAAKFWLESEQSAAIceeLANFDYLYLSGISLAilSPTSREKLLS 151
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEAL---LAGADILHLGGITLA--SEPPREALLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 152 LLRECRANGGKVIFDNNYRPRLWaskEETQQVYQQMLECTDIAFLTLDDEDALWGQQPVEDVIARTHNAGVKEVVVKRGA 231
Cdd:COG0524 150 ALEAARAAGVPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111606 232 DSCLVSIAGEgLVDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAiipREAMP 308
Cdd:COG0524 227 EGALLYTGGE-VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGA---QPALP 296
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-302 |
4.76e-75 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 231.85 E-value: 4.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIGECMIELSE----------KGADVKRGFGGDTLNTSVYIARQVdpaaLTVHYVTALGTDSFSQQMLDAWHGENVD 73
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvRVSTVEKGPGGKGANVAVALARLG----GDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 74 TSLTQRMENRLPGLYYIETDSTGERTFYYWRNEAAAKFWLESEQSAAICEelaNFDYLYLSGIslaiLSPTSREKLLSLL 153
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLE---NADLLYISGS----LPLGLPEATLEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 154 RECRANGGKviFDNNYRPRLWAskeeTQQVYQQMLECTDIAFLTLDDEDALWGQQ--PVEDVIARTHN---AGVKEVVVK 228
Cdd:pfam00294 150 IEAAKNGGT--FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHKllaKGIKTVIVT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111606 229 RGADSCLVSIaGEGLVDVPAVklPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAII 302
Cdd:pfam00294 224 LGADGALVVE-GDGEVHVPAV--PKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-301 |
7.52e-44 |
|
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: 151.63 E-value: 7.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIGECMIELSEKGADVKRGF----GGDTLNTSVYIARQVDPAALtvhyVTALGTDSFSQQMLDAWHGENVDTSLTQR 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALARLGGKAAF----IGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 80 MENRLPGLYYIETDSTGERTFYYWRNEAAAKFWLESEQSAAiceeLANFDYLYLSGISLAilSPTSREKLLSLLRECRAN 159
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDL----LSEADILHFGSIALA--SEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 160 GGKVIFDNNYRPRLWASKEETQQVYQQMLECTDIafLTLDDEDALW--GQQPVEDVIARTHNAGVKEVVVKRGADSCLVS 237
Cdd:cd01167 151 GVLISFDPNLRPPLWRDEEEARERIAELLELADI--VKLSDEELELlfGEEDPEEIAALLLLFGLKLVLVTRGADGALLY 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111606 238 IaGEGLVDVPAvklPKEKVIDTTAAGDSFSAGYLA-------VRLTGGSAEDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01167 229 T-KGGVGEVPG---IPVEVVDTTGAGDAFVAGLLAqllsrglLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
20-301 |
1.16e-28 |
|
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: 111.25 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 20 ADVKRGFGGDTLNTSVYIAR---QVDPAAltvhyvtALGTDSFSQQMLDAWHGENVDTSLTQRMENRLPGLYYIETDSTG 96
Cdd:cd01942 29 KDLRREFGGSAGNTAVALAKlglSPGLVA-------AVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 97 ERTFY-YWrneAAAKFWleseqsaaicEELANFDYLYLsgisLAILSPTSREKLLSLLRECRANGGKVIFDNNyrPRLWA 175
Cdd:cd01942 102 NQIAYfYP---GAMDEL----------EPNDEADPDGL----ADIVHLSSGPGLIELARELAAGGITVSFDPG--QELPR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 176 -SKEEtqqvYQQMLECTDIAF-----LTLDDEDALWGQQPVedviarthNAGVKEVVVKRGADSCLVsIAGEGLVDVPAV 249
Cdd:cd01942 163 lSGEE----LEEILERADILFvndyeAELLKERTGLSEAEL--------ASGVRVVVVTLGPKGAIV-FEDGEEVEVPAV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 90111606 250 klPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01942 230 --PAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-272 |
2.56e-24 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 100.01 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 1 MSKKIAVIGECMIEL-SEKGADVKRGFGGDTLNTSVYIARQVDPAAltvhYVTALGTDSFSQQMLDAWHGENVDTSL--- 76
Cdd:PRK09434 1 MMNKVWVLGDAVVDLiPEGENRYLKCPGGAPANVAVGIARLGGESG----FIGRVGDDPFGRFMQQTLQDEGVDTTYlrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 77 --TQRMENRLPGLyyietDSTGERTFYYWRNEAAAKFwLESEqsaaiceELANF---DYLYLSGISLAilSPTSREKLLS 151
Cdd:PRK09434 77 dpAHRTSTVVVDL-----DDQGERSFTFMVRPSADLF-LQPQ-------DLPPFrqgEWLHLCSIALS--AEPSRSTTFE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 152 LLRECRANGGKVIFDNNYRPRLWASKEETQQVYQQMLECTDIAFLTLDDEDALWGQQPVEDVIAR-THNAGVKEVVVKRG 230
Cdd:PRK09434 142 AMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 90111606 231 ADSCLVSIAGEGLVdVPAVKLpkeKVIDTTAAGDSFSAGYLA 272
Cdd:PRK09434 222 AEGVLVHTRGQVQH-FPAPSV---DPVDTTGAGDAFVAGLLA 259
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-308 |
1.12e-22 |
|
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: 95.31 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIGECMIEL------------SEKGADVKRGFGGDTLNTSVYIARqvdpAALTVHYVTALGTDSFSQQMLDAWHGEN 71
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrlpkpgeTVLGSSFETGPGGKGANQAVAAAR----LGARVAMIGAVGDDAFGDELLENLREEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 72 VDTSLTQRMENRLPGLYYIETDSTGErtfyywrN------EAAAKFWLESEQSAAicEELANFDYLYLSG-ISLailsPT 144
Cdd:cd01174 77 IDVSYVEVVVGAPTGTAVITVDESGE-------NrivvvpGANGELTPADVDAAL--ELIAAADVLLLQLeIPL----ET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 145 SREKLlsllRECRANGGKVIFdnNYRPrlwaskeeTQQVYQQMLECTDI--------AFLTLDDEDALWGQQPVEDVIar 216
Cdd:cd01174 144 VLAAL----RAARRAGVTVIL--NPAP--------ARPLPAELLALVDIlvpneteaALLTGIEVTDEEDAEKAARLL-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 217 tHNAGVKEVVVKRGADSCLVsIAGEGLVDVPAvklPKEKVIDTTAAGDSFsAGYLAVRLT-GGSAEDAAKRGHLTASTVI 295
Cdd:cd01174 208 -LAKGVKNVIVTLGAKGALL-ASGGEVEHVPA---FKVKAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAAAALSV 281
|
330
....*....|...
gi 90111606 296 QYRGAIiprEAMP 308
Cdd:cd01174 282 TRPGAQ---PSIP 291
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
27-300 |
2.20e-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: 93.96 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 27 GGDTLNTSVYIARQVDPAAltvhYVTALGTDSFSQQMLDAWHGENVDTS--LTQRMENRlpglYYIETDSTGERTFyywr 104
Cdd:cd01940 22 GGNALNVAVYAKRLGHESA----YIGAVGNDDAGAHVRSTLKRLGVDIShcRVKEGENA----VADVELVDGDRIF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 105 neaaakfwLESEQSAAICEELANFDYLYLSGISLAILSPTSREK-LLSLLRECRANGGKVIFDNNYRprlWASKEetqqv 183
Cdd:cd01940 90 --------GLSNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGhLEKALQALVGAGALISFDFSDR---WDDDY----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 184 YQQMLECTDIAFLTLDDEDAlwgqQPVEDVIARTHNAGVKEVVVKRGADSCLVSiAGEGLVDVPAVKlpkEKVIDTTAAG 263
Cdd:cd01940 154 LQLVCPYVDFAFFSASDLSD----EEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRP---VEVVDTLGAG 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 90111606 264 DSFSAGYLAVRLTGGSA-EDAAKRGHLTASTVIQYRGA 300
Cdd:cd01940 226 DSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
27-303 |
1.70e-20 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 90.09 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 27 GGDTLNTsVYIARQVDPAALT-VHYVTALGTDSFSQQMLDAWHGENVDTsltqrmenrlpgLYYIETDS-TGERTFYYWR 104
Cdd:PTZ00247 62 GGSALNT-ARVAQWMLQAPKGfVCYVGCVGDDRFAEILKEAAEKDGVEM------------LFEYTTKApTGTCAVLVCG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 105 NE--------AAAKFWLESEQSAAICEELANFDYLYLSGISLAilspTSREKLLSLLRECRANGGKVIFDNNYRPRLWAS 176
Cdd:PTZ00247 129 KErslvanlgAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFLT----VSPNNVLQVAKHARESGKLFCLNLSAPFISQFF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 177 KEETQQVyqqmLECTDIAFLtlDDEDAL-------WGQQPVEDVIART-----HNAGVKEVVV-KRGADSCLVSIAGeGL 243
Cdd:PTZ00247 205 FERLLQV----LPYVDILFG--NEEEAKtfakamkWDTEDLKEIAARIamlpkYSGTRPRLVVfTQGPEPTLIATKD-GV 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 244 VDVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAIIP 303
Cdd:PTZ00247 278 TSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
18-303 |
6.67e-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: 88.05 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 18 KGADVKRGFGGDTLNTSVyIARQVDPAAltvHYVTALGTDSFSQQMLDAWHGENVDTSLtQRMENRLPGLYYIETDSTGE 97
Cdd:cd01168 46 AKLPVKYIAGGSAANTIR-GAAALGGSA---AFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 98 RTFYywRNEAAAKFWLESEQSAAIceeLANFDYLYLSGIslaiLSPTSREKLLSLLRECRANGGKVIFD-------NNYR 170
Cdd:cd01168 121 RTMC--TYLGAANELSPDDLDWSL---LAKAKYLYLEGY----LLTVPPEAILLAAEHAKENGVKIALNlsapfivQRFK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 171 PRLWaskeetqqvyqQMLECTDIAFLTLDDEDALWGQQPVEDVIA--RTHNAGVKEVVVKRGADSCLVsIAGEGLVDVPA 248
Cdd:cd01168 192 EALL-----------ELLPYVDILFGNEEEAEALAEAETTDDLEAalKLLALRCRIVVITQGAKGAVV-VEGGEVYPVPA 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90111606 249 VklPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAIIP 303
Cdd:cd01168 260 I--PVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
3-300 |
6.00e-19 |
|
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: 84.96 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 3 KKIAVIGECMIelsekGADVKRGFGGDTLNTSVYIARqvdpAALTVHYVTALGTDSFSQQMLDAWHGENVDTSLTQRMEN 82
Cdd:TIGR02152 12 DRLPKPGETVH-----GHSFQIGPGGKGANQAVAAAR----LGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 83 RLPGLYYIETDSTGERTFYYWrneAAAKFWLESEQSAAICEELANFDYLYLSgisLAILSPTSREkllsLLRECRANGGK 162
Cdd:TIGR02152 83 TPTGTAFITVDDTGENRIVVV---AGANAELTPEDIDAAEALIAESDIVLLQ---LEIPLETVLE----AAKIAKKHGVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 163 VIFdnNYRPRLWASKEEtqqvyqqMLECTDI--------AFLT---LDDEDAlwgqqpVEDVIARTHNAGVKEVVVKRGA 231
Cdd:TIGR02152 153 VIL--NPAPAIKDLDDE-------LLSLVDIitpneteaEILTgieVTDEED------AEKAAEKLLEKGVKNVIITLGS 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 232 DSCLVSIAGEgLVDVPAVKLpkeKVIDTTAAGDSFSAGyLAVRLT-GGSAEDAAKRGHLTASTVIQYRGA 300
Cdd:TIGR02152 218 KGALLVSKDE-SKLIPAFKV---KAVDTTAAGDTFNGA-FAVALAeGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-300 |
8.78e-16 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 75.54 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 3 KKIAVIGECMIELSEKgadVKRGF-GGDTLNTSVYIARQVDPAAltvhYVTALGTDSFSQQMLDAWHGENVDTSLTQRME 81
Cdd:PRK09813 1 KKLATIGDNCVDIYPQ---LGKAFsGGNAVNVAVYCTRYGIQPG----CITWVGDDDYGTKLKQDLARMGVDISHVHTKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 82 NRlPGLYYIETDStGERTFYYWRNEAAAKFWLESEQSAAICEelanFDYlylsgISLAILSPTSrekllSLLRECRANGG 161
Cdd:PRK09813 74 GV-TAQTQVELHD-NDRVFGDYTEGVMADFALSEEDYAWLAQ----YDI-----VHAAIWGHAE-----DAFPQLHAAGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 162 KVIFDNNYRPR--LWaskeetqqvyQQMLECTDIAFLTLDDEDAlWGQQPVEDVIARthnaGVKEVVVKRGADSCLvSIA 239
Cdd:PRK09813 138 LTAFDFSDKWDspLW----------QTLVPHLDYAFASAPQEDE-FLRLKMKAIVAR----GAGVVIVTLGENGSI-AWD 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111606 240 GEGLVDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGA 300
Cdd:PRK09813 202 GAQFWRQAPEPV---TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
125-272 |
3.42e-14 |
|
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: 69.82 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 125 LANFDYLYLSGISLAilsptsREKLLSLLRECRANGGKVIFDNNYRPRLWASKEetqqvYQQMLECTDIAFLTLDDEDAL 204
Cdd:cd00287 55 LVGADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111606 205 WGQQ--PVEDVIART---HNAGVKEVVVKRGADSCLVSIAGEGLVDVPAVKlpkEKVIDTTAAGDSFSAGYLA 272
Cdd:cd00287 124 TGRRdlEVKEAAEAAallLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFP---VKVVDTTGAGDAFLAALAA 193
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
3.65e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 71.69 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 1 MSKKIAVIGECMIEL------------SEKGADVKRGFGGDTLNTSVYIARqvdpAALTVHYVTALGTDSFSQQMLDAWH 68
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLigyvdrmpqvgeTLHGTSFHKGFGGKGANQAVMASK----LGAKVAMVGMVGTDGFGSDTIKNFK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 69 GENVDTSLTQRMENRLPGLYYIETD-------------STGERTFYYWRNEAAAkfwLESEQSAAICEelanfdylylSG 135
Cdd:PTZ00292 90 RNGVNTSFVSRTENSSTGLAMIFVDtktgnneiviipgANNALTPQMVDAQTDN---IQNICKYLICQ----------NE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 136 ISLailsptsrEKLLSLLRECRANGGKVIFdnNYRPrlwASKEETQQVYQQMLECTDIaFLTLDDEDALWGQQPVED--V 213
Cdd:PTZ00292 157 IPL--------ETTLDALKEAKERGCYTVF--NPAP---APKLAEVEIIKPFLKYVSL-FCVNEVEAALITGMEVTDteS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 214 IARTHNA----GVKEVVVKRGADSCLVSIAGEGLVDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHL 289
Cdd:PTZ00292 223 AFKASKElqqlGVENVIITLGANGCLIVEKENEPVHVPGKRV---KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANR 299
|
330
....*....|.
gi 90111606 290 TASTVIQYRGA 300
Cdd:PTZ00292 300 IAAISVTRHGT 310
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
14-303 |
9.30e-13 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 67.82 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 14 ELSEKGaDVKRGFGGDTLNtSVYIARQV--DPAALTvhYVTALGTDSFSQQMLDAWHGENVDtsltqrmenrlpgLYYIE 91
Cdd:PLN02548 40 ELASKY-NVEYIAGGATQN-SIRVAQWMlqIPGATS--YMGCIGKDKFGEEMKKCATAAGVN-------------VHYYE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 92 TDST-----------GERTFYywRNEAAAKFW----LESEQSAAICEELanfDYLYLSGISLAIlSPTSreklLSLLREC 156
Cdd:PLN02548 103 DESTptgtcavlvvgGERSLV--ANLSAANCYkvehLKKPENWALVEKA---KFYYIAGFFLTV-SPES----IMLVAEH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 157 RANGGKVIFDNNYRPRLwaskeetQQVY--QQM--LECTDIAFLTLDDEDAL-----WGQQPVEDV---IARTHNAGVKE 224
Cdd:PLN02548 173 AAANNKTFMMNLSAPFI-------CEFFkdQLMeaLPYVDFLFGNETEARTFakvqgWETEDVEEIalkISALPKASGTH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 225 ---VVVKRGADSCLVSIAGEgLVDVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAI 301
Cdd:PLN02548 246 krtVVITQGADPTVVAEDGK-VKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCT 324
|
..
gi 90111606 302 IP 303
Cdd:PLN02548 325 YP 326
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
18-308 |
4.13e-12 |
|
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: 65.39 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 18 KGADVKRGFGGDTLNTSVYIARQVDPAALtvhyVTALGTDSFSQQMLDAWHGENVDTSLTQRMENRLPGLYYIeTDSTGE 97
Cdd:cd01945 27 VATDYAVIGGGNAANAAVAVARLGGQARL----IGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSI-TDITGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 98 R--TFYYWRNEAAAKFWLESeqsaaicEELANFDYLYLSGislailspTSREKLLSLLRECRANGGKVIFDNNyrprlWA 175
Cdd:cd01945 102 RatISITAIDTQAAPDSLPD-------AILGGADAVLVDG--------RQPEAALHLAQEARARGIPIPLDLD-----GG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 176 SKEETqqvyQQMLECTDIAFLTlddEDAL--WGQQPVEDVIARTHNAGVKEVVVKRGADSCL-VSIAGEgLVDVPAvklP 252
Cdd:cd01945 162 GLRVL----EELLPLADHAICS---ENFLrpNTGSADDEALELLASLGIPFVAVTLGEAGCLwLERDGE-LFHVPA---F 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111606 253 KEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAiipREAMP 308
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG---RAGLP 283
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
15-271 |
2.58e-11 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 63.49 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 15 LSEKGAdVKRGFGGDTLNTSVYIARQVDPAAltvhYVTALGTDSFSQQMLDAWHGENVDTSLTQRMENRLPGLYYIETDS 94
Cdd:PLN02323 32 LAEAPA-FKKAPGGAPANVAVGISRLGGSSA----FIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 95 TGERTFYYWRNEAAAKFWLESE------QSAAIceelanFDYlylSGISLaILSPtSREKLLSLLRECRANGGKVIFDNN 168
Cdd:PLN02323 107 DGEREFMFYRNPSADMLLRESEldldliRKAKI------FHY---GSISL-ITEP-CRSAHLAAMKIAKEAGALLSYDPN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 169 YRPRLWASKEETQQVYQQMLECTDI--------AFLTlddedalWGQQPVEDVIARTHNAGVKEVVVKRGADSCLV---S 237
Cdd:PLN02323 176 LRLPLWPSAEAAREGIMSIWDEADIikvsdeevEFLT-------GGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYytkD 248
|
250 260 270
....*....|....*....|....*....|....
