|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-295 |
5.16e-139 |
|
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: 394.08 E-value: 5.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HlvSHP-ESSFPTSIVISSASRGTRTILHTNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaH 163
Cdd:cd01939 81 H--CYRkDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 164 QRVSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSD 243
Cdd:cd01939 158 IRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2129534694 244 AFPPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 295
Cdd:cd01939 238 AHKPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-293 |
1.30e-42 |
|
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: 148.11 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESsfPTSI-VISSASRGTRTILHTNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYN 157
Cdd:COG0524 81 GVRRDPGA--PTGLaFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 158 QTC---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRvrPGATVICAWAEAGADAL 233
Cdd:COG0524 159 VPVsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLAR--GVKLVVVTLGAEGALLY 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 234 GpDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:COG0524 233 T-GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-293 |
1.54e-24 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 100.11 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESsfPTSIVISSASRGTRTILHTNRNLP-DVTAQDFEQV--DLTQYKWIHWEGRNAAE-QVKMIQRVEEynqTC 160
Cdd:pfam00294 79 YVVIDEDT--RTGTALIEVDGDGERTIVFNRGAAaDLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIE---AA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 161 PAHQRVSTSV--EVEKPREELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALG 234
Cdd:pfam00294 154 KNGGTFDPNLldPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129534694 235 PDGElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:pfam00294 234 GDGE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
4-293 |
3.99e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.28 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 4 KRILCIGLVCldiisvVDMYPAEDtdtrclsqRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVEL 83
Cdd:PRK09813 1 KKLATIGDNC------VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 84 PHLVSHPESSFPTSIVISSASRgtrtIL--HTNRNLPDVTAQDFEQVDLTQYKWIH---WEgrNAAEQVKMIQRveeynq 158
Cdd:PRK09813 67 SHVHTKHGVTAQTQVELHDNDR----VFgdYTEGVMADFALSEEDYAWLAQYDIVHaaiWG--HAEDAFPQLHA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 159 tcpAHQRVStsvevekpreelyqlFGYADVV---FVSKDVAK-DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEA 228
Cdd:PRK09813 135 ---AGKLTA---------------FDFSDKWdspLWQTLVPHlDYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGEN 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129534694 229 GAdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:PRK09813 196 GS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
203-285 |
2.77e-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: 53.76 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 203 SAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 282
Cdd:TIGR02152 195 DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFNGAFAVALAEGKSLEDAIRFAN 270
|
...
gi 2129534694 283 QVA 285
Cdd:TIGR02152 271 AAA 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-295 |
5.16e-139 |
|
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: 394.08 E-value: 5.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HlvSHP-ESSFPTSIVISSASRGTRTILHTNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaH 163
Cdd:cd01939 81 H--CYRkDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 164 QRVSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSD 243
Cdd:cd01939 158 IRITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2129534694 244 AFPPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 295
Cdd:cd01939 238 AHKPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-293 |
1.30e-42 |
|
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: 148.11 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESsfPTSI-VISSASRGTRTILHTNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYN 157
Cdd:COG0524 81 GVRRDPGA--PTGLaFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 158 QTC---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRvrPGATVICAWAEAGADAL 233
Cdd:COG0524 159 VPVsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLAR--GVKLVVVTLGAEGALLY 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 234 GpDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:COG0524 233 T-GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-293 |
1.37e-35 |
|
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: 129.34 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPES-SFPTSIVISSASRGTRTIlhtNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRveeynqtcpAH 163
Cdd:cd01945 81 FIVVAPGArSPISSITDITGDRATISI---TAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQE---------AR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 164 QR---VSTSVEVEKPR--EELYQLfgyADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPgaTVICAWAEAGADALGPDGE 238
