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Conserved domains on  [gi|1715415498|gb|TWA49226|]
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hypothetical protein FB005_101620 [Sinorhizobium medicae]

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 ...
 3-297 1.58e-55

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 cd01942:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 279  Bit Score: 181.35  E-value: 1.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   3 PLAAIGNVNVDLILgPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFG----AWLKEALGDR 78
Cdd:cd01942     1 DVAVVGHLNYDIIL-KVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGrlylEELREEGVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  79 SRDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSfqevrtMLDGNRLRGGYALLSGSFLTDALSLAYDALfdwadAH 158
Cdd:cd01942    80 SHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELE------PNDEADPDGLADIVHLSSGPGLIELARELA-----AG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 159 EIAVALDTGWPLEGWTEANRLKtlaWLKRCHCALFNEVETT---TLTGQSDPAEAARslksempaDAIVVVKRGPNGALA 235
Cdd:cd01942   149 GITVSFDPGQELPRLSGEELEE---ILERADILFVNDYEAEllkERTGLSEAELASG--------VRVVVVTLGPKGAIV 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715415498 236 IDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTLPRR 297
Cdd:cd01942   218 FEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
 
Name Accession Description Interval E-value
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 3-297 1.58e-55

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: 181.35  E-value: 1.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   3 PLAAIGNVNVDLILgPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFG----AWLKEALGDR 78
Cdd:cd01942     1 DVAVVGHLNYDIIL-KVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGrlylEELREEGVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  79 SRDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSfqevrtMLDGNRLRGGYALLSGSFLTDALSLAYDALfdwadAH 158
Cdd:cd01942    80 SHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELE------PNDEADPDGLADIVHLSSGPGLIELARELA-----AG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 159 EIAVALDTGWPLEGWTEANRLKtlaWLKRCHCALFNEVETT---TLTGQSDPAEAARslksempaDAIVVVKRGPNGALA 235
Cdd:cd01942   149 GITVSFDPGQELPRLSGEELEE---ILERADILFVNDYEAEllkERTGLSEAELASG--------VRVVVVTLGPKGAIV 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715415498 236 IDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTLPRR 297
Cdd:cd01942   218 FEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 4-293 5.36e-54

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: 178.15  E-value: 5.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLILGpAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALG----DRS 79
Cdd:COG0524     2 VLVIGEALVDLVAR-VDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRaegvDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  80 RDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSFQEvrtmLDGNRLRG-GYALLSGSFLTDALSL-AYDALFDWADA 157
Cdd:COG0524    81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPED----LDEALLAGaDILHLGGITLASEPPReALLAALEAARA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 158 HEIAVALDTGWPLEGWTEAnRLKTLAWLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEMPAdaIVVVKRGPNGALAID 237
Cdd:COG0524   157 AGVPVSLDPNYRPALWEPA-RELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVK--LVVVTLGAEGALLYT 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1715415498 238 RnGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:COG0524   234 G-GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTR 288
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 4-292 1.28e-28

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 111.28  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLIlgPAEPWPKPGTeIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDR----S 79
Cdd:pfam00294   2 VVVIGEANIDLI--GNVEGLPGEL-VRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEgvdtD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  80 RDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSFQEVRTMLDGNRlRGGYALLSGSFLTDALSLAYDALFDWADAH- 158
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLE-NADLLYISGSLPLGLPEATLEELIEAAKNGg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 159 -EIAVALDTGWPLegwteanRLKTLAWLKRCHCALFNEVETTTLTGQS--DPAEAARSLKSEMPA-DAIVVVKRGPNGAL 234
Cdd:pfam00294 158 tFDPNLLDPLGAA-------REALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHKLLAKgIKTVIVTLGADGAL 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1715415498 235 AIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIS 292
Cdd:pfam00294 231 VVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQ 288
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 4-294 3.22e-18

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: 83.03  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLIlgpaepwpkpGTEIIVDHDELR-----VGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDR 78
Cdd:TIGR04382   4 VITIGRVGVDLY----------PQQIGVPLEDVTsfakyLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  79 SRD--WPVEAAGTTLSVGITHPDGERTFfttrghlPLLSFQE--VRTMLDGNRLRGGYALLSGSFLTD--ALSL-----A 147
Cdd:TIGR04382  74 GVDtsHVVTDPGRRTSLVFLEIKPPDEF-------PLLFYREnaADLALTPDDVDEDYIASARALLVSgtALSQepsreA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 148 YDALFDWADAHEIAVALDTGWPLEGW---TEANRLKTLAwLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEmpADAIV 224
Cdd:TIGR04382 147 VLKALEYARAAGVRVVLDIDYRPYLWkspEEAGIYLRLV-LPLVDVIIGTREEFDIAGGEGDDEAAARALLDA--GVEIL 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 225 VVKRGPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTL 294
Cdd:TIGR04382 224 VVKRGPEGSLVYTGDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRH 293
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 39-293 1.50e-15

