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Conserved domains on  [gi|1785367607|ref|XP_031757777|]
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ketohexokinase isoform X1 [Xenopus tropicalis]

Protein Classification

ketohexokinase( domain architecture ID 10112592)

ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose; it can also phosphorylate several other furanose sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 6-340 1.00e-143

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: 407.95  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:cd01939     2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VmsrpgcsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvsWQSRGDMPCACCLVNVSSGSRTVTLYDTNLPDV 165
Cdd:cd01939    82 C----------------------------------------------YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEV 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEDFRSVDLTRYKWIHWEGRNAAEQVKMIRRVEEHNSGRGaEERITVSVEIEKEREELYQLFPHGDVVFVSKDVARHFG 245
Cdd:cd01939   116 TYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRG 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FHSAQEAVRGLYPRVRKGAYLVCAWAEEGADALGPDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALS-HGRGMQEALT 324
Cdd:cd01939   195 YKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALD 274

                         330
                  ....*....|....*.
gi 1785367607 325 YGCQMAGKKCGVQGFD 340
Cdd:cd01939   275 FGNRVASQKCTGVGFD 290
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 6-340 1.00e-143

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: 407.95  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:cd01939     2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VmsrpgcsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvsWQSRGDMPCACCLVNVSSGSRTVTLYDTNLPDV 165
Cdd:cd01939    82 C----------------------------------------------YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEV 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEDFRSVDLTRYKWIHWEGRNAAEQVKMIRRVEEHNSGRGaEERITVSVEIEKEREELYQLFPHGDVVFVSKDVARHFG 245
Cdd:cd01939   116 TYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRG 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FHSAQEAVRGLYPRVRKGAYLVCAWAEEGADALGPDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALS-HGRGMQEALT 324
Cdd:cd01939   195 YKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALD 274

                         330
                  ....*....|....*.
gi 1785367607 325 YGCQMAGKKCGVQGFD 340
Cdd:cd01939   275 FGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 6-338 3.86e-37

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: 135.01  E-value: 3.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:COG0524     2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvswqsrgdmPCACCLVNVS-SGSRTVTLYDTNLPD 164
Cdd:COG0524    82 VRRDPGA-----------------------------------------------PTGLAFILVDpDGERTIVFYRGANAE 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 165 VTEEDFRSVDLTRYKWIHWEGRNAAE------QVKMIRRVEEHNsgrgaeerITVSV-------EIEKEREELYQLFPHG 231
Cdd:COG0524   115 LTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAG--------VPVSLdpnyrpaLWEPARELLRELLALV 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 232 DVVFVSKDVARH-FGFHSAQEAVRGLypRVRKGAYLVCAWAEEGADALGPDGsVVHSCAFPPDcIVDTLGAGDTFNASVI 310
Cdd:COG0524   187 DILFPNEEEAELlTGETDPEEAAAAL--LARGVKLVVVTLGAEGALLYTGGE-VVHVPAFPVE-VVDTTGAGDAFAAGFL 262

                         330       340
                  ....*....|....*....|....*...
gi 1785367607 311 YALSHGRGMQEALTYGCQMAGKKCGVQG 338
Cdd:COG0524   263 AGLLEGLDLEEALRFANAAAALVVTRPG 290
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-338 2.22e-17

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 81.24  E-value: 2.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRwqRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCSfPASVVISNISNGSRTIVhmnsfivsdfrrrgIGTPNVSWQSRGDMPCACCLVNVSSGSRTVTLYDTNLPDV 165
Cdd:pfam00294  80 VVIDEDTR-TGTALIEVDGDGERTIV--------------FNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEdfrsvdltrykwihwEGRNAAEQvkmirrveehnsgRGAEERITVSVEIEKeREELYQLFPHGDVVFVSKDVARHFG 245
Cdd:pfam00294 145 TLE---------------ELIEAAKN-------------GGTFDPNLLDPLGAA-REALLELLPLADLLKPNEEELEALT 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FH---SAQEAVRGLYPRVRKGA-YLVCAWAEEGADALGPDGSVVHScAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQE 321
Cdd:pfam00294 196 GAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGDGEVHVP-AVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEE 274

                         330
                  ....*....|....*..
gi 1785367607 322 ALTYGCQMAGKKCGVQG 338
Cdd:pfam00294 275 ALRFANAAAALVVQKSG 291
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 8-338 4.69e-08

