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Conserved domains on  [gi|26340850|dbj|BAC34087|]
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unnamed protein product, partial [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

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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 ...
 1-149 4.40e-85

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: 252.33  E-value: 4.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAA 80
Cdd:PLN02548 183 NLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISALPKASGTHKRTVVITQGADPTVVAE 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26340850   81 ENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFPEKPDF 149
Cdd:PLN02548 263 DGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYPEKPDF 331
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 1-149 4.40e-85

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 252.33  E-value: 4.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAA 80
Cdd:PLN02548 183 NLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISALPKASGTHKRTVVITQGADPTVVAE 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26340850   81 ENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFPEKPDF 149
Cdd:PLN02548 263 DGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYPEKPDF 331
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 1-144 2.18e-58

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: 183.58  E-value: 2.18e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREqgfETKDIKEIAKKAQALpkvnskRQRTVIFTQGRDDTIVAa 80
Cdd:cd01168 180 NLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLLAL------RCRIVVITQGAKGAVVV- 249

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26340850  81 eNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFP 144
Cdd:cd01168 250 -EGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 1-143 1.17e-35

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 124.76  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850     1 NLSAPFISqfFKEALMDVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAa 80
Cdd:pfam00294 162 NLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIVTLGADGALVV- 232

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26340850    81 eNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTF 143
Cdd:pfam00294 233 -EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 11-142 2.34e-24

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: 95.34  E-value: 2.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  11 FKEALMDVMPYVDILFGNETEAATFareqgFETKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAEND---VTAF 87
Cdd:COG0524 175 ARELLRELLALVDILFPNEEEAELL-----TGETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAF 243

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26340850  88 PVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 142
Cdd:COG0524 244 PV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 18-142 5.00e-11

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: 59.15  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    18 VMPYVDILFGNETEAATFAREqgfetKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAENDVT----AFPVldqn 93
Cdd:TIGR04382 185 VLPLVDVIIGTREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDGEGvevpGFPV---- 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 26340850    94 qeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 142
Cdd:TIGR04382 250 --EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 1-149 4.40e-85

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 252.33  E-value: 4.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAA 80
Cdd:PLN02548 183 NLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISALPKASGTHKRTVVITQGADPTVVAE 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26340850   81 ENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFPEKPDF 149
Cdd:PLN02548 263 DGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYPEKPDF 331
PTZ00247 PTZ00247
adenosine kinase; Provisional
 1-149 1.17e-76

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 231.45  E-value: 1.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAA 80
Cdd:PTZ00247 194 NLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIAT 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26340850   81 ENDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFPEKPDF 149
Cdd:PTZ00247 274 KDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYPEKPPF 342
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 1-144 2.18e-58

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: 183.58  E-value: 2.18e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   1 NLSAPFISQFFKEALMDVMPYVDILFGNETEAATFAREqgfETKDIKEIAKKAQALpkvnskRQRTVIFTQGRDDTIVAa 80
Cdd:cd01168 180 NLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLLAL------RCRIVVITQGAKGAVVV- 249

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26340850  81 eNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTFP 144
Cdd:cd01168 250 -EGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 1-143 1.17e-35

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 124.76  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850     1 NLSAPFISqfFKEALMDVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAa 80
Cdd:pfam00294 162 NLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIVTLGADGALVV- 232

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26340850    81 eNDVTAFPVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCTF 143
Cdd:pfam00294 233 -EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 11-142 2.34e-24

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: 95.34  E-value: 2.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  11 FKEALMDVMPYVDILFGNETEAATFareqgFETKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAEND---VTAF 87
Cdd:COG0524 175 ARELLRELLALVDILFPNEEEAELL-----TGETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAF 243

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26340850  88 PVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 142
Cdd:COG0524 244 PV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 11-116 2.30e-20

