|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
28-360 |
0e+00 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 548.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 28 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSMKVAQWLIQEPHkAATFFGCIG 107
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 108 IDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACITGGNRSLVANLAAANCYKKEkHLDLERNWVLVEKARVYYIAGFF 187
Cdd:PLN02548 80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 188 LTVSPESVLKVARYAAENNRVFTLNLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQAL 267
Cdd:PLN02548 159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 268 PKVNSKRQRTVIFTQGRDDTIVAAENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVII 347
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318
|
330
....*....|...
gi 19527306 348 RRTGCTFPEKPDF 360
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
19-360 |
2.19e-167 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 470.66 E-value: 2.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 19 ALSENVLFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSMKVAQWLIQEPHK 98
Cdd:PTZ00247 2 SSAPKKLLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 99 AATFFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACITGGNRSLVANLAAANCYKKEkHLDLERNWVLVEKA 178
Cdd:PTZ00247 82 FVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 179 RVYYIAGFFLTVSPESVLKVARYAAENNRVFTLNLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIK 258
Cdd:PTZ00247 161 QLYYLEGFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 259 EIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAAENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRA 338
Cdd:PTZ00247 241 EIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEA 320
|
330 340
....*....|....*....|..
gi 19527306 339 GHYAASVIIRRTGCTFPEKPDF 360
Cdd:PTZ00247 321 GHYSAQVIIQHNGCTYPEKPPF 342
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
22-355 |
1.22e-141 |
|
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: 403.92 E-value: 1.22e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 22 ENVLFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSMKVAQWLiqepHKAAT 101
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 102 FFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACIT-GGNRSLVANLAAANCYKKEKHldlerNWVLVEKARV 180
Cdd:cd01168 74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTpDAERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 181 YYIAGFFLTVSPESVLKVARYAAENNRVFTLNLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREqgfETKDIKEI 260
Cdd:cd01168 149 LYLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 261 AKKAQALpkvnskRQRTVIFTQGRDDTIVAaeNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGH 340
Cdd:cd01168 226 ALKLLAL------RCRIVVITQGAKGAVVV--EGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGS 297
|
330
....*....|....*
gi 19527306 341 YAASVIIRRTGCTFP 355
Cdd:cd01168 298 YAAAEVIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
43-354 |
4.18e-76 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 236.47 E-value: 4.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 43 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSMKVAQWLiqepHKAATFFGCIGIDKFGEILKRKAADA 122
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARL----GGDVAFIGAVGDDNFGEFLLQELKKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 123 HVDAHYYEQNEQ-PTGTCAACITG-GNRSLVANLAAANCYKKEKHLDlerNWVLVEKARVYYIAGFFLTVSPESVLKVAR 200
Cdd:pfam00294 74 GVDTDYVVIDEDtRTGTALIEVDGdGERTIVFNRGAAADLTPEELEE---NEDLLENADLLYISGSLPLGLPEATLEELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 201 YAAENNRVFTLNLSAPFISqfFKEALMDVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKAQALPKVNSKRQRTVIF 280
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527306 281 TQGRDDTIVAaeNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTF 354
Cdd:pfam00294 223 TLGADGALVV--EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
100-353 |
6.36e-39 |
|
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: 140.40 E-value: 6.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 100 ATFFGCIGIDKFGEILKRKAADAHVDAHYYEQ-NEQPTGTCAACIT-GGNRSLVANLAAANcykkekHLDLER-NWVLVE 176
Cdd:COG0524 53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDpDGERTIVFYRGANA------ELTPEDlDEALLA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 177 KARVYYIAGFFLT--VSPESVLKVARYAAENNR--VFTLNLSAPFISQFfKEALMDVMPYVDILFGNETEAATFareqgF 252
Cdd:COG0524 127 GADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEPA-RELLRELLALVDILFPNEEEAELL-----T 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 253 ETKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAEND---VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSD 329
Cdd:COG0524 201 GETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEG 268
|
250 260
....*....|....*....|....
gi 19527306 330 KPLTECIRAGHYAASVIIRRTGCT 353
Cdd:COG0524 269 LDLEEALRFANAAAALVVTRPGAQ 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
101-351 |
2.87e-30 |
|
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: 116.88 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 101 TFFGCIGIDKFGEILKRKAADAHVDAHYYEQ-NEQPTGTcaACIT----GGNRSLVAnlAAANCYKKEKhlDLERNWVLV 175
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENRIVVV--PGANGELTPA--DVDAALELI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 176 EKARVyyiagfFLT---VSPESVLKVARYAAENNRVFTLNlSAPFISQffkeaLMDVMPYVDILFGNETEAATFAREQGF 252
Cdd:cd01174 128 AAADV------LLLqleIPLETVLAALRAARRAGVTVILN-PAPARPL-----PAELLALVDILVPNETEAALLTGIEVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 253 ETKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAENDVTAFPVLdqnQEEIIDTNGAGDAFVGGFLSQLVSDKPL 332
Cdd:cd01174 196 DEEDAEKAARLLLAKGV------KNVIVTLGAKGALLASGGEVEHVPAF---KVKAVDTTGAGDTFIGALAAALARGLSL 266
|
250
....*....|....*....
gi 19527306 333 TECIRAGHYAASVIIRRTG 351
Cdd:cd01174 267 EEAIRFANAAAALSVTRPG 285
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
77-353 |
6.51e-29 |
|
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: 113.44 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 77 HAGGSTQNsmkVAQWLIQEPHKAAtFFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQ-PTGTcAACITGGN--RSLVAN 153
Cdd:cd01166 29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGgeRRVLYY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 154 LA-AANCYKKEKHLDLErnwvLVEKARVYYIAGFFLTVSP---ESVLKVARYAAENN--RVFTLNLSAPFIS-QFFKEAL 226
Cdd:cd01166 104 RAgSAASRLTPEDLDEA----ALAGADHLHLSGITLALSEsarEALLEALEAAKARGvtVSFDLNYRPKLWSaEEAREAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 227 MDVMPYVDILFGNETEAATFAREQGfeTKDIKEIAKKAQALPKvnskrqrTVIFTQGRDDTIVAAENDVTAFPVLdqnQE 306
Cdd:cd01166 180 EELLPYVDIVLPSEEEAEALLGDED--PTDAAERALALALGVK-------AVVVKLGAEGALVYTGGGRVFVPAY---PV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19527306 307 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 353
Cdd:cd01166 248 EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
188-327 |
2.74e-24 |
|
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: 98.32 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 188 LTVSPESVLKVARYAAENNRVFTLNLSAPFISQFfKEALMDVMPYVDILFGNETEAATFAREQGFETKDIkeiakkAQAL 267
Cdd:cd00287 66 LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLD-GEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEA------AEAA 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 268 PKVNSKRQRTVIFTQGRDDTIVaAENDVTAFPVLDQNqEEIIDTNGAGDAFVGGFLSQLV 327
Cdd:cd00287 139 ALLLSKGPKVVIVTLGEKGAIV-ATRGGTEVHVPAFP-VKVVDTTGAGDAFLAALAAGLA 196
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
100-351 |
7.37e-20 |
|
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: 88.46 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 100 ATFFGCIGIDKFGEILKRKAADAHVD-AHYYEQNEQPTGTCAACITG-GNRSLVanlaaanCYKKEK---HLDLERNWVL 174
Cdd:cd01167 45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDAdGERSFE-------FYRGPAadlLLDTELNPDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 175 VEKARVYYIAGFFLTVSP--ESVLKVARYAAENNRV--FTLNLSAPFISQF--FKEALMDVMPYVDILFGNETEAATFar 248
Cdd:cd01167 118 LSEADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWRDEeeARERIAELLELADIVKLSDEELELL-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 249 eqgFETKDIKEIAKKAQALPkvnskrQRTVIFTQGRDDTIV---AAENDVTAFPVldqnqeEIIDTNGAGDAFVGGFLSQ 325
Cdd:cd01167 196 ---FGEEDPEEIAALLLLFG------LKLVLVTRGADGALLytkGGVGEVPGIPV------EVVDTTGAGDAFVAGLLAQ 260
|
250 260 270
....*....|....*....|....*....|...
gi 19527306 326 LVSDK-------PLTECIRAGHYAASVIIRRTG 351
Cdd:cd01167 261 LLSRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
53-352 |
1.50e-19 |
|
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: 87.37 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 53 DQILAEDKHKELFDE-LVKKFKVEYhaGGSTQNSMKVAQWLIQEPhkaaTFFGCIGIDKFGEILKRKAADAHVD-AHYYE 130
Cdd:cd01942 11 DIILKVESFPGPFESvLVKDLRREF--GGSAGNTAVALAKLGLSP----GLVAAVGEDFHGRLYLEELREEGVDtSHVRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 131 QNEQPTGTcaACIT---GGNRSLVANLAAANCYKKEKHLDLERNW---------VLVEKARVYYIAGFFLTVSPesvlkv 198
Cdd:cd01942 85 VDEDSTGV--AFILtdgDDNQIAYFYPGAMDELEPNDEADPDGLAdivhlssgpGLIELARELAAGGITVSFDP------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 199 aryaaennrvftlnlsAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKdikEIAKKAqalpkvnskrqRTV 278
Cdd:cd01942 157 ----------------GQELPRLSGEELEEILERADILFVNDYEAELLKERTGLSEA---ELASGV-----------RVV 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527306 279 IFTQGRDDTIVAAENDVTAFPVLdqNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGC 352
Cdd:cd01942 207 VVTLGPKGAIVFEDGEEVEVPAV--PAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
79-353 |
1.06e-13 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 70.70 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 79 GGSTQNsmkVAQWLIQEPHKAAtFFGCIGIDKFGEILKRKAADAHVDA-HYYEQNEQPTGtcaACITG----GNRSLVan 153
Cdd:TIGR04382 34 GGSPAN---IAVGAARLGLKTA-FITRVGDDQFGRFVRDYLRREGVDTsHVVTDPGRRTS---LVFLEikppDEFPLL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 154 laaancYKKEKHLDL-----ERNWVLVEKARVYYIAGFFLTVSP--ESVLKVARYAAENNRVFTLNL--------SAPFI 218
Cdd:TIGR04382 105 ------FYRENAADLaltpdDVDEDYIASARALLVSGTALSQEPsrEAVLKALEYARAAGVRVVLDIdyrpylwkSPEEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 219 SQFFKEALmdvmPYVDILFGNETEAATFAREqgfetKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAENDVT-- 296
Cdd:TIGR04382 179 GIYLRLVL----PLVDVIIGTREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDGEGve 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19527306 297 --AFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 353
Cdd:TIGR04382 244 vpGFPV------EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
101-351 |
6.80e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 101 TFFGCIGIDKFGEILKRKAADAHVDAHY-YEQNEQPTGtCAACI---TGGNRSLVAnLAAANCYKKEKHLDleRNWVLVE 176
Cdd:PTZ00292 70 AMVGMVGTDGFGSDTIKNFKRNGVNTSFvSRTENSSTG-LAMIFvdtKTGNNEIVI-IPGANNALTPQMVD--AQTDNIQ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 177 KARVYYIAGffLTVSPESVLKVARYAAENNrVFTLNLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAreqGFETKD 256
Cdd:PTZ00292 146 NICKYLICQ--NEIPLETTLDALKEAKERG-CYTVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALIT---GMEVTD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 257 IKEIAKKAQALPKVNSkrqRTVIFTQG-RDDTIVAAENDVTAFPVLdqnQEEIIDTNGAGDAFVGGFLSQLVSDKPLTEC 335
Cdd:PTZ00292 220 TESAFKASKELQQLGV---ENVIITLGaNGCLIVEKENEPVHVPGK---RVKAVDTTGAGDCFVGSMAYFMSRGKDLKES 293
|
250
....*....|....*.
gi 19527306 336 IRAGHYAASVIIRRTG 351
Cdd:PTZ00292 294 CKRANRIAAISVTRHG 309
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
84-346 |
2.61e-12 |
|
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: 66.22 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 84 NSMKVAQWLIQEPHKAAtFFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACITGGNRSLVAnlaaancYKKE 163
Cdd:cd01940 24 NALNVAVYAKRLGHESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVDGDRIFGL-------SNKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 164 KHLDLERnwvlvEKARVYYIAGFFLTVSpeSVLKVARYAAENNRvfTLNLSAPFISQFFK-----EALMDVMPYVDILFg 238
Cdd:cd01940 96 GVAREHP-----FEADLEYLSQFDLVHT--GIYSHEGHLEKALQ--ALVGAGALISFDFSdrwddDYLQLVCPYVDFAF- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 239 neteaatFAREqGFETKDIKEIAKKAQalpkvnSKRQRTVIFTQGRDDTIVAAENDVTAFPVLdqnQEEIIDTNGAGDAF 318
Cdd:cd01940 166 -------FSAS-DLSDEEVKAKLKEAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEVVDTLGAGDSF 228
|
250 260 270
....*....|....*....|....*....|
gi 19527306 319 VGGFL-SQLVSDKPLTECIRAG-HYAASVI 346
Cdd:cd01940 229 IAGFLlSLLAGGTAIAEAMRQGaQFAAKTC 258
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
102-351 |
3.29e-11 |
|
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: 63.21 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 102 FFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACIT-GGNRSLVANLAAancykkEKHLDLErnwvlvekarv 180
Cdd:cd01944 54 NAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEpDGERSFISISGA------EQDWSTE----------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 181 yYIAGffLTVSPESVLKVARYAAEN---NRVFTLNL-------------SAPFISQFFKEALMDVMPYVDILFGNETEAA 244
Cdd:cd01944 117 -WFAT--LTVAPYDYVYLSGYTLASenaSKVILLEWlealpagttlvfdPGPRISDIPDTILQALMAKRPIWSCNREEAA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 245 TFAREQGFETKD-IKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAAendvtaFPVldqnqeEIIDTNGAGDAFVGGFL 323
Cdd:cd01944 194 IFAERGDPAAEAsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPG------FKV------KAVDTIGAGDTHAGGML 261
|
250 260
....*....|....*....|....*...
gi 19527306 324 SQLVSDKPLTECIRAGHYAASVIIRRTG 351
Cdd:cd01944 262 AGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
100-344 |
3.55e-11 |
|
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: 63.10 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 100 ATFFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACIT-GGNrsLVANLAAANCYKKEKHLDLERNWVLVEKA 178
Cdd:cd01941 52 VALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTAILDkDGD--LVVALADMDIYELLTPDFLRKIREALKEA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 179 RVYYIAGfflTVSPESVLKVARYAAENN-RVFTLNLSAPFISqffkeALMDVMPYVDILFGNETEAATFAREQGFETKDI 257
Cdd:cd01941 130 KPIVVDA---NLPEEALEYLLALAAKHGvPVAFEPTSAPKLK-----KLFYLLHAIDLLTPNRAELEALAGALIENNEDE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 258 KeIAKKAQALPKVNskrqrTVIFTQGRDDTIVAAEND---VTAFPVldQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTE 334
Cdd:cd01941 202 N-KAAKILLLPGIK-----NVIVTLGAKGVLLSSREGgveTKLFPA--PQPETVVNVTGAGDAFVAGLVAGLLEGMSLDD 273
|
250
....*....|
gi 19527306 335 CIRAGHYAAS 344
Cdd:cd01941 274 SLRFAQAAAA 283
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
101-351 |
3.83e-10 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 60.27 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 101 TFFGCIGIDKFGEILKRKAADAHVD-AHYYEQNEQPTGTcaACI----TGGNRSLVAnlAAANCYKKEKHLdlERNWVLV 175
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDtAPVSVIKGESTGV--ALIfvndEGENSIGIH--AGANAALTPALV--EAHRELI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 176 EKARVYYIAgffLTVSPESVLKVARYAAENNRVFTLNlSAPfisqffKEALMD-VMPYVDILFGNETEAATFAreqGFET 254
Cdd:PRK11142 131 ANADALLMQ---LETPLETVLAAAKIAKQHGTKVILN-PAP------ARELPDeLLALVDIITPNETEAEKLT---GIRV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 255 KDIKEIAKKAQALpkvNSKRQRTVIFTQGRDDtIVAAEND----VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDK 330
Cdd:PRK11142 198 EDDDDAAKAAQVL---HQKGIETVLITLGSRG-VWLSENGegqrVPGFRV------QAVDTIAAGDTFNGALVTALLEGK 267
|
250 260
....*....|....*....|.
gi 19527306 331 PLTECIRAGHYAASVIIRRTG 351
Cdd:PRK11142 268 PLPEAIRFAHAAAAIAVTRKG 288
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
27-351 |
1.92e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 58.67 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 27 GMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELV-KKFKVEyhAGGSTQNSM----KVAQWLIQEPHKAA 100
Cdd:PLN02813 74 GLGQAMVDFSGMVDDEFLERLGLeKGTRKVINHEERGKVLRALDgCSYKAS--AGGSLSNTLvalaRLGSQSAAGPALNV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 101 TFFGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACIT-GGNRSLVANLAAANCYKkekhLDlERNWVLVEKAR 179
Cdd:PLN02813 152 AMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTpDAQRTMLSYQGTSSTVN----YD-SCLASAISKSR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 180 VYYIAGFF--LTVSPESVLKVARYAAENNRVFTLNLSAPFISQFFKEALMDVMP-YVDILFGNETEAATFAreqGFETKD 256
Cdd:PLN02813 227 VLVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGnYADILFANSDEARALC---GLGSEE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 257 IKEIAkkAQALpkvnSKRQRTVIFTQGRDDTIVAAENDVTAFPVLDQnqeEIIDTNGAGDAFVGGFLSQL---VSDkplt 333
Cdd:PLN02813 304 SPESA--TRYL----SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPC---VPVDTCGAGDAYAAGILYGLlrgVSD---- 370
|
330 340
....*....|....*....|..
gi 19527306 334 ecIR-AGHYA---ASVIIRRTG 351
Cdd:PLN02813 371 --LRgMGELAarvAATVVGQQG 390
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
216-351 |
2.87e-08 |
|
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: 54.65 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 216 PFISQFFKEALmdvmPYVDILFGNETEAATFAREQGFETK--DIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAAEN 293
Cdd:cd01943 168 PENLEDLLQAL----PRVDVFSPNLEEAARLLGLPTSEPSsdEEKEAVLQALLFSGILQDPGGGVVLRCGKLGCYVGSAD 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 294 DVTAF--PVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 351
Cdd:cd01943 244 SGPELwlPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
223-334 |
2.66e-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: 51.31 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 223 KEALMDVMPYVDILFGNETEAatfareqgfetKDIKEIAKKAQALPKVNSKRQRTVIFTQGR-------DDTIVAAendv 295
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEA-----------RQLTGAANLVKAARLILAMGPKALIIKRGEygallftDDGYFAA---- 218
|
90 100 110
....*....|....*....|....*....|....*....
gi 19527306 296 TAFPVldqnqEEIIDTNGAGDAFVGGFLSQLVSDKPLTE 334
Cdd:cd01946 219 PAYPL-----ESVFDPTGAGDTFAGGFIGYLASQKDTSE 252
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
78-351 |
6.98e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 50.56 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 78 AGGSTQNSMK-------VAQWLIqephkaatffGCIGIDKFGEILKRKAADAHVDAHYYEQNEQPTGTCAACITG-GNRS 149
Cdd:PLN02379 85 AGGSVANTIRglsagfgVSTGII----------GACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVDAlGNRT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 150 LVANLAAA-----NCYKKEkhlDLE-RNWVLVEkarvYYIAGFfltvspESVLKVARYAAENNRVFTLNLSAPFISQFFK 223
Cdd:PLN02379 155 MRPCLSSAvklqaDELTKE---DFKgSKWLVLR----YGFYNL------EVIEAAIRLAKQEGLSVSLDLASFEMVRNFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 224 EALMDVMPY--VDILFGNETEAATFAReqGFETKDikeiakkAQALPKVNSKRQRTVIFTQGRDDTIVAAENDVTAFPVL 301
Cdd:PLN02379 222 SPLLQLLESgkIDLCFANEDEARELLR--GEQESD-------PEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAI 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19527306 302 DQNQeeIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 351
Cdd:PLN02379 293 GETN--AVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
185-349 |
2.08e-06 |
|
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: 48.57 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 185 GFFLTvsPESVLKVARYAAENNRVFTLNLSAPFISQFFKEALMdvmpYVDILFGNETEAAtfarEQGFETKDIKeiakka 264
Cdd:cd01947 124 GVFIT--AAAVDKEAIRKCRETKLVILQVTPRVRVDELNQALI----PLDILIGSRLDPG----ELVVAEKIAG------ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 265 qalpkvnsKRQRTVIFTQGRDDTIV---AAENDVTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG-H 340
Cdd:cd01947 188 --------PFPRYLIVTEGELGAILypgGRYNHVPAKKA------KVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGaQ 253
|
....*....
gi 19527306 341 YAASVIIRR 349
Cdd:cd01947 254 CGAICVSHF 262
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
230-347 |
3.13e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 47.81 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 230 MPYVDILFGNETEAATFAREQgfeTKDIKEIAKKaqalpkvnskrqrTVIFTQGRDDTIVAAENDVTAFPVLdqnQEEII 309
Cdd:PRK09813 156 VPHLDYAFASAPQEDEFLRLK---MKAIVARGAG-------------VVIVTLGENGSIAWDGAQFWRQAPE---PVTVV 216
|
90 100 110
....*....|....*....|....*....|....*...
gi 19527306 310 DTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVII 347
Cdd:PRK09813 217 DTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
295-334 |
2.16e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.77 E-value: 2.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 19527306 295 VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTE 334
Cdd:PLN02323 253 VEGFKV------KAVDTTGAGDAFVGGLLSQLAKDLSLLE 286
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
223-339 |
3.13e-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: 45.22 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 223 KEALMDVMPY-VDILFGNETEAATFAreqGFETKDIKEIAKKAQALpkvNSKRQRTVIFTQGRDDTIVAAENDV---TAF 298
Cdd:cd01164 167 GEALLAALAAkPFLIKPNREELEELF---GRPLGDEEDVIAAARKL---IERGAENVLVSLGADGALLVTKDGVyraSPP 240
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19527306 299 PVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 339
Cdd:cd01164 241 KV------KVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
27-243 |
8.69e-05 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 44.23 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 27 GMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELVKKFKVEYH-AGGSTQNSMKVAQWLIQEphkAATFFG 104
Cdd:PRK15074 38 GIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTLHNYSVLADD---RSVLLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 105 CIGID-KFGEILKRKAAD--AHVDAHYYEQNEQPTGTCAACIT-GGNRSLVANLAAANCYKKEkHLDLErnwvLVEKARV 180
Cdd:PRK15074 115 VMSSNiEIGSYAYRYLCNtsSRTDLNYLQGVDGPIGRCFTLISeDGERTFAISPGHMNQLRPE-SIPED----VIAGASA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527306 181 YYIAGFFLTVS-----PESVLKVARYAAENNRVFTLNLSAPFI----SQFFKEALMDvmpYVDILFGNETEA 243
Cdd:PRK15074 190 LVLTAYLVRCKpgepmPEATMKAIEYAKKHNVPVVLTLGTKFViednPQWWQEFLKE---HVSILAMNEDEA 258
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
223-339 |
2.49e-04 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 42.43 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 223 KEALMDVMPY-VDILFGNETEAATFAreqGFETKDIKEIAKKAQALPKVNSKRqrtVIFTQGRDDTIVAAENDVTAFPVL 301
Cdd:COG1105 167 GEALKAALEAgPDLIKPNLEELEELL---GRPLETLEDIIAAARELLERGAEN---VVVSLGADGALLVTEDGVYRAKPP 240
|
90 100 110
....*....|....*....|....*....|....*...
gi 19527306 302 DQnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 339
Cdd:COG1105 241 KV---EVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
276-328 |
3.48e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 41.85 E-value: 3.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527306 276 RTVIFTQGRDDTIVAAENDVTAFP---VldqnqeEIIDTNGAGDAFVGGFLSQLVS 328
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
221-350 |
5.04e-04 |
|
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: 41.03 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 221 FFKEALMDVM-----PYVDILFGNETEAATFAreqGFETKDIKEIAKKAQALPKvnsKRQRTVIFT----QGRDDTIVAA 291
Cdd:cd01173 120 VVAEEIVPVYrdllvPLADIITPNQFELELLT---GKKINDLEDAKAAARALHA---KGPKTVVVTsvelADDDRIEMLG 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527306 292 ----ENDVTAFPVLDQNQeeiiDTNGAGDAFVGGFLSQLVSDKPLTEciRAGHYAASV--IIRRT 350
Cdd:cd01173 194 statEAWLVQRPKIPFPA----YFNGTGDLFAALLLARLLKGKSLAE--ALEKALNFVheVLEAT 252
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
223-344 |
1.50e-03 |
|
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: 40.08 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 223 KEALMDVMPYVDILFgnetEAATFAREQGFETkdikeiAKKAQALPKVNSKRQRTVIFTQGRDDT-IVAAENDVTAFPVl 301
Cdd:cd01939 170 REELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWGDQGAgALGPDGEYVHSPA- 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19527306 302 dQNQEEIIDTNGAGDAFVGGFLSQL-VSDKPLTECIRAGHYAAS 344
Cdd:cd01939 239 -HKPIRVVDTLGAGDTFNAAVIYALnKGPDDLSEALDFGNRVAS 281
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
295-351 |
2.18e-03 |
|
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: 39.58 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527306 295 VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 351
Cdd:cd01945 227 VPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
240-352 |
2.23e-03 |
|
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: 39.47 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 240 ETEAATfareqGFETKDIKEIAKKAQALPKvnSKRQRTVIFTQGRDD-TIVAAENDVTAFPVLDQnqeEIIDTNGAGDAF 318
Cdd:cd01172 191 EAREAL-----GDEINDDDELEAAGEKLLE--LLNLEALLVTLGEEGmTLFERDGEVQHIPALAK---EVYDVTGAGDTV 260
|
90 100 110
....*....|....*....|....*....|....
gi 19527306 319 VGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGC 352
Cdd:cd01172 261 IATLALALAAGADLEEAAFLANAAAGVVVGKVGT 294
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
231-345 |
6.52e-03 |
|
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: 37.77 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 231 PYVDILFGNETEAAtfareqgfETKDIKEIAKKAQALPK----VNSKRQRTVIFTQGRDDTIVAAENDVtafpvldqnqe 306
Cdd:cd01937 154 KLHDVLKLSRVEAE--------VISTPTELARLIKETGVkeiiVTDGEEGGYIFDGNGKYTIPASKKDV----------- 214
|
90 100 110
....*....|....*....|....*....|....*....
gi 19527306 307 eiIDTNGAGDAFVGGFLSQLVSDKpltECIRAGHYAASV 345
Cdd:cd01937 215 --VDPTGAGDVFLAAFLYSRLSGK---DIKEAAEFAAAA 248
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
274-351 |
7.57e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 37.86 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 274 RQRT-VIFTQGRDDTIVAAEND---VTAFPVLDqnqeeiIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRR 349
Cdd:PLN02630 201 RQKCcVIVTNGKKGCRIYWKDGemrVPPFPAIQ------VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQ 274
|
..
gi 19527306 350 TG 351
Cdd:PLN02630 275 VG 276
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
223-337 |
9.08e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 37.35 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527306 223 KEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVN---------SKRQRTVIFTQGRDDTIVAaen 293
Cdd:PRK12413 120 RQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAvvikggnrlSQKKAIDLFYDGKEFVILE--- 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19527306 294 dvtaFPVLDQNQeeiidtNGAGDAFVGGFLSQLVSDKPLTECIR 337
Cdd:PRK12413 197 ----SPVLEKNN------IGAGCTFASSIASQLVKGKSPLEAVK 230
|
|
| |