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 53.20  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   8 CIGLVCLDIisvvdkYPEEDsdsrclsqRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSHVM 87
Cdd:PRK09813    5 TIGDNCVDI------YPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  88 SRPGcsfPASVVISNISNGSRTIVHMNSFIVSDFRrrgigtpnvswqsrgdmpcacclvnvssgsrtvtlydtnlpdVTE 167
Cdd:PRK09813   71 TKHG---VTAQTQVELHDNDRVFGDYTEGVMADFA------------------------------------------LSE 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 168 EDFRSvdLTRYKWIH---WEgrNAAEQVKMIrrveeHNSGrgaeerITVSVEI-EKEREELYQ-LFPHGDVVFVSKdvar 242
Cdd:PRK09813  106 EDYAW--LAQYDIVHaaiWG--HAEDAFPQL-----HAAG------KLTAFDFsDKWDSPLWQtLVPHLDYAFASA---- 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 243 hfgfHSAQEAVRG-LYPRVRKGAYLVCA-WAEEGAdaLGPDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQ 320
Cdd:PRK09813  167 ----PQEDEFLRLkMKAIVARGAGVVIVtLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLP 240

                         330
                  ....*....|....*...
gi 1785367607 321 EALTYGCQMAGKKCGVQG 338
Cdd:PRK09813  241 QAMAQGTACAAKTIQYHG 258
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 278-326 3.04e-04

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: 41.82  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785367607 278 LGPDGSVVHSCA----FPPDCI--VDTLGAGDTFNASVIYALSHGRGMQEALTYG 326
Cdd:TIGR02152 215 LGSKGALLVSKDesklIPAFKVkaVDTTAAGDTFNGAFAVALAEGKSLEDAIRFA 269
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 6-340 1.00e-143

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: 407.95  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:cd01939     2 VLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VmsrpgcsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvsWQSRGDMPCACCLVNVSSGSRTVTLYDTNLPDV 165
Cdd:cd01939    82 C----------------------------------------------YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEV 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEDFRSVDLTRYKWIHWEGRNAAEQVKMIRRVEEHNSGRGaEERITVSVEIEKEREELYQLFPHGDVVFVSKDVARHFG 245
Cdd:cd01939   116 TYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRG 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FHSAQEAVRGLYPRVRKGAYLVCAWAEEGADALGPDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALS-HGRGMQEALT 324
Cdd:cd01939   195 YKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALD 274

                         330
                  ....*....|....*.
gi 1785367607 325 YGCQMAGKKCGVQGFD 340
Cdd:cd01939   275 FGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 6-338 3.86e-37

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: 135.01  E-value: 3.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:COG0524     2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvswqsrgdmPCACCLVNVS-SGSRTVTLYDTNLPD 164
Cdd:COG0524    82 VRRDPGA-----------------------------------------------PTGLAFILVDpDGERTIVFYRGANAE 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 165 VTEEDFRSVDLTRYKWIHWEGRNAAE------QVKMIRRVEEHNsgrgaeerITVSV-------EIEKEREELYQLFPHG 231
Cdd:COG0524   115 LTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAG--------VPVSLdpnyrpaLWEPARELLRELLALV 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 232 DVVFVSKDVARH-FGFHSAQEAVRGLypRVRKGAYLVCAWAEEGADALGPDGsVVHSCAFPPDcIVDTLGAGDTFNASVI 310
Cdd:COG0524   187 DILFPNEEEAELlTGETDPEEAAAAL--LARGVKLVVVTLGAEGALLYTGGE-VVHVPAFPVE-VVDTTGAGDAFAAGFL 262

                         330       340
                  ....*....|....*....|....*...
gi 1785367607 311 YALSHGRGMQEALTYGCQMAGKKCGVQG 338
Cdd:COG0524   263 AGLLEGLDLEEALRFANAAAALVVTRPG 290
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 6-338 1.49e-24