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 74.77  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  39 GGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDRSRDwpveaagttlsvgITHpdgertffttrghlplLSFQE 118
Cdd:PRK09813   23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVD-------------ISH----------------VHTKH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 119 VRT------MLDGNRLRGGY--ALLSGSFLTDAlSLAYDALFD------WADAHEIAVALDTGWPLEGWTEANRLKTLAW 184
Cdd:PRK09813   74 GVTaqtqveLHDNDRVFGDYteGVMADFALSEE-DYAWLAQYDivhaaiWGHAEDAFPQLHAAGKLTAFDFSDKWDSPLW 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 185 LkrchcALFNEVETTTLTGQSDPAEAARSLKSEMPADA-IVVVKRGPNGALAIDrnGAAF-SFPAPSVQVVDTIGAGDVF 262
Cdd:PRK09813  153 Q-----TLVPHLDYAFASAPQEDEFLRLKMKAIVARGAgVVIVTLGENGSIAWD--GAQFwRQAPEPVTVVDTMGAGDSF 225

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1715415498 263 NAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:PRK09813  226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQY 256
 
Name Accession Description Interval E-value
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 3-297 1.58e-55

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: 181.35  E-value: 1.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   3 PLAAIGNVNVDLILgPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFG----AWLKEALGDR 78
Cdd:cd01942     1 DVAVVGHLNYDIIL-KVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGrlylEELREEGVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  79 SRDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSfqevrtMLDGNRLRGGYALLSGSFLTDALSLAYDALfdwadAH 158
Cdd:cd01942    80 SHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELE------PNDEADPDGLADIVHLSSGPGLIELARELA-----AG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 159 EIAVALDTGWPLEGWTEANRLKtlaWLKRCHCALFNEVETT---TLTGQSDPAEAARslksempaDAIVVVKRGPNGALA 235
Cdd:cd01942   149 GITVSFDPGQELPRLSGEELEE---ILERADILFVNDYEAEllkERTGLSEAELASG--------VRVVVVTLGPKGAIV 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715415498 236 IDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTLPRR 297
Cdd:cd01942   218 FEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 4-293 5.36e-54

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: 178.15  E-value: 5.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLILGpAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALG----DRS 79
Cdd:COG0524     2 VLVIGEALVDLVAR-VDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRaegvDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  80 RDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSFQEvrtmLDGNRLRG-GYALLSGSFLTDALSL-AYDALFDWADA 157
Cdd:COG0524    81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPED----LDEALLAGaDILHLGGITLASEPPReALLAALEAARA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 158 HEIAVALDTGWPLEGWTEAnRLKTLAWLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEMPAdaIVVVKRGPNGALAID 237
Cdd:COG0524   157 AGVPVSLDPNYRPALWEPA-RELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVK--LVVVTLGAEGALLYT 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1715415498 238 RnGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:COG0524   234 G-GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTR 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 4-294 5.45e-30

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 114.98  E-value: 5.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLIlgpaepwPKPGTEII-VDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALG------ 76
Cdd:cd01166     2 VVTIGEVMVDLS-------PPGGGRLEqADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRregvdt 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  77 DRSRDWPVEAAGTTLSVgiTHPDGERTFFTTRGHLPLLSFQEvrTMLDGNRLRG-GYALLSGSFLtdALSL-AYDALFDW 154
Cdd:cd01166    75 SHVRVDPGRPTGLYFLE--IGAGGERRVLYYRAGSAASRLTP--EDLDEAALAGaDHLHLSGITL--ALSEsAREALLEA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 155 AD---AHEIAVALDTGWPLEGWTEANRLKTL-AWLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEMPADAIVVVKRGP 230
Cdd:cd01166   149 LEaakARGVTVSFDLNYRPKLWSAEEAREALeELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVVKLGA 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715415498 231 NGALAIDRNGAAFSfPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTL 294
Cdd:cd01166   229 EGALVYTGGGRVFV-PAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRP 291
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 4-292 1.28e-28

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 111.28  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLIlgPAEPWPKPGTeIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDR----S 79
Cdd:pfam00294   2 VVVIGEANIDLI--GNVEGLPGEL-VRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEgvdtD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  80 RDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSFQEVRTMLDGNRlRGGYALLSGSFLTDALSLAYDALFDWADAH- 158
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLE-NADLLYISGSLPLGLPEATLEELIEAAKNGg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 159 -EIAVALDTGWPLegwteanRLKTLAWLKRCHCALFNEVETTTLTGQS--DPAEAARSLKSEMPA-DAIVVVKRGPNGAL 234
Cdd:pfam00294 158 tFDPNLLDPLGAA-------REALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHKLLAKgIKTVIVTLGADGAL 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1715415498 235 AIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIS 292
Cdd:pfam00294 231 VVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQ 288
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 37-291 9.54e-24

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: 98.09  E-value: 9.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  37 RVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDRSRD----WPVEAAGTTLSVGITHPDGERTFFTTRGHLP 112
Cdd:cd01167    26 APGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDtrgiQFDPAAPTTLAFVTLDADGERSFEFYRGPAA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 113 LLSFqevRTMLDGNRLRGGYALLSGS--FLTDALSLAYDALFDWADAHEIAVALDTGWPLEGWTEANRLKTL--AWLKRC 188
Cdd:cd01167   106 DLLL---DTELNPDLLSEADILHFGSiaLASEPSRSALLELLEAAKKAGVLISFDPNLRPPLWRDEEEARERiaELLELA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 189 HCALFNEVETTTLTGQSDPAEAARSLKsEMPAdAIVVVKRGPNGALAIDRNGAAFsFPAPSVQVVDTIGAGDVFNAGFLA 268
Cdd:cd01167   183 DIVKLSDEELELLFGEEDPEEIAALLL-LFGL-KLVLVTRGADGALLYTKGGVGE-VPGIPVEVVDTTGAGDAFVAGLLA 259

                         250       260
                  ....*....|....*....|...
gi 1715415498 269 ALAADMPLIDCLKTGVTIASRAI 291
Cdd:cd01167   260 QLLSRGLLALDEDELAEALRFAN 282
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 3-291 7.28e-23

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: 95.95  E-value: 7.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   3 PLAAIGNVNVDLILGpAEPWPKPGTEIIVDHDELRVGGcAGNNALAWESLGVDYVIAANVGNDQFGAWLKEA---LGDRS 79
Cdd:cd01944     1 KVLVIGAAVVDIVLD-VDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAmrdEGIEI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  80 RDWPVEAAGTTLSVGITHPDGERTFFTTRG---HLPLLSFQEVRTMLDGnrlrggYALLSGSFLTDAlSLAYDALFDW-- 154
Cdd:cd01944    79 LLPPRGGDDGGCLVALVEPDGERSFISISGaeqDWSTEWFATLTVAPYD------YVYLSGYTLASE-NASKVILLEWle 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 155 ADAHEIAVALDTG--WPLEGWTEANRLKTLAWLKRChcalfNEVETTTLTGQSDPAEAARSLKSEMPADAIVVVKRGPNG 232
Cdd:cd01944   152 ALPAGTTLVFDPGprISDIPDTILQALMAKRPIWSC-----NREEAAIFAERGDPAAEASALRIYAKTAAPVVVRLGSNG 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1715415498 233 ALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAI 291
Cdd:cd01944   227 AWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVV 285
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
24-293 4.14e-21

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 91.35  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  24 KPGTEIIVDHDELRVGGcAGNN---ALAweSLGVDYVIAANVGNDQfGAWLKEALGDRS-RDWPVEAAGTT-LSVGITHP 98
Cdd:COG1105    20 EPGEVNRASEVRLDPGG-KGINvarVLK--ALGVDVTALGFLGGFT-GEFIEELLDEEGiPTDFVPIEGETrINIKIVDP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  99 DGERTF-FTTRGhlPLLS---FQEVRTMLDGNRLRGGYALLSGSF---LTDALslaYDALFDWADAHEIAVALDT-GWPL 170
Cdd:COG1105    96 SDGTETeINEPG--PEISeeeLEALLERLEELLKEGDWVVLSGSLppgVPPDF---YAELIRLARARGAKVVLDTsGEAL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 171 EgwtEAnrLKTLAWL----KRCHCALFNevetTTLTGQSDPAEAARSLKsEMPADaIVVVKRGPNGALAIDRNGAaFSFP 246
Cdd:COG1105   171 K---AA--LEAGPDLikpnLEELEELLG----RPLETLEDIIAAARELL-ERGAE-NVVVSLGADGALLVTEDGV-YRAK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1715415498 247 APSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:COG1105   239 PPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALS 285
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 7-291 4.75e-20

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 87.99  E-value: 4.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   7 IGNVNVDLILGPAEPwPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALgdrsrdwpvEA 86
Cdd:cd01174     5 VGSINVDLVTRVDRL-PKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENL---------RE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  87 AGTTLSvGITHPDGERTffttrGHLPLlsfqevrtMLDG---NRLrggyALLSG--SFLTDALSLAYDALFDWADA---- 157
Cdd:cd01174    75 EGIDVS-YVEVVVGAPT-----GTAVI--------TVDEsgeNRI----VVVPGanGELTPADVDAALELIAAADVlllq 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 158 HEIavaldtgwPLEGWTEA------NRLKTL-----------AWLKRCHCALFNEVETTTLTGQSDP-----AEAARSLk 215
Cdd:cd01174   137 LEI--------PLETVLAAlraarrAGVTVIlnpaparplpaELLALVDILVPNETEAALLTGIEVTdeedaEKAARLL- 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1715415498 216 SEMPADAiVVVKRGPNGALAIDRNGAaFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAI 291
Cdd:cd01174   208 LAKGVKN-VIVTLGAKGALLASGGEV-EHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSV 281
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 3-293 6.14e-19

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: 85.06  E-value: 6.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   3 PLAAIGNVNVDLILGPAEPWPK----PGTEIIvdhdelRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEAL--- 75
Cdd:cd01941     1 EIVVIGAANIDLRGKVSGSLVPgtsnPGHVKQ------SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESeka 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  76 GDRSRDWPVEAAGTTLSVGITHPDGER-------------TFFTTRGHLPLLSFQEVrTMLDGNrlrggyallsgsfltd 142
Cdd:cd01941    75 GLNVRGIVFEGRSTASYTAILDKDGDLvvaladmdiyellTPDFLRKIREALKEAKP-IVVDAN---------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 143 alsLAYDALFDWADAHEIAVALDtgwPLEGWTEANRLKTLAWLKRCHCALFNEVETTTLTGQS------DPAEAARSLKS 216
Cdd:cd01941   138 ---LPEEALEYLLALAAKHGVPV---AFEPTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALiennedENKAAKILLLP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 217 EMPAdaiVVVKRGPNGALAIDRNGA--AFSFPAPSVQ-VVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:cd01941   212 GIKN---VIVTLGAKGVLLSSREGGveTKLFPAPQPEtVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 4-294 3.22e-18

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: 83.03  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLIlgpaepwpkpGTEIIVDHDELR-----VGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDR 78
Cdd:TIGR04382   4 VITIGRVGVDLY----------PQQIGVPLEDVTsfakyLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  79 SRD--WPVEAAGTTLSVGITHPDGERTFfttrghlPLLSFQE--VRTMLDGNRLRGGYALLSGSFLTD--ALSL-----A 147
Cdd:TIGR04382  74 GVDtsHVVTDPGRRTSLVFLEIKPPDEF-------PLLFYREnaADLALTPDDVDEDYIASARALLVSgtALSQepsreA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 148 YDALFDWADAHEIAVALDTGWPLEGW---TEANRLKTLAwLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEmpADAIV 224
Cdd:TIGR04382 147 VLKALEYARAAGVRVVLDIDYRPYLWkspEEAGIYLRLV-LPLVDVIIGTREEFDIAGGEGDDEAAARALLDA--GVEIL 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 225 VVKRGPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTL 294
Cdd:TIGR04382 224 VVKRGPEGSLVYTGDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRH 293
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 68-294 3.28e-18

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: 82.97  E-value: 3.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  68 GAWLKEALGDRS-RDWPVEAAGTT-LSVGITHPDGERTFFTTRGhlPLLS---FQEVRTMLDGNRLRGGYALLSGSFLTD 142
Cdd:cd01164    64 GDFFEALLKEEGiPDDFVEVAGETrINVKIKEEDGTETEINEPG--PEISeeeLEALLEKLKALLKKGDIVVLSGSLPPG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 143 ALSLAYDALFDWADAHEIAVALDT-GWPLegwTEAnrLKTLAWL-KRCH---CALFNevetTTLTGQSDPAEAARSLKsE 217
Cdd:cd01164   142 VPADFYAELVRLAREKGARVILDTsGEAL---LAA--LAAKPFLiKPNReelEELFG----RPLGDEEDVIAAARKLI-E 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1715415498 218 MPADaIVVVKRGPNGALAIDRNGAAFSFPaPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAISTL 294
Cdd:cd01164   212 RGAE-NVLVSLGADGALLVTKDGVYRASP-PKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSP 286
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 4-293 5.19e-18

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: 82.08  E-value: 5.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLILGPAEPwPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEAL---GDRSR 80
Cdd:cd01947     2 IAVVGHVEWDIFLSLDAP-PQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELesgGDKHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  81 D-WPVEAAGTTLSVgiTHPDGERTFFTTRGHLpllsfqevRTMLDGNRLRGGYALLSGSFLTDALSLAYDAlfdwadaHE 159
Cdd:cd01947    81 VaWRDKPTRKTLSF--IDPNGERTITVPGERL--------EDDLKWPILDEGDGVFITAAAVDKEAIRKCR-------ET 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 160 IAVALDTGWPLegwteanRLKTLAWLKRcHCALFnevetttLTGQSDPAEAARSLKSEMPADAIVVVKRGPNGALAIDrN 239
Cdd:cd01947   144 KLVILQVTPRV-------RVDELNQALI-PLDIL-------IGSRLDPGELVVAEKIAGPFPRYLIVTEGELGAILYP-G 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715415498 240 GAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:cd01947   208 GRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 4-292 2.46e-17

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: 80.74  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDlILGPAEPWP------KPGTEIIVDHDELRV-----------GGCAGNNALAWESLGVDYVIAANVGNDQ 66
Cdd:cd01168     4 VLGLGNALVD-ILAQVDDAFleklglKKGDMILADMEEQEEllaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGDDK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  67 FGAWLKEAL---GDRSRDWPVEAAGTTLSVGITHPDGERTFFTTRGHLPLLSFQEvrtmLDGNRLRG-GYALLSGSFLTD 142
Cdd:cd01168    83 LGDFLLKDLraaGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDD----LDWSLLAKaKYLYLEGYLLTV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 143 ALSLAYDALfdwADAHEIA--VALDtgwpLEGWTEANRLKTLAWLKRCHCALF--NEVETTTLTGQS--DPAEAARSLKS 216
Cdd:cd01168   159 PPEAILLAA---EHAKENGvkIALN----LSAPFIVQRFKEALLELLPYVDILfgNEEEAEALAEAEttDDLEAALKLLA 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1715415498 217 EMPAdaIVVVKRGPNGALAIDrNGAAFSFPA-PSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIS 292
Cdd:cd01168   232 LRCR--IVVITQGAKGAVVVE-GGEVYPVPAiPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQ 305
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 39-293 1.50e-15

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 74.77  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  39 GGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDRSRDwpveaagttlsvgITHpdgertffttrghlplLSFQE 118
Cdd:PRK09813   23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVD-------------ISH----------------VHTKH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 119 VRT------MLDGNRLRGGY--ALLSGSFLTDAlSLAYDALFD------WADAHEIAVALDTGWPLEGWTEANRLKTLAW 184
Cdd:PRK09813   74 GVTaqtqveLHDNDRVFGDYteGVMADFALSEE-DYAWLAQYDivhaaiWGHAEDAFPQLHAAGKLTAFDFSDKWDSPLW 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 185 LkrchcALFNEVETTTLTGQSDPAEAARSLKSEMPADA-IVVVKRGPNGALAIDrnGAAF-SFPAPSVQVVDTIGAGDVF 262
Cdd:PRK09813  153 Q-----TLVPHLDYAFASAPQEDEFLRLKMKAIVARGAgVVIVTLGENGSIAWD--GAQFwRQAPEPVTVVDTMGAGDSF 225

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1715415498 263 NAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:PRK09813  226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQY 256
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 7-280 1.62e-15

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: 75.02  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   7 IGNVNVDLILgPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEAL---GDRSRDWP 83
Cdd:cd01945     5 VGLAVLDLIY-LVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELaaeGVDTSFIV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  84 VEAAGTTLSVGIT--HPDGERTFFTTRGH------LPLLSFQEVRTMLDGNRLRGGyallsgsfltdALSLAydalfdwA 155
Cdd:cd01945    84 VAPGARSPISSITdiTGDRATISITAIDTqaapdsLPDAILGGADAVLVDGRQPEA-----------ALHLA-------Q 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 156 DAHEIAVALDTGWPLEGWTEANRLktlawLKRCHCALFNEVETTTLTGQSDPaEAARSLKSemPADAIVVVKRGPNGALA 235
Cdd:cd01945   146 EARARGIPIPLDLDGGGLRVLEEL-----LPLADHAICSENFLRPNTGSADD-EALELLAS--LGIPFVAVTLGEAGCLW 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1715415498 236 IDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCL 280
Cdd:cd01945   218 LERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREAL 262
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 140-271 1.86e-15

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: 73.28  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 140 LTDALSLAYDALFDWADA---HEIAVALDTGWPLEGWTEANRLKTLAwlkRCHCALFNEVETTTLTGQSDP-----AEAA 211
Cdd:cd00287    62 VISGLSPAPEAVLDALEEarrRGVPVVLDPGPRAVRLDGEELEKLLP---GVDILTPNEEEAEALTGRRDLevkeaAEAA 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 212 RSLKSEMPAdaIVVVKRGPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALA 271
Cdd:cd00287   139 ALLLSKGPK--VVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 83-293 7.63e-15

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 73.38  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  83 PVEAAGTT-LSVGITHPDGERTFFTTRGhlPLLSFQEVRTMLdgNRLR-----GGYALLSGSFltdALSLAYDALFDWAD 156
Cdd:TIGR03168  79 FVEVKGETrINVKIKESSGEETELNEPG--PEISEEELEQLL--EKLRellasGDIVVISGSL---PPGVPPDFYAQLIA 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 157 -AHE--IAVALDT-GWPLegwTEAnrLKTLAWL-KRCH---CALFNevetTTLTGQSDPAEAARSLKsEMPADAiVVVKR 228
Cdd:TIGR03168 152 iARKkgAKVILDTsGEAL---REA--LAAKPFLiKPNHeelEELFG----RELKTLEEIIEAARELL-DRGAEN-VLVSL 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1715415498 229 GPNGALAIDRNGAAFSfPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:TIGR03168 221 GADGALLVTKEGALKA-TPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFS 284
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 8-292 1.73e-14

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: 72.25  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   8 GNVNVDLILgPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALgdRSRDWPVEAA 87
Cdd:TIGR02152   1 GSINMDLVL-RTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENL--KSNGIDTEYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  88 GTT--LSVGITH----PDGERTFFTTRGHLPLLSFQEVRTMldgnrlrggYALLSGSfltDALSL-------AYDALFDW 154
Cdd:TIGR02152  78 GTVkdTPTGTAFitvdDTGENRIVVVAGANAELTPEDIDAA---------EALIAES---DIVLLqleipleTVLEAAKI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 155 ADAHEIAVALDTGwPlegwteANRLKTLAWLKRCHCALFNEVETTTLTGQS-----DPAEAARSLKSEMPAdaIVVVKRG 229
Cdd:TIGR02152 146 AKKHGVKVILNPA-P------AIKDLDDELLSLVDIITPNETEAEILTGIEvtdeeDAEKAAEKLLEKGVK--NVIITLG 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715415498 230 PNGALAIDRNGAAFsFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIAsrAIS 292
Cdd:TIGR02152 217 SKGALLVSKDESKL-IPAFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAA--AIS 276
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 4-280 6.28e-13