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: 82.53  E-value: 2.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  11 FKEALMDVMPYVDILFGNETEAATFAREQGFETKDIkeiakkAQALPKVNSKRQRTVIFTQGRDDTIVaAENDVTAFPVL 90
Cdd:cd00287  99 DGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEA------AEAAALLLSKGPKVVIVTLGEKGAIV-ATRGGTEVHVP 171

                        90       100
                ....*....|....*....|....*.
gi 26340850  91 DQNqEEIIDTNGAGDAFVGGFLSQLV 116
Cdd:cd00287 172 AFP-VKVVDTTGAGDAFLAALAAGLA 196
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 12-142 2.84e-20

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: 84.16  E-value: 2.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  12 KEALMDVMPYVDILFGNETEAATFAREQGfeTKDIKEIAKKAQALPKvnskrqrTVIFTQGRDDTIVAAENDVTAFPVLd 91
Cdd:cd01166 176 REALEELLPYVDIVLPSEEEAEALLGDED--PTDAAERALALALGVK-------AVVVKLGAEGALVYTGGGRVFVPAY- 245

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 26340850  92 qnQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 142
Cdd:cd01166 246 --PVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 17-140 3.32e-19

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: 81.44  E-value: 3.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  17 DVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAENDVTAFPVLdqnQEE 96
Cdd:cd01174 171 ELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGV------KNVIVTLGAKGALLASGGEVEHVPAF---KVK 241

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26340850  97 IIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:cd01174 242 AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPG 285
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 7-141 1.05e-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: 76.97  E-value: 1.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   7 ISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKdikEIAKKAqalpkvnskrqRTVIFTQGRDDTIVAAENDVTA 86
Cdd:cd01942 160 LPRLSGEELEEILERADILFVNDYEAELLKERTGLSEA---ELASGV-----------RVVVVTLGPKGAIVFEDGEEVE 225

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26340850  87 FPVLdqNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGC 141
Cdd:cd01942 226 VPAV--PAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
PTZ00292 PTZ00292
ribokinase; Provisional
 3-140 1.71e-12

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 63.22  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    3 SAPFISQFFKEALMDVMPYVDILFGNETEAATFAreqGFETKDIKEIAKKAQALPKVNSkrqRTVIFTQG-RDDTIVAAE 81
Cdd:PTZ00292 180 PAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALIT---GMEVTDTESAFKASKELQQLGV---ENVIITLGaNGCLIVEKE 253

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26340850   82 NDVTAFPVLdqnQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:PTZ00292 254 NEPVHVPGK---RVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 5-140 1.50e-11

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 60.51  E-value: 1.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   5 PFISQFFKEALMDVMPYVDILFGNETEAATFAREQGFETKD-IKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAAend 83
Cdd:cd01944 165 PRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEAsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPG--- 241

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26340850  84 vtaFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:cd01944 242 ---FKV------KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 18-135 2.41e-11

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: 59.68  E-value: 2.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  18 VMPYVDILFgneteaatFAREqGFETKDIKEIAKKAQalpkvnSKRQRTVIFTQGRDDTIVAAENDVTAFPVLdqnQEEI 97
Cdd:cd01940 157 VCPYVDFAF--------FSAS-DLSDEEVKAKLKEAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEV 218

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 26340850  98 IDTNGAGDAFVGGFL-SQLVSDKPLTECIRAG-HYAASVI 135
Cdd:cd01940 219 VDTLGAGDSFIAGFLlSLLAGGTAIAEAMRQGaQFAAKTC 258
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 18-142 5.00e-11

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: 59.15  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850    18 VMPYVDILFGNETEAATFAREqgfetKDIKEIAKKAQALPKvnskrqRTVIFTQGRDDTIVAAENDVT----AFPVldqn 93
Cdd:TIGR04382 185 VLPLVDVIIGTREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDGEGvevpGFPV---- 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 26340850    94 qeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGCT 142
Cdd:TIGR04382 250 --EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 15-133 5.12e-11

