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Conserved domains on  [gi|320461539|ref|NP_001189379|]
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adenosine kinase isoform d [Homo sapiens]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 29-304 7.56e-143

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).


The actual alignment was detected with superfamily member PLN02548:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 332  Bit Score: 405.64  E-value: 7.56e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548   1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 185
Cdd:PLN02548  80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 186 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 211
Cdd:PLN02548 159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 212 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 291
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                        330
                 ....*....|...
gi 320461539 292 RRTGCTFPEKPDF 304
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 29-304 7.56e-143

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 405.64  E-value: 7.56e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548   1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 185
Cdd:PLN02548  80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 186 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 211
Cdd:PLN02548 159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 212 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 291
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                        330
                 ....*....|...
gi 320461539 292 RRTGCTFPEKPDF 304
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 23-299 3.83e-95

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: 283.74  E-value: 3.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  23 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 102
Cdd:cd01168    1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 103 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 181
Cdd:cd01168   74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 182 CYIA------------EAATFAREQGF------------------------------------------ETKDIKEIAKK 207
Cdd:cd01168  149 LYLEgylltvppeailLAAEHAKENGVkialnlsapfivqrfkeallellpyvdilfgneeeaealaeaETTDDLEAALK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 208 TQALpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAA 287
Cdd:cd01168  229 LLAL------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300

                        330
                 ....*....|..
gi 320461539 288 SIIIRRTGCTFP 299
Cdd:cd01168  301 AEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 44-298 3.56e-48

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 162.51  E-value: 3.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539   44 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 123
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  124 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIA-------------EAA 188
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISgslplglpeatleELI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  189 TFAREQGFET------------------------------------KDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTI 232
Cdd:pfam00294 151 EAAKNGGTFDpnlldplgaareallellpladllkpneeelealtgAKLDDIEEALAALHKLLAKGIKTVIVTLGADGAL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320461539  233 MATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTF 298
Cdd:pfam00294 231 VVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 101-297 4.01e-20

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: 88.40  E-value: 4.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 101 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 178
Cdd:COG0524   53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 179 ARVCYI--------------AEAATFAREQG-----------------------------------------FETKDIKE 203
Cdd:COG0524  128 ADILHLggitlasepprealLAALEAARAAGvpvsldpnyrpalweparellrellalvdilfpneeeaellTGETDPEE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 204 IAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECI 280
Cdd:COG0524  208 AAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEAL 275

                        250
                 ....*....|....*..
gi 320461539 281 RAGHYAASIIIRRTGCT 297
Cdd:COG0524  276 RFANAAAALVVTRPGAQ 292
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 251-297 1.63e-07

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: 51.83  E-value: 1.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 320461539  251 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 297
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 29-304 7.56e-143

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 405.64  E-value: 7.56e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548   1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 185
Cdd:PLN02548  80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 186 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 211
Cdd:PLN02548 159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 212 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 291
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                        330
                 ....*....|...
gi 320461539 292 RRTGCTFPEKPDF 304
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
PTZ00247 PTZ00247
adenosine kinase; Provisional
 26-304 7.43e-118

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 342.78  E-value: 7.43e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  26 LFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFG 105
Cdd:PTZ00247   8 LLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 106 CIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA 185
Cdd:PTZ00247  88 CVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTAQLYYLE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 186 ---------------------------------------------------------EAATFAREQGFETKDIKEIAKKT 208
Cdd:PTZ00247 167 gffltvspnnvlqvakharesgklfclnlsapfisqffferllqvlpyvdilfgneeEAKTFAKAMKWDTEDLKEIAARI 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 209 QALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAAS 288
Cdd:PTZ00247 247 AMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQ 326

                        330
                 ....*....|....*.
gi 320461539 289 IIIRRTGCTFPEKPDF 304
Cdd:PTZ00247 327 VIIQHNGCTYPEKPPF 342
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 23-299 3.83e-95

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: 283.74  E-value: 3.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  23 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 102
Cdd:cd01168    1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 103 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 181
Cdd:cd01168   74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 182 CYIA------------EAATFAREQGF------------------------------------------ETKDIKEIAKK 207
Cdd:cd01168  149 LYLEgylltvppeailLAAEHAKENGVkialnlsapfivqrfkeallellpyvdilfgneeeaealaeaETTDDLEAALK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 208 TQALpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAA 287
Cdd:cd01168  229 LLAL------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300

                        330
                 ....*....|..
gi 320461539 288 SIIIRRTGCTFP 299
Cdd:cd01168  301 AEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 44-298 3.56e-48

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 162.51  E-value: 3.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539   44 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 123
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  124 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIA-------------EAA 188
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISgslplglpeatleELI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  189 TFAREQGFET------------------------------------KDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTI 232
Cdd:pfam00294 151 EAAKNGGTFDpnlldplgaareallellpladllkpneeelealtgAKLDDIEEALAALHKLLAKGIKTVIVTLGADGAL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320461539  233 MATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTF 298
Cdd:pfam00294 231 VVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 102-295 2.56e-20

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: 88.76  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 102 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTcaACIT----GDNRslIANLAAANcykkeKHL---DLEKNW 173
Cdd:cd01174   54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENR--IVVVPGAN-----GELtpaDVDAAL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 174 MLVEKARVCY---------IAEAATFAREQGFET--------KDIKEIAKKT-------------------------QAL 211
Cdd:cd01174  125 ELIAAADVLLlqleipletVLAALRAARRAGVTVilnpaparPLPAELLALVdilvpneteaalltgievtdeedaeKAA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 212 PKMNSKRQRIVIFTQGRDDTIMATESEVT---AFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAAS 288
Cdd:cd01174  205 RLLLAKGVKNVIVTLGAKGALLASGGEVEhvpAFKV------KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278


                 ....*..
gi 320461539 289 IIIRRTG 295
Cdd:cd01174  279 LSVTRPG 285
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 101-297 4.01e-20

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: 88.40  E-value: 4.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 101 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 178
Cdd:COG0524   53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 179 ARVCYI--------------AEAATFAREQG-----------------------------------------FETKDIKE 203
Cdd:COG0524  128 ADILHLggitlasepprealLAALEAARAAGvpvsldpnyrpalweparellrellalvdilfpneeeaellTGETDPEE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 204 IAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECI 280
Cdd:COG0524  208 AAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEAL 275

                        250
                 ....*....|....*..
gi 320461539 281 RAGHYAASIIIRRTGCT 297
Cdd:COG0524  276 RFANAAAALVVTRPGAQ 292
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 26-271 5.38e-16

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: 74.82  E-value: 5.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  26 LFGMGNPLLDISAVVDKDFLDkyslkpndqilaedkhkelfDELVKKFKVEYHAGGSTQNSIKVAQWMIQqphkAATFFG 105
Cdd:cd00287    2 VLVVGSLLVDVILRVDALPLP--------------------GGLVRPGDTEERAGGGAANVAVALARLGV----SVTLVG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 106 CIGIDKFGEILKRKAAEAHVdahyyeqneqptgtcAACITGdNRSLIANLAAANCYKKEKhldleknwMLVEKARVCYI- 184
Cdd:cd00287   58 ADAVVISGLSPAPEAVLDAL---------------EEARRR-GVPVVLDPGPRAVRLDGE--------ELEKLLPGVDIl 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 185 ----AEAATFAREQGFETKDIkeiakkTQALPKMNSKRQRIVIFTQGRDDTIMATEsEVTAFAVLDQDqKEIIDTNGAGD 260
Cdd:cd00287  114 tpneEEAEALTGRRDLEVKEA------AEAAALLLSKGPKVVIVTLGEKGAIVATR-GGTEVHVPAFP-VKVVDTTGAGD 185

                        250
                 ....*....|.
gi 320461539 261 AFVGGFLSQLV 271
Cdd:cd00287  186 AFLAALAAGLA 196
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 101-296 1.12e-14

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: 72.73  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 101 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTcaACIT---GDNRSLIANLAAANCYKKEKHLDLEKNW--- 173
Cdd:cd01942   53 PGLVAAVGEDFHGRLYLEELREEGVDtSHVRVVDEDSTGV--AFILtdgDDNQIAYFYPGAMDELEPNDEADPDGLAdiv 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 174 ------MLVEKARVCYiAEAATFA-----REQGFETKDIKEIAKKTQALpKMN------------------SKRQRIVIF 224
Cdd:cd01942  131 hlssgpGLIELARELA-AGGITVSfdpgqELPRLSGEELEEILERADIL-FVNdyeaellkertglseaelASGVRVVVV 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320461539 225 TQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGC 296
Cdd:cd01942  209 TLGPKGAIVFEDGEEVEVPAVPAV--KVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 78-297 5.97e-12

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: 64.90  E-value: 5.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  78 HAGGSTQNsikVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQ-PTGTcAACITGDNRS---LIA 153
Cdd:cd01166   29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGGErrvLYY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 154 NLAAANCYKKEKHLDLEknwmLVEKARVCYIA---------------EAATFAREQG----F------------ETKD-I 201
Cdd:cd01166  104 RAGSAASRLTPEDLDEA----ALAGADHLHLSgitlalsesareallEALEAAKARGvtvsFdlnyrpklwsaeEAREaL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 202 KEIAKKTQ-ALP---------------------KMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAG 259
Cdd:cd01166  180 EELLPYVDiVLPseeeaeallgdedptdaaeraLALALGVKAVVVKLGAEGALVYTGGGRVFVPAY---PVEVVDTTGAG 256

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 320461539 260 DAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 297
Cdd:cd01166  257 DAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 85-290 1.58e-10

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: 60.45  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539  85 NSIKVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTG-TCAACITGDNRSLIAN--------- 154
Cdd:cd01940   24 NALNVAVYAKRLGHESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAvADVELVDGDRIFGLSNkggvarehp 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 155 ------------LAAANCYKKEKHL----------------DLEKNWMLVEKARVCYIAEAATFAREqGFETKDIKEIAK 206
Cdd:cd01940  103 feadleylsqfdLVHTGIYSHEGHLekalqalvgagalisfDFSDRWDDDYLQLVCPYVDFAFFSAS-DLSDEEVKAKLK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 207 KTQalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAGDAFVGGFL-SQLVSDKPLTECIRAG-H 284
Cdd:cd01940  182 EAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEVVDTLGAGDSFIAGFLlSLLAGGTAIAEAMRQGaQ 252


                 ....*.
gi 320461539 285 YAASII 290
Cdd:cd01940  253 FAAKTC 258
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 101-295 1.31e-09

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: 58.03  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 101 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTCAACITGD-NRS-LIANLAAANCykkekHLDLEKNWMLVE 177
Cdd:cd01167   45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDADgERSfEFYRGPAADL-----LLDTELNPDLLS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 178 KARVCY--------------IAEAATFAREQG--------------------------------------------FETK 199
Cdd:cd01167  120 EADILHfgsialasepsrsaLLELLEAAKKAGvlisfdpnlrpplwrdeeeareriaelleladivklsdeelellFGEE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 200 DIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMAT---ESEVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDK-- 274
Cdd:cd01167  200 DPEEIAALLLLFG------LKLVLVTRGADGALLYTkggVGEVPGIPV------EVVDTTGAGDAFVAGLLAQLLSRGll 267

                        250       260
                 ....*....|....*....|....*.
gi 320461539 275 -----PLTECIRAGHYAASIIIRRTG 295
Cdd:cd01167  268 aldedELAEALRFANAVGALTCTKAG 293
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 185-289 1.26e-07

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: 51.93  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 185 AEAATFAREQGFETKDIKeIAKKTQALPKMNskrqrIVIFTQGRDDTI---MATESEVTAFAVLDQDqkEIIDTNGAGDA 261
Cdd:cd01941  185 AELEALAGALIENNEDEN-KAAKILLLPGIK-----NVIVTLGAKGVLlssREGGVETKLFPAPQPE--TVVNVTGAGDA 256

                         90       100
                 ....*....|....*....|....*...
gi 320461539 262 FVGGFLSQLVSDKPLTECIRAGHYAASI 289
Cdd:cd01941  257 FVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 251-297 1.63e-07

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: 51.83  E-value: 1.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 320461539  251 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 297
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 186-295 7.42e-07

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: 49.73  E-value: 7.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 186 EAATFAREQGFETKD-IKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMAtesevtAFAVldqdqkEIIDTNGAGDAFVG 264
Cdd:cd01944  191 EAAIFAERGDPAAEAsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIP------GFKV------KAVDTIGAGDTHAG 258

                         90       100       110
                 ....*....|....*....|....*....|.
gi 320461539 265 GFLSQLVSDKPLTECIRAGHYAASIIIRRTG 295
Cdd:cd01944  259 GMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
PTZ00292 PTZ00292
ribokinase; Provisional
 195-295 2.11e-06

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 48.58  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 195 GFETKDIKEIAKKTQALPKMNSkrqRIVIFTQG-RDDTIMATESEVTAfavLDQDQKEIIDTNGAGDAFVGGFLSQLVSD 273
Cdd:PTZ00292 214 GMEVTDTESAFKASKELQQLGV---ENVIITLGaNGCLIVEKENEPVH---VPGKRVKAVDTTGAGDCFVGSMAYFMSRG 287

