NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907166189|ref|XP_036021385|]
View 

ribokinase isoform X4 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-170 4.69e-70

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 TIGR02152:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 293  Bit Score: 213.62  E-value: 4.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERG 80
Cdd:TIGR02152 128 VLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:TIGR02152 208 VKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQ 283

                         170
                  ....*....|
gi 1907166189 161 SSYPYKKDLP 170
Cdd:TIGR02152 284 SSIPYLEEVE 293
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 1-170 4.69e-70

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: 213.62  E-value: 4.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERG 80
Cdd:TIGR02152 128 VLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:TIGR02152 208 VKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQ 283

                         170
                  ....*....|
gi 1907166189 161 SSYPYKKDLP 170
Cdd:TIGR02152 284 SSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 1-165 7.12e-62

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: 192.76  E-value: 7.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERG 80
Cdd:cd01174   133 LLLQLEIPLETVLAALRAARRAGVTVILNPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKG 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSqaEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:cd01174   212 VKNVIVTLGAKGALLAS--GGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQ 287


                  ....*
gi 1907166189 161 SSYPY 165
Cdd:cd01174   288 PSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
 1-170 1.54e-58

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 185.33  E-value: 1.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMIL 76
Cdd:PTZ00292  151 LICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKEL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  77 LERGCQVVVITLGASGCVILSQaEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQA 156
Cdd:PTZ00292  231 QQLGVENVIITLGANGCLIVEK-ENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISVTR 307

                         170
                  ....*....|....
gi 1907166189 157 TGTQSSYPYKKDLP 170
Cdd:PTZ00292  308 HGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 6-169 7.51e-38

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: 131.55  E-value: 7.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   6 EISPAASLEALTMARRSGVKTLFNPA------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLER 79
Cdd:COG0524   141 EPPREALLAALEAARAAGVPVSLDPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLAR 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  80 GCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQATGT 159
Cdd:COG0524   216 GVKLVVVTLGAEGALLYTGGEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAAAALVVTRPGA 291

                         170
                  ....*....|
gi 1907166189 160 QSSYPYKKDL 169
Cdd:COG0524   292 QPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 8-161 8.29e-32

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 115.52  E-value: 8.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   8 SPAASLEALTMARRSGVKT---LFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVV 84
Cdd:pfam00294 141 LPEATLEELIEAAKNGGTFdpnLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTV 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166189  85 VITLGASGCVILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEEMLKRSNFIAAVSVQATGTQS 161
Cdd:pfam00294 221 IVTLGADGALVVEGDGEV-HVPAVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALVVQKSGAQT 294
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 1-170 4.69e-70

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: 213.62  E-value: 4.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERG 80
Cdd:TIGR02152 128 VLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:TIGR02152 208 VKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGAQ 283

                         170
                  ....*....|
gi 1907166189 161 SSYPYKKDLP 170
Cdd:TIGR02152 284 SSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 1-165 7.12e-62

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: 192.76  E-value: 7.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERG 80
Cdd:cd01174   133 LLLQLEIPLETVLAALRAARRAGVTVILNPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKG 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSqaEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPnlSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:cd01174   212 VKNVIVTLGAKGALLAS--GGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQ 287


                  ....*
gi 1907166189 161 SSYPY 165
Cdd:cd01174   288 PSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
 1-170 1.54e-58

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 185.33  E-value: 1.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   1 MICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMIL 76
Cdd:PTZ00292  151 LICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKEL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  77 LERGCQVVVITLGASGCVILSQaEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQA 156
Cdd:PTZ00292  231 QQLGVENVIITLGANGCLIVEK-ENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISVTR 307

                         170
                  ....*....|....
gi 1907166189 157 TGTQSSYPYKKDLP 170
Cdd:PTZ00292  308 HGTQSSYPHPSELP 321
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 6-169 7.51e-38

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: 131.55  E-value: 7.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   6 EISPAASLEALTMARRSGVKTLFNPA------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLER 79
Cdd:COG0524   141 EPPREALLAALEAARAAGVPVSLDPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLAR 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  80 GCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQATGT 159
Cdd:COG0524   216 GVKLVVVTLGAEGALLYTGGEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAAAALVVTRPGA 291

                         170
                  ....*....|
gi 1907166189 160 QSSYPYKKDL 169
Cdd:COG0524   292 QPALPTREEV 301
PRK11142 PRK11142
ribokinase; Provisional
 4-170 1.14e-34