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 58.86  E-value: 5.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  15 LMDVMPYVDILFGNETEAATFAREQGFETKDIKeIAKKAQALPKVNskrqrTVIFTQGRDDTIVAAEND---VTAFPVld 91
Cdd:cd01941 170 LFYLLHAIDLLTPNRAELEALAGALIENNEDEN-KAAKILLLPGIK-----NVIVTLGAKGVLLSSREGgveTKLFPA-- 241

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 26340850  92 QNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAAS 133
Cdd:cd01941 242 PQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAA 283
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 1-140 1.08e-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: 54.95  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   1 NLSAPFISQF--FKEALMDVMPYVDILFGNETEAATFareqgFETKDIKEIAKKAQALPkvnskrQRTVIFTQGRDDTIV 78
Cdd:cd01167 159 NLRPPLWRDEeeARERIAELLELADIVKLSDEELELL-----FGEEDPEEIAALLLLFG------LKLVLVTRGADGALL 227

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26340850  79 ---AAENDVTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDK-------PLTECIRAGHYAASVIIRRTG 140
Cdd:cd01167 228 ytkGGVGEVPGIPV------EVVDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 5-140 1.75e-09

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


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 54.65  E-value: 1.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   5 PFISQFFKEALmdvmPYVDILFGNETEAATFAREQGFETK--DIKEIAKKAQALPKVNSKRQRTVIFTQGRDDTIVAAEN 82
Cdd:cd01943 168 PENLEDLLQAL----PRVDVFSPNLEEAARLLGLPTSEPSsdEEKEAVLQALLFSGILQDPGGGVVLRCGKLGCYVGSAD 243

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  83 DVTAF--PVLDQNQEEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:cd01943 244 SGPELwlPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
PRK11142 PRK11142
ribokinase; Provisional
 22-140 2.02e-08

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 51.41  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   22 VDILFGNETEAATFAreqGFETKDIKEIAKKAQALpkvNSKRQRTVIFTQGRDDtIVAAEND----VTAFPVldqnqeEI 97
Cdd:PRK11142 179 VDIITPNETEAEKLT---GIRVEDDDDAAKAAQVL---HQKGIETVLITLGSRG-VWLSENGegqrVPGFRV------QA 245

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 26340850   98 IDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:PRK11142 246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 12-123 6.43e-08

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: 50.16  E-value: 6.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  12 KEALMDVMPYVDILFGNETEAatfareqgfetKDIKEIAKKAQALPKVNSKRQRTVIFTQGR-------DDTIVAAendv 84
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEA-----------RQLTGAANLVKAARLILAMGPKALIIKRGEygallftDDGYFAA---- 218

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 26340850  85 TAFPVldqnqEEIIDTNGAGDAFVGGFLSQLVSDKPLTE 123
Cdd:cd01946 219 PAYPL-----ESVFDPTGAGDTFAGGFIGYLASQKDTSE 252
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 19-136 3.19e-07

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 47.81  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   19 MPYVDILFGNETEAATFAREQgfeTKDIKEIAKKaqalpkvnskrqrTVIFTQGRDDTIVAAENDVTAFPVLdqnQEEII 98
Cdd:PRK09813 156 VPHLDYAFASAPQEDEFLRLK---MKAIVARGAG-------------VVIVTLGENGSIAWDGAQFWRQAPE---PVTVV 216

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 26340850   99 DTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVII 136
Cdd:PRK09813 217 DTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
PLN02323 PLN02323
probable fructokinase
 84-123 2.22e-06

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 45.77  E-value: 2.22e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 26340850   84 VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTE 123
Cdd:PLN02323 253 VEGFKV------KAVDTTGAGDAFVGGLLSQLAKDLSLLE 286
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 22-138 2.75e-06