                         90       100
                 ....*....|....*....|..
gi 320461539 274 KPLTECIRAGHYAASIIIRRTG 295
Cdd:PTZ00292 288 KDLKESCKRANRIAAISVTRHG 309
PLN02323 PLN02323
probable fructokinase
 253-278 1.57e-05

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 45.77  E-value: 1.57e-05
                         10        20
                 ....*....|....*....|....*.
gi 320461539 253 IDTNGAGDAFVGGFLSQLVSDKPLTE 278
Cdd:PLN02323 261 VDTTGAGDAFVGGLLSQLAKDLSLLE 286
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
195-283 2.62e-05

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 45.13  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 195 GFETKDIKEIAKKTQALPKMNSkrqRIVIFTQGRDDTIMATESEVTAFAVLDQdqkEIIDTNGAGDAFVGGFLSQLVSDK 274
Cdd:COG1105  193 GRPLETLEDIIAAARELLERGA---ENVVVSLGADGALLVTEDGVYRAKPPKV---EVVSTVGAGDSMVAGFLAGLARGL 266


                 ....*....
gi 320461539 275 PLTECIRAG 283
Cdd:COG1105  267 DLEEALRLA 275
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 195-291 4.29e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.96  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 195 GFETKDIKEIAKKTQALPKMNSKrqrIVIFTQGRDDTIMATESEVTAFAVldqDQKEIIDTNGAGDAFVGGFLSQLVSDK 274
Cdd:PRK09813 164 ASAPQEDEFLRLKMKAIVARGAG---VVIVTLGENGSIAWDGAQFWRQAP---EPVTVVDTMGAGDSFIAGFLCGWLAGM 237

                         90
                 ....*....|....*..
gi 320461539 275 PLTECIRAGHYAASIII 291
Cdd:PRK09813 238 TLPQAMAQGTACAAKTI 254
PRK11142 PRK11142
ribokinase; Provisional
 239-295 6.25e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 43.70  E-value: 6.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320461539 239 VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 295
Cdd:PRK11142 238 VPGFRV------QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 249-297 7.79e-05

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: 43.56  E-value: 7.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 320461539 249 QKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 297
Cdd:cd01947  217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 199-283 1.21e-04

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: 42.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 199 KDIKEIAKKtqalpkMNSKRQRIVIFTQGRDDTIMATESEV---TAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKP 275
Cdd:cd01164  200 EDVIAAARK------LIERGAENVLVSLGADGALLVTKDGVyraSPPKV------KVVSTVGAGDSMVAGFVAGLAQGLS 267


                 ....*...
gi 320461539 276 LTECIRAG 283
Cdd:cd01164  268 LEEALRLA 275
PRK15074 PRK15074
inosine/guanosine kinase; Provisional
 16-87 1.49e-04

inosine/guanosine kinase; Provisional


Pssm-ID: 185033  Cd Length: 434  Bit Score: 43.07  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320461539  16 EAPQALRENILfGMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELVKKFKVEYH-AGGSTQNSI 87
Cdd:PRK15074  27 PENETSRTYIV-GIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 175-295 1.61e-04

MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 42.71  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 175 LVEKARVCYIAEAATFAREQGFETKDIkeiAKKTQALPKMNSkrqrIVIFTQGRDDTIMATESEVTAF---AVlDQDQKE 251
Cdd:cd01943  188 LEEAARLLGLPTSEPSSDEEKEAVLQA---LLFSGILQDPGG----GVVLRCGKLGCYVGSADSGPELwlpAY-HTKSTK 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 320461539 252 IIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 295
Cdd:cd01943  260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 220-272 3.15e-04

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 41.85  E-value: 3.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320461539 220 RIVIFTQGRDDTIMATESEVTAFA---VldqdqkEIIDTNGAGDAFVGGFLSQLVS 272
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 253-295 5.89e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 40.93  E-value: 5.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 320461539 253 IDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 295
Cdd:PLN02379 298 VDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 208-295 8.37e-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: 40.35  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 208 TQALPKMNSKRQRIVIFTQGRDDTIMATES----EVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 283
Cdd:cd01945  192 DEALELLASLGIPFVAVTLGEAGCLWLERDgelfHVPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFA 265

                         90
                 ....*....|..
gi 320461539 284 HYAASIIIRRTG 295
Cdd:cd01945  266 SAAAALKCRGLG 277
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 197-278 5.67e-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: 37.83  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461539 197 ETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPL 276
Cdd:cd01946  173 EARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGY--FAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDT 250


                 ..
gi 320461539 277 TE 278
Cdd:cd01946  251 SE 252
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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