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 68.70  E-value: 6.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   4 LAAIGNVNVDLILGPAE--PWPKPGTEIIV--------DHDELRVGG-CagNNALAWESLGVDYVIAANVGNDQFGAWLK 72
Cdd:PLN02341   75 VATLGNLCVDIVLPVPElpPPSREERKAYMeelaasppDKKSWEAGGnC--NFAIAAARLGLRCSTIGHVGDEIYGKFLL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  73 EAL------------GDRSRDWPVEAAGTTLSVGITHPDGeRTFFTTR---GHLPLLSF-----QEVRTMLDGNRlrggy 132
Cdd:PLN02341  153 DVLaeegisvvglieGTDAGDSSSASYETLLCWVLVDPLQ-RHGFCSRadfGPEPAFSWisklsAEAKMAIRQSK----- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 133 ALLSGSFLTDALSL-AYDALFDWADAHEIAVALDTGwP-----LEGwTEANRLKTLAWLKRCHCALFNEVETTTLTGQSD 206
Cdd:PLN02341  227 ALFCNGYVFDELSPsAIASAVDYAIDVGTAVFFDPG-PrgkslLVG-TPDERRALEHLLRMSDVLLLTSEEAEALTGIRN 304

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715415498 207 PAEAARSLKSEMPADAIVVVKRGPNGALAIDRNGAAFSfPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCL 280
Cdd:PLN02341  305 PILAGQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCA-PAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTL 377
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
 83-293 1.01e-12

1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).


Pssm-ID: 274804 [Multi-domain]  Cd Length: 304  Bit Score: 67.23  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  83 PVEAAGTT-LSVGITHPDGERTFFTTRGhlPLLS---FQEVRTMLDGNRLRGGYALLSGSFltdALSLAYDALFDWAD-A 157
Cdd:TIGR03828  79 FVRVPGETrINVKIKEPSGTETKLNGPG--PEISeeeLEALLEKLRAQLAEGDWLVLSGSL---PPGVPPDFYAELIAlA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 158 HE--IAVALDTgwplEGWTEANRLKTLAWL-KRCH---CALFNevetTTLTGQSDPAEAARSLKsEMPADAiVVVKRGPN 231
Cdd:TIGR03828 154 REkgAKVILDT----SGEALRDGLKAKPFLiKPNDeelEELFG----RELKTLEEIIEAARELL-DLGAEN-VLISLGAD 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715415498 232 GALAIDRNGAAFSFPaPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAIST 293
Cdd:TIGR03828 224 GALLVTKEGALFAQP-PKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFS 284
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 193-272 3.05e-12

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 66.11  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 193 FNEVETTTLTGQSDPAEAARSLKSEMPaDAIVVVKRGPNGALAIDRnGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAA 272
Cdd:PRK09434  186 LSEEELCFLSGTSQLEDAIYALADRYP-IALLLVTLGAEGVLVHTR-GQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQ 263
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 31-279 1.70e-10

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: 60.65  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  31 VDHDELRVGGcAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGDRSRDWPveaagttlsvGITHPdGERTFFTTR-- 108
Cdd:cd01172    32 VEREEIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTD----------GIVDE-GRPTTTKTRvi 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 109 ---GHLPLLSFQEvRTMLDGNRLRGGYALLSGS---------------FLTDALSlayDALFDWADAHEIAVALDtgwpl 170
Cdd:cd01172   100 arnQQLLRVDRED-DSPLSAEEEQRLIERIAERlpeadvvilsdygkgVLTPRVI---EALIAAARELGIPVLVD----- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 171 egwteanrLKTLAWLKRCHCALF--NEVETTTLTGQSDP-----AEAARSLKSEMPADAiVVVKRGPNGALAIDRNGAAF 243
Cdd:cd01172   171 --------PKGRDYSKYRGATLLtpNEKEAREALGDEINdddelEAAGEKLLELLNLEA-LLVTLGEEGMTLFERDGEVQ 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1715415498 244 SFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDC 279
Cdd:cd01172   242 HIPALAKEVYDVTGAGDTVIATLALALAAGADLEEA 277
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 162-268 1.96e-10

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: 60.11  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 162 VALDtgwpLEGWT---EANRLKTLAWLKRCHCALFNEVETTTLtgqSDPAEAARSLKSEMPAdaIVVVKRGPNGALAIDR 238
Cdd:cd01937   131 ISLD----AQGFLrraNQEKLIKCVILKLHDVLKLSRVEAEVI---STPTELARLIKETGVK--EIIVTDGEEGGYIFDG 201

                          90       100       110
                  ....*....|....*....|....*....|
gi 1715415498 239 NGAaFSFPAPSVQVVDTIGAGDVFNAGFLA 268
Cdd:cd01937   202 NGK-YTIPASKKDVVDPTGAGDVFLAAFLY 230
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 162-272 3.91e-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: 59.40  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 162 VALDTgwpLEGWTEANRLKTLAWLKRCHCALFNEVETTTLTGQSDPAEAARSLKSEMPAdaIVVVKRGPNGALAIDRNG- 240
Cdd:cd01946   141 VVMDT---MNFWISIKPEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPK--ALIIKRGEYGALLFTDDGy 215

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1715415498 241 -AAFSFPAPSVqvVDTIGAGDVFNAGFLAALAA 272
Cdd:cd01946   216 fAAPAYPLESV--FDPTGAGDTFAGGFIGYLAS 246
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 26-303 6.05e-10

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 59.82  E-value: 6.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  26 GTEIIVDHDE--------------LRVGGCAGNNALAWESLG--------VDYVIAANVGNDQFGAWLKEAL---GDRSR 80
Cdd:PLN02813   99 GTRKVINHEErgkvlraldgcsykASAGGSLSNTLVALARLGsqsaagpaLNVAMAGSVGSDPLGDFYRTKLrraNVHFL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  81 DWPVeAAGTTLSVGI-THPDGERTFFTTRGHLPLLSFQEV-RTMLDGNRLR--GGYaLLSGSFLTDALSLAYDAlfdwAD 156
Cdd:PLN02813  179 SQPV-KDGTTGTVIVlTTPDAQRTMLSYQGTSSTVNYDSClASAISKSRVLvvEGY-LWELPQTIEAIAQACEE----AH 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 157 AHEIAVALDTGWPlegwTEANRLKTLAWLKRCHCA--LF-NEVETTTLTG---QSDPAEAARSLKSEMPadaIVVVKRGP 230
Cdd:PLN02813  253 RAGALVAVTASDV----SCIERHRDDFWDVMGNYAdiLFaNSDEARALCGlgsEESPESATRYLSHFCP---LVSVTDGA 325

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715415498 231 NGALaIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPliDcLKTGVTIASRAISTLPRRYGEPLS 303
Cdd:PLN02813  326 RGSY-IGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYGLLRGVS--D-LRGMGELAARVAATVVGQQGTRLR 394
PTZ00292 PTZ00292
ribokinase; Provisional
 1-288 9.26e-10

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 58.60  E-value: 9.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   1 MRPLAAIGNVNVDLIlGPAEPWPKPGTEIIVDHDELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGAWLKEALGD--- 77
Cdd:PTZ00292   15 EPDVVVVGSSNTDLI-GYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRngv 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  78 ------RSRDWPVEAAgtTLSVGITHPDGERTFFTTRGHLplLSFQEVRTMLDGNRLRGGYALLSGSFltdALSLAYDAL 151
Cdd:PTZ00292   94 ntsfvsRTENSSTGLA--MIFVDTKTGNNEIVIIPGANNA--LTPQMVDAQTDNIQNICKYLICQNEI---PLETTLDAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 152 fdwADAHEIAVAldTGWPLegwTEANRLKTLAWLKRC--HCALF--NEVETTTLTGQ--SDPAEAARSLK-SEMPADAIV 224
Cdd:PTZ00292  167 ---KEAKERGCY--TVFNP---APAPKLAEVEIIKPFlkYVSLFcvNEVEAALITGMevTDTESAFKASKeLQQLGVENV 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715415498 225 VVKRGPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIAS 288
Cdd:PTZ00292  239 IITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAA 302
PTZ00247 PTZ00247
adenosine kinase; Provisional
 19-291 2.44e-09

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 57.73  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  19 AEPWPKPGTEIIVDHDELRV--GGCAGNNA--LAW----ESLGVDYVIAanVGNDQFGAWLKEALGDRSRDWPVE---AA 87
Cdd:PTZ00247   40 AEEKQLPIFEELESIPNVSYvpGGSALNTArvAQWmlqaPKGFVCYVGC--VGDDRFAEILKEAAEKDGVEMLFEyttKA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  88 GT-TLSVGITHPdgERTFFTTRGHLPLLSFQEVRT-----MLDGNRLrggyALLSGSFLT-DALSLAYdaLFDWADAHEI 160
Cdd:PTZ00247  118 PTgTCAVLVCGK--ERSLVANLGAANHLSAEHMQShavqeAIKTAQL----YYLEGFFLTvSPNNVLQ--VAKHARESGK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 161 AVALDTGWP--LEGWTEanrlKTLAWLKRCHCALFNEVETTTLT-----GQSDPAEAARSLKSEMPA----DAIVVVKRG 229
Cdd:PTZ00247  190 LFCLNLSAPfiSQFFFE----RLLQVLPYVDILFGNEEEAKTFAkamkwDTEDLKEIAARIAMLPKYsgtrPRLVVFTQG 265

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1715415498 230 PNGALaIDRNGAAFSFPAPSV---QVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGVTIASRAI 291
Cdd:PTZ00247  266 PEPTL-IATKDGVTSVPVPPLdqeKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVII 329
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 223-293 1.25e-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: 55.05  E-value: 1.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715415498 223 IVVVKRGPNGALAIDrnGAAFSFPAP-SVQVVDTIGAGDVFNAGFLAA-LAADMPLIDCLKTGVTIASRAIST 293
Cdd:cd01940   190 LVIVTRGEDGAIAYD--GAVFYSVAPrPVEVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQGAQFAAKTCGH 260
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 203-292 1.33e-08

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: 55.11  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 203 GQSDPAEAARSLKSEMPADAIVVVKRGPNGALAIDRNGAAFSFPA-PSVQVVDTIGAGDVFNAGFLAALA-ADMPLIDCL 280
Cdd:cd01939   194 GYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAhKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEAL 273

                          90
                  ....*....|..
gi 1715415498 281 KTGVTIASRAIS 292
Cdd:cd01939   274 DFGNRVASQKCT 285
PRK11142 PRK11142
ribokinase; Provisional
 194-278 6.80e-08

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 52.95  E-value: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 194 NEVETTTLTG-----QSDPAEAARSLKSEMPAdaIVVVKRGPNGALaIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLA 268
Cdd:PRK11142  185 NETEAEKLTGirvedDDDAAKAAQVLHQKGIE--TVLITLGSRGVW-LSENGEGQRVPGFRVQAVDTIAAGDTFNGALVT 261