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 45.49  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  22 VDILFGNETEAAtfarEQGFETKDIKeiakkaqalpkvnsKRQRTVIFTQGRDDTIV---AAENDVTAFPVldqnqeEII 98
Cdd:cd01947 166 LDILIGSRLDPG----ELVVAEKIAG--------------PFPRYLIVTEGELGAILypgGRYNHVPAKKA------KVP 221

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26340850  99 DTNGAGDAFVGGFLSQLVSDKPLTECIRAG-HYAASVIIRR 138
Cdd:cd01947 222 DSTGAGDSFAAGFIYGLLKGWSIEEALELGaQCGAICVSHF 262
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 11-140 2.82e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 45.55  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   11 FKEALMDVMPY--VDILFGNETEAATFAReqGFETKDikeiakkAQALPKVNSKRQRTVIFTQGRDDTIVAAENDVTAFP 88
Cdd:PLN02379 220 FRSPLLQLLESgkIDLCFANEDEARELLR--GEQESD-------PEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVP 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26340850   89 VLDQNQeeIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:PLN02379 291 AIGETN--AVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 12-128 4.29e-06

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: 44.83  E-value: 4.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  12 KEALMDVMPY-VDILFGNETEAATFAreqGFETKDIKEIAKKAQALpkvNSKRQRTVIFTQGRDDTIVAAENDV---TAF 87
Cdd:cd01164 167 GEALLAALAAkPFLIKPNREELEELF---GRPLGDEEDVIAAARKL---IERGAENVLVSLGADGALLVTKDGVyraSPP 240

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26340850  88 PVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 128
Cdd:cd01164 241 KV------KVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 12-140 1.35e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 43.64  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   12 KEALMDVMP-YVDILFGNETEAATFAreqGFETKDIKEIAkkAQALpkvnSKRQRTVIFTQGRDDTIVAAENDVTAFPVL 90
Cdd:PLN02813 272 RDDFWDVMGnYADILFANSDEARALC---GLGSEESPESA--TRYL----SHFCPLVSVTDGARGSYIGVKGEAVYIPPS 342

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26340850   91 DQnqeEIIDTNGAGDAFVGGFLSQL---VSDkpltecIR-AGHYA---ASVIIRRTG 140
Cdd:PLN02813 343 PC---VPVDTCGAGDAYAAGILYGLlrgVSD------LRgMGELAarvAATVVGQQG 390
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
12-128 3.29e-05

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 42.43  E-value: 3.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  12 KEALMDVMPY-VDILFGNETEAATFAreqGFETKDIKEIAKKAQALPKVNSKRqrtVIFTQGRDDTIVAAENDVTAFPVL 90
Cdd:COG1105 167 GEALKAALEAgPDLIKPNLEELEELL---GRPLETLEDIIAAARELLERGAEN---VVVSLGADGALLVTEDGVYRAKPP 240

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 26340850  91 DQnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 128
Cdd:COG1105 241 KV---EVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 65-117 6.10e-05

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 41.46  E-value: 6.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 26340850   65 RTVIFTQGRDDTIVAAENDVTAFP---VldqnqeEIIDTNGAGDAFVGGFLSQLVS 117
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 10-139 7.11e-05

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


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 41.03  E-value: 7.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  10 FFKEALMDVM-----PYVDILFGNETEAATFAreqGFETKDIKEIAKKAQALPKvnsKRQRTVIFT----QGRDDTIVAA 80
Cdd:cd01173 120 VVAEEIVPVYrdllvPLADIITPNQFELELLT---GKKINDLEDAKAAARALHA---KGPKTVVVTsvelADDDRIEMLG 193

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26340850  81 ----ENDVTAFPVLDQNQeeiiDTNGAGDAFVGGFLSQLVSDKPLTEciRAGHYAASV--IIRRT 139
Cdd:cd01173 194 statEAWLVQRPKIPFPA----YFNGTGDLFAALLLARLLKGKSLAE--ALEKALNFVheVLEAT 252
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 12-133 2.11e-04

