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Conserved domains on  [gi|2129534692|ref|XP_044868029|]
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ketohexokinase isoform X1 [Mauremys mutica]

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

CATH:  3.40.1190.20
EC:  2.7.1.3
Gene Ontology:  GO:0005524|GO:0004454|GO:0006000
PubMed:  8382990
SCOP:  4000759

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 ...
 5-295 2.26e-146

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: 412.57  E-value: 2.26e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVaWQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaHQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 165 RVSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129534692 245 FPPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 295
Cdd:cd01939   239 HKPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 5-295 2.26e-146

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: 412.57  E-value: 2.26e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVaWQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaHQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 165 RVSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129534692 245 FPPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 295
Cdd:cd01939   239 HKPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-293 1.19e-43

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: 150.81  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:COG0524     1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTLCACCLVnSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYNQ 158
Cdd:COG0524    81 GVRRDPGAPTGLAFILV-DPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 159 TC---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSrvRPGATVICAWAEAGADALG 234
Cdd:COG0524   160 PVsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLA--RGVKLVVVTLGAEGALLYT 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2129534692 235 pDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:COG0524   234 -GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 5-293 1.07e-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: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTlCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQV--DLTQYKWIHWEGRNAAE-QVKMIQRVEEynqTCP 161
Cdd:pfam00294  79 YVVIDEDTRT-GTALIEVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIE---AAK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 162 AHQRVSTSV--EVEKPREELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALGP 235
Cdd:pfam00294 155 NGGTFDPNLldPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2129534692 236 DGElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:pfam00294 235 DGE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 4-293 1.62e-10

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 60.14  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   4 KRILCIGLVCldiisvVDMYPAEDtdtrclsqRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDV 83
Cdd:PRK09813    1 KKLATIGDNC------VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  84 AHVawqSRGDTLCACCLVNSTTGSRTVTLYDTN-LPDVTAQDFEQVDLTQYKWIH---WEgrNAAEQVKMIQRveeynqt 159
Cdd:PRK09813   67 SHV---HTKHGVTAQTQVELHDNDRVFGDYTEGvMADFALSEEDYAWLAQYDIVHaaiWG--HAEDAFPQLHA------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 160 cpAHQRVStsvevekpreelyqlFGYADVV---FVSKDVAK-DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEAG 229
Cdd:PRK09813  135 --AGKLTA---------------FDFSDKWdspLWQTLVPHlDYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGENG 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 230 AdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:PRK09813  197 S--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 1.69e-08

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: 54.53  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  40 GGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVAHVAWQSRGDTLCACCLVNSTTGSRTVTLYDTNL-- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAel 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 118 -PDVTA---QDFEQVDLT--QYKwIHWEGRNAAeqvkmIQRVEEYNQT-----CPAHQRVSTS----VEVEKPRE-ELYQ 181
Cdd:TIGR02152 111 tPEDIDaaeALIAESDIVllQLE-IPLETVLEA-----AKIAKKHGVKvilnpAPAIKDLDDEllslVDIITPNEtEAEI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 182 LFGyadvVFVsKDVAkdfgfhSAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFN 261
Cdd:TIGR02152 185 LTG----IEV-TDEE------DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFN 249

                         250       260
                  ....*....|....*....|....
gi 2129534692 262 AAVLFALSRGQRLQEALTFGCQVA 285
Cdd:TIGR02152 250 GAFAVALAEGKSLEDAIRFANAAA 273
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 5-295 2.26e-146

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: 412.57  E-value: 2.26e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVaWQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaHQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 165 RVSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129534692 245 FPPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 295
Cdd:cd01939   239 HKPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-293 1.19e-43

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: 150.81  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:COG0524     1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTLCACCLVnSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYNQ 158
Cdd:COG0524    81 GVRRDPGAPTGLAFILV-DPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 159 TC---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSrvRPGATVICAWAEAGADALG 234
Cdd:COG0524   160 PVsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLA--RGVKLVVVTLGAEGALLYT 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2129534692 235 pDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:COG0524   234 -GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 5-293 7.43e-33

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: 122.02  E-value: 7.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01945     1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVawQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRveeynqtcpAHQ 164
Cdd:cd01945    81 FI--VVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQE---------ARA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 165 R---VSTSVEVEKPR--EELYQLfgyADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPgaTVICAWAEAGADALGPDGEL 239
Cdd:cd01945   150 RgipIPLDLDGGGLRvlEELLPL---ADHAICSENFLRPNTGSADDEALELLASLGIP--FVAVTLGEAGCLWLERDGEL 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 240 VHSDAFpPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01945   225 FHVPAF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 5-293 9.10e-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: 114.21  E-value: 9.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIIsvvdmypAEDTDTRCLSQRWQR--GGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVD 82
Cdd:cd01166     1 DVVTIGEVMVDLS-------PPGGGRLEQADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  83 VAHVAwQSRGDTLCACCLVNSTTGSRTVtLYDTN---LPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQT 159
Cdd:cd01166    74 TSHVR-VDPGRPTGLYFLEIGAGGERRV-LYYRAgsaASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 160 CPAHQrVSTSVEV---------EKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRVRPGATVICAWAEAG 229
Cdd:cd01166   152 AKARG-VTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEEEAEAlLGDEDPTDAAERALALALGVKAVVVKLGAEG 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 230 ADALGpDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01166   231 ALVYT-GGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 5-293 1.07e-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: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTlCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQV--DLTQYKWIHWEGRNAAE-QVKMIQRVEEynqTCP 161
Cdd:pfam00294  79 YVVIDEDTRT-GTALIEVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIE---AAK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 162 AHQRVSTSV--EVEKPREELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALGP 235
Cdd:pfam00294 155 NGGTFDPNLldPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2129534692 236 DGElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:pfam00294 235 DGE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 3-293 9.47e-23

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: 95.76  E-value: 9.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   3 EKRILCIGLVCLDIISVVDMYPAEDTD----TRCLSQRWQR-------------GGNASNSCTVLSLLGAPCAFMGSLAP 65
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  66 GHAADFIVADFRRRGVDVaHVAWQSRGDTlcACCLVNSTTG-SRTvtlYDTNL---PDVTAQDFEQVDLTQYKWIHWEGR 141
Cdd:cd01168    81 DKLGDFLLKDLRAAGVDT-RYQVQPDGPT--GTCAVLVTPDaERT---MCTYLgaaNELSPDDLDWSLLAKAKYLYLEGY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 142 NAAEQVKMIQRVEEYnqtcpAHQ---RVSTSV----EVEKPREELYQLFGYADVVFVSKDVAKDFGF----HSAPEAVKR 210
Cdd:cd01168   155 LLTVPPEAILLAAEH-----AKEngvKIALNLsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEaettDDLEAALKL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 211 LRSRVRpgaTVICAwaeAGADA--LGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRK 288
Cdd:cd01168   230 LALRCR---IVVIT---QGAKGavVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEV 303


                  ....*
gi 2129534692 289 CGVHG 293
Cdd:cd01168   304 IQQLG 308
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 5-293 3.43e-20

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 88.08  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDmyPAEDTDTRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01167     1 KVVCFGEALIDFIPEGS--GAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTLCAccLVNST-TGSRTVTLYDTNLPDVTAQDFEQVD-LTQYKWIH--------WEGRNAAEQVkmIQRVE 154
Cdd:cd01167    73 GIQFDPAAPTTLA--FVTLDaDGERSFEFYRGPAADLLLDTELNPDlLSEADILHfgsialasEPSRSALLEL--LEAAK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 155 EYNQTC-------PAHQRvstsvEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEavKRLRSRVRPG-ATVICAWA 226
Cdd:cd01167   149 KAGVLIsfdpnlrPPLWR-----DEEEARERIAELLELADIVKLSDEELELLFGEEDPE--EIAALLLLFGlKLVLVTRG 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 227 EAGADALGPDGElVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQ-------RLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01167   222 ADGALLYTKGGV-GEVPGIPVEV-VDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 5-288 5.36e-19

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: 84.67  E-value: 5.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01942     1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVAWQSRGDTLCACCLVNSTtGSRTVTLYdtnlPDVtAQDFEQVDLTQYkwihwEGRNAAEQVKMIQRVEEYNQTC-PAH 163
Cdd:cd01942    81 HVRVVDEDSTGVAFILTDGD-DNQIAYFY----PGA-MDELEPNDEADP-----DGLADIVHLSSGPGLIELARELaAGG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 164 QRVS---TSVEVEKPREELYQLFGYADVVFVSKDVAKDF----GFHSAPEAVKrlrsrVRpgaTVICAWAEAGADALGPD 236
Cdd:cd01942   150 ITVSfdpGQELPRLSGEELEEILERADILFVNDYEAELLkertGLSEAELASG-----VR---VVVVTLGPKGAIVFEDG 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129534692 237 GELVHsDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRK 288
Cdd:cd01942   222 EEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 5-293 2.72e-18

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: 82.40  E-value: 2.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDI-ISVVDMYPaedtdtrclsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDV 83
Cdd:cd01940     1 RLAAIGDNVVDKyLHLGKMYP---------------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDI 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  84 AHVAwQSRGDTLCACCLVNSttGSRTVTLYDTN-----LPDvtAQDFEQvdLTQYKWIH---WEGRNAAEqvkmiqrvEE 155
Cdd:cd01940    66 SHCR-VKEGENAVADVELVD--GDRIFGLSNKGgvareHPF--EADLEY--LSQFDLVHtgiYSHEGHLE--------KA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 156 YNQTCPAHQRVSTSVEVEKPREELYQLFGYADVVFVSkdvAKDFgfhSAPEAVKRLRSRVRPGATVICawAEAGAD-ALG 234
Cdd:cd01940   131 LQALVGAGALISFDFSDRWDDDYLQLVCPYVDFAFFS---ASDL---SDEEVKAKLKEAVSRGAKLVI--VTRGEDgAIA 202

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 235 PDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQ-RLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01940   203 YDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEG 262
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 5-286 6.57e-13

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: 67.45  E-value: 6.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGnASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01944     1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 hvaWQSRG--DTLCACCLVnSTTGSRTVTLYDTNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPA 162
Cdd:cd01944    80 ---LPPRGgdDGGCLVALV-EPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 163 HQ--------RVStsvevEKPREELYQLFGYADVVFVSKDVAKDF-GFHSAPEAVKRLRSRVRPGATVICAWAEAGADAL 233
Cdd:cd01944   156 GTtlvfdpgpRIS-----DIPDTILQALMAKRPIWSCNREEAAIFaERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIR 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129534692 234 GPDGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAG 286
Cdd:cd01944   231 LPDGNTHIIPGFK-VKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 5-293 1.29e-10

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: 61.03  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYP-------AEDTDTRClsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFR 77
Cdd:cd01174     1 KVVVVGSINVDLVTRVDRLPkpgetvlGSSFETGP-------GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  78 RRGVDVAHVAwqsrgdtlcacCLVNSTTGSRTVTLYDT--NLPDVTAqdfeqvdltqykwihweGRNAAEQVKMIQRVEE 155
Cdd:cd01174    74 EEGIDVSYVE-----------VVVGAPTGTAVITVDESgeNRIVVVP-----------------GANGELTPADVDAALE 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 156 YNQTC---------P----------AHQRVSTSV----EVEKPREELYQLfgyADVVFV----SKDVAKDFG--FHSAPE 206
Cdd:cd01174   126 LIAAAdvlllqleiPletvlaalraARRAGVTVIlnpaPARPLPAELLAL---VDILVPneteAALLTGIEVtdEEDAEK 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 207 AVKRLRSRvrPGATVICAWAEAGAdALGPDGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAG 286
Cdd:cd01174   203 AARLLLAK--GVKNVIVTLGAKGA-LLASGGEVEHVPAFK-VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278


