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Conserved domains on  [gi|1034566518|ref|XP_016871187|]
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adenosine kinase isoform X1 [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 ...
29-315 2.91e-153

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: 433.76  E-value: 2.91e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIAGFF 188
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 189 LTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQAL 268
Cdd:PLN02548  159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034566518 269 PKMNSKRQRIVIFTQGRDDTIMAT-GRIKRkedkwaqwlTPVTLAPWE 315
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEdGKVKE---------FPVIPLPKE 277
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
29-315 2.91e-153

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 433.76  E-value: 2.91e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIAGFF 188
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 189 LTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQAL 268
Cdd:PLN02548  159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034566518 269 PKMNSKRQRIVIFTQGRDDTIMAT-GRIKRkedkwaqwlTPVTLAPWE 315
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEdGKVKE---------FPVIPLPKE 277
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
23-293 4.09e-110

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: 323.41  E-value: 4.09e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  23 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 102
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 103 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 181
Cdd:cd01168    74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 182 CYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREqgfETKDIKEI 261
Cdd:cd01168   149 LYLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEA 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034566518 262 AKKTQALpkmnskRQRIVIFTQGRDDTIMATG 293
Cdd:cd01168   226 ALKLLAL------RCRIVVITQGAKGAVVVEG 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
44-293 9.13e-50

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 168.29  E-value: 9.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  44 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 123
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 124 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAH 201
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISGSLPLGLPEATLEELI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 202 HASENNRIFTLNLSAPFISqfYKESLMKVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKTQALPKMNSKRQRIVIF 281
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIV 222
                         250
                  ....*....|..
gi 1034566518 282 TQGRDDTIMATG 293
Cdd:pfam00294 223 TLGADGALVVEG 234
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
101-293 8.22e-18

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: 82.62  E-value: 8.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 101 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 178
Cdd:COG0524    53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 179 ARVCYIAGFFLT--VSPESVLKVAHHASENNR--IFTLNLSAPFISQfYKESLMKVMPYVDILFGNETEAATFareqgFE 254
Cdd:COG0524   128 ADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEP-ARELLRELLALVDILFPNEEEAELL-----TG 201
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034566518 255 TKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATG 293
Cdd:COG0524   202 ETDPEEAAAALLARGV------KLVVVTLGAEGALLYTG 234
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
29-315 2.91e-153

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 433.76  E-value: 2.91e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  29 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 108
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 109 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIAGFF 188
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 189 LTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQAL 268
Cdd:PLN02548  159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034566518 269 PKMNSKRQRIVIFTQGRDDTIMAT-GRIKRkedkwaqwlTPVTLAPWE 315
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEdGKVKE---------FPVIPLPKE 277
PTZ00247 PTZ00247
adenosine kinase; Provisional
26-293 8.97e-127

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 367.04  E-value: 8.97e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  26 LFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFG 105
Cdd:PTZ00247    8 LLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 106 CIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA 185
Cdd:PTZ00247   88 CVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTAQLYYLE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 186 GFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKT 265
Cdd:PTZ00247  167 GFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARI 246
                         250       260
                  ....*....|....*....|....*...
gi 1034566518 266 QALPKMNSKRQRIVIFTQGRDDTIMATG 293
Cdd:PTZ00247  247 AMLPKYSGTRPRLVVFTQGPEPTLIATK 274
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
23-293 4.09e-110

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: 323.41  E-value: 4.09e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  23 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 102
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 103 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 181
Cdd:cd01168    74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 182 CYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREqgfETKDIKEI 261
Cdd:cd01168   149 LYLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEA 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034566518 262 AKKTQALpkmnskRQRIVIFTQGRDDTIMATG 293
Cdd:cd01168   226 ALKLLAL------RCRIVVITQGAKGAVVVEG 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
44-293 9.13e-50

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 168.29  E-value: 9.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  44 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 123
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 124 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAH 201
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISGSLPLGLPEATLEELI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 202 HASENNRIFTLNLSAPFISqfYKESLMKVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKTQALPKMNSKRQRIVIF 281
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIV 222
                         250
                  ....*....|..
gi 1034566518 282 TQGRDDTIMATG 293
Cdd:pfam00294 223 TLGADGALVVEG 234
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
179-294 5.01e-18