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 40.08  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  12 KEALMDVMPYVDILFgnetEAATFAREQGFETkdikeiAKKAQALPKVNSKRQRTVIFTQGRDDT-IVAAENDVTAFPVl 90
Cdd:cd01939 170 REELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWGDQGAgALGPDGEYVHSPA- 238

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26340850  91 dQNQEEIIDTNGAGDAFVGGFLSQL-VSDKPLTECIRAGHYAAS 133
Cdd:cd01939 239 -HKPIRVVDTLGAGDTFNAAVIYALnKGPDDLSEALDFGNRVAS 281
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 29-141 3.69e-04

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 39.08  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  29 ETEAATfareqGFETKDIKEIAKKAQALPKvnSKRQRTVIFTQGRDD-TIVAAENDVTAFPVLDQnqeEIIDTNGAGDAF 107
Cdd:cd01172 191 EAREAL-----GDEINDDDELEAAGEKLLE--LLNLEALLVTLGEEGmTLFERDGEVQHIPALAK---EVYDVTGAGDTV 260

                        90       100       110
                ....*....|....*....|....*....|....
gi 26340850 108 VGGFLSQLVSDKPLTECIRAGHYAASVIIRRTGC 141
Cdd:cd01172 261 IATLALALAAGADLEEAAFLANAAAGVVVGKVGT 294
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 84-140 5.03e-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: 38.81  E-value: 5.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26340850  84 VTAFPVldqnqeEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRRTG 140
Cdd:cd01945 227 VPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
12-126 1.43e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 37.35  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   12 KEALMDVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKAQALPKVN---------SKRQRTVIFTQGRDDTIVAaen 82
Cdd:PRK12413 120 RQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAvvikggnrlSQKKAIDLFYDGKEFVILE--- 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26340850   83 dvtaFPVLDQNQeeiidtNGAGDAFVGGFLSQLVSDKPLTECIR 126
Cdd:PRK12413 197 ----SPVLEKNN------IGAGCTFASSIASQLVKGKSPLEAVK 230
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
 63-140 2.17e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 37.09  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850   63 RQRT-VIFTQGRDDTIVAAEND---VTAFPVLDqnqeeiIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASVIIRR 138
Cdd:PLN02630 201 RQKCcVIVTNGKKGCRIYWKDGemrVPPFPAIQ------VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQ 274


                 ..
gi 26340850  139 TG 140
Cdd:PLN02630 275 VG 276
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 20-134 3.64e-03

Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 36.23  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  20 PYVDILFGNETEAAtfareqgfETKDIKEIAKKAQALPK----VNSKRQRTVIFTQGRDDTIVAAENDVtafpvldqnqe 95
Cdd:cd01937 154 KLHDVLKLSRVEAE--------VISTPTELARLIKETGVkeiiVTDGEEGGYIFDGNGKYTIPASKKDV----------- 214

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 26340850  96 eiIDTNGAGDAFVGGFLSQLVSDKpltECIRAGHYAASV 134
Cdd:cd01937 215 --VDPTGAGDVFLAAFLYSRLSGK---DIKEAAEFAAAA 248
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 13-139 4.95e-03

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 35.89  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26340850  13 EALMD-VMPYVDILFGNETEAATFAreqGFETKDIKEIAKKAQALpkvNSKRQRTVIFT-----QGRDDTIVAAendvta 86
Cdd:COG2240 129 EFIMRrLVPLADIITPNLTELALLT---GRPYETLEEALAAARAL---LALGPKIVVVTsvpldDTPADKIGNL------ 196

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26340850  87 fpVLDQNQEEIIDT-------NGAGDAFVGGFLSQLVSDKPLTECI-RAGHYAASViIRRT 139
Cdd:COG2240 197 --AVTADGAWLVETpllpfspNGTGDLFAALLLAHLLRGKSLEEALeRAAAFVYEV-LERT 254
 
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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