gi 90111606 238 IAGEglvdVPAVKLpkeKVIDTTAAGDSFSAGYL 271
Cdd:PLN02323 249 FKGR----VEGFKV---KAVDTTGAGDAFVGGLL 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-301 |
3.97e-11 |
|
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: 62.44 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 4 KIAVIG--ECMIELS-----EKGA-----DVKRGFGGDTLNTSVYIARQVDPaaltVHYVTALGTDSFSQQMLDAWhgEN 71
Cdd:cd01947 1 KIAVVGhvEWDIFLSldappQPGGishssDSRESPGGGGANVAVQLAKLGND----VRFFSNLGRDEIGIQSLEEL--ES 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 72 VDTSLTQRMENRLPGLYYIETDSTGERTFYY-WRNEAAAKFWleseqsaaicEELANFDYLYLSgiSLAILSPTsrekll 150
Cdd:cd01947 75 GGDKHTVAWRDKPTRKTLSFIDPNGERTITVpGERLEDDLKW----------PILDEGDGVFIT--AAAVDKEA------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 151 slLRECRaNGGKVIFDNNYRPRLWASKEETQQVyqQMLECTDIAFLTLDDEDALWGQQPvedviarthnagvKEVVVKRG 230
Cdd:cd01947 137 --IRKCR-ETKLVILQVTPRVRVDELNQALIPL--DILIGSRLDPGELVVAEKIAGPFP-------------RYLIVTEG 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111606 231 ADSCLVSIAGEGLvdvpAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01947 199 ELGAILYPGGRYN----HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
119-287 |
5.21e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 59.38 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 119 AAICEELANFDYLYLSGiSLAilSPTSREKLLSLLRECRANGGKVIFDnnyrprlwASKEETQQVYQ-----------QM 187
Cdd:COG1105 120 ERLEELLKEGDWVVLSG-SLP--PGVPPDFYAELIRLARARGAKVVLD--------TSGEALKAALEagpdlikpnleEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 188 LECTDIAFLTLDDedalwgqqpVEDVIARTHNAGVKEVVVKRGAD-SCLVSiaGEGLVDVPAvklPKEKVIDTTAAGDSF 266
Cdd:COG1105 189 EELLGRPLETLED---------IIAAARELLERGAENVVVSLGADgALLVT--EDGVYRAKP---PKVEVVSTVGAGDSM 254
|
170 180
....*....|....*....|.
gi 90111606 267 SAGYLAVRLTGGSAEDAAKRG 287
Cdd:COG1105 255 VAGFLAGLARGLDLEEALRLA 275
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
26-300 |
9.67e-09 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 55.65 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 26 FGGDTLNTSVYIAR-QVDpaaltVHYVTALGTDSFSQQMLDAWHGENVDTSLTQRMENRLPGLYYIETDSTGErtfyywr 104
Cdd:PRK11142 38 FGGKGANQAVAAARlGAD-----IAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGE------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 105 N----EAAAKFWLESEQSAAICEELANFDYLylsgisLAIL-SPTsrEKLLSLLRECRANGGKVIFdnNYRPrlwaskee 179
Cdd:PRK11142 106 NsigiHAGANAALTPALVEAHRELIANADAL------LMQLeTPL--ETVLAAAKIAKQHGTKVIL--NPAP-------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 180 TQQVYQQMLECTDI--------AFLT----LDDEDALWGQQpvedviaRTHNAGVKEVVVKRGADSCLVSIAGEGLVdVP 247
Cdd:PRK11142 168 ARELPDELLALVDIitpneteaEKLTgirvEDDDDAAKAAQ-------VLHQKGIETVLITLGSRGVWLSENGEGQR-VP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 90111606 248 AVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGA 300
Cdd:PRK11142 240 GFRV---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
192-296 |
2.29e-08 |
|
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: 54.24 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 192 DIAFLTLDDEDALWGQ-----QPVEDVIARTHNAGVKEVVVKRGADSCLVS--IAGEGLVDVPAVKlpKEKVIDTTAAGD 264
Cdd:cd01941 178 DLLTPNRAELEALAGAliennEDENKAAKILLLPGIKNVIVTLGAKGVLLSsrEGGVETKLFPAPQ--PETVVNVTGAGD 255
|
90 100 110
....*....|....*....|....*....|..
gi 90111606 265 SFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQ 296
Cdd:cd01941 256 AFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
90-299 |
6.73e-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: 52.81 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 90 IETDstGERTFYYWrneAAAKFWLESEQSAAIceELANFDYLYLSGISLAilSPTSREKLLSLLRECRANGGKVIFDnnY 169
Cdd:cd01944 95 VEPD--GERSFISI---SGAEQDWSTEWFATL--TVAPYDYVYLSGYTLA--SENASKVILLEWLEALPAGTTLVFD--P 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 170 RPRLwaskeetQQVYQQMLE--CTDIAFLTLDDEDALW----GQQPVEDVIARTHNAGVKEVVVKRGADSCLVSIAGEGL 243
Cdd:cd01944 164 GPRI-------SDIPDTILQalMAKRPIWSCNREEAAIfaerGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNT 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111606 244 VDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRG 299
Cdd:cd01944 237 HIIPGFKV---KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
125-287 |
1.51e-07 |
|
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: 51.76 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 125 LANFDYLYLSGiSL-AILSPtsrEKLLSLLRECRANGGKVIFDNNYRPRLWASKEetqQVY-----QQMLEctDIAFLTL 198
Cdd:cd01164 126 LKKGDIVVLSG-SLpPGVPA---DFYAELVRLAREKGARVILDTSGEALLAALAA---KPFlikpnREELE--ELFGRPL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 199 DDEDAlwgqqpVEDVIARTHNAGVKEVVVKRGADSCLVSIAGEGLVdvpaVKLPKEKVIDTTAAGDSFSAGYLAVRLTGG 278
Cdd:cd01164 197 GDEED------VIAAARKLIERGAENVLVSLGADGALLVTKDGVYR----ASPPKVKVVSTVGAGDSMVAGFVAGLAQGL 266
|
....*....
gi 90111606 279 SAEDAAKRG 287
Cdd:cd01164 267 SLEEALRLA 275
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
128-271 |
1.74e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 52.14 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 128 FDYLYLSGISLAILSPTSrekllsllrecraNGGKVIFDNNYRPR-LWASKEETQQVYQQMLECTDIAFLTLDDEDALWG 206
Cdd:PLN02341 235 FDELSPSAIASAVDYAID-------------VGTAVFFDPGPRGKsLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTG 301
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111606 207 QQPVEDV---IARThNAGVKEVVVKRGAD-SCLVSIAGegLVDVPAvklPKEKVIDTTAAGDSFSA----GYL 271
Cdd:PLN02341 302 IRNPILAgqeLLRP-GIRTKWVVVKMGSKgSILVTRSS--VSCAPA---FKVNVVDTVGCGDSFAAaialGYI 368
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
225-304 |
5.51e-07 |
|
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: 50.42 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 225 VVVKRGADSCLVSIAGEGLVD-VPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGaiIP 303
Cdd:cd01943 228 VVLRCGKLGCYVGSADSGPELwLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG--LP 305
|
.
gi 90111606 304 R 304
Cdd:cd01943 306 R 306
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
147-305 |
3.44e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 47.86 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 147 EKLLSLLRECRANGGKVIFD-------NNYRPRLwaskeetqqvyQQMLECTDIAFLTLDDEDA---LWGQQPVEDVIAR 216
Cdd:PLN02379 191 EVIEAAIRLAKQEGLSVSLDlasfemvRNFRSPL-----------LQLLESGKIDLCFANEDEArelLRGEQESDPEAAL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 217 THNAG-VKEVVVKRGADSCLVSiAGEGLVDVPAVKlpKEKVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVI 295
Cdd:PLN02379 260 EFLAKyCNWAVVTLGSKGCIAR-HGKEVVRVPAIG--ETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVV 336
|
170
....*....|
gi 90111606 296 QYRGAIIPRE 305
Cdd:PLN02379 337 RALGGEVTPE 346
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
192-295 |
3.79e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 192 DIAFLTLDDEDALWGQQPVEdvIARTH-NAGVKEVVVKRGADSCLVSIAGeglvDVPAVKLPKEKVIDTTAAGDSFSAGY 270