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: 80.99  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 179 ARVCYIAGffLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKEsLMKVMPYVDILFGNETEAATFAREQGFETKDI 258
Cdd:cd00287    58 ADAVVISG--LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-LEKLLPGVDILTPNEEEAEALTGRRDLEVKEA 134
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034566518 259 keiakkTQALPKMNSKRQRIVIFTQGRDDTIMATGR 294
Cdd:cd00287   135 ------AEAAALLLSKGPKVVIVTLGEKGAIVATRG 164
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
101-293 8.22e-18

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: 82.62  E-value: 8.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 101 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 178
Cdd:COG0524    53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 179 ARVCYIAGFFLT--VSPESVLKVAHHASENNR--IFTLNLSAPFISQfYKESLMKVMPYVDILFGNETEAATFareqgFE 254
Cdd:COG0524   128 ADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEP-ARELLRELLALVDILFPNEEEAELL-----TG 201
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034566518 255 TKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATG 293
Cdd:COG0524   202 ETDPEEAAAALLARGV------KLVVVTLGAEGALLYTG 234
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
102-284 1.60e-14

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: 72.97  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 102 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTcaACIT----GDNRslIANLAAANcykkeKHL---DLEKNW 173
Cdd:cd01174    54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENR--IVVVPGAN-----GELtpaDVDAAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 174 MLVEKARVCYIAgffLTVSPESVLKVAHHASENNRIFTLNlSAPFISQFYkeslmKVMPYVDILFGNETEAATFAREQGF 253
Cdd:cd01174   125 ELIAAADVLLLQ---LEIPLETVLAALRAARRAGVTVILN-PAPARPLPA-----ELLALVDILVPNETEAALLTGIEVT 195
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034566518 254 ETKDIKEIAKKTQALPKmnskrqRIVIFTQG 284
Cdd:cd01174   196 DEEDAEKAARLLLAKGV------KNVIVTLG 220
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
101-293 2.70e-07

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: 51.48  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 101 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTCAACITGD-NRS-LIANLAAANCykkekHLDLEKNWMLVE 177
Cdd:cd01167    45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDADgERSfEFYRGPAADL-----LLDTELNPDLLS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 178 KARVCYIAGFFLTVSP--ESVLKVAHHASENNRI--FTLNLSAPFISQFY--KESLMKVMPYVDILFGNETEAATFareq 251
Cdd:cd01167   120 EADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWRDEEeaRERIAELLELADIVKLSDEELELL---- 195
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034566518 252 gFETKDIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMATG 293
Cdd:cd01167   196 -FGEEDPEEIAALLLLFG------LKLVLVTRGADGALLYTK 230
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
5-268 3.60e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 48.27  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518   5 EEEPKPKKLKVEAPQALRENILfGMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDEL-VKKFKVEyhAGGS 82
Cdd:PLN02813   52 EEQPEGFGPIPEKAVPERWDVL-GLGQAMVDFSGMVDDEFLERLGLeKGTRKVINHEERGKVLRALdGCSYKAS--AGGS 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518  83 TQNSI----KVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAA 157
Cdd:PLN02813  129 LSNTLvalaRLGSQSAAGPALNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDaQRTMLSYQGT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566518 158 ANCYKKEKHLDleknwMLVEKARVCYIAGFF--LTVSPESVLKVAHHASENNRIFTLNLSAP-FISQFYKESLMKVMPYV 234
Cdd:PLN02813  209 SSTVNYDSCLA-----SAISKSRVLVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVsCIERHRDDFWDVMGNYA 283
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034566518 235 DILFGNETEAATFAreqGFETKDIKEIAkkTQAL 268
Cdd:PLN02813  284 DILFANSDEARALC---GLGSEESPESA--TRYL 312
PRK15074 PRK15074
inosine/guanosine kinase; Provisional
16-87 1.92e-04

inosine/guanosine kinase; Provisional


Pssm-ID: 185033  Cd Length: 434  Bit Score: 43.07  E-value: 1.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034566518  16 EAPQALRENILfGMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELVKKFKVEYH-AGGSTQNSI 87
Cdd:PRK15074   27 PENETSRTYIV-GIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
 
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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