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 123.44  E-value: 1.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   4 QLEiSPAAS-LEALTMARRSGVKTLFNPAPAMAdLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQ 82
Cdd:PRK11142  139 QLE-TPLETvLAAAKIAKQHGTKVILNPAPARE-LPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIE 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  83 VVVITLGASGcVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVGALAfyLAYYPNLSLEEMLKRSNFIAAVSVQATGTQSS 162
Cdd:PRK11142  217 TVLITLGSRG-VWLSENGE-GQRVPGFRVQAVDTIAAGDTFNGALV--TALLEGKPLPEAIRFAHAAAAIAVTRKGAQPS 292


                  ....*...
gi 1907166189 163 YPYKKDLP 170
Cdd:PRK11142  293 IPWREEID 300
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 8-161 8.29e-32

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 115.52  E-value: 8.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   8 SPAASLEALTMARRSGVKT---LFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVV 84
Cdd:pfam00294 141 LPEATLEELIEAAKNGGTFdpnLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTV 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166189  85 VITLGASGCVILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEEMLKRSNFIAAVSVQATGTQS 161
Cdd:pfam00294 221 IVTLGADGALVVEGDGEV-HVPAVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALVVQKSGAQT 294
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 7-159 5.47e-23

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 92.57  E-value: 5.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   7 ISPAASLEALTMARRSGVKTLFNPAPAmadlDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLER-GCQVVV 85
Cdd:COG2870   165 LTPELIQALIALARAAGKPVLVDPKGR----DFSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAAAELLERlGLEALL 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166189  86 ITLGASGCVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSVQATGT 159
Cdd:COG2870   241 VTRGEEGMTLFDADGP-PHHLPAQAREVFDVTGAGDTVIATLALALAA--GASLEEAAELANLAAGIVVGKLGT 311
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 7-158 1.23e-22

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: 91.48  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   7 ISPAAS-------LEALTMARRSGVKTLF--NPAPAMADLD------PQFYTLSSIFCCNESEAEILTGHAvSDPTTAGK 71
Cdd:cd01166   133 ITLALSesarealLEALEAAKARGVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDE-DPTDAAER 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  72 AAMilLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEEMLKRSNFIA 150
Cdd:cd01166   212 ALA--LALGVKAVVVKLGAEGALVYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLE---GWDLEEALRFANAAA 284


                  ....*...
gi 1907166189 151 AVSVQATG 158
Cdd:cd01166   285 ALVVTRPG 292
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 5-159 3.01e-22

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: 90.75  E-value: 3.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   5 LEISPAASLEALTMARRSGVKTLFN-PAPAMAD-----LDPQFYTLSSIFCcNESEAEILTGHAVSDPTTAGKAamiLLE 78
Cdd:cd01168   156 LTVPPEAILLAAEHAKENGVKIALNlSAPFIVQrfkeaLLELLPYVDILFG-NEEEAEALAEAETTDDLEAALK---LLA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  79 RGCQVVVITLGASGCVILSQAE--PVPkhiPTEAVKAVDTTGAGDSFVGalAFYLAYYPNLSLEEMLKRSNFIAAVSVQA 156
Cdd:cd01168   232 LRCRIVVITQGAKGAVVVEGGEvyPVP---AIPVEKIVDTNGAGDAFAG--GFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306


                  ...
gi 1907166189 157 TGT 159
Cdd:cd01168   307 LGP 309
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 7-164 1.14e-21

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: 88.77  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   7 ISPAASLEALTMARRSGVKTLFNPAPamadLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLER-GCQVVV 85
Cdd:cd01172   148 LTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALL 223

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907166189  86 ITLGASGCVILSQAEPvPKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATGTQSSYP 164
Cdd:cd01172   224 VTLGEEGMTLFERDGE-VQHIPALAKEVYDVTGAGDTVIATLALALA--AGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 10-158 2.03e-21

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: 88.08  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  10 AASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLSSIFCCNESEAEILTGHavSDPTtagKAAMILLERG 80
Cdd:cd01167   138 SALLELLEAAKKAGVLISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGE--EDPE---EIAALLLLFG 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  81 CQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPNLS-----LEEMLKRSNFIAAVSVQ 155
Cdd:cd01167   213 LKLVLVTRGADGALLYTKGGVG--EVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedeLAEALRFANAVGALTCT 290


                  ...
gi 1907166189 156 ATG 158
Cdd:cd01167   291 KAG 293
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 8-132 2.52e-21

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: 85.99  E-value: 2.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   8 SPAASLEALTMARRSGVKTLFNPAPAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQV 83
Cdd:cd00287    69 APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKV 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907166189  84 VVITLGASGCVILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGALAFYLA 132
Cdd:cd00287   149 VIVTLGEKGAIVATRGGTE-VHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
51-160 9.95e-19

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 80.95  E-value: 9.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 130
Cdd:COG1105   184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFL-- 259

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907166189 131 LAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:COG1105   260 AGLARGLDLEEALRLAVAAGAAAALSPGTG 289
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 9-165 1.15e-18

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: 80.42  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   9 PAASLEALTMARRSGVktlfnpaPAMADLDPQF-------YTLSSIFCCNESEAEILTGhaVSDPttagKAAMILLERGC 81
Cdd:cd01945   137 PEAALHLAQEARARGI-------PIPLDLDGGGlrvleelLPLADHAICSENFLRPNTG--SADD----EALELLASLGI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  82 QVVVITLGASGCVILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATGTQS 161
Cdd:cd01945   204 PFVAVTLGEAGCLWLERDGEL-FHVPAFPVEVVDTTGAGDVFHGAFAHALA--EGMPLREALRFASAAAALKCRGLGGRA 280


                  ....
gi 1907166189 162 SYPY 165
Cdd:cd01945   281 GLPT 284
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 28-160 4.52e-17

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: 76.20  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  28 FNPAPAMADLD----PQFYTLSSIFCCNESEAEIL---TGhaVSDPTTAgkaamilleRGCQVVVITLGASGCVILSQAE 100
Cdd:cd01942   154 FDPGQELPRLSgeelEEILERADILFVNDYEAELLkerTG--LSEAELA---------SGVRVVVVTLGPKGAIVFEDGE 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189 101 PVpKHIPTEAVKAVDTTGAGDSFvgALAFYLAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:cd01942   223 EV-EVPAVPAVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 51-160 7.34e-16

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: 72.95  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGALAfy 130
Cdd:cd01164   184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFV-- 259

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907166189 131 LAYYPNLSLEEMLKRSNFIAAVSVQATGTQ 160
Cdd:cd01164   260 AGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 6-158 1.78e-15

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 72.94  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   6 EISPAASLEALTMARRSGVKTLFNPAP---AMADLDP-------QFYTLSSIFCCNESEAEILTGhaVSDPTTAGKAami 75
Cdd:PLN02341  237 ELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPderraleHLLRMSDVLLLTSEEAEALTG--IRNPILAGQE--- 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  76 LLERGC--QVVVITLGASGCVILSQAEPVPKhiPTEAVKAVDTTGAGDSFVGALAFylAYYPNLSLEEMLKRSNFIAAVS 153
Cdd:PLN02341  312 LLRPGIrtKWVVVKMGSKGSILVTRSSVSCA--PAFKVNVVDTVGCGDSFAAAIAL--GYIHNLPLVNTLTLANAVGAAT 387


                  ....*
gi 1907166189 154 vqATG 158
Cdd:PLN02341  388 --AMG 390
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 22-158 2.71e-14

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: 68.60  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  22 SGVKTLFNPAPAMADLDPQFYT----LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGcqvVVITLGASGCVILS 97
Cdd:cd01944   155 AGTTLVFDPGPRISDIPDTILQalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAP---VVVRLGSNGAWIRL 231

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166189  98 QAEPvPKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATG 158
Cdd:cd01944   232 PDGN-THIIPGFKVKAVDTIGAGDTHAGGMLAGLA--KGMSLADAVLLANAAAAIVVTRSG 289
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 2-155 1.11e-13

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: 66.95  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   2 ICQLEISPAASLEALTMARRSGVKTLFNPA-----PAMADLDPQFYTLSsifcCNESEAEILTGHAVSDPTTAGKAAMIL 76
Cdd:cd01941   133 VVDANLPEEALEYLLALAAKHGVPVAFEPTsapklKKLFYLLHAIDLLT----PNRAELEALAGALIENNEDENKAAKIL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  77 LERGCQVVVITLGASGCVILSQAEPV-PKHIPTEAV-KAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKRSNFIAAVSV 154
Cdd:cd01941   209 LLPGIKNVIVTLGAKGVLLSSREGGVeTKLFPAPQPeTVVNVTGAGDAFVAGLVAGLLE--GMSLDDSLRFAQAAAALTL 286


                  .
gi 1907166189 155 Q 155
Cdd:cd01941   287 E 287
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 6-169 5.69e-13

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 65.34  E-value: 5.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   6 EISPAASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLSSIFCCNESEAEILTGhavSDPTTAGKAAmIL 76
Cdd:PRK09434  133 EPSRSTTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALADVVKLSEEELCFLSG---TSQLEDAIYA-LA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  77 LERGCQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPNLS----LEEMLKRSNFIAAV 152
Cdd:PRK09434  209 DRYPIALLLVTLGAEGVLVHTRGQV--QHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTdeaeLAEIIAQAQACGAL 286

                         170
                  ....*....|....*..
gi 1907166189 153 SVQATGTQSSYPYKKDL 169
Cdd:PRK09434  287 ATTAKGAMTALPNRQEL 303
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 51-144 2.50e-11

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 60.96  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEA-EILTGHAVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIP-TEAVKAVDTTGAGDSFVGalA 128
Cdd:PLN02379  239 NEDEArELLRGEQESDP----EAALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPaIGETNAVDATGAGDLFAS--G 310

                          90
                  ....*....|....*.
gi 1907166189 129 FYLAYYPNLSLEEMLK 144
Cdd:PLN02379  311 FLYGLIKGLSLEECCK 326
PLN02323 PLN02323
probable fructokinase
 52-168 1.52e-10

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 58.48  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  52 ESEAEILTGhavSDPTTaGKAAMILLERGCQVVVITLGASGCVILSQAepVPKHIPTEAVKAVDTTGAGDSFVGALAFYL 131
Cdd:PLN02323  205 DEEVEFLTG---GDDPD-DDTVVKLWHPNLKLLLVTEGEEGCRYYTKD--FKGRVEGFKVKAVDTTGAGDAFVGGLLSQL 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907166189 132 AYYPNL-----SLEEMLKRSNFIAAVSVQATGTQSSYPYKKD 168
Cdd:PLN02323  279 AKDLSLledeeRLREALRFANACGAITTTERGAIPALPTKEA 320
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 47-142 2.95e-10

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: 57.48  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  47 IFCCNESEAEILTGHAvsdptTAGKAAMILLERGCQVVVITLGASGCVILSQ----AEPVpkhIPTEAVkaVDTTGAGDS 122
Cdd:cd01946   166 VVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPA---YPLESV--FDPTGAGDT 235

                          90       100
                  ....*....|....*....|
gi 1907166189 123 FVGALAFYLAYYPNLSLEEM 142
Cdd:cd01946   236 FAGGFIGYLASQKDTSEANM 255
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 47-132 2.14e-08

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


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 52.34  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  47 IFCCNESEAEILTGHAVSDPTTAGKA----AMILLERGCQ----VVVITLGASGCVILSQAEPVPKHIP---TEAVKAVD 115
Cdd:cd01943   183 VFSPNLEEAARLLGLPTSEPSSDEEKeavlQALLFSGILQdpggGVVLRCGKLGCYVGSADSGPELWLPayhTKSTKVVD 262

                          90
                  ....*....|....*..
gi 1907166189 116 TTGAGDSFVGALAFYLA 132
Cdd:cd01943   263 PTGGGNSFLGGFAAGLA 279
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 65-132 2.57e-08

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: 51.59  E-value: 2.57e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907166189  65 DPTTAGKAAMI-LLERGCQVVVITLGASGCVILSQAEPVPKHIptEAVKAVDTTGAGDSFVGALAFYLA 132
Cdd:cd01940   171 LSDEEVKAKLKeAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAP--RPVEVVDTLGAGDSFIAGFLLSLL 237
PTZ00247 PTZ00247
adenosine kinase; Provisional
 5-169 6.68e-08

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 50.80  E-value: 6.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189   5 LEISPAASLEALTMARRSGVKTLFN-PAP-AMADLDPQFYTL---SSIFCCNESEAEILtGHAVSDPTT-----AGKAAM 74
Cdd:PTZ00247  170 LTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyVDILFGNEEEAKTF-AKAMKWDTEdlkeiAARIAM 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  75 ILLERGCQ--VVVITLGASGCVILSQAE----PVPkhiPTEAVKAVDTTGAGDSFVGAlafYLAYYPN-LSLEEMLKRSN 147
Cdd:PTZ00247  249 LPKYSGTRprLVVFTQGPEPTLIATKDGvtsvPVP---PLDQEKIVDTNGAGDAFVGG---FLAQYANgKDIDRCVEAGH 322