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: 101.11  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIisvvdkYPEEDSDSRClSQRWQR--GGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDV 83
Cdd:cd01166     2 VVTIGEVMVDL------SPPGGGRLEQ-ADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  84 SHVMSRPGcSFPASVVISNISNGSRTIVhmnsfivsdFRRRGigtpnvswqsrgdmpcacclvnvSSGSRtvtlydtnlp 163
Cdd:cd01166    75 SHVRVDPG-RPTGLYFLEIGAGGERRVL---------YYRAG-----------------------SAASR---------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 164 dVTEEDFRSVDLTRYKWIHWEG-------------RNAAEQVKmirrveehnsgrgaEERITVSVEI---------EKER 221
Cdd:cd01166   112 -LTPEDLDEAALAGADHLHLSGitlalsesarealLEALEAAK--------------ARGVTVSFDLnyrpklwsaEEAR 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 222 EELYQLFPHGDVVFVSKDVAR-HFGFHSAQEAVRGLYPRVRKGAYLVCAWAEEGADALGPDGSVvHSCAFPPDcIVDTLG 300
Cdd:cd01166   177 EALEELLPYVDIVLPSEEEAEaLLGDEDPTDAAERALALALGVKAVVVKLGAEGALVYTGGGRV-FVPAYPVE-VVDTTG 254

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1785367607 301 AGDTFNASVIYALSHGRGMQEALTYGCQMAGKKCGVQG 338
Cdd:cd01166   255 AGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 6-341 1.08e-20

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: 90.43  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:cd01945     2 VLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCSFPASVVIsnisngsrtivhmnsfivsdfrrrgigtpnvswqsrgdmpcacclvnVSSGSRTVTLYDTNLPDV 165
Cdd:cd01945    82 IVVAPGARSPISSIT-----------------------------------------------DITGDRATISITAIDTQA 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEDFRSVDLTRYKWIHWEGRN---AAEQVKMIRRveehnsgRGAEERITVSVEIEKEREELYqlfPHGDVVFVSKDVAR 242
Cdd:cd01945   115 APDSLPDAILGGADAVLVDGRQpeaALHLAQEARA-------RGIPIPLDLDGGGLRVLEELL---PLADHAICSENFLR 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 243 HFGFHSAQEAVRGLypRVRKGAYLVCAWAEEGADALGPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYALSHGRGMQEA 322
Cdd:cd01945   185 PNTGSADDEALELL--ASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVE-VVDTTGAGDVFHGAFAHALAEGMPLREA 261

                         330
                  ....*....|....*....
gi 1785367607 323 LTYGCQMAGKKCgvQGFDG 341
Cdd:cd01945   262 LRFASAAAALKC--RGLGG 278
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-338 2.22e-17

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 81.24  E-value: 2.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRwqRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCSfPASVVISNISNGSRTIVhmnsfivsdfrrrgIGTPNVSWQSRGDMPCACCLVNVSSGSRTVTLYDTNLPDV 165
Cdd:pfam00294  80 VVIDEDTR-TGTALIEVDGDGERTIV--------------FNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEdfrsvdltrykwihwEGRNAAEQvkmirrveehnsgRGAEERITVSVEIEKeREELYQLFPHGDVVFVSKDVARHFG 245
Cdd:pfam00294 145 TLE---------------ELIEAAKN-------------GGTFDPNLLDPLGAA-REALLELLPLADLLKPNEEELEALT 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FH---SAQEAVRGLYPRVRKGA-YLVCAWAEEGADALGPDGSVVHScAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQE 321
Cdd:pfam00294 196 GAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGDGEVHVP-AVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEE 274

                         330
                  ....*....|....*..
gi 1785367607 322 ALTYGCQMAGKKCGVQG 338
Cdd:pfam00294 275 ALRFANAAAALVVQKSG 291
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 3-338 2.44e-15

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: 75.34  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   3 EKGILCIGLVCLDIISVVDKYPEE----DSDSRCLSQRWQR-------------GGNASNSCTILALLGAPCAFMGSLAP 65
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEklglKKGDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  66 GHMADFTLNSLRRYGIDVShvmsrpgcsfpasvvisnisngsrtivhmnsfivsdfrrrgigtpnvsWQSRGDMPCACCL 145
Cdd:cd01168    81 DKLGDFLLKDLRAAGVDTR------------------------------------------------YQVQPDGPTGTCA 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 146 VNVSSG-SRTvtlYDTNL---PDVTEEDFRSVDLTRYKWIHWEGRNAAEQVKMIRRVEEHNSGRGAeeRITVSV----EI 217
Cdd:cd01168   113 VLVTPDaERT---MCTYLgaaNELSPDDLDWSLLAKAKYLYLEGYLLTVPPEAILLAAEHAKENGV--KIALNLsapfIV 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 218 EKEREELYQLFPHGDVVFVSKDVARHFG---FHSAQEAVRGL---YPRV------RKGAYLVcawaeegadalgPDGSVV 285
Cdd:cd01168   188 QRFKEALLELLPYVDILFGNEEEAEALAeaeTTDDLEAALKLlalRCRIvvitqgAKGAVVV------------EGGEVY 255

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1785367607 286 HSCAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQEALTYGCQMAGKKCGVQG 338
Cdd:cd01168   256 PVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 6-333 3.70e-15

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: 74.65  E-value: 3.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLApghmADF----TLNSLRRYGI 81
Cdd:cd01942     2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVG----EDFhgrlYLEELREEGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  82 DVSHVMSRPGCSFPASVVIsnisngsrtivhmnsfiVSDFRRRgigtpnVSWQSRGDMPCACclvnvssgsrtvtlydtn 161
Cdd:cd01942    78 DTSHVRVVDEDSTGVAFIL-----------------TDGDDNQ------IAYFYPGAMDELE------------------ 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 162 lPDVTEEDFRSVDLtrykwIHWEGRNAaeqvkMIRRVEEHnsgrgAEERITVSV----EIEK-EREELYQLFPHGDVVFV 236
Cdd:cd01942   117 -PNDEADPDGLADI-----VHLSSGPG-----LIELAREL-----AAGGITVSFdpgqELPRlSGEELEEILERADILFV 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 237 SKDVARHF----GFHSAQEAVRGLYPRVRKGAylvcawaeEGADALGPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYA 312
Cdd:cd01942   181 NDYEAELLkertGLSEAELASGVRVVVVTLGP--------KGAIVFEDGEEVEVPAVPAVK-VVDTTGAGDAFRAGFLYG 251

                         330       340
                  ....*....|....*....|.
gi 1785367607 313 LSHGRGMQEALTYGCQMAGKK 333
Cdd:cd01942   252 LLRGYDLEESLRLGNLAASLK 272
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 19-338 2.42e-14

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: 72.00  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  19 VVDKYPEEDsdsrclsqRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSHVMSRPGcsfPASV 98
Cdd:cd01940     9 VVDKYLHLG--------KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEG---ENAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  99 VISNISNGSRTIVHMNSFIVSDFRRrgigtpnvswqsrgdmpcacclvnvssgsrtvtlydtnlpdvTEEDFRSvdLTRY 178
Cdd:cd01940    78 ADVELVDGDRIFGLSNKGGVAREHP------------------------------------------FEADLEY--LSQF 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 179 KWIH---WEGRNAAEQVKmirrveehNSGRGAEERITVSVEIEKEREELYQLFPHGDVVFVSKDvarhfgfHSAQEAVRG 255
Cdd:cd01940   114 DLVHtgiYSHEGHLEKAL--------QALVGAGALISFDFSDRWDDDYLQLVCPYVDFAFFSAS-------DLSDEEVKA 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 256 LYPR-VRKGAYLVCA-WAEEGADALgpDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALSHGRG-MQEALTYGCQMAGK 332
Cdd:cd01940   179 KLKEaVSRGAKLVIVtRGEDGAIAY--DGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTaIAEAMRQGAQFAAK 256


                  ....*.
gi 1785367607 333 KCGVQG 338
Cdd:cd01940   257 TCGHEG 262
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 6-338 2.43e-10

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: 60.73  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEdsdsrclsqrWQR--GGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDV 83
Cdd:cd01167     2 VVCFGEALIDFIPEGSGAPET----------FTKapGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  84 SHVMSRPGcSFPASVVISNISNGSRTIVHMNSFIVSDFRRRGIgtpNVSWQSRGDMPCACCLVNVSSGSRTVTL------ 157
Cdd:cd01167    72 RGIQFDPA-APTTLAFVTLDADGERSFEFYRGPAADLLLDTEL---NPDLLSEADILHFGSIALASEPSRSALLelleaa 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 158 --------YDTNLPDVteedfrsvdltrykwiHWEGRNAAeqvkmirrveehnsgrgaeeritvsveiekeREELYQLFP 229
Cdd:cd01167   148 kkagvlisFDPNLRPP----------------LWRDEEEA-------------------------------RERIAELLE 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 230 HGDVVFVSKDVARHFGFHSAQEAVRGLyprvrkgaylvcaWAEEGADAL----GPDGS-------VVHSCAFPPDCiVDT 298
Cdd:cd01167   181 LADIVKLSDEELELLFGEEDPEEIAAL-------------LLLFGLKLVlvtrGADGAllytkggVGEVPGIPVEV-VDT 246