Cdd:cd01945 149 ARgipIPLDLDGGGLRvlEELLPL---ADHAICSENFLRPNTGSADDEALELLASLGIP--FVAVTLGEAGCLWLERDGE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2129534694 239 LVHSDAFpPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01945 224 LFHVPAF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-293 |
1.28e-28 |
|
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: 111.13 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIIsvvdmypAEDTDTRCLSQRWQR--GGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVE 82
Cdd:cd01166 1 DVVTIGEVMVDLS-------PPGGGRLEQADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 83 LPHLVSHPESsfPTSI-VISSASRGTRTILHtNRN---LPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQ 158
Cdd:cd01166 74 TSHVRVDPGR--PTGLyFLEIGAGGERRVLY-YRAgsaASRLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 159 TCPAHQrVSTSVEV---------EKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRVRPGATVICAWAEA 228
Cdd:cd01166 151 AAKARG-VTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEEEAEAlLGDEDPTDAAERALALALGVKAVVVKLGAE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129534694 229 GADALGpDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01166 230 GALVYT-GGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-293 |
1.54e-24 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 100.11 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESsfPTSIVISSASRGTRTILHTNRNLP-DVTAQDFEQV--DLTQYKWIHWEGRNAAE-QVKMIQRVEEynqTC 160
Cdd:pfam00294 79 YVVIDEDT--RTGTALIEVDGDGERTIVFNRGAAaDLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIE---AA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 161 PAHQRVSTSV--EVEKPREELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALG 234
Cdd:pfam00294 154 KNGGTFDPNLldPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129534694 235 PDGElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:pfam00294 234 GDGE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-293 |
1.24e-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: 98.07 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 3 EKRILCIGLVCLDIISVVDMYPAEDTD----TRCLSQRWQR-------------GGNASNSCTVLSLLGAPCAFMGSLAP 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 66 GHAADFVLADLRRYAVELpHLVSHPESsfPTsivissasrGTRTILHT-------NRNL---PDVTAQDFEQVDLTQYKW 135
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDT-RYQVQPDG--PT---------GTCAVLVTpdaertmCTYLgaaNELSPDDLDWSLLAKAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 136 IHWEGRNAAEQVKMIQRVEEYnqtcpAHQ---RVSTSV----EVEKPREELYQLFGYADVVFVSKDVAKDFG---FHSAP 205
Cdd:cd01168 149 LYLEGYLLTVPPEAILLAAEH-----AKEngvKIALNLsapfIVQRFKEALLELLPYVDILFGNEEEAEALAeaeTTDDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 206 E-AVKRLRSRVRpgaTVICAwaeAGADA--LGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 282
Cdd:cd01168 224 EaALKLLALRCR---IVVIT---QGAKGavVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGS 297
|
330
....*....|.
gi 2129534694 283 QVAGRKCGVHG 293
Cdd:cd01168 298 YAAAEVIQQLG 308
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
5-293 |
4.76e-19 |
|
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: 84.71 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDI-ISVVDMYPaedtdtrclsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVEL 83
Cdd:cd01940 1 RLAAIGDNVVDKyLHLGKMYP---------------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 84 PHL-VSHPESSFpTSIVISSasrGTRTILHTN-----RNLPDvtAQDFEQvdLTQYKWIH---WEGRNAAEqvkmiqrvE 154
Cdd:cd01940 66 SHCrVKEGENAV-ADVELVD---GDRIFGLSNkggvaREHPF--EADLEY--LSQFDLVHtgiYSHEGHLE--------K 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 155 EYNQTCPAHQRVSTSVEVEKPREELYQLFGYADVVFVSkdvAKDFgfhSAPEAVKRLRSRVRPGATVICawAEAGAD-AL 233
Cdd:cd01940 130 ALQALVGAGALISFDFSDRWDDDYLQLVCPYVDFAFFS---ASDL---SDEEVKAKLKEAVSRGAKLVI--VTRGEDgAI 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129534694 234 GPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQ-RLQEALTFGCQVAGRKCGVHG 293
Cdd:cd01940 202 AYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEG 262
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-293 |
8.10e-16 |
|
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: 76.14 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDmyPAEDTDTRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:cd01167 1 KVVCFGEALIDFIPEGS--GAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESsfPTSIV-ISSASRGTRT----------ILHTNRNLPDVtaqdfeqvdLTQYKWIH--------WEGRNAAE 145
Cdd:cd01167 73 GIQFDPAA--PTTLAfVTLDADGERSfefyrgpaadLLLDTELNPDL---------LSEADILHfgsialasEPSRSALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 146 QVkmIQRVEEYNQTC-------PAHQRvstsvEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEavKRLRSRVRPG 218
Cdd:cd01167 142 EL--LEAAKKAGVLIsfdpnlrPPLWR-----DEEEARERIAELLELADIVKLSDEELELLFGEEDPE--EIAALLLLFG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 219 -ATVICAWAEAGADALGPDGElVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQ-------RLQEALTFGCQVAGRKCG 290
Cdd:cd01167 213 lKLVLVTRGADGALLYTKGGV-GEVPGIPVEV-VDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCT 290
|
...