                         170       180
                  ....*....|....*....|..
gi 1907166189 148 FIAAVSVQATGtqSSYPYKKDL 169
Cdd:PTZ00247  323 YSAQVIIQHNG--CTYPEKPPF 342
fruK PRK09513
1-phosphofructokinase; Provisional
 51-154 9.16e-08

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 50.46  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILS-----QAEPvPKhipteaVKAVDTTGAGDSFVG 125
Cdd:PRK09513  187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNasgewIAKP-PA------CDVVSTVGAGDSMVG 259

                          90       100
                  ....*....|....*....|....*....
gi 1907166189 126 ALAFYLAYypNLSLEEMLKRSNFIAAVSV 154
Cdd:PRK09513  260 GLIYGLLM--RESSEHTLRLATAVSALAV 286
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 47-155 1.41e-07

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: 49.72  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  47 IFCCNESEAEILTghavsdptTAGKAAMilleRGCQVVVITLGASGCVILSQAEPvpKHIPTEAVKAVDTTGAGDSFVGA 126
Cdd:cd01947   168 ILIGSRLDPGELV--------VAEKIAG----PFPRYLIVTEGELGAILYPGGRY--NHVPAKKAKVPDSTGAGDSFAAG 233

                          90       100
                  ....*....|....*....|....*....
gi 1907166189 127 LAFYLAYypNLSLEEMLKRSNFIAAVSVQ 155
Cdd:cd01947   234 FIYGLLK--GWSIEEALELGAQCGAICVS 260
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 51-144 4.01e-07

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 48.63  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDPTTAGKAAMILLERG-CQVVVITLGASGCVILS-----QAEPVPkhipteaVKAVDTTGAGDSFV 124
Cdd:PRK10294  187 NQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDsenciQVVPPP-------VKSQSTVGAGDSMV 259

                          90       100
                  ....*....|....*....|
gi 1907166189 125 GALAFYLAyyPNLSLEEMLK 144
Cdd:PRK10294  260 GAMTLKLA--ENASLEEMVR 277
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 19-159 4.77e-07

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 48.29  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  19 ARRSGVKTLFNPAPAmadlDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQ 98
Cdd:PRK11316  167 ARKAGVPVLIDPKGT----DFERYRGATLLTPNLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLLQP 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166189  99 AEPvPKHIPTEAVKAVDTTGAGDSFVGALAFYLAyyPNLSLEEMLKRSNFIAAVSVQATGT 159
Cdd:PRK11316  243 GKA-PLHLPTQAREVYDVTGAGDTVISVLAAALA--AGNSLEEACALANAAAGVVVGKLGT 300
PLN02548 PLN02548
adenosine kinase
 50-169 1.92e-06

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 46.63  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  50 CNESEAEILT---GHAVSD-PTTAGKAAMILLERGCQ--VVVITLGAsGCVILSQAEPVPKH--IPTEAVKAVDTTGAGD 121
Cdd:PLN02548  209 GNETEARTFAkvqGWETEDvEEIALKISALPKASGTHkrTVVITQGA-DPTVVAEDGKVKEFpvIPLPKEKLVDTNGAGD 287

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907166189 122 SFVGalAFYLAYYPNLSLEEMLKRSNFIAAVSVQATGTqsSYPYKKDL 169
Cdd:PLN02548  288 AFVG--GFLSQLVQGKDIEECVRAGNYAANVIIQRSGC--TYPEKPDF 331
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 37-153 4.67e-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: 45.08  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  37 LDPQFY-----TLSSIFCCNESEAEILTGHAVS--DPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTE 109
Cdd:cd01937   133 LDAQGFlrranQEKLIKCVILKLHDVLKLSRVEaeVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKY--TIPAS 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907166189 110 AVKAVDTTGAGDSFVGALaFYLAYYPNlsleEMLKRSNFIAAVS 153
Cdd:cd01937   211 KKDVVDPTGAGDVFLAAF-LYSRLSGK----DIKEAAEFAAAAA 249
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
 79-158 1.96e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 43.64  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  79 RGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFVGalAFYLAYYPNLSLEEMLKRSNFIAAVSVQATG 158
Cdd:PLN02630  201 RQKCCVIVTNGKKGCRIYWKDGEM--RVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 51-160 2.17e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 43.64  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDpttAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTGAGDSFV-GALAF 129
Cdd:PLN02813  289 NSDEARALCGLGSEE---SPESATRYLSHFCPLVSVTDGARGSYIGVKGEAV--YIPPSPCVPVDTCGAGDAYAaGILYG 363

