|
Name |
Accession |
Description |
Interval |
E-value |
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-299 |
4.40e-133 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 379.61 E-value: 4.40e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 2 IYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLKNSAIQSNFI 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 82 EVDEDTRINVKLK--TGQETEINAPGPHITSAQFEQLLQQIKNTTSE-DIVIVAGSVPSSIPSDAYAQIAQITAQTGAKL 158
Cdd:TIGR03168 81 EVKGETRINVKIKesSGEETELNEPGPEISEEELEQLLEKLRELLASgDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 159 VVDAEKELAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQ 238
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586063391 239 GKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATAFDEDL--ATRDAIEKIKSQVT 299
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTglPDPEDVEELLDQVT 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-286 |
1.11e-131 |
|
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: 375.72 E-value: 1.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 1 MIYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLKNSAIQSNF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 81 IEVDEDTRINVKLKT--GQETEINAPGPHITSAQFEQLLQQIKNTTSE-DIVIVAGSVPSSIPSDAYAQIAQITAQTGAK 157
Cdd:cd01164 81 VEVAGETRINVKIKEedGTETEINEPGPEISEEELEALLEKLKALLKKgDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 158 LVVDAEKELAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNP 237
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 586063391 238 QGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATAFDEDLA 286
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-300 |
9.06e-131 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 373.85 E-value: 9.06e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 2 IYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLKNSAIQSNFI 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 82 EVDEDTRINVKLK--TGQETEINAPGPHITSAQFEQLLQQIK-NTTSEDIVIVAGSVPSSIPSDAYAQIAQITAQTGAKL 158
Cdd:TIGR03828 81 RVPGETRINVKIKepSGTETKLNGPGPEISEEELEALLEKLRaQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 159 VVDAEKELAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQ 238
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586063391 239 GKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATAFDED--LATRDAIEKIKSQVTI 300
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPEDIEELLPQVTI 304
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-299 |
1.49e-130 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 373.32 E-value: 1.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 2 IYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLKNSAIQSNFI 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 82 EVDEDTRINVKLK---TGQETEINAPGPHITSAQFEQLLQQIKNTTSE-DIVIVAGSVPSSIPSDAYAQIAQITAQTGAK 157
Cdd:COG1105 81 PIEGETRINIKIVdpsDGTETEINEPGPEISEEELEALLERLEELLKEgDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 158 LVVDAEKELAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNP 237
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586063391 238 QGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATAFDED--LATRDAIEKIKSQVT 299
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGtgLPDREDVEELLAQVE 304
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-263 |
8.28e-58 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 188.01 E-value: 8.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 1 MIYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLkNSAIQSNF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHL-DDQIKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 81 IEVDEDTR--INVkLKTGQETEINAPGPHIT---SAQFEQLLQQIKNTTseDIVIVAGSVPSSIPSDAYAQIAQITAQTG 155
Cdd:PRK13508 80 YKIKGETRncIAI-LHEGQQTEILEKGPEISvqeADGFLHHFKQLLESV--EVVAISGSLPAGLPVDYYAQLIELANQAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 156 AKLVVDAEKELAESVL--PYHPLFIKPNKDELEVMFNTTVNSDEDVIKygRLLVD---KGAQSVIVSLGGDGAIYIDKEI 230
Cdd:PRK13508 157 KPVVLDCSGAALQAVLesPYKPTVIKPNIEELSQLLGKEVSEDLDELK--EVLQQplfEGIEWIIVSLGADGAFAKHNDT 234
|
250 260 270
....*....|....*....|....*....|...
gi 586063391 231 SIKAVNPQGKVVNTVGSGDSTvagmVAGIASGL 263
Cdd:PRK13508 235 FYKVDIPKIEVVNPVGSGDST----VAGIASGL 263
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-303 |
1.04e-52 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 174.88 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 4 TVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAG-----GFPGKFiidtlKNSAIQS 78
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGkdnqdGFQQLF-----SELGIAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 79 NFIEVDEDTRINVKL--KTGQETEINAPGPHITSAQFEQL----LQQIKNTtseDIVIVAGSVPSSIPSDAYAQIAQITA 152
Cdd:PRK09513 82 RFQVVQGRTRINVKLteKDGEVTDFNFSGFEVTPADWERFvtdsLSWLGQF---DMVAVSGSLPRGVSPEAFTDWMTRLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 153 QTGAKLVVDAEKELAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISI 232
Cdd:PRK09513 159 SQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEW 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586063391 233 KAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTIEK--AFQQAVACGTATAFDEDLATRDAIEKIKSQVTISVL 303
Cdd:PRK09513 239 IAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHtlRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTPF 311
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-280 |
5.03e-51 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 170.22 E-value: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 7 FNPSID----YVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFP-GKFIIDTLKNSAIQSNFI 81
Cdd:pfam00294 1 KVVVIGeaniDLIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNfGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 82 EVDEDTRINVKLKT---GQETEINAPGPHITSAQFEQLLQQIKNTTSEDIVIVAGSVPSSIPSDAYAQIAQITAQTG-AK 157
Cdd:pfam00294 81 VIDEDTRTGTALIEvdgDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGtFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 158 LVVD----AEKELAESVLPyHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIK 233
Cdd:pfam00294 161 PNLLdplgAAREALLELLP-LADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVH 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 586063391 234 AVN-PQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATA 280
Cdd:pfam00294 240 VPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVV 287
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-294 |
1.15e-43 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 151.48 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 2 IYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAGGFPGKFIIDTLKNSAIQSNFI 81
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 82 EVDEDTRINVKL---KTGQETEINAPGPHITSAQFEQLLQQIKNTTSEDIVIVAGSVPSSIPSDAYAQIAQITAQTGAKL 158
Cdd:PRK10294 84 EAKDWTRQNLHVhveASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 159 VVDAEKE-LAESVLPYHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKG-AQSVIVSLGGDGAIYIDKEISIKAVN 236
Cdd:PRK10294 164 IIDSSGDaLSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 237 PQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTATAFDE--DLATRDAIEKI 294
Cdd:PRK10294 244 PPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQgtRLCSHDDTQKI 303
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-276 |
8.46e-26 |
|
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: 103.81 E-value: 8.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 11 IDYVIFTNDF-KIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFAG-GFPGKFIIDTLKNSAIQSNFIEVDED-- 86
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGdDPFGDFLLAELRAEGVDTSGVRRDPGap 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 87 TRINVKL--KTGQETEINAPGP--HITSAQFEQLLqqIKNTtseDIVIVAGSVPSS-IPSDAYAQIAQITAQTGAKLVVD 161
Cdd:COG0524 90 TGLAFILvdPDGERTIVFYRGAnaELTPEDLDEAL--LAGA---DILHLGGITLASePPREALLAALEAARAAGVPVSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 162 ---------AEKELAESVLPYHPLfIKPNKDELEVMFNTTvnsdeDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISI 232
Cdd:COG0524 165 pnyrpalwePARELLRELLALVDI-LFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 586063391 233 KAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACG 276
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
11-279 |
1.29e-19 |
|
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: 86.84 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 11 IDYVIFTNDFKIDG-LNRATATYKFAGGKGIN----VSRvlktLDVESTALGFAG--GFpGKFIIDTLKNSAIQSