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Conserved domains on  [gi|1151099508|ref|NP_001335995|]
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ketohexokinase isoform 4 [Mus musculus]

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 ...
 5-295 1.51e-151

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: 425.67  E-value: 1.51e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVvLQTEGSIPTSTVIINEASGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1151099508 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 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 1.51e-151

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: 425.67  E-value: 1.51e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVvLQTEGSIPTSTVIINEASGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1151099508 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939   239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-289 8.48e-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: 148.49  E-value: 8.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:COG0524     1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVVLQTEGSIPTSTVIINEaSGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEG------RNASEQVKMLQRIEEHNa 158
Cdd:COG0524    81 GVRRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 159 kqplpqkVRVSV-------EIEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSR------VKKGAtlvca 224
Cdd:COG0524   159 -------VPVSLdpnyrpaLWEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARgvklvvVTLGA----- 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151099508 225 waeEGADALGpDGQLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKC 289
Cdd:COG0524   227 ---EGALLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-293 3.62e-26

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 104.35  E-value: 3.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRY 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  86 VVLQTEGSIPTSTVIINEAsGSRTILHayrNLPDVSAKDFEKVDLTR-----FKWIHIEGRNASE-QVKMLQRIEE--HN 157
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGD-GERTIVF---NRGAAADLTPEELEENEdllenADLLYISGSLPLGlPEATLEELIEaaKN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 158 AKQPLPqkvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGA-TLVCAWAEEGADAL 233
Cdd:pfam00294 156 GGTFDP---NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVV 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 234 GPDGQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:pfam00294 233 EGDGEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 3.07e-10

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: 59.92  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVVLQTEGSIPTSTVIINEASGSRTILHAYRNL-- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAel 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 118 -PDVSAKDFEKVDLTRFKWIHIEGR-NASEQVkmLQRIEEHN---------AKQPLPQKVRVSVEIEKPREElfqlfsyg 186
Cdd:TIGR02152 111 tPEDIDAAEALIAESDIVLLQLEIPlETVLEA--AKIAKKHGvkvilnpapAIKDLDDELLSLVDIITPNET-------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 187 EVVFVSKDVAKHLgfQSAVEALRGLYSRVKKGATLvcawaeegadALGPDGQLLHSDA----FPPPRV--VDTLGAGDTF 260
Cdd:TIGR02152 181 EAEILTGIEVTDE--EDAEKAAEKLLEKGVKNVII----------TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDTF 248

                         250       260
                  ....*....|....*....|....*
gi 1151099508 261 NASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:TIGR02152 249 NGAFAVALAEGKSLEDAIRFANAAA 273
PTZ00292 PTZ00292
ribokinase; Provisional
 3-285 5.68e-08

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 53.20  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   3 EKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLapGHVADFV--LDDLRQHS 80
Cdd:PTZ00292   15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMV--GTDGFGSdtIKNFKRNG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  81 VDLRYVVLQTEGSIPTSTVIINEASGSRTILHayrnLPdvSAKDFEKVDLTRFKWIHIEGR------------NASEQVk 148
Cdd:PTZ00292   93 VNTSFVSRTENSSTGLAMIFVDTKTGNNEIVI----IP--GANNALTPQMVDAQTDNIQNIckylicqneiplETTLDA- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 149 mLQRIEEHNAK---QPLPQKVRVSVEIEKPreelfqLFSYGEVVFVSKdvakhlgfqsaVEA-------LRGLYSRVKKG 218
Cdd:PTZ00292  166 -LKEAKERGCYtvfNPAPAPKLAEVEIIKP------FLKYVSLFCVNE-----------VEAalitgmeVTDTESAFKAS 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151099508 219 ATLVCAWAEEGADALGPDGQLLHSDAFPPP-------RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PTZ00292  228 KELQQLGVENVIITLGANGCLIVEKENEPVhvpgkrvKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 5-295 1.51e-151

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: 425.67  E-value: 1.51e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:cd01939     1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVvLQTEGSIPTSTVIINEASGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939    81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939   159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1151099508 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939   239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-289 8.48e-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: 148.49  E-value: 8.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:COG0524     1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVVLQTEGSIPTSTVIINEaSGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEG------RNASEQVKMLQRIEEHNa 158
Cdd:COG0524    81 GVRRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 159 kqplpqkVRVSV-------EIEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSR------VKKGAtlvca 224
Cdd:COG0524   159 -------VPVSLdpnyrpaLWEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARgvklvvVTLGA----- 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151099508 225 waeEGADALGpDGQLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKC 289
Cdd:COG0524   227 ---EGALLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 5-296 6.82e-31

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: 117.01  E-value: 6.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLR 84
Cdd:cd01945     1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 YVVLqTEGSIPTSTVIINEASGSRTILHaYRNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQriEEHNAKQPLPq 164
Cdd:cd01945    81 FIVV-APGARSPISSITDITGDRATISI-TAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQ--EARARGIPIP- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 165 kVRVSVEIEKPREELFQLFSYgevVFVSKDVAKHLGFQSAVEALRGLYSRvkkGATLVCAWA-EEGADALGPDGQLLHSD 243
Cdd:cd01945   156 -LDLDGGGLRVLEELLPLADH---AICSENFLRPNTGSADDEALELLASL---GIPFVAVTLgEAGCLWLERDGELFHVP 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1151099508 244 AFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCglQGFDG 296
Cdd:cd01945   229 AF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKC--RGLGG 278
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-293 3.62e-26

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 104.35  E-value: 3.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRY 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  86 VVLQTEGSIPTSTVIINEAsGSRTILHayrNLPDVSAKDFEKVDLTR-----FKWIHIEGRNASE-QVKMLQRIEE--HN 157
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGD-GERTIVF---NRGAAADLTPEELEENEdllenADLLYISGSLPLGlPEATLEELIEaaKN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 158 AKQPLPqkvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGA-TLVCAWAEEGADAL 233
Cdd:pfam00294 156 GGTFDP---NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVV 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 234 GPDGQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:pfam00294 233 EGDGEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 5-293 1.23e-23

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: 97.65  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIinvvdkYPEEDtDRRCLSQRWQR--GGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVD 82
Cdd:cd01166     1 DVVTIGEVMVDL------SPPGG-GRLEQADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  83 LRYVVLQTEGsiPTSTVII-NEASGSRTILHaYRN---LPDVSAKDFEKVDLTRFKWIHIEG----RNASEQVKMLQRIE 154
Cdd:cd01166    74 TSHVRVDPGR--PTGLYFLeIGAGGERRVLY-YRAgsaASRLTPEDLDEAALAGADHLHLSGitlaLSESAREALLEALE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 155 EHNAKQplpqkVRVSVEI---------EKPREELFQLFSYGEVVFVSK-DVAKHLGFQSAVEALRGLYSRVKKGATLVCA 224
Cdd:cd01166   151 AAKARG-----VTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVK 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151099508 225 WAEEGADALGPDGQLlHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:cd01166   226 LGAEGALVYTGGGRV-FVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 6-288 4.13e-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: 85.06  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLApghvADF----VLDDLRQHSV 81
Cdd:cd01942     2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVG----EDFhgrlYLEELREEGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  82 DLRYVVLQTEGSIPTStVIINEASGSRtILHAYRNLPDVSAKDFEKVDLTRFKWIHIEGRnaseqvkmlqRIEEHNAKQP 161
Cdd:cd01942    78 DTSHVRVVDEDSTGVA-FILTDGDDNQ-IAYFYPGAMDELEPNDEADPDGLADIVHLSSG----------PGLIELAREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 162 LPQKVRVSV----EIEK-PREELFQLFSYGEVVFVSKDVAKHL----GFQSAVEALRGLYSRVKKGAtlvcawaeEGADA 232
Cdd:cd01942   146 AAGGITVSFdpgqELPRlSGEELEEILERADILFVNDYEAELLkertGLSEAELASGVRVVVVTLGP--------KGAIV 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1151099508 233 LGPDGQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 288
Cdd:cd01942   218 FEDGEEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 3-293 1.82e-17

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 80.74  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   3 EKQILCVGLVVLDIINVVDKYPEEDTD----RRCLSQRWQR-------------GGNASNSCTVLSLLGARCAFMGSLAP 65
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  66 GHVADFVLDDLRQHSVDLRYVVlQTEGSIPTSTVIINEaSGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEG--RNA 143
Cdd:cd01168    81 DKLGDFLLKDLRAAGVDTRYQV-QPDGPTGTCAVLVTP-DAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGylLTV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 144 SEQV--KMLQRIEEHNakqplpqkVRVSV------EIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ----SAVEALRGL 211
Cdd:cd01168   159 PPEAilLAAEHAKENG--------VKIALnlsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEAettdDLEAALKLL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 212 YSRVKkgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGL 291
Cdd:cd01168   231 ALRCR---IVVITQGAKGA-VVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306


                  ..
gi 1151099508 292 QG 293
Cdd:cd01168   307 LG 308
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 18-293 1.99e-15

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: 74.31  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  18 NVVDKYPEEDTDRRclsqrwqrGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVvLQTEGsiPTS 97
Cdd:cd01940     8 NVVDKYLHLGKMYP--------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEG--ENA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  98 TVIINEASGSRTILHA-----YRNLPDvsAKDFEKvdLTRFKWIHI-EGRNASEQVKMLQriEEHNAKQPLPQKVRVSVE 171
Cdd:cd01940    77 VADVELVDGDRIFGLSnkggvAREHPF--EADLEY--LSQFDLVHTgIYSHEGHLEKALQ--ALVGAGALISFDFSDRWD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 172 IEkpreELFQLFSYGEVVFVSkdvAKHLGFQSAVEALRGLYSRvkkGATLVCAwaeegadALGPDGQLLHSDAF---PPP 248
Cdd:cd01940   151 DD----YLQLVCPYVDFAFFS---ASDLSDEEVKAKLKEAVSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAP 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1151099508 249 R---VVDTLGAGDTFNASVIFS-LSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:cd01940   214 RpveVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQGAQFAAKTCGHEG 262
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 5-293 2.46e-14

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: 71.90  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIInvvdkyPEEDTDrrclSQRWQR--GGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVD 82
Cdd:cd01167     1 KVVCFGEALIDFI------PEGSGA----PETFTKapGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  83 LRYVvlQTEGSIPTSTVIINE-ASGSRTIL----HAYRNLPDvsaKDFEKVDLTRFKWIH------IEGRNASEQVKMLQ 151
Cdd:cd01167    71 TRGI--QFDPAAPTTLAFVTLdADGERSFEfyrgPAADLLLD---TELNPDLLSEADILHfgsialASEPSRSALLELLE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 152 RIEEHNAKqplpqkvrVSVEI----------EKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLysrvkkgatl 221
Cdd:cd01167   146 AAKKAGVL--------ISFDPnlrpplwrdeEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAAL---------- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 222 vcaWAEEGADAL----GPDGQLLHSDAF------PPPRVVDTLGAGDTFNASVIFSLSKGNSMQ-------EALRFGCQV 284
Cdd:cd01167   208 ---LLLFGLKLVlvtrGADGALLYTKGGvgevpgIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedelaEALRFANAV 284


                  ....*....
gi 1151099508 285 AGKKCGLQG 293
Cdd:cd01167   285 GALTCTKAG 293
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
31-281 9.16e-14

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 70.16  E-value: 9.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  31 RCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLApGHVADFVLDDLRQHSVDLRYVvlQTEGSIPTSTVIINEASGSRTI 110
Cdd:COG1105    26 RASEVRLDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFV--PIEGETRINIKIVDPSDGTETE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 111 LHAYRnlPDVSAKDFEKV------DLTRFKWIHIEG---RNASEQ--VKMLQRIEEHNAK-------QPLPQKVRVSVEI 172
Cdd:COG1105   103 INEPG--PEISEEELEALlerleeLLKEGDWVVLSGslpPGVPPDfyAELIRLARARGAKvvldtsgEALKAALEAGPDL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 173 EKP-REELFQLFSygevvfvsKDVAkhlGFQSAVEALRGLysrVKKGATLVCAwaeegadALGPDGQLL-------HSDA 244
Cdd:COG1105   181 IKPnLEELEELLG--------RPLE---TLEDIIAAAREL---LERGAENVVV-------SLGADGALLvtedgvyRAKP 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1151099508 245 fPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:COG1105   240 -PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 14-281 2.77e-12

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 65.63  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  14 LDIINVVDKyPEEDTDRRCLSQRWQRGG---NASNsctVLSLLGARCAFMGsLAPGHVADFVLDDLRQHSVDLRYVVLqt 90
Cdd:cd01164    11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGkgiNVAR---VLKDLGVEVTALG-FLGGFTGDFFEALLKEEGIPDDFVEV-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  91 EGSIPTStVIINEASGSRTILhayrNL--PDVSAKDFEKVdLTRFK-------WIHIEG---RNASEQ--VKMLQRIEEH 156
Cdd:cd01164    84 AGETRIN-VKIKEEDGTETEI----NEpgPEISEEELEAL-LEKLKallkkgdIVVLSGslpPGVPADfyAELVRLAREK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 157 NAK-------QPLPQKVRVSVEIEKP-REELFQLFSygevvfvskdvAKHLGFQSAVEALRGLysrVKKGATLVCAwaee 228
Cdd:cd01164   158 GARvildtsgEALLAALAAKPFLIKPnREELEELFG-----------RPLGDEEDVIAAARKL---IERGAENVLV---- 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1151099508 229 gadALGPDGQLL-HSDAF-----PPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:cd01164   220 ---SLGADGALLvTKDGVyraspPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 40-286 4.43e-12