gi 2129534694 291 VHG 293
Cdd:cd01167 291 KAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-288 |
1.20e-15 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 75.43 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELP 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESSFPTSIVIssASRGTRTILHTNRNlpdvTAQDFEQVDLTQYkwihwEGRNAAEQVKMIQRVEEYNQTC-PAH 163
Cdd:cd01942 81 HVRVVDEDSTGVAFIL--TDGDDNQIAYFYPG----AMDELEPNDEADP-----DGLADIVHLSSGPGLIELARELaAGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 164 QRVS---TSVEVEKPREELYQLFGYADVVFVSKDVAKDF----GFHSAPEAVKrlrsrVRpgaTVICAWAEAGADALGPD 236
Cdd:cd01942 150 ITVSfdpGQELPRLSGEELEEILERADILFVNDYEAELLkertGLSEAELASG-----VR---VVVVTLGPKGAIVFEDG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2129534694 237 GELVHsDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRK 288
Cdd:cd01942 222 EEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
5-286 |
6.11e-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: 61.67 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGnASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRryAVELP 84
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMR--DEGIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 HLVSHPESSFPTSIVISSASRGTRTILHTNRNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPAHQ 164
Cdd:cd01944 78 ILLPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 165 --------RVStsvevEKPREELYQLFGYADVVFVSKDVAKDF-GFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGP 235
Cdd:cd01944 158 tlvfdpgpRIS-----DIPDTILQALMAKRPIWSCNREEAAIFaERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2129534694 236 DGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAG 286
Cdd:cd01944 233 DGNTHIIPGFK-VKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-268 |
1.35e-10 |
|
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: 59.42 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFmgslapgHAADFVLADLRRYAVELp 84
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTL-------VGADAVVISGLSPAPEA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 85 hlvshpessfpTSIVISSASRgtrtilhtnRNLPDVtaqdfeqVDLTqykwihwegrnaaeqvkmiqrveeynqtcpahq 164
Cdd:cd00287 73 -----------VLDALEEARR---------RGVPVV-------LDPG--------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 165 rvstSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGA----TVICAWAEAGADALGPDGELV 240
Cdd:cd00287 93 ----PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSkgpkVVIVTLGEKGAIVATRGGTEV 168
|
250 260
....*....|....*....|....*...
gi 2129534694 241 HSDAFPPEtIVDTLGAGDTFNAAVLFAL 268
Cdd:cd00287 169 HVPAFPVK-VVDTTGAGDAFLAALAAGL 195
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-292 |
4.44e-10 |
|
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: 58.97 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 6 ILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVELPH 85
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 86 LVSHPESSFPTSIVissASRGTRTILHTNRNLPDvtaqDFEQVDLTQYKWIHWegrNAAEQVKMIQRVEEYN-----QTC 160
Cdd:cd01947 82 AWRDKPTRKTLSFI---DPNGERTITVPGERLED----DLKWPILDEGDGVFI---TAAAVDKEAIRKCRETklvilQVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 161 PaHQRVSTSVEVEKPreelyqlfgyADVVFVSKDvakDFGFHSAPEAVKRLRSRvrpgaTVICAWAEAGAdALGPDGELV 240
Cdd:cd01947 152 P-RVRVDELNQALIP----------LDILIGSRL---DPGELVVAEKIAGPFPR-----YLIVTEGELGA-ILYPGGRYN 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2129534694 241 HSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVaGRKCGVH 292
Cdd:cd01947 212 HVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQC-GAICVSH 261
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
201-293 |
1.06e-09 |
|
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: 58.33 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 201 FHSAPEAVKRLRSRvrPGATVICAWAEAGAdALGPDGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTF 280
Cdd:cd01174 197 EEDAEKAARLLLAK--GVKNVIVTLGAKGA-LLASGGEVEHVPAFK-VKAVDTTGAGDTFIGALAAALARGLSLEEAIRF 272
|
90
....*....|...
gi 2129534694 281 GCQVAGRKCGVHG 293
Cdd:cd01174 273 ANAAAALSVTRPG 285
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
4-293 |
3.99e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.28 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 4 KRILCIGLVCldiisvVDMYPAEDtdtrclsqRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAADFVLADLRRYAVEL 83
Cdd:PRK09813 1 KKLATIGDNC------VDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 84 PHLVSHPESSFPTSIVISSASRgtrtIL--HTNRNLPDVTAQDFEQVDLTQYKWIH---WEgrNAAEQVKMIQRveeynq 158
Cdd:PRK09813 67 SHVHTKHGVTAQTQVELHDNDR----VFgdYTEGVMADFALSEEDYAWLAQYDIVHaaiWG--HAEDAFPQLHA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 159 tcpAHQRVStsvevekpreelyqlFGYADVV---FVSKDVAK-DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEA 228
Cdd:PRK09813 135 ---AGKLTA---------------FDFSDKWdspLWQTLVPHlDYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGEN 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129534694 229 GAdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 293
Cdd:PRK09813 196 GS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
203-285 |
2.77e-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: 53.76 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 203 SAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 282
Cdd:TIGR02152 195 DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFNGAFAVALAEGKSLEDAIRFAN 270
|
...
gi 2129534694 283 QVA 285
Cdd:TIGR02152 271 AAA 273
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
40-293 |
1.74e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 52.12 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 40 GGNASNSCTVLSLLGAP--------CAFMGSLAPGHAADFVLADLRRYAVelpHLVSHP--ESSFPTSIVISS------- 102
Cdd:PLN02813 126 GGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANV---HFLSQPvkDGTTGTVIVLTTpdaqrtm 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 103 -ASRGTRTILhtnrNLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPAHQRVSTSVeVEKPREELYQ 181
Cdd:PLN02813 203 lSYQGTSSTV----NYDSCLASAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDVSC-IERHRDDFWD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 182 LFG-YADVVFVSKDVAK---DFGFHSAPEAVKRLRSRVRPGATVIcawAEAGADALGPDGElVHSDAFPPETIVDTLGAG 257
Cdd:PLN02813 278 VMGnYADILFANSDEARalcGLGSEESPESATRYLSHFCPLVSVT---DGARGSYIGVKGE-AVYIPPSPCVPVDTCGAG 353
|
250 260 270
....*....|....*....|....*....|....*..
gi 2129534694 258 DTFNAAVLFALSRG-QRLQEALTFGCQVAGRKCGVHG 293
Cdd:PLN02813 354 DAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQG 390
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
31-281 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 31 RCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLApGHAADFVLADLRRYAVElPHLVSHPESSfPTSIVISSASRGTRTI 110
Cdd:COG1105 26 RASEVRLDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIP-TDFVPIEGET-RINIKIVDPSDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 111 LhtnrNL--PDVTAQDFEQVdLTQYKWIHWEG----------RNAAEQ--VKMIQRVEEYNQTC-------PAHQRVSTS 169
Cdd:COG1105 103 I----NEpgPEISEEELEAL-LERLEELLKEGdwvvlsgslpPGVPPDfyAELIRLARARGAKVvldtsgeALKAALEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 170 VEVEKP-REELYQLFGY-----ADVVfvskdvakdfgfhsapEAVKRLRSRvrpGATVICAwaeagadALGPDGEL-VHS 242
Cdd:COG1105 178 PDLIKPnLEELEELLGRpletlEDII----------------AAARELLER---GAENVVV-------SLGADGALlVTE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2129534694 243 DAF-----PPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFG 281
Cdd:COG1105 232 DGVyrakpPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
206-286 |
6.97e-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: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 206 EAVKRLRSRVRPGATVICAwAEAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVA 285
Cdd:COG2870 225 AAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELANLAA 302
|
.
gi 2129534694 286 G 286
Cdd:COG2870 303 G 303
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
251-281 |
1.05e-04 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 42.93 E-value: 1.05e-04
10 20 30
....*....|....*....|....*....|.
gi 2129534694 251 VDTLGAGDTFNAAVLFALSRGQRLQEALTFG 281
Cdd:PRK11142 246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
233-288 |
1.13e-04 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 43.07 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129534694 233 LGPDGELVHSDA-------FPP---ETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGcQVAGRK 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 ... |
185-288 |
4.57e-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: 40.85 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 185 YADVVFVSKDVAKDFgfHSAPEAVKRLRsrVRPGATVICAWAEAGADALgpDGELVHSDAFPPETIVDTLGAGDTFNAAV 264
Cdd:cd01937 155 LHDVLKLSRVEAEVI--STPTELARLIK--ETGVKEIIVTDGEEGGYIF--DGNGKYTIPASKKDVVDPTGAGDVFLAAF 228
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90 100
....*....|....*....|....
gi 2129534694 265 LFALSRGQRLQEALTFGCQVAGRK 288
Cdd:cd01937 229 LYSRLSGKDIKEAAEFAAAAAAKF 252
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|
| 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 2129534694 172 VEKPREELYQLFGYADVVFVSKDVAKDFGfhSAPEAVKRLRSRVRPGA-TVICAWAEAGAdALGPDGELVHSDAFPPETI 250
Cdd:cd01946 150 ISIKPEKLKKVLAKVDVVIINDGEARQLT--GAANLVKAARLILAMGPkALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226
|
90 100
....*....|....*....|....*..
gi 2129534694 251 VDTLGAGDTFNAAVLFALSRGQRLQEA 277
Cdd:cd01946 227 FDPTGAGDTFAGGFIGYLASQKDTSEA 253
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|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
172-282 |
9.81e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 40.16 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534694 172 VEKPREELYQLF--GYADVVFVSKDVAKDF---GFHSAPEAVKRLRSRVrpgatviCAWAEAgadALGPDG-------EL 239
Cdd:PLN02379 217 VRNFRSPLLQLLesGKIDLCFANEDEARELlrgEQESDPEAALEFLAKY-------CNWAVV---TLGSKGciarhgkEV 286
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2129534694 240 VHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 282
Cdd:PLN02379 287 VRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
233-276 |
2.68e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 38.76 E-value: 2.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2129534694 233 LGPDGELVHSD------AFPPETIVDTLGAGDTFNAAVLFALSRGQRLQE 276
Cdd:PRK09434 220 LGAEGVLVHTRgqvqhfPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTD 269
|
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| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
227-290 |
6.08e-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: 6.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534694 227 EAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCG 290
Cdd:cd01172 228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
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