Cdd:cd01937 155 LHDVLKLSRVEAEVISTPTE--LARLIkETGVKEIIVTDGEEGGYIFDGN----GKYTIPASKKDVVDPTGAGDVFLAAF 228
|
90 100
....*....|....*....|....*
gi 90111606 271 LAVRLTGGSAEDAAKRGHLTASTVI 295
Cdd:cd01937 229 LYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| PLN02967 |
PLN02967 |
kinase |
48-212 |
4.44e-05 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 45.04 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 48 VHYVTALGTDSFSQQMLDAWHGENVDTSlTQRMENRLPGLYYIETDSTGERTFYYWRNEAAAKFWLESEQSAAICEELAN 127
Cdd:PLN02967 260 VAFMGKLGDDDYGQAMLYYLNVNKVQTR-SVCIDGKRATAVSTMKIAKRGRLKTTCVKPCAEDSLSKSEINIDVLKEAKM 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 128 FdylYLSgiSLAILSPTSREKLLSLLRECRANGGKVIFDNNYRPRLWASKEETQQVYQQMLECTDIAFLTLDDEDALWGQ 207
Cdd:PLN02967 339 F---YFN--THSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFIQEAWNLADIIEVTKQELEFLCGI 413
|
....*
gi 90111606 208 QPVED 212
Cdd:PLN02967 414 EPTEE 418
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
218-301 |
4.74e-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: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 218 HNAGVKEVVVKRGADSCLVSIAGEGLVDVPAVKLPkekVIDTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQY 297
Cdd:cd01172 215 ELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKE---VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGK 291
|
....
gi 90111606 298 RGAI 301
Cdd:cd01172 292 VGTA 295
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
184-300 |
3.98e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 41.72 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 184 YQQMLE----CTDIAFLTLDDEDALWGQQPVEDVI--ARTHNAGVKEVVVKRGADSCLVSIAGEGLVDVPAVKLPkekvI 257
Cdd:PLN02813 272 RDDFWDvmgnYADILFANSDEARALCGLGSEESPEsaTRYLSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVP----V 347
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 90111606 258 DTTAAGDSFSAGYLAVRLTGGSaeDAAKRGHLT---ASTVIQYRGA 300
Cdd:PLN02813 348 DTCGAGDAYAAGILYGLLRGVS--DLRGMGELAarvAATVVGQQGT 391
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
221-296 |
1.32e-03 |
|
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: 39.76 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 221 GVKEVVVKRGADSCLVsIAGEGLVDVPAvkLPKEKVIDTTAAGDSFSA---GYLAVrlTGGSAEDAAKR----GHLTAST 293
Cdd:cd01946 194 GPKALIIKRGEYGALL-FTDDGYFAAPA--YPLESVFDPTGAGDTFAGgfiGYLAS--QKDTSEANMRRaiiyGSAMASF 268
|
...
gi 90111606 294 VIQ 296
Cdd:cd01946 269 CVE 271
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
178-304 |
2.50e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 39.02 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 178 EETQqvYQQMLEctDIAFLTLDDEDALWgqQPVEDVIARTHnagvkeVVVKRGADSCLVSIAgEGLVDVPAvkLPKEKVi 257
Cdd:PLN02630 171 EETG--FYDMLP--RIGFLKASSEEALF--IDVEEVRQKCC------VIVTNGKKGCRIYWK-DGEMRVPP--FPAIQV- 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 90111606 258 DTTAAGDSFSAGYLAVRLTGGSAEDAAKRGHLTASTVIQYRGaiIPR 304
Cdd:PLN02630 235 DPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG--IPK 279
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
106-193 |
4.39e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 38.35 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111606 106 EAAAKFWLESEQSAAICEELANFDYlylsgISLAILSPTSREKLLSLLRECRANGGKVIFDNNYRPRLWASKEETQQVYQ 185
Cdd:PLN02543 248 EAAEDSLLASELNLAVLKEARMFHF-----NSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIK 322
|
....*...
gi 90111606 186 QMLECTDI 193
Cdd:PLN02543 323 KAWNEADI 330
|
|
| |