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1785367607 299 LGAGDTFNASVIYALSHG-------RGMQEALTYGCQMAGKKCGVQG 338
Cdd:cd01167   247 TGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 8-338 4.69e-08

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 53.20  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   8 CIGLVCLDIisvvdkYPEEDsdsrclsqRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSHVM 87
Cdd:PRK09813    5 TIGDNCVDI------YPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  88 SRPGcsfPASVVISNISNGSRTIVHMNSFIVSDFRrrgigtpnvswqsrgdmpcacclvnvssgsrtvtlydtnlpdVTE 167
Cdd:PRK09813   71 TKHG---VTAQTQVELHDNDRVFGDYTEGVMADFA------------------------------------------LSE 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 168 EDFRSvdLTRYKWIH---WEgrNAAEQVKMIrrveeHNSGrgaeerITVSVEI-EKEREELYQ-LFPHGDVVFVSKdvar 242
Cdd:PRK09813  106 EDYAW--LAQYDIVHaaiWG--HAEDAFPQL-----HAAG------KLTAFDFsDKWDSPLWQtLVPHLDYAFASA---- 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 243 hfgfHSAQEAVRG-LYPRVRKGAYLVCA-WAEEGAdaLGPDGSVVHSCAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQ 320
Cdd:PRK09813  167 ----PQEDEFLRLkMKAIVARGAGVVIVtLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLP 240

                         330
                  ....*....|....*...
gi 1785367607 321 EALTYGCQMAGKKCGVQG 338
Cdd:PRK09813  241 QAMAQGTACAAKTIQYHG 258
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 171-313 4.50e-07

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: 49.79  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 171 RSVDLTRYKWIHWEGRN--AAEQVKMIRRVEEHNSGRGAEeriTVSVEIEKEREELYQLFPHGDVVFVSKDVARHFGF-- 246
Cdd:cd00287    51 VSVTLVGADAVVISGLSpaPEAVLDALEEARRRGVPVVLD---PGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGrr 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785367607 247 -HSAQEAVRGLYPRVRKGAYLVCAWAEEGADAL-GPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYAL 313
Cdd:cd00287   128 dLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVaTRGGTEVHVPAFPVK-VVDTTGAGDAFLAALAAGL 195
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 6-332 7.57e-07

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


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 49.72  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGIDVSH 85
Cdd:cd01947     2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607  86 VMSRPGCSFPASVVISNisnGSRTIvhmnsfivsdfrrrgigtpnvswqsrgdmpcacclvnvssgsrtvtlydTNLPDV 165
Cdd:cd01947    82 AWRDKPTRKTLSFIDPN---GERTI-------------------------------------------------TVPGER 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 166 TEEDFRSVDLTRYKWIHWegrNAAEQVKMIRRVEEHNSGRGAEERITVSVEiekEREELYQLFphgDVVFVSKdvaRHFG 245
Cdd:cd01947   110 LEDDLKWPILDEGDGVFI---TAAAVDKEAIRKCRETKLVILQVTPRVRVD---ELNQALIPL---DILIGSR---LDPG 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 246 FHSAQEAVRGLYPRvrkgaYLVCAWAEEGAdALGPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYALSHGRGMQEALTY 325
Cdd:cd01947   178 ELVVAEKIAGPFPR-----YLIVTEGELGA-ILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALEL 250


                  ....*..
gi 1785367607 326 GCQMAGK 332
Cdd:cd01947   251 GAQCGAI 257
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 278-331 3.25e-06

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: 47.93  E-value: 3.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785367607 278 LGPDGSVVHSC-------AFPPDcIVDTLGAGDTFNASVIYALSHGRGMQEALTYGCQMAG 331
Cdd:cd01174   219 LGAKGALLASGgevehvpAFKVK-AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 6-61 7.73e-06

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: 45.93  E-value: 7.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785367607   6 ILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMG 61
Cdd:cd00287     2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG 57
PTZ00292 PTZ00292
ribokinase; Provisional
 3-110 8.02e-06

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 47.04  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   3 EKGILCIGLVCLDIISVVDKYPEEDSDSRCLSQRWQRGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRRYGID 82
Cdd:PTZ00292   15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94