                  ....*..
gi 2129534692 287 RKCGVHG 293
Cdd:cd01174   279 LSVTRPG 285
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 4-293 1.62e-10

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 60.14  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   4 KRILCIGLVCldiisvVDMYPAEDtdtrclsqRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDV 83
Cdd:PRK09813    1 KKLATIGDNC------VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  84 AHVawqSRGDTLCACCLVNSTTGSRTVTLYDTN-LPDVTAQDFEQVDLTQYKWIH---WEgrNAAEQVKMIQRveeynqt 159
Cdd:PRK09813   67 SHV---HTKHGVTAQTQVELHDNDRVFGDYTEGvMADFALSEEDYAWLAQYDIVHaaiWG--HAEDAFPQLHA------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 160 cpAHQRVStsvevekpreelyqlFGYADVV---FVSKDVAK-DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEAG 229
Cdd:PRK09813  135 --AGKLTA---------------FDFSDKWdspLWQTLVPHlDYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGENG 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 230 AdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:PRK09813  197 S--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 5-268 5.58e-09

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: 54.79  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFmgslapgHAADFIVadfrrrgvdva 84
Cdd:cd00287     1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTL-------VGADAVV----------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 hvawqsrgdtlcacclvnstTGSRTVTLydtnlpdvtaqdfeqvdltqykwihwegrnaAEQVKMIQRVEEYNQT---CP 161
Cdd:cd00287    63 --------------------ISGLSPAP-------------------------------EAVLDALEEARRRGVPvvlDP 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 162 AhqrvstSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGA----TVICAWAEAGADALGPDG 237
Cdd:cd00287    92 G------PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSkgpkVVIVTLGEKGAIVATRGG 165

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2129534692 238 ELVHSDAFPPEtIVDTLGAGDTFNAAVLFAL 268
Cdd:cd00287   166 TEVHVPAFPVK-VVDTTGAGDAFLAALAAGL 195
PTZ00292 PTZ00292
ribokinase; Provisional
 3-293 8.07e-09

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 55.90  E-value: 8.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   3 EKRILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLapGHAADFI--VADFRRRG 80
Cdd:PTZ00292   15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMV--GTDGFGSdtIKNFKRNG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  81 VDVAHVAWQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFeqvdltqykwihwegRNAAEQVKMIQRVEEYNQTC 160
Cdd:PTZ00292   93 VNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMV---------------DAQTDNIQNICKYLICQNEI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 161 P----------AHQRVSTSVEVEKP------REELYQLFGYADVVFVSK-DVAKDFGFHSAPEAVKRLRSR---VRPGAT 220
Cdd:PTZ00292  158 PlettldalkeAKERGCYTVFNPAPapklaeVEIIKPFLKYVSLFCVNEvEAALITGMEVTDTESAFKASKelqQLGVEN 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129534692 221 VICAWAEAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:PTZ00292  238 VIITLGANGCLIVEKENEPVHVPGKRVK-AVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 1.69e-08

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: 54.53  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  40 GGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVAHVAWQSRGDTLCACCLVNSTTGSRTVTLYDTNL-- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAel 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 118 -PDVTA---QDFEQVDLT--QYKwIHWEGRNAAeqvkmIQRVEEYNQT-----CPAHQRVSTS----VEVEKPRE-ELYQ 181
Cdd:TIGR02152 111 tPEDIDaaeALIAESDIVllQLE-IPLETVLEA-----AKIAKKHGVKvilnpAPAIKDLDDEllslVDIITPNEtEAEI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 182 LFGyadvVFVsKDVAkdfgfhSAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFN 261
Cdd:TIGR02152 185 LTG----IEV-TDEE------DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFN 249

                         250       260
                  ....*....|....*....|....
gi 2129534692 262 AAVLFALSRGQRLQEALTFGCQVA 285
Cdd:TIGR02152 250 GAFAVALAEGKSLEDAIRFANAAA 273
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 6-292 2.70e-08

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: 53.58  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   6 ILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVaH 85
Cdd:cd01947     2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH-T 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  86 VAW--QSRGDTLcaccLVNSTTGSRTVTlydtNLPDVTAQDFEQVDLTQYKWIHWegrNAAEQVKMIQRVEEYN-----Q 158
Cdd:cd01947    81 VAWrdKPTRKTL----SFIDPNGERTIT----VPGERLEDDLKWPILDEGDGVFI---TAAAVDKEAIRKCRETklvilQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 159 TCPaHQRVSTSVEVEKPreelyqlfgyADVVFVSKDvakDFGFHSAPEAVKRLRSRvrpgaTVICAWAEAGAdALGPDGE 238
Cdd:cd01947   150 VTP-RVRVDELNQALIP----------LDILIGSRL---DPGELVVAEKIAGPFPR-----YLIVTEGELGA-ILYPGGR 209

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 239 LVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVaGRKCGVH 292
Cdd:cd01947   210 YNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQC-GAICVSH 261
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
31-281 2.48e-07

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 51.29  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  31 RCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLApGHAADFIVADFRRRGVDVAHVawQSRGDTlcacclvnsttgsRT- 109
Cdd:COG1105    26 RASEVRLDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFV--PIEGET-------------RIn 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 110 VTLYDT--------NL--PDVTAQDFEQVdLTQYKWIHWEG----------RNAAEQ--VKMIQRVEEYNQTC------- 160
Cdd:COG1105    90 IKIVDPsdgteteiNEpgPEISEEELEAL-LERLEELLKEGdwvvlsgslpPGVPPDfyAELIRLARARGAKVvldtsge 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 161 PAHQRVSTSVEVEKP-REELYQLFGY-----ADVVfvskdvakdfgfhsapEAVKRLRSRvrpGATVICAwaeagadALG 234
Cdd:COG1105   169 ALKAALEAGPDLIKPnLEELEELLGRpletlEDII----------------AAARELLER---GAENVVV-------SLG 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129534692 235 PDGEL-VHSDAF-----PPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFG 281
Cdd:COG1105   223 ADGALlVTEDGVyrakpPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 40-282 4.56e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 47.48  E-value: 4.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  40 GGNASNSCTVLSL-LGAPCAFMGSLAPGHAADFIVADFRRRGVDVAHVAWQSrGDTLCACCLVNSTtGSRTVTLYDTNLP 118
Cdd:PLN02379   86 GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKK-GPTAQCVCLVDAL-GNRTMRPCLSSAV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 119 DVTAQDFEQVDLTQYKWIHWE-GRNAAEQVKMIQRVEEYNQTCPAHQRVSTSVeVEKPREELYQLF--GYADVVFVSKDV 195
Cdd:PLN02379  164 KLQADELTKEDFKGSKWLVLRyGFYNLEVIEAAIRLAKQEGLSVSLDLASFEM-VRNFRSPLLQLLesGKIDLCFANEDE 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 196 AKDF---GFHSAPEAVKRLRSRVrpgatviCAWAEAgadALGPDG-------ELVHSDAFPPETIVDTLGAGDTFNAAVL 265
Cdd:PLN02379  243 ARELlrgEQESDPEAALEFLAKY-------CNWAVV---TLGSKGciarhgkEVVRVPAIGETNAVDATGAGDLFASGFL 312

                         250
                  ....*....|....*..
gi 2129534692 266 FALSRGQRLQEALTFGC 282
Cdd:PLN02379  313 YGLIKGLSLEECCKVGA 329
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 172-293 1.11e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 46.34  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 172 VEKPREELYQLFG-YADVVFVSKDVAK---DFGFHSAPEAVKRLRSRVRPGATVIcawAEAGADALGPDGElVHSDAFPP 247
Cdd:PLN02813  268 IERHRDDFWDVMGnYADILFANSDEARalcGLGSEESPESATRYLSHFCPLVSVT---DGARGSYIGVKGE-AVYIPPSP 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2129534692 248 ETIVDTLGAGDTFNAAVLFALSRG-QRLQEALTFGCQVAGRKCGVHG 293
Cdd:PLN02813  344 CVPVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQG 390
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 6-288 2.15e-05

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: 45.00  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692   6 ILCIGLVCLDIIS-VVDMYPAEDTDTRCLSQRWqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFIVADFRRRGVDVA 84
Cdd:cd01941     2 IVVIGAANIDLRGkVSGSLVPGTSNPGHVKQSP--GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692  85 HVawQSRGDTLCACCLVNSTTGSRTVTLYDTNLPDVTAQDFEQvdltqykwiHWEGRNAAEQVKMIqrveEYNQTCPAHQ 164
Cdd:cd01941    80 GI--VFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLR---------KIREALKEAKPIVV----DANLPEEALE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 165 RVSTSVevekpREELYQlfgyadVVFVSKDVAKdfgfhsapeaVKRLRSRVRPGATVI------CAWAEAGADA------ 232
Cdd:cd01941   145 YLLALA-----AKHGVP------VAFEPTSAPK----------LKKLFYLLHAIDLLTpnraelEALAGALIENnedenk 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 233 ----------------LGPDGELVHSDA-------FPP---ETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGcQVAG 286
Cdd:cd01941   204 aakilllpgiknvivtLGAKGVLLSSREggvetklFPApqpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAA 282


                  ..
gi 2129534692 287 RK 288
Cdd:cd01941   283 AL 284
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 206-286 8.12e-05

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 43.65  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 206 EAVKRLRSRVRPGATVICAwAEAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVA 285
Cdd:COG2870   225 AAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELANLAA 302


                  .
gi 2129534692 286 G 286
Cdd:COG2870   303 G 303
PRK11142 PRK11142
ribokinase; Provisional
 251-281 1.03e-04

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 43.32  E-value: 1.03e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2129534692 251 VDTLGAGDTFNAAVLFALSRGQRLQEALTFG 281
Cdd:PRK11142  246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 185-288 3.95e-04

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: 41.23  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 185 YADVVFVSKDVAKDFgfHSAPEAVKRLRsrVRPGATVICAWAEAGADALgpDGELVHSDAFPPETIVDTLGAGDTFNAAV 264
Cdd:cd01937   155 LHDVLKLSRVEAEVI--STPTELARLIK--ETGVKEIIVTDGEEGGYIF--DGNGKYTIPASKKDVVDPTGAGDVFLAAF 228

                          90       100
                  ....*....|....*....|....
gi 2129534692 265 LFALSRGQRLQEALTFGCQVAGRK 288
Cdd:cd01937   229 LYSRLSGKDIKEAAEFAAAAAAKF 252
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 172-277 4.61e-04

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: 40.91  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534692 172 VEKPREELYQLFGYADVVFVSKDVAKDFGfhSAPEAVKRLRSRVRPGA-TVICAWAEAGAdALGPDGELVHSDAFPPETI 250
Cdd:cd01946   150 ISIKPEKLKKVLAKVDVVIINDGEARQLT--GAANLVKAARLILAMGPkALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226

                          90       100
                  ....*....|....*....|....*..
gi 2129534692 251 VDTLGAGDTFNAAVLFALSRGQRLQEA 277
Cdd:cd01946   227 FDPTGAGDTFAGGFIGYLASQKDTSEA 253
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 233-276 3.32e-03

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 38.38  E-value: 3.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2129534692 233 LGPDGELVHSD------AFPPETIVDTLGAGDTFNAAVLFALSRGQRLQE 276
Cdd:PRK09434  220 LGAEGVLVHTRgqvqhfPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTD 269
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 227-290 6.83e-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: 37.54  E-value: 6.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534692 227 EAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCG 290
Cdd:cd01172   228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
 
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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