|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-250 |
1.15e-123 |
|
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: 353.25 E-value: 1.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAE-------------- 70
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFEsllddfqsrgidis 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 71 ------------------------------NLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaHQR 120
Cdd:cd01939 81 hcyrkdidepassyiirsraggrttivndnNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 121 VSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDAF 200
Cdd:cd01939 160 ITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2129534696 201 PPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 250
Cdd:cd01939 240 KPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-248 |
6.60e-29 |
|
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: 110.74 E-value: 6.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENL------------ 72
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLlaelraegvdts 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 73 --------------------------------PDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYNQT 114
Cdd:COG0524 81 gvrrdpgaptglafilvdpdgertivfyrganAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 115 C---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRvrPGATVICAWAEAGADALGp 190
Cdd:COG0524 161 VsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLAR--GVKLVVVTLGAEGALLYT- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2129534696 191 DGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:COG0524 234 GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-248 |
8.90e-18 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 80.46 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENLPDVTAQdfEQVD 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKK--EGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 85 LTQYKWIH---------------------WEGRNAAEQVKMIQRVEEYNQtCPAHQRVSTSVEVEKP------------- 130
Cdd:pfam00294 77 TDYVVIDEdtrtgtalievdgdgertivfNRGAAADLTPEELEENEDLLE-NADLLYISGSLPLGLPeatleelieaakn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 131 ---------------REELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALGPD 191
Cdd:pfam00294 156 ggtfdpnlldplgaaREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2129534696 192 GElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:pfam00294 236 GE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
153-248 |
1.66e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.97 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 153 DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEAGAdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRG 226
Cdd:PRK09813 160 DYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAG 236
|
90 100
....*....|....*....|..
gi 2129534696 227 QRLQEALTFGCQVAGRKCGVHG 248
Cdd:PRK09813 237 MTLPQAMAQGTACAAKTIQYHG 258
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
158-240 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 158 SAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 237
Cdd:TIGR02152 195 DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFNGAFAVALAEGKSLEDAIRFAN 270
|
...
gi 2129534696 238 QVA 240
Cdd:TIGR02152 271 AAA 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
5-250 |
1.15e-123 |
|
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: 353.25 E-value: 1.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAE-------------- 70
Cdd:cd01939 1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFEsllddfqsrgidis 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 71 ------------------------------NLPDVTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCPaHQR 120
Cdd:cd01939 81 hcyrkdidepassyiirsraggrttivndnNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 121 VSTSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDAF 200
Cdd:cd01939 160 ITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2129534696 201 PPETIVDTLGAGDTFNAAVLFALSRGQR-LQEALTFGCQVAGRKCGVHGYD 250
Cdd:cd01939 240 KPIRVVDTLGAGDTFNAAVIYALNKGPDdLSEALDFGNRVASQKCTGVGFD 290
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-248 |
6.60e-29 |
|
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: 110.74 E-value: 6.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENL------------ 72
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLlaelraegvdts 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 73 --------------------------------PDVTAQDFEQVDLTQYKWIHWEGRNAAE------QVKMIQRVEEYNQT 114
Cdd:COG0524 81 gvrrdpgaptglafilvdpdgertivfyrganAELTPEDLDEALLAGADILHLGGITLASeppreaLLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 115 C---PAHQrvstSVEVEKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRvrPGATVICAWAEAGADALGp 190
Cdd:COG0524 161 VsldPNYR----PALWEPARELLRELLALVDILFPNEEEAELlTGETDPEEAAAALLAR--GVKLVVVTLGAEGALLYT- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2129534696 191 DGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:COG0524 234 GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-248 |
8.75e-26 |
|
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: 101.99 E-value: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENLPDVTAQdfEQVD 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAA--EGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 85 LTQYKwihwEGRNAAEQVKMIQRVEEYNQTCP----------------------------------------AHQR---V 121
Cdd:cd01945 79 TSFIV----VAPGARSPISSITDITGDRATISitaidtqaapdslpdailggadavlvdgrqpeaalhlaqeARARgipI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 122 STSVEVEKPR--EELYQLfgyADVVFVSKDVAKDFGFHSAPEAVKRLRSRVRPgaTVICAWAEAGADALGPDGELVHSDA 199
Cdd:cd01945 155 PLDLDGGGLRvlEELLPL---ADHAICSENFLRPNTGSADDEALELLASLGIP--FVAVTLGEAGCLWLERDGELFHVPA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2129534696 200 FPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:cd01945 230 FP-VEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-248 |
4.09e-19 |
|
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: 84.16 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIIsvvdmypAEDTDTRCLSQRWQR--GGNASNSCTVLSLLGAPCAFMGSL---APGHAA---------- 69
Cdd:cd01166 1 DVVTIGEVMVDLS-------PPGGGRLEQADSFRKffGGAEANVAVGLARLGHRVALVTAVgddPFGRFIlaelrregvd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 70 -----------------ENLPD----------------VTAQDFEQVDLTQYKWIHWEGRNAAEQVKMIQRVEEYNQTCP 116
Cdd:cd01166 74 tshvrvdpgrptglyflEIGAGgerrvlyyragsaasrLTPEDLDEAALAGADHLHLSGITLALSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 117 AHQrVSTSVEV---------EKPREELYQLFGYADVVFVSKDVAKD-FGFHSAPEAVKRLRSRVRPGATVICAWAEAGAD 186
Cdd:cd01166 154 ARG-VTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEEEAEAlLGDEDPTDAAERALALALGVKAVVVKLGAEGAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129534696 187 ALGpDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:cd01166 233 VYT-GGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-248 |
8.90e-18 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 80.46 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRwqRGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENLPDVTAQdfEQVD 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKK--EGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 85 LTQYKWIH---------------------WEGRNAAEQVKMIQRVEEYNQtCPAHQRVSTSVEVEKP------------- 130
Cdd:pfam00294 77 TDYVVIDEdtrtgtalievdgdgertivfNRGAAADLTPEELEENEDLLE-NADLLYISGSLPLGLPeatleelieaakn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 131 ---------------REELYQLFGYADVVFVSKDVAKDFGFH---SAPEAVKRLRSRVRPGA-TVICAWAEAGADALGPD 191
Cdd:pfam00294 156 ggtfdpnlldplgaaREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2129534696 192 GElVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGVHG 248
Cdd:pfam00294 236 GE-VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-248 |
2.04e-15 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 74.19 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 3 EKRILCIGLVCLDIISVVDMYPAEDTD----TRCLSQRWQR-------------GGNASNSCTVLSLLGAPCAFMGSLA- 64
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 65 ------------------------------------PGH---------AAENLpdvTAQDFEQVDLTQYKWIHWEGRNAA 99
Cdd:cd01168 81 dklgdfllkdlraagvdtryqvqpdgptgtcavlvtPDAertmctylgAANEL---SPDDLDWSLLAKAKYLYLEGYLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 100 EQVKMIQRVEEYnqtcpAHQ---RVSTSV----EVEKPREELYQLFGYADVVFVSKDVAKDFGF----HSAPEAVKRLRS 168
Cdd:cd01168 158 VPPEAILLAAEH-----AKEngvKIALNLsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEaettDDLEAALKLLAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 169 RVRpgaTVICAwaeAGADA--LGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCGV 246
Cdd:cd01168 233 RCR---IVVIT---QGAKGavVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306
|
..
gi 2129534696 247 HG 248
Cdd:cd01168 307 LG 308
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-223 |
2.30e-15 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 72.13 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGslapghaaenlpdvtaqdfeqvd 84
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 85 ltqYKWIHWEGRN--AAEQVKMIQRVEEYNQT---CPAhqrvstSVEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSA 159
Cdd:cd00287 58 ---ADAVVISGLSpaPEAVLDALEEARRRGVPvvlDPG------PRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRD 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129534696 160 PEAVKRLRSRVRPGA----TVICAWAEAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFAL 223
Cdd:cd00287 129 LEVKEAAEAAALLLSkgpkVVIVTLGEKGAIVATRGGTEVHVPAFPVK-VVDTTGAGDAFLAALAAGL 195
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
5-248 |
1.76e-13 |
|
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: 68.15 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDI-ISVVDMYPaedtdtrclsqrwqrGGNASNSCTVLSLLGAPCAFMGSLAPGHAAENLPDVTAQdfEQV 83
Cdd:cd01940 1 RLAAIGDNVVDKyLHLGKMYP---------------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKR--LGV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 84 DLTQYKwiHWEGRNAAEQVKMIQ--RV-EEYNQTCPAHQR--------------VSTSV-EVEKPREELYQLFGYADVVf 145
Cdd:cd01940 64 DISHCR--VKEGENAVADVELVDgdRIfGLSNKGGVAREHpfeadleylsqfdlVHTGIySHEGHLEKALQALVGAGAL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 146 VSKDVAK--------------DFGFHSAP----EAVKR-LRSRVRPGATVICAwaEAGAD-ALGPDGELVHSDAFPPETI 205
Cdd:cd01940 141 ISFDFSDrwdddylqlvcpyvDFAFFSASdlsdEEVKAkLKEAVSRGAKLVIV--TRGEDgAIAYDGAVFYSVAPRPVEV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2129534696 206 VDTLGAGDTFNAAVLFALSRGQ-RLQEALTFGCQVAGRKCGVHG 248
Cdd:cd01940 219 VDTLGAGDSFIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-243 |
1.69e-12 |
|
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: 65.41 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDMYPAEDTDTRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSLAP------------------G 66
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEdfhgrlyleelreegvdtS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 67 HAAENLPDVTAQDFEQVD----------------LTQYKWIHWEGRNAAEQVKMIQRVEEYNQTC-PAHQRVS---TSVE 126
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDgddnqiayfypgamdeLEPNDEADPDGLADIVHLSSGPGLIELARELaAGGITVSfdpGQEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 127 VEKPREELYQLFGYADVVFVSKDVAKDF----GFHSAPEAVKrlrsrVRpgaTVICAWAEAGADALGPDGELVHsDAFPP 202
Cdd:cd01942 161 PRLSGEELEEILERADILFVNDYEAELLkertGLSEAELASG-----VR---VVVVTLGPKGAIVFEDGEEVEV-PAVPA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2129534696 203 ETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRK 243
Cdd:cd01942 232 VKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
5-248 |
3.74e-11 |
|
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: 61.88 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 5 RILCIGLVCLDIISVVDmyPAEDTDTRCLsqrwqrGGNASNSCTVLSLLGAPCAFMGSL--------------------- 63
Cdd:cd01167 1 KVVCFGEALIDFIPEGS--GAPETFTKAP------GGAPANVAVALARLGGKAAFIGKVgddefgdflletlkeagvdtr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 64 -------AP--------------------GHAAENLPDVTAQDfeqVDLTQYKWIH--------WEGRNAAEQVkmIQRV 108
Cdd:cd01167 73 giqfdpaAPttlafvtldadgersfefyrGPAADLLLDTELNP---DLLSEADILHfgsialasEPSRSALLEL--LEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 109 EEYNQTC-------PAHQRvstsvEVEKPREELYQLFGYADVVFVSKDVAKDFGFHSAPEavKRLRSRVRPG-ATVICAW 180
Cdd:cd01167 148 KKAGVLIsfdpnlrPPLWR-----DEEEARERIAELLELADIVKLSDEELELLFGEEDPE--EIAALLLLFGlKLVLVTR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129534696 181 AEAGADALGPDGElVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQ-------RLQEALTFGCQVAGRKCGVHG 248
Cdd:cd01167 221 GADGALLYTKGGV-GEVPGIPVEV-VDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
156-248 |
8.10e-10 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 57.95 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 156 FHSAPEAVKRLRSRvrPGATVICAWAEAGAdALGPDGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTF 235
Cdd:cd01174 197 EEDAEKAARLLLAK--GVKNVIVTLGAKGA-LLASGGEVEHVPAFK-VKAVDTTGAGDTFIGALAAALARGLSLEEAIRF 272
|
90
....*....|...
gi 2129534696 236 GCQVAGRKCGVHG 248
Cdd:cd01174 273 ANAAAALSVTRPG 285
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
153-248 |
1.66e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.97 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 153 DFGFHSAPEAVKRLRSRVR------PGaTVICAWAEAGAdaLGPDGELVHSDAFPPETIVDTLGAGDTFNAAVLFALSRG 226
Cdd:PRK09813 160 DYAFASAPQEDEFLRLKMKaivargAG-VVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAG 236
|
90 100
....*....|....*....|..
gi 2129534696 227 QRLQEALTFGCQVAGRKCGVHG 248
Cdd:PRK09813 237 MTLPQAMAQGTACAAKTIQYHG 258
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
158-240 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 158 SAPEAVKRLRSRVRpgATVICAWAEAGADALGPDgELVHSDAFPPETiVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 237
Cdd:TIGR02152 195 DAEKAAEKLLEKGV--KNVIITLGSKGALLVSKD-ESKLIPAFKVKA-VDTTAAGDTFNGAFAVALAEGKSLEDAIRFAN 270
|
...
gi 2129534696 238 QVA 240
Cdd:TIGR02152 271 AAA 273
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
129-236 |
3.39e-07 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 50.13 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 129 KP-REELYQLFGY-----ADVVfvskdvakdfgfhsapEAVKRLRSRvrpGATVICAwaeagadALGPDGEL-VHSDAF- 200
Cdd:COG1105 182 KPnLEELEELLGRpletlEDII----------------AAARELLER---GAENVVV-------SLGADGALlVTEDGVy 235
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2129534696 201 ----PPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFG 236
Cdd:COG1105 236 rakpPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
159-241 |
2.00e-06 |
|
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: 47.80 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 159 APEAVKRLRSRVRPGATVICAWAEAGADALGPDGELVHSDAFPpETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQ 238
Cdd:cd01944 201 PAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFK-VKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANA 279
|
...
gi 2129534696 239 VAG 241
Cdd:cd01944 280 AAA 282
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
127-248 |
5.87e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 46.73 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 127 VEKPREELYQLFG-YADVVFVSKDVAK---DFGFHSAPEAVKRLRSRVRPGATVIcawaeAGADA--LGPDGElVHSDAF 200
Cdd:PLN02813 268 IERHRDDFWDVMGnYADILFANSDEARalcGLGSEESPESATRYLSHFCPLVSVT-----DGARGsyIGVKGE-AVYIPP 341
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2129534696 201 PPETIVDTLGAGDTFNAAVLFALSRG-QRLQEALTFGCQVAGRKCGVHG 248
Cdd:PLN02813 342 SPCVPVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQG 390
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
161-241 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 161 EAVKRLRSRVRPGATVICAwAEAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVA 240
Cdd:COG2870 225 AAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELANLAA 302
|
.
gi 2129534696 241 G 241
Cdd:COG2870 303 G 303
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
132-247 |
6.99e-05 |
|
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: 43.18 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 132 EELYQLFGYADVVFVSKDvakDFGFHSAPEAVKRLRSRvrpgaTVICAWAEAGAdALGPDGELVHSDAFPPEtIVDTLGA 211
Cdd:cd01947 157 DELNQALIPLDILIGSRL---DPGELVVAEKIAGPFPR-----YLIVTEGELGA-ILYPGGRYNHVPAKKAK-VPDSTGA 226
|
90 100 110
....*....|....*....|....*....|....*.
gi 2129534696 212 GDTFNAAVLFALSRGQRLQEALTFGCQVaGRKCGVH 247
Cdd:cd01947 227 GDSFAAGFIYGLLKGWSIEEALELGAQC-GAICVSH 261
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
188-243 |
7.00e-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: 43.07 E-value: 7.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129534696 188 LGPDGELVHSDA-------FPP---ETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGcQVAGRK 243
Cdd:cd01941 220 LGAKGVLLSSREggvetklFPApqpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
206-236 |
8.08e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 42.93 E-value: 8.08e-05
10 20 30
....*....|....*....|....*....|.
gi 2129534696 206 VDTLGAGDTFNAAVLFALSRGQRLQEALTFG 236
Cdd:PRK11142 246 VDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
140-243 |
2.92e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 41.23 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 140 YADVVFVSKDVAKDFgfHSAPEAVKRLRsrVRPGATVICAWAEAGADALgpDGELVHSDAFPPETIVDTLGAGDTFNAAV 219
Cdd:cd01937 155 LHDVLKLSRVEAEVI--STPTELARLIK--ETGVKEIIVTDGEEGGYIF--DGNGKYTIPASKKDVVDPTGAGDVFLAAF 228
|
90 100
....*....|....*....|....
gi 2129534696 220 LFALSRGQRLQEALTFGCQVAGRK 243
Cdd:cd01937 229 LYSRLSGKDIKEAAEFAAAAAAKF 252
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
127-232 |
3.37e-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: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 127 VEKPREELYQLFGYADVVFVSKDVAKDFGfhSAPEAVKRLRSRVRPGA-TVICAWAEAGAdALGPDGELVHSDAFPPETI 205
Cdd:cd01946 150 ISIKPEKLKKVLAKVDVVIINDGEARQLT--GAANLVKAARLILAMGPkALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226
|
90 100
....*....|....*....|....*..
gi 2129534696 206 VDTLGAGDTFNAAVLFALSRGQRLQEA 232
Cdd:cd01946 227 FDPTGAGDTFAGGFIGYLASQKDTSEA 253
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
127-237 |
1.19e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.77 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129534696 127 VEKPREELYQLF--GYADVVFVSKDVAKDF---GFHSAPEAVKRLRSRVrpgatviCAWAEAgadALGPDG-------EL 194
Cdd:PLN02379 217 VRNFRSPLLQLLesGKIDLCFANEDEARELlrgEQESDPEAALEFLAKY-------CNWAVV---TLGSKGciarhgkEV 286
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2129534696 195 VHSDAFPPETIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGC 237
Cdd:PLN02379 287 VRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
188-231 |
2.22e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 38.76 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2129534696 188 LGPDGELVHSD------AFPPETIVDTLGAGDTFNAAVLFALSRGQRLQE 231
Cdd:PRK09434 220 LGAEGVLVHTRgqvqhfPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTD 269
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
182-245 |
4.56e-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: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129534696 182 EAGADALGPDGELVHSDAFPPEtIVDTLGAGDTFNAAVLFALSRGQRLQEALTFGCQVAGRKCG 245
Cdd:cd01172 228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
|
|
| |