                          90       100
                  ....*....|....*....|....*...
gi 1785367607  83 VSHVmsrpgcsfpasVVISNISNGSRTI 110
Cdd:PTZ00292   95 TSFV-----------SRTENSSTGLAMI 111
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
272-326 9.39e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 46.67  E-value: 9.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785367607 272 EEGADA----LGPDGSV------VHSCAFPPDCIVDTLGAGDTFNASVIYALSHGRGMQEALTYG 326
Cdd:COG1105   211 ERGAENvvvsLGADGALlvtedgVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 212-330 5.21e-05

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: 44.38  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 212 TVSVEIEKEREELYQLFPHGDVVFVSKDVARHF----GFHSAQEAVRGLYPRVrkgayLVCAWAEEGAdALGPDGSVVHS 287
Cdd:cd01946   145 TMNFWISIKPEKLKKVLAKVDVVIINDGEARQLtgaaNLVKAARLILAMGPKA-----LIIKRGEYGA-LLFTDDGYFAA 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1785367607 288 CAFPPDCIVDTLGAGDTFNASVI-YALSHGR----GMQEALTYGCQMA 330
Cdd:cd01946   219 PAYPLESVFDPTGAGDTFAGGFIgYLASQKDtseaNMRRAIIYGSAMA 266
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 278-326 3.04e-04

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: 41.82  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785367607 278 LGPDGSVVHSCA----FPPDCI--VDTLGAGDTFNASVIYALSHGRGMQEALTYG 326
Cdd:TIGR02152 215 LGSKGALLVSKDesklIPAFKVkaVDTTAAGDTFNGAFAVALAEGKSLEDAIRFA 269
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 278-323 3.72e-04

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: 41.53  E-value: 3.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785367607 278 LGPDGSVVHSCA-------FPP---DCIVDTLGAGDTFNASVIYALSHGRGMQEAL 323
Cdd:cd01941   220 LGAKGVLLSSREggvetklFPApqpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSL 275
PRK11142 PRK11142
ribokinase; Provisional
 296-326 7.81e-04

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 40.62  E-value: 7.81e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1785367607 296 VDTLGAGDTFNASVIYALSHGRGMQEALTYG 326
Cdd:PRK11142  246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 5-93 1.59e-03

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: 39.84  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607   5 GILCIGLVCLDIISVVDKYPEE------DSDSRCLsqrwqrGGNASNSCTILALLGAPCAFMGSLAPGHMADFTLNSLRR 78
Cdd:cd01174     1 KVVVVGSINVDLVTRVDRLPKPgetvlgSSFETGP------GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLRE 74

                          90
                  ....*....|....*
gi 1785367607  79 YGIDVSHVMSRPGCS 93
Cdd:cd01174    75 EGIDVSYVEVVVGAP 89
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 192-321 1.79e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 39.79  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785367607 192 VKMIRRVEEHNSGRGAEERIT---VSVeIEKEREELYQLFPHG-DVVFVSKDVARHF-GF------HSAQEAVRGLYPRV 260
Cdd:PLN02813  241 IEAIAQACEEAHRAGALVAVTasdVSC-IERHRDDFWDVMGNYaDILFANSDEARALcGLgseespESATRYLSHFCPLV 319

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785367607 261 R-----KGAYLvcawaeegadalGPDGSVVhscAFPPD-CI-VDTLGAGDTFNASVIYALSHG----RGMQE 321
Cdd:PLN02813  320 SvtdgaRGSYI------------GVKGEAV---YIPPSpCVpVDTCGAGDAYAAGILYGLLRGvsdlRGMGE 376
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 272-338 2.38e-03

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: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785367607 272 EEGADALGPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYALSHGRGMQEALTYGCQMAGKKCGVQG 338
Cdd:cd01172   228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 279-326 5.95e-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: 38.09  E-value: 5.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785367607 279 GPDGSVVHSCA-----------FPPDCIVDTLGAGDTFNASVIYALSHGRGMQEALTYG 326
Cdd:cd01943   233 GKLGCYVGSADsgpelwlpayhTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYG 291
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 272-330 7.68e-03

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 37.87  E-value: 7.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785367607 272 EEGADALGPDGSVVHSCAFPPDcIVDTLGAGDTFNASVIYALSHGRGMQEAltygCQMA 330
Cdd:COG2870   245 EEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEA----AELA 298
 
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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