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907166189 130 YLAYYPNL-SLEEMLKRsnfIAAVSVQATGTQ 160
Cdd:PLN02813  364 LLRGVSDLrGMGELAAR---VAATVVGQQGTR 392
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 74-158 2.38e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.19  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  74 MILLERGCQVVVITLGASGCVILSQAEpVPKHiPTEAVKAVDTTGAGDSFVGalAFYLAYYPNLSLEEMLKRSNFIAAVS 153
Cdd:PRK09813  178 KAIVARGAGVVIVTLGENGSIAWDGAQ-FWRQ-APEPVTVVDTMGAGDSFIA--GFLCGWLAGMTLPQAMAQGTACAAKT 253


                  ....*
gi 1907166189 154 VQATG 158
Cdd:PRK09813  254 IQYHG 258
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 32-157 3.06e-05

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: 42.83  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  32 PAMADLDPQFYTLSSIFCC--------------NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT--------LG 89
Cdd:COG2240   112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpAD 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907166189  90 ASGCVILSQAEpvPKHIPTEAVkAVDTTGAGDSFVGALAFYLAYypNLSLEEMLKR-SNFIAAVsVQAT 157
Cdd:COG2240   192 KIGNLAVTADG--AWLVETPLL-PFSPNGTGDLFAALLLAHLLR--GKSLEEALERaAAFVYEV-LERT 254
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 51-132 3.53e-05

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 42.72  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  51 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT---LGASGCV-ILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGA 126
Cdd:COG0351   133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghLPGDEAVdVLYDGDGV-REFSAPRIDTGNTHGTGCTLSSA 211


                  ....*.
gi 1907166189 127 LAFYLA 132
Cdd:COG0351   212 IAALLA 217
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 54-141 4.08e-05

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 42.47  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  54 EAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT----LGASGCV--ILSQAEPVpKHIPTEAVKAVDTTGAGDSFVGAL 127
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVVtdVLYDGGGF-YTLEAPRIPTKNTHGTGCTLSAAI 207

                          90
                  ....*....|....
gi 1907166189 128 AFYLAYypNLSLEE 141
Cdd:pfam08543 208 AANLAK--GLSLPE 219
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 50-157 1.47e-04

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 40.65  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  50 CNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT-----LGASGCVILSQAEPVpKHIPTEAVKAVDT-TGAGDSF 123
Cdd:cd01173   142 PNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelaDDDRIEMLGSTATEA-WLVQRPKIPFPAYfNGTGDLF 220

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907166189 124 VGALAFYLAYYPnlSLEEMLKRS-NFIAAVsVQAT 157
Cdd:cd01173   221 AALLLARLLKGK--SLAEALEKAlNFVHEV-LEAT 252
PRK09850 PRK09850
pseudouridine kinase; Provisional
 40-128 2.94e-04

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 39.97  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  40 QFYTLSSifccNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPVPKHIPTEAVKAVDTTGA 119
Cdd:PRK09850  180 QIHTLKP----NRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG-VYYSDISGESGWSAPIKTNVINVTGA 254


                  ....*....
gi 1907166189 120 GDSFVGALA 128
Cdd:PRK09850  255 GDAMMAGLA 263
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 54-137 1.93e-03

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 37.41  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166189  54 EAEILTGHAVSDPTTAGK-AAMILLERGCQVVVITlgasGCVILSQAEPVP--------KHIPTEAVKAVDTTGAGDSFV 124
Cdd:PRK06427  143 EAEALTGLPIADTEDEMKaAARALHALGCKAVLIK----GGHLLDGEESVDwlfdgegeERFSAPRIPTKNTHGTGCTLS 218

                          90
                  ....*....|...
gi 1907166189 125 GALAFYLAYYPNL 137
Cdd:PRK06427  219 AAIAAELAKGASL 231
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 44-87 2.03e-03

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 37.75  E-value: 2.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907166189  44 LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 87
Cdd:PTZ00344  139 YADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 102-159 4.88e-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: 36.62  E-value: 4.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166189 102 VPKHIPteaVKAVDTTGAGDSFVGALAFYLAYYPNlSLEEMLKRSNFIAAVSVQATGT 159
Cdd:cd01939   236 SPAHKP---IRVVDTLGAGDTFNAAVIYALNKGPD-DLSEALDFGNRVASQKCTGVGF 289
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH