|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
12-344 |
0e+00 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 556.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 12 MGNPLLDICAVVDKDFLDKYGLKPNDQILAEDKHKEMFEEMVKKFKVEYRAGGATQNSVKVAQWMIQEPHnVGTFFGCIG 91
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 92 KDKFGKILKEKAEEAHVDAHYYEQSEEPTGSCAACITGDNRSLVANLAAANCYKKEkHLDLEENWKLVEKAQVYYIAGFF 171
Cdd:PLN02548 80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 172 LTVSLESILKVAKHASENNKIFCLNLSAPFICEFFKEALMKVMPYVDILFGNETEAAAFAREQGFETEDIEEIAKKAQSL 251
Cdd:PLN02548 159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 252 PKENKKRQRIVVFTQGKEGTVMAKGDKVETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVII 331
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318
|
330
....*....|...
gi 440918717 332 RHAGCTFPEKPDF 344
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
9-344 |
6.37e-171 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 478.75 E-value: 6.37e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 9 LFGMGNPLLDICAVVDKDFLDKYGLKPNDQILAEDKHKEMFEEMVKKFKVEYRAGGATQNSVKVAQWMIQEPHNVGTFFG 88
Cdd:PTZ00247 8 LLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 89 CIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTGSCAACITGDNRSLVANLAAANCYKKEkHLDLEENWKLVEKAQVYYIA 168
Cdd:PTZ00247 88 CVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTAQLYYLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 169 GFFLTVSLESILKVAKHASENNKIFCLNLSAPFICEFFKEALMKVMPYVDILFGNETEAAAFAREQGFETEDIEEIAKKA 248
Cdd:PTZ00247 167 GFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 249 QSLPKENKKRQRIVVFTQGKEGTVMAKGDKVETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAAN 328
Cdd:PTZ00247 247 AMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQ 326
|
330
....*....|....*.
gi 440918717 329 VIIRHAGCTFPEKPDF 344
Cdd:PTZ00247 327 VIIQHNGCTYPEKPPF 342
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-339 |
4.14e-149 |
|
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: 422.41 E-value: 4.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 9 LFGMGNPLLDICAVVDKDFLDKYGLKPNDQILAedkHKEMFEEMVKKFKVEYRAGGATQNSVKVAQWMiqepHNVGTFFG 88
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAAFIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 89 CIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTGSCAACITGD-NRSLVANLAAANCYKKEKHldleeNWKLVEKAQVYYI 167
Cdd:cd01168 77 RVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKYLYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 168 AGFFLTVSLESILKVAKHASENNKIFCLNLSAPFICEFFKEALMKVMPYVDILFGNETEAAAFAREqgfETEDIEEIAKK 247
Cdd:cd01168 152 EGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 248 AQslpkenKKRQRIVVFTQGKEGTVMAkgDKVETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAA 327
Cdd:cd01168 229 LL------ALRCRIVVITQGAKGAVVV--EGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300
|
330
....*....|..
gi 440918717 328 NVIIRHAGCTFP 339
Cdd:cd01168 301 AEVIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
27-338 |
4.00e-74 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 231.08 E-value: 4.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 27 FLDKYGLKPNDQILAEDKHkemFEEMVKKFKVEYRAGGATQNSVKVAQWMIQEPHnvgtFFGCIGKDKFGKILKEKAEEA 106
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGDVA----FIGAVGDDNFGEFLLQELKKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 107 HVDAHYYEQSE-EPTGSCAACITGD-NRSLVANLAAANCYKKEKhldLEENWKLVEKAQVYYIAGFFLTVSLESILKVAK 184
Cdd:pfam00294 74 GVDTDYVVIDEdTRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISGSLPLGLPEATLEELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 185 HASENNKIFCLNLSAPFICefFKEALMKVMPYVDILFGNETEAAAFAREQGFETEDIeeiakkAQSLPKENKKRQRIVVF 264
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAKLDDIEEA------LAALHKLLAKGIKTVIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440918717 265 TQGKEGTVMAkgDKVETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAGCTF 338
Cdd:pfam00294 223 TLGADGALVV--EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
85-337 |
1.64e-44 |
|
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: 154.66 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEE-PTGSCAACITGD-NRSLVANLAAANcykkekHLDLEE-NWKLVEK 161
Cdd:COG0524 54 ALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGaPTGLAFILVDPDgERTIVFYRGANA------ELTPEDlDEALLAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 162 AQVYYIAGFFLT--VSLESILKVAKHASENNKIFCLNLSA-PFICEFFKEALMKVMPYVDILFGNETEAAAFareqgFET 238
Cdd:COG0524 128 ADILHLGGITLAsePPREALLAALEAARAAGVPVSLDPNYrPALWEPARELLRELLALVDILFPNEEEAELL-----TGE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 239 EDIEEIAKKAQSLPKenkkrqRIVVFTQGKEGTVMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGGFLSQLVQDKTFEQ 318
Cdd:COG0524 203 TDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEVVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEE 273
|
250
....*....|....*....
gi 440918717 319 CIRAGHYAANVIIRHAGCT 337
Cdd:COG0524 274 ALRFANAAAALVVTRPGAQ 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
85-327 |
1.14e-35 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 131.13 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSE-EPTGscAACIT----GDNRSLVAnlAAANcykkeKHL---DLEENW 156
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVVVgAPTG--TAVITvdesGENRIVVV--PGAN-----GELtpaDVDAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 157 KLVEKAQVyyiagfFLT---VSLESILKVAKHASENNKIFCLNlSAPFiceffKEALMKVMPYVDILFGNETEAAAFARE 233
Cdd:cd01174 125 ELIAAADV------LLLqleIPLETVLAALRAARRAGVTVILN-PAPA-----RPLPAELLALVDILVPNETEAALLTGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 234 QGFETEDIEEIAKKAQSLPKENkkrqriVVFTQGKEGTVMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGGFLSQLVQD 313
Cdd:cd01174 193 EVTDEEDAEKAARLLLAKGVKN------VIVTLGAKGALLASGGEVEHVPAFKV---KAVDTTGAGDTFIGALAAALARG 263
|
250
....*....|....
gi 440918717 314 KTFEQCIRAGHYAA 327
Cdd:cd01174 264 LSLEEAIRFANAAA 277
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
61-337 |
1.51e-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: 114.60 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 61 RAGGATQNsvkVAQWMIQEPHNVGtFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEE-PTGScAACITGDN--RSLV-- 135
Cdd:cd01166 29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGgeRRVLyy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 136 -ANLAAAncykkekHLDLEE-NWKLVEKAQVYYIAGFFLTVSL---ESILKVAKHASENNKIFC--LNLSAPFIC-EFFK 207
Cdd:cd01166 104 rAGSAAS-------RLTPEDlDEAALAGADHLHLSGITLALSEsarEALLEALEAAKARGVTVSfdLNYRPKLWSaEEAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 208 EALMKVMPYVDILFGNETEAAAFAREQGfeTEDIEEIAKKAQSLPKEnkkrqriVVFTQGKEGTVMAKGDKVETFPVLEI 287
Cdd:cd01166 177 EALEELLPYVDIVLPSEEEAEALLGDED--PTDAAERALALALGVKA-------VVVKLGAEGALVYTGGGRVFVPAYPV 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 440918717 288 dqsEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAGCT 337
Cdd:cd01166 248 ---EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
85-327 |
1.38e-28 |
|
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: 112.31 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVDAHYYEQ-SEEPTGScaACI----TGDNRSLVAnlAAANcykkeKHL---DLEENW 156
Cdd:TIGR02152 49 SMIGKVGDDAFGDELLENLKSNGIDTEYVGTvKDTPTGT--AFItvddTGENRIVVV--AGAN-----AELtpeDIDAAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 157 KLVEKAQVYYIAgffLTVSLESILKVAKHASENNKIFCLNlSAPFICEFFKEALMkvmpYVDILFGNETEAAAFAreqGF 236
Cdd:TIGR02152 120 ALIAESDIVLLQ---LEIPLETVLEAAKIAKKHGVKVILN-PAPAIKDLDDELLS----LVDIITPNETEAEILT---GI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 237 ETEDIEEIAKKAQSLPKenkKRQRIVVFTQGKEGTVMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGGFLSQLVQDKTF 316
Cdd:TIGR02152 189 EVTDEEDAEKAAEKLLE---KGVKNVIITLGSKGALLVSKDESKLIPAFKV---KAVDTTAAGDTFNGAFAVALAEGKSL 262
|
250
....*....|.