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: 65.26  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVVLQTEGsiPTSTVIIN-EASGSRTIL-----HA 113
Cdd:cd01174    36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGA--PTGTAVITvDESGENRIVvvpgaNG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 114 YRNLPDVSA--KDFEKVD--LTRFKwIHIEgrnASEQVkmLQRIEEHNAK--------QPLPQKVRVSVEIEKPRE-ELF 180
Cdd:cd01174   114 ELTPADVDAalELIAAADvlLLQLE-IPLE---TVLAA--LRAARRAGVTvilnpapaRPLPAELLALVDILVPNEtEAA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 181 QLFsyGEVVfvskdvakhLGFQSAVEALRGLYSRVKKgaTLVCAWAEEGADALGPDGQLLHsdAFPPPRVVDTLGAGDTF 260
Cdd:cd01174   188 LLT--GIEV---------TDEEDAEKAARLLLAKGVK--NVIVTLGAKGALLASGGEVEHV--PAFKVKAVDTTGAGDTF 252

                         250       260
                  ....*....|....*....|....*.
gi 1151099508 261 NASVIFSLSKGNSMQEALRFGCQVAG 286
Cdd:cd01174   253 IGALAAALARGLSLEEAIRFANAAAA 278
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 6-287 8.90e-12

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: 63.98  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLrY 85
Cdd:cd01947     2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH-T 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  86 VVLQTEGSIPTSTVIINEasGSRTILHAYRNLPDvsakDFEKVDLTRFKWIHIegrNASEQVKMLQRIEEHNAKQPLPQK 165
Cdd:cd01947    81 VAWRDKPTRKTLSFIDPN--GERTITVPGERLED----DLKWPILDEGDGVFI---TAAAVDKEAIRKCRETKLVILQVT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 166 VRVSVEIEKPREELFQLFsygevvfvskdVAKHLGFQSAVEALRGLYSRVKkgaTLVCAWAEEGAdALGPDGQLLHSDAF 245
Cdd:cd01947   152 PRVRVDELNQALIPLDIL-----------IGSRLDPGELVVAEKIAGPFPR---YLIVTEGELGA-ILYPGGRYNHVPAK 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1151099508 246 PPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGK 287
Cdd:cd01947   217 KAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 6-286 5.06e-11

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


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 62.05  E-value: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGnASNSCTVLSLLGARCAFMGSLAPGHVADFvlddLRQHSVDLRY 85
Cdd:cd01944     2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQ----IRQAMRDEGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  86 VVLQTEGSIPTS--TVIINEASGSRTILHAYRNLPDVSAKDFEKVDLTRFKWIHIEG-----RNASEQVkMLQRIEEHNA 158
Cdd:cd01944    77 EILLPPRGGDDGgcLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGytlasENASKVI-LLEWLEALPA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 159 KQPL-----PqkvRVSveiEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSRVKKGATLVCAWAEEGADA 232
Cdd:cd01944   156 GTTLvfdpgP---RIS---DIPDTILQALMAKRPIWSCNREEAAIFaERGDPAAEASALRIYAKTAAPVVVRLGSNGAWI 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1151099508 233 LGPDGQLLHSDAFPPpRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAG 286
Cdd:cd01944   230 RLPDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 3.07e-10

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: 59.92  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVVLQTEGSIPTSTVIINEASGSRTILHAYRNL-- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAel 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 118 -PDVSAKDFEKVDLTRFKWIHIEGR-NASEQVkmLQRIEEHN---------AKQPLPQKVRVSVEIEKPREElfqlfsyg 186
Cdd:TIGR02152 111 tPEDIDAAEALIAESDIVLLQLEIPlETVLEA--AKIAKKHGvkvilnpapAIKDLDDELLSLVDIITPNET-------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 187 EVVFVSKDVAKHLgfQSAVEALRGLYSRVKKGATLvcawaeegadALGPDGQLLHSDA----FPPPRV--VDTLGAGDTF 260
Cdd:TIGR02152 181 EAEILTGIEVTDE--EDAEKAAEKLLEKGVKNVII----------TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDTF 248

                         250       260
                  ....*....|....*....|....*
gi 1151099508 261 NASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:TIGR02152 249 NGAFAVALAEGKSLEDAIRFANAAA 273
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 6-268 4.27e-08

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: 52.48  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGslapghvadfvlddlrqhsvdlry 85
Cdd:cd00287     2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  86 vvlqtegsiptstviineasgsrtilhayrnlpdvsakdfekvdltrFKWIHIEGRNAS--EQVKMLQRIEEHNakqplp 163
Cdd:cd00287    58 -----------------------------------------------ADAVVISGLSPApeAVLDALEEARRRG------ 84

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 164 qkVRVSVE-----IEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGATLVCAWAEEGADAL-G 234
Cdd:cd00287    85 --VPVVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTGRrdlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVaT 162

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1151099508 235 PDGQLLHSDAFPPpRVVDTLGAGDTFNASVIFSL 268
Cdd:cd00287   163 RGGTEVHVPAFPV-KVVDTTGAGDAFLAALAAGL 195
PTZ00292 PTZ00292
ribokinase; Provisional
 3-285 5.68e-08

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 53.20  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   3 EKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLapGHVADFV--LDDLRQHS 80
Cdd:PTZ00292   15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMV--GTDGFGSdtIKNFKRNG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  81 VDLRYVVLQTEGSIPTSTVIINEASGSRTILHayrnLPdvSAKDFEKVDLTRFKWIHIEGR------------NASEQVk 148
Cdd:PTZ00292   93 VNTSFVSRTENSSTGLAMIFVDTKTGNNEIVI----IP--GANNALTPQMVDAQTDNIQNIckylicqneiplETTLDA- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 149 mLQRIEEHNAK---QPLPQKVRVSVEIEKPreelfqLFSYGEVVFVSKdvakhlgfqsaVEA-------LRGLYSRVKKG 218
Cdd:PTZ00292  166 -LKEAKERGCYtvfNPAPAPKLAEVEIIKP------FLKYVSLFCVNE-----------VEAalitgmeVTDTESAFKAS 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151099508 219 ATLVCAWAEEGADALGPDGQLLHSDAFPPP-------RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PTZ00292  228 KELQQLGVENVIITLGANGCLIVEKENEPVhvpgkrvKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 18-293 7.65e-06

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 46.27  E-value: 7.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  18 NVVDKYPEEDtdrrclsqRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVVLQtEGsiPTS 97
Cdd:PRK09813    9 NCVDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK-HG--VTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  98 TVIINEASGSRtILHAYRN--LPDVSAKDFEKVDLTRFKWIH--IEGrNASEQvkmLQRIEEHNakqplpqkVRVSVEI- 172
Cdd:PRK09813   78 QTQVELHDNDR-VFGDYTEgvMADFALSEEDYAWLAQYDIVHaaIWG-HAEDA---FPQLHAAG--------KLTAFDFs 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 173 EKPREELFQ-LFSYGEVVFVSKDvakhlgfqSAVEALRG-LYSRVKKGATLVCA-WAEEGAdaLGPDGQLLHSDAFPPPR 249
Cdd:PRK09813  145 DKWDSPLWQtLVPHLDYAFASAP--------QEDEFLRLkMKAIVARGAGVVIVtLGENGS--IAWDGAQFWRQAPEPVT 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1151099508 250 VVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:PRK09813  215 VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 40-282 9.28e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 46.71  E-value: 9.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  40 GGNASNSCTVLSL-LGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYvvLQTEGSIPTSTVIINEASGSRTILHAYRNLP 118
Cdd:PLN02379   86 GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSR--LRAKKGPTAQCVCLVDALGNRTMRPCLSSAV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 119 DVSAKDFEKVDLTRFKWIHIE-GRNASEQVKMLQRIeehnAKQplpQKVRVSVE------IEKPREELFQLFSYGEV--V 189
Cdd:PLN02379  164 KLQADELTKEDFKGSKWLVLRyGFYNLEVIEAAIRL----AKQ---EGLSVSLDlasfemVRNFRSPLLQLLESGKIdlC 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 190 FVSKDVAKHL---GFQSAVEALRGLYSRVkkgatlvCAWAeegADALGPDG-------QLLHSDAFPPPRVVDTLGAGDT 259
Cdd:PLN02379  237 FANEDEARELlrgEQESDPEAALEFLAKY-------CNWA---VVTLGSKGciarhgkEVVRVPAIGETNAVDATGAGDL 306

                         250       260
                  ....*....|....*....|...
gi 1151099508 260 FNASVIFSLSKGNSMQEALRFGC 282
Cdd:PLN02379  307 FASGFLYGLIKGLSLEECCKVGA 329
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 233-288 1.25e-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: 45.77  E-value: 1.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151099508 233 LGPDGQLLHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGcQVAGKK 288
Cdd:cd01941   220 LGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 5-288 1.33e-05

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


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 45.47  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508   5 QILCVGLVVLDIINVVDkypeedtdrrclSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFvlDDLRqhsvdlr 84
Cdd:cd01937     1 KIVIIGHVTIDEIVTNG------------SGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLF------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  85 yvvlqtegsIPTSTVIINEASGSRTILHAYRNLPDVsakdfekvdltrfKWIHIEGRNASEQVKMLQRIE-EHNAKQPLP 163
Cdd:cd01937    60 ---------DNGIEVISLLSTETTTFELNYTNEGRT-------------RTLLAKCAAIPDTESPLSTITaEIVILGPVP 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 164 QKV-RVSVEIEKP---------------REELFQLFSYGEVVFVSKDVAKHLgfQSAVEALRGLysRVKKGATLVCAWAE 227
Cdd:cd01937   118 EEIsPSLFRKFAFisldaqgflrranqeKLIKCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGE 193

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151099508 228 EGA---DALGPDgqllhsdAFPPPR--VVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 288
Cdd:cd01937   194 EGGyifDGNGKY-------TIPASKkdVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 202-286 2.70e-05

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 44.80  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 202 QSAVEALRGLYSRVKKGATLVCAwAEEGADALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:COG2870   221 EELVAAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELA 298


                  ....*
gi 1151099508 282 CQVAG 286
Cdd:COG2870   299 NLAAG 303
PRK11142 PRK11142
ribokinase; Provisional
 233-281 2.72e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 44.86  E-value: 2.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1151099508 233 LGPDGQLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:PRK11142  222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 172-282 5.47e-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: 43.99  E-value: 5.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 172 IEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSRVKKgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRV 250
Cdd:cd01946   150 ISIKPEKLKKVLAKVDVVIINDGEARQLtGAANLVKAARLILAMGPK--ALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1151099508 251 VDTLGAGDTFNASVIFSL-SKGNSMQEALRFGC 282
Cdd:cd01946   227 FDPTGAGDTFAGGFIGYLaSQKDTSEANMRRAI 259
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 227-290 1.01e-04

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


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 43.32  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151099508 227 EEGADALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCG 290
Cdd:cd01172   228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 19-276 1.09e-03

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 39.92  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  19 VVDKYPEEDTDR-RCLsqrwqrGGNASNSCTVLSLLGARCAFMGSLAPGHVADFVLDDLRQHSVDLRYVVLQTEGSipTS 97
Cdd:PRK09434   12 VVDLIPEGENRYlKCP------GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHR--TS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508  98 TVIIN-EASGSRTILHAYRnlPdvSAKDF-EKVDLTRFK---WIHI--------EGRNASEQVkmLQRIEEHNAKQPLPQ 164
Cdd:PRK09434   84 TVVVDlDDQGERSFTFMVR--P--SADLFlQPQDLPPFRqgeWLHLcsialsaePSRSTTFEA--MRRIKAAGGFVSFDP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151099508 165 KVRVSV--EIEKPREELFQLFSYGEVVFVSKDvakHLGF-------QSAVEALRGLYSR----VKKGATLVCAWAEegad 231
Cdd:PRK09434  158 NLREDLwqDEAELRECLRQALALADVVKLSEE---ELCFlsgtsqlEDAIYALADRYPIalllVTLGAEGVLVHTR---- 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1151099508 232 algpdGQLLHsdaFPPPRV--VDTLGAGDTFNASVIFSLSKGNSMQE 276
Cdd:PRK09434  231 -----GQVQH---FPAPSVdpVDTTGAGDAFVAGLLAGLSQAGLWTD 269
fruK PRK09513
1-phosphofructokinase; Provisional
 219-285 1.87e-03

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 39.29  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151099508 219 ATLVCAWAEEGADALGPDGQLLhsdAFPPP-RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PRK09513  218 AHVVISLGAEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
 
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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