                          90
                  ....*....|
gi 1715415498 269 ALAADMPLID 278
Cdd:PRK11142  262 ALLEGKPLPE 271
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 194-290 4.51e-07

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 50.55  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 194 NEVETTTLTGQS-----DPAEAARSLKSEMPADAiVVVKRGPNGALAIDRNGAAFSFPaPSVQVVDTIGAGDVFNAGFLA 268
Cdd:PRK10294  187 NQKELSALVNRDltqpdDVRKAAQELVNSGKAKR-VVVSLGPQGALGVDSENCIQVVP-PPVKSQSTVGAGDSMVGAMTL 264

                          90       100
                  ....*....|....*....|..
gi 1715415498 269 ALAADMPLIDCLKTGVTIASRA 290
Cdd:PRK10294  265 KLAENASLEEMVRFGVAAGSAA 286
PLN02323 PLN02323
probable fructokinase
 195-278 2.01e-05

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 45.38  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 195 EVETTTLTGQSDPAEAArSLKSEMPADAIVVVKRGPNGA--LAIDRNGAAFSFpapSVQVVDTIGAGDVFNAGFLAALAA 272
Cdd:PLN02323  205 DEEVEFLTGGDDPDDDT-VVKLWHPNLKLLLVTEGEEGCryYTKDFKGRVEGF---KVKAVDTTGAGDAFVGGLLSQLAK 280


                  ....*.
gi 1715415498 273 DMPLID 278
Cdd:PLN02323  281 DLSLLE 286
PRK09954 PRK09954
sugar kinase;
7-267 8.13e-05

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 43.77  E-value: 8.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498   7 IGNVNVDlILGPAE-PWPK----PGTEiivdhdELRVGGCAGNNALAWESLGVDYVIAANVGNDQFGawlkEALGDRSRD 81
Cdd:PRK09954   63 VGAINMD-IRGMADiRYPQaashPGTI------HCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYG----ETLLEETRR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498  82 WPVEAAG--------TTLSVGITHPDGERTFFTTRGH-LPLLSFQevrtMLDGNR--LRGGYALLSGSFLTDAlslAYDA 150
Cdd:PRK09954  132 AGVNVSGcirlhgqsTSTYLAIANRQDETVLAINDTHiLQQLTPQ----LLNGSRdlIRHAGVVLADCNLTAE---ALEW 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 151 LFDWADahEIAVALDTGWPLEgwteANRLKTlaWLKRCHCALFNEVETTTLTGQ-----SDPAEAARSLKSEMPADAIVV 225
Cdd:PRK09954  205 VFTLAD--EIPVFVDTVSEFK----AGKIKH--WLAHIHTLKPTQPELEILWGQaitsdADRNAAVNALHQQGVQQIFVY 276

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1715415498 226 VKrgPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFL 267
Cdd:PRK09954  277 LP--DESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLV 316
fruK PRK09513
1-phosphofructokinase; Provisional
 201-292 3.45e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 41.60  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 201 LTGQSDPAEAARSLKSEMPADaiVVVKRGPNGALAIDRNGAAFSFPaPSVQVVDTIGAGDVFNAGFLAALAADMPLIDCL 280
Cdd:PRK09513  199 LPELKDVIEAAHALREQGIAH--VVISLGAEGALWVNASGEWIAKP-PACDVVSTVGAGDSMVGGLIYGLLMRESSEHTL 275

                          90
                  ....*....|..
gi 1715415498 281 KTGVTIASRAIS 292
Cdd:PRK09513  276 RLATAVSALAVS 287
PLN02548 PLN02548
adenosine kinase
 223-291 3.89e-04

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 41.62  E-value: 3.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715415498 223 IVVVKRGPNGALaIDRNGAAFSFPA---PSVQVVDTIGAGDVFNAGFLAALAADMPLIDCLKTGvTIASRAI 291
Cdd:PLN02548  248 TVVITQGADPTV-VAEDGKVKEFPViplPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAG-NYAANVI 317
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 189-271 2.06e-03

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: 39.25  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 189 HCALF--NEVETTTLTGQSDPAEAARSLKSE-----------MPADAIVVVKRGPNGAL-AIDRNGAAFSFPA---PSVQ 251
Cdd:cd01943   180 RVDVFspNLEEAARLLGLPTSEPSSDEEKEAvlqallfsgilQDPGGGVVLRCGKLGCYvGSADSGPELWLPAyhtKSTK 259

                          90       100
                  ....*....|....*....|
gi 1715415498 252 VVDTIGAGDVFNAGFLAALA 271
Cdd:cd01943   260 VVDPTGGGNSFLGGFAAGLA 279
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 194-283 4.94e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 38.23  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715415498 194 NEVETTTLTG---QSDPaEAARSLKSEMPADAIVVVkrGPNGALAIDRNGAAFSFPAPSVQVVDTIGAGDVFNAGFLAAL 270
Cdd:PLN02379  239 NEDEARELLRgeqESDP-EAALEFLAKYCNWAVVTL--GSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGL 315

                          90
                  ....*....|...
gi 1715415498 271 AADMPLIDCLKTG 283
Cdd:PLN02379  316 IKGLSLEECCKVG 328
 
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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