gi 440918717 317 EQCIRAGHYAA 327
Cdd:TIGR02152 263 EDAIRFANAAA 273
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
172-311 |
2.42e-25 |
|
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: 101.02 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 172 LTVSLESILKVAKHASENNKIFCLNLsAPFICEFFKEALMKVMPYVDILFGNETEAAAFAREQGFETEDIEEIAKKAQSl 251
Cdd:cd00287 66 LSPAPEAVLDALEEARRRGVPVVLDP-GPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLS- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 252 pkenkKRQRIVVFTQGKEGTVMAkGDKVETFPVLEIDqSEIVDTNGAGDAFVGGFLSQLV 311
Cdd:cd00287 144 -----KGPKVVIVTLGEKGAIVA-TRGGTEVHVPAFP-VKVVDTTGAGDAFLAALAAGLA 196
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
37-336 |
2.75e-20 |
|
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: 88.91 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 37 DQILAEDKHKEMFEEMVKKFKVEYRAGGATqNsvkVAQWMIQEPHNVGtFFGCIGKDKFGKILKEKAEEAHVD-AHYYEQ 115
Cdd:cd01942 11 DIILKVESFPGPFESVLVKDLRREFGGSAG-N---TAVALAKLGLSPG-LVAAVGEDFHGRLYLEELREEGVDtSHVRVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 116 SEEPTGScaACIT--GDNRSLVANLAAANcykkekhldleENWKLVEKAQVYYIAGFfltVSLESILKVAKHASEnnkif 193
Cdd:cd01942 86 DEDSTGV--AFILtdGDDNQIAYFYPGAM-----------DELEPNDEADPDGLADI---VHLSSGPGLIELARE----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 194 CLNLSAPFICE-------FFKEALMKVMPYVDILFGNETEAAAFareqgfetedieeIAKKAQSLPKENKKRQRIVVfTQ 266
Cdd:cd01942 145 LAAGGITVSFDpgqelprLSGEELEEILERADILFVNDYEAELL-------------KERTGLSEAELASGVRVVVV-TL 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440918717 267 GKEG-TVMAKGDKVETFPVLEIDqseIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAGC 336
Cdd:cd01942 211 GPKGaIVFEDGEEVEVPAVPAVK---VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
86-335 |
5.49e-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: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 86 FFGCIGKDKFGKILKEKAEEAHVD-AHYYEQSEEPTGsCAacitgdnrsLVANLAAAN----CYKKEK---HLDLEENWK 157
Cdd:cd01167 47 FIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTT-LA---------FVTLDADGErsfeFYRGPAadlLLDTELNPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 158 LVEKAQVYYiagfFLTVSL------ESILKVAKHASENNKIFCL--NLSAPFIC--EFFKEALMKVMPYVDILFGNETEA 227
Cdd:cd01167 117 LLSEADILH----FGSIALasepsrSALLELLEAAKKAGVLISFdpNLRPPLWRdeEEARERIAELLELADIVKLSDEEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 228 AAFareqgFETEDIEEIAkkaQSLPKENKKRqriVVFTQGKEGTVMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGGFL 307
Cdd:cd01167 193 ELL-----FGEEDPEEIA---ALLLLFGLKL---VLVTRGADGALLYTKGGVGEVPGIPV---EVVDTTGAGDAFVAGLL 258
|
250 260 270
....*....|....*....|....*....|....*
gi 440918717 308 SQLVQDK-------TFEQCIRAGHYAANVIIRHAG 335
Cdd:cd01167 259 AQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
55-333 |
4.69e-15 |
|
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: 74.27 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 55 KFKVEYRAGGATQNSVKVaqwmIQEP----HNVG----------TFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEEPT 120
Cdd:cd01941 13 RGKVSGSLVPGTSNPGHV----KQSPggvgRNIAenlarlgvsvALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 121 GSCAAcITGDNRSLVANLAAANCYKKEKHLDLEENWKLVEKAQVYYIAGfflTVSLESILKVAKHASENNkifclnlsAP 200
Cdd:cd01941 89 ASYTA-ILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDA---NLPEEALEYLLALAAKHG--------VP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 201 FICEFFKEA----LMKVMPYVDILFGNETEAAAFArEQGFETEDIEEIAKKAQSLPKENkkrqrIVVFTQGKEGTVMA-K 275
Cdd:cd01941 157 VAFEPTSAPklkkLFYLLHAIDLLTPNRAELEALA-GALIENNEDENKAAKILLLPGIK-----NVIVTLGAKGVLLSsR 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 440918717 276 GDKVETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRH 333
Cdd:cd01941 231 EGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
85-327 |
1.04e-14 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 73.75 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVD-AHYYEQSEEPTGScaACI----TGDNRSLVAnlAAANCYKKEKHLdlEENWKLV 159
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDtAPVSVIKGESTGV--ALIfvndEGENSIGIH--AGANAALTPALV--EAHRELI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 160 EKAQVYYIAgffLTVSLESILKVAKHASENNKIFCLNlSAPfICEFFKEALmkvmPYVDILFGNETEAAAFAreqGFETE 239
Cdd:PRK11142 131 ANADALLMQ---LETPLETVLAAAKIAKQHGTKVILN-PAP-ARELPDELL----ALVDIITPNETEAEKLT---GIRVE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 240 DIEEIAKKAQSLpkeNKKRQRIVVFTQGKEG---TVMAKGDKVETFPVleidqsEIVDTNGAGDAFVGGFLSQLVQDKTF 316
Cdd:PRK11142 199 DDDDAAKAAQVL---HQKGIETVLITLGSRGvwlSENGEGQRVPGFRV------QAVDTIAAGDTFNGALVTALLEGKPL 269
|
250
....*....|.
gi 440918717 317 EQCIRAGHYAA 327
Cdd:PRK11142 270 PEAIRFAHAAA 280
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
85-333 |
1.80e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 73.23 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVDAHY-YEQSEEPTGsCAACI----TGDNRSLVanLAAANCYKKEKHLDleENWKLV 159
Cdd:PTZ00292 70 AMVGMVGTDGFGSDTIKNFKRNGVNTSFvSRTENSSTG-LAMIFvdtkTGNNEIVI--IPGANNALTPQMVD--AQTDNI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 160 EKAQVYYIAGffLTVSLESILKVAKHASENNKIFCLNlSAPFICEFFKEALMKVMPYVDILFGNETEAAAFAreqGFETE 239
Cdd:PTZ00292 145 QNICKYLICQ--NEIPLETTLDALKEAKERGCYTVFN-PAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALIT---GMEVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 240 DiEEIAKKAQslpKENKKRQ-RIVVFTQGKEGTVMAKGDKVETFpvLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTF-E 317
Cdd:PTZ00292 219 D-TESAFKAS---KELQQLGvENVIITLGANGCLIVEKENEPVH--VPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLkE 292
|
250
....*....|....*.
gi 440918717 318 QCIRAGHYAANVIIRH 333
Cdd:PTZ00292 293 SCKRANRIAAISVTRH 308
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
68-330 |
4.18e-14 |
|
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: 71.23 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 68 NSVKVAQWMIQEPHNVGtFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTGscAACIT---GDNRSLVANLAAAncy 144
Cdd:cd01940 24 NALNVAVYAKRLGHESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENA--VADVElvdGDRIFGLSNKGGV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 145 kkEKHLDLEENWKLVEKAQVYYIAGFFLTVSLESILKVAKHASennkifcLNLSAPFICEFFKEALMKVMPYVDIlfgne 224
Cdd:cd01940 98 --AREHPFEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAG-------ALISFDFSDRWDDDYLQLVCPYVDF----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 225 teaaAFAREQGFETEDIEEIAKKAQSlpkenkKRQRIVVFTQGKEGTVMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVG 304
Cdd:cd01940 164 ----AFFSASDLSDEEVKAKLKEAVS------RGAKLVIVTRGEDGAIAYDGAVFYSVAPRPV---EVVDTLGAGDSFIA 230
|
250 260
....*....|....*....|....*...
gi 440918717 305 GFL-SQLVQDKTFEQCIRAG-HYAANVI 330
Cdd:cd01940 231 GFLlSLLAGGTAIAEAMRQGaQFAAKTC 258
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
86-337 |
2.70e-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: 69.55 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 86 FFGCIGKDKFGKILKEKAEEAHVDA-HYYEQSEEPTGscaACITG----DNRSLVanlaaancYKKEKHLDL-----EEN 155
Cdd:TIGR04382 53 FITRVGDDQFGRFVRDYLRREGVDTsHVVTDPGRRTS---LVFLEikppDEFPLL--------FYRENAADLaltpdDVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 156 WKLVEKAQVYYIAGFFLTV--SLESILKVAKHASENNKIFCLNL-------SAPficEFFKEALMKVMPYVDILFGNETE 226
Cdd:TIGR04382 122 EDYIASARALLVSGTALSQepSREAVLKALEYARAAGVRVVLDIdyrpylwKSP---EEAGIYLRLVLPLVDVIIGTREE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 227 AAAFAREqgfetEDIEEIAKKAQSLPKEnkkrqrIVVFTQGKEGT-VMAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGG 305
Cdd:TIGR04382 199 FDIAGGE-----GDDEAAARALLDAGVE------ILVVKRGPEGSlVYTGDGEGVEVPGFPV---EVLNVLGAGDAFASG 264
|
250 260 270
....*....|....*....|....*....|..
gi 440918717 306 FLSQLVQDKTFEQCIRAGHYAANVIIRHAGCT 337
Cdd:TIGR04382 265 FLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
11-307 |
4.52e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 66.76 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 11 GMGNPLLDICAVVDKDFLDKYGL-KPNDQILAEDKHKEMFEEMV-KKFKVEyrAGGATQNS-VKVAQWMIQEPH----NV 83
Cdd:PLN02813 74 GLGQAMVDFSGMVDDEFLERLGLeKGTRKVINHEERGKVLRALDgCSYKAS--AGGSLSNTlVALARLGSQSAAgpalNV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 84 GtFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTGSCAACITGD-NRSLVANLAAANCykkekhLDLEENW-KLVEK 161
Cdd:PLN02813 152 A-MAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDaQRTMLSYQGTSST------VNYDSCLaSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 162 AQVYYIAGFF--LTVSLESILKVAKHASENNKIFCLNLSAPFICEFFKEALMKVMP-YVDILFGNETEAAAFAreqGFET 238
Cdd:PLN02813 225 SRVLVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGnYADILFANSDEARALC---GLGS 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440918717 239 EDIEEIAKK--AQSLPkenkkrqrIVVFTQGKEGT-VMAKGDKVETFPVLEIDqseiVDTNGAGDAFVGGFL 307
Cdd:PLN02813 302 EESPESATRylSHFCP--------LVSVTDGARGSyIGVKGEAVYIPPSPCVP----VDTCGAGDAYAAGIL 361
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
60-335 |
5.93e-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: 62.44 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 60 YRAGGAtqnsVKVAQWMIQEPHNVGtFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTGSCAACITGD-NRSLVANL 138
Cdd:cd01944 33 YVIGGG----FNVMVAASRLGIPTV-NAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDgERSFISIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 139 AAancykkEKHLDLEENWKL-VEKAQVYYIAGFFLTVSLES--ILKVAKHASENNKIFCLNLSaPFICEFFKEALMKVMP 215
Cdd:cd01944 108 GA------EQDWSTEWFATLtVAPYDYVYLSGYTLASENASkvILLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 216 YVDILFGNETEAAAFAREQGFEtediEEIAKKAQSLpkenkKRQRIVVFTQGKEGT-VMAKGDK---VETFPVleidqsE 291
Cdd:cd01944 181 KRPIWSCNREEAAIFAERGDPA----AEASALRIYA-----KTAAPVVVRLGSNGAwIRLPDGNthiIPGFKV------K 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 440918717 292 IVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAG 335
Cdd:cd01944 246 AVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
199-345 |
1.58e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 61.30 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 199 APFICEFFKEALMKVMPY-VDILFGNETEAAAFAreqGFETEDIEEIAKKAQSLPKENKkrqRIVVFTQGKEGTVMAKGD 277
Cdd:COG1105 159 AKVVLDTSGEALKAALEAgPDLIKPNLEELEELL---GRPLETLEDIIAAARELLERGA---ENVVVSLGADGALLVTED 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440918717 278 KVETFPVLEIdqsEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIR----AGhyAANViiRHAGCTFPEKPDFH 345
Cdd:COG1105 233 GVYRAKPPKV---EVVSTVGAGDSMVAGFLAGLARGLDLEEALRlavaAG--AAAA--LSPGTGLPDREDVE 297
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
37-335 |
2.79e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 60.96 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 37 DQILAE-DKHKEMFEEMVKKFKVeyRAGGATQNSVK-------VAQWMIqephnvgtffGCIGKDKFGKILKEKAEEAHV 108
Cdd:PLN02379 61 EHILREvNAHILPSPDDLSPIKT--MAGGSVANTIRglsagfgVSTGII----------GACGDDEQGKLFVSNMGFSGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 109 DAHYYEQSEEPTGSCAaCITGD--NRSLVANLAAAncYKKEKHLDLEENWKLVEKAQVYYiaGFFltvSLESILKVAKHA 186
Cdd:PLN02379 129 DLSRLRAKKGPTAQCV-CLVDAlgNRTMRPCLSSA--VKLQADELTKEDFKGSKWLVLRY--GFY---NLEVIEAAIRLA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 187 SENNKIFCLNLSAPFICEFFKEALMKVMPY--VDILFGNETEAAAFAReqGFETEDIEEiakkaqSLPKENKKRQRIVVf 264
Cdd:PLN02379 201 KQEGLSVSLDLASFEMVRNFRSPLLQLLESgkIDLCFANEDEARELLR--GEQESDPEA------ALEFLAKYCNWAVV- 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440918717 265 TQGKEGtVMAKGDKvETFPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAG 335
Cdd:PLN02379 272 TLGSKG-CIARHGK-EVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
21-333 |
6.17e-10 |
|
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: 58.97 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 21 AVVDKDFLDKYGLkpNDQILAEDKHKEmfeemVKKFKVEYRAGGATqnsvkVAQWMIQEPHNVgTFFGCIGKDKFGKILK 100
Cdd:cd01947 3 AVVGHVEWDIFLS--LDAPPQPGGISH-----SSDSRESPGGGGAN-----VAVQLAKLGNDV-RFFSNLGRDEIGIQSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 101 EKAEeAHVDAHYYEQSEEPTGSCAACITGDNRSLVANLAAAncykkekhldLEENWKLVEKAQvyyIAGFFLTVSLESIL 180
Cdd:cd01947 70 EELE-SGGDKHTVAWRDKPTRKTLSFIDPNGERTITVPGER----------LEDDLKWPILDE---GDGVFITAAAVDKE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 181 KVAKHASENNKIFCLNLSAPFIceFFKEALMkvmpYVDILFGNETEaaafareqgFETEDIEEiakkaqslpKENKKRQR 260
Cdd:cd01947 136 AIRKCRETKLVILQVTPRVRVD--ELNQALI----PLDILIGSRLD---------PGELVVAE---------KIAGPFPR 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440918717 261 IVVFTQGKEGTVMakGDKVETFPVlEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAG-HYAANVIIRH 333
Cdd:cd01947 192 YLIVTEGELGAIL--YPGGRYNHV-PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGaQCGAICVSHF 262
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
212-335 |
4.57e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.28 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 212 KVMPYVDILFGNETEaaafareqgfETEDIEEIAKKAQSlpkenkKRQRIVVFTQGKEGTVMAKGDKVETFPvleIDQSE 291
Cdd:PRK09813 154 TLVPHLDYAFASAPQ----------EDEFLRLKMKAIVA------RGAGVVIVTLGENGSIAWDGAQFWRQA---PEPVT 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 440918717 292 IVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVIIRHAG 335
Cdd:PRK09813 215 VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
194-323 |
7.41e-09 |
|
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: 56.00 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 194 CLNLSAPFICEFFKEALMKVMPY-VDILFGNETEAAAFAreqGFETEDIEEIAKKAQSLpkeNKKRQRIVVFTQGKEGTV 272
Cdd:cd01164 154 AREKGARVILDTSGEALLAALAAkPFLIKPNREELEELF---GRPLGDEEDVIAAARKL---IERGAENVLVSLGADGAL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 440918717 273 MAKGDKVETFPVLEIdqsEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAG 323
Cdd:cd01164 228 LVTKDGVYRASPPKV---KVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
85-340 |
4.13e-07 |
|
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: 51.02 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 85 TFFGCIGKDKFGKILKEKAEEAHVDAHYYEQSEEPTgscaaciTGDNRSLVAN--LAAANcYKKEKHLDLEENWKLVEK- 161
Cdd:cd01172 57 TLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPT-------TTKTRVIARNqqLLRVD-REDDSPLSAEEEQRLIERi 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 162 ------AQVY----YIAGFFLTVSLESILKVAKHASennkIFCLNLSAPFICEFFKEAlmkvmpyvDILFGNETEAAAFA 231
Cdd:cd01172 129 aerlpeADVVilsdYGKGVLTPRVIEALIAAARELG----IPVLVDPKGRDYSKYRGA--------TLLTPNEKEAREAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 232 reqGFETEDIEEIAKKAQSLPKenKKRQRIVVFTQGKEG-TVMAKGDKVETFPVLeidQSEIVDTNGAGDAFVGGFLSQL 310
Cdd:cd01172 197 ---GDEINDDDELEAAGEKLLE--LLNLEALLVTLGEEGmTLFERDGEVQHIPAL---AKEVYDVTGAGDTVIATLALAL 268
|
250 260 270
....*....|....*....|....*....|...
gi 440918717 311 VQDKTFEQCIRAGHYAANV---IIRHAGCTFPE 340
Cdd:cd01172 269 AAGADLEEAAFLANAAAGVvvgKVGTAPVTPKE 301
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
260-312 |
4.67e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 50.70 E-value: 4.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 440918717 260 RIVVFTQGKEGTVMAKGDKVETFPVLEIDqseIVDTNGAGDAFVGGFLSQLVQ 312
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPAPSVD---PVDTTGAGDAFVAGLLAGLSQ 263
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
260-315 |
4.83e-07 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 50.78 E-value: 4.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 260 RIVVFTQGKEG----TVMAKGdKVETFPVleidqsEIVDTNGAGDAFVGGFLSQLVQDKT 315
Cdd:PLN02323 231 KLLLVTEGEEGcryyTKDFKG-RVEGFKV------KAVDTTGAGDAFVGGLLSQLAKDLS 283
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
200-331 |
1.43e-06 |
|
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: 49.26 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 200 PFICEFF-KEALMKVMPYVDILFGNETEAAAFAREQGFETEDIEE------IAKKAQSLPKENKkrqrIVVFTQGKEGT- 271
Cdd:cd01943 163 PDSCDPEnLEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEkeavlqALLFSGILQDPGG----GVVLRCGKLGCy 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440918717 272 VMAKGDKVET-FPVLEIDQSEIVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVII 331
Cdd:cd01943 239 VGSADSGPELwLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAI 299
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
203-329 |
2.58e-06 |
|
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: 48.17 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 203 CEFFKEALMKVMPYVDILFGNETEAAafareqgfETEDIEEIAKKAQSLPkenkkrQRIVVFTQGKEGTVMAKGDKVETF 282
Cdd:cd01937 142 ANQEKLIKCVILKLHDVLKLSRVEAE--------VISTPTELARLIKETG------VKEIIVTDGEEGGYIFDGNGKYTI 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 440918717 283 PVLEIDqseIVDTNGAGDAFVGGFLSQLVQDKTFEqciRAGHYAANV 329
Cdd:cd01937 208 PASKKD---VVDPTGAGDVFLAAFLYSRLSGKDIK---EAAEFAAAA 248
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
254-335 |
3.64e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 48.26 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 254 ENKKRQRIVVFTQGKEG-TVMAKGDK--VETFPVLEidqseiVDTNGAGDAFVGGFLSQLVQDKTFEQCIRAGHYAANVI 330
Cdd:PLN02630 198 EEVRQKCCVIVTNGKKGcRIYWKDGEmrVPPFPAIQ------VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLA 271
|
....*
gi 440918717 331 IRHAG 335
Cdd:PLN02630 272 VEQVG 276
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
207-315 |
2.82e-05 |
|
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: 45.15 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 207 KEALMKVMPYVDILFGNETEAaafarEQGFETEDIEEIAKKAQSL-PKenkkrqrIVVFTQGKEGTVMAKGDKVETFPVL 285
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEA-----RQLTGAANLVKAARLILAMgPK-------ALIIKRGEYGALLFTDDGYFAAPAY 221
|
90 100 110
....*....|....*....|....*....|
gi 440918717 286 EIDqsEIVDTNGAGDAFVGGFLSQLVQDKT 315
Cdd:cd01946 222 PLE--SVFDPTGAGDTFAGGFIGYLASQKD 249
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
229-307 |
2.06e-04 |
|
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: 42.28 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 229 AFAREQGFE--TEDIEEIAKKAQSLPKenkkrQRIVVFTQGKEGTVMAKGDK-VETFPVLeidQSEIVDTNGAGDAFVGG 305
Cdd:cd01945 176 AICSENFLRpnTGSADDEALELLASLG-----IPFVAVTLGEAGCLWLERDGeLFHVPAF---PVEVVDTTGAGDVFHGA 247
|
..
gi 440918717 306 FL 307
Cdd:cd01945 248 FA 249
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
207-321 |
1.23e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 40.05 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 207 KEALMKVMPYVDILFGNETEAAAFAREQGFETEDIEEIAKKAQSLPKEN---------KKRQRIVVFTQGKEGTVMAKgd 277
Cdd:PRK12413 120 RQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAvvikggnrlSQKKAIDLFYDGKEFVILES-- 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 440918717 278 kvetfPVLEidqseiVDTNGAGDAFVGGFLSQLVQDKTFEQCIR 321
Cdd:PRK12413 198 -----PVLE------KNNIGAGCTFASSIASQLVKGKSPLEAVK 230
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
203-307 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 203 CEFFKEALMKVMPYVDILFgnetEAAAFAREQGFETedieeiAKKAQSLPKENKKRQRIVVFTQGKEGT--VMAKGDKVE 280
Cdd:cd01939 166 VEKPREELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWGDQGAgaLGPDGEYVH 235
|
90 100
....*....|....*....|....*..
gi 440918717 281 tFPVLEIDQseIVDTNGAGDAFVGGFL 307
Cdd:cd01939 236 -SPAHKPIR--VVDTLGAGDTFNAAVI 259
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
11-70 |
2.71e-03 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 39.22 E-value: 2.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440918717 11 GMGNPLLDICAVVDKDFLDKYGL-KPNDQILAEDKHKEMFEEMVKKFKVEYR-AGGATQNSV 70
Cdd:PRK15074 38 GIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
208-332 |
8.93e-03 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 37.43 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440918717 208 EALM-KVMPYVDILFGNETEAAAFAREQGFETEDIEEIAKKAQ----------SLPKENKKRQRIVVFTQGKEGTVMAKG 276
Cdd:COG2240 129 EFIMrRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLalgpkivvvtSVPLDDTPADKIGNLAVTADGAWLVET 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 440918717 277 DKVETFPvleidqseivdtNGAGDAFVGGFLSQLVQDKTFEQCI-RAGHYAANVIIR 332
Cdd:COG2240 209 PLLPFSP------------NGTGDLFAALLLAHLLRGKSLEEALeRAAAFVYEVLER 253
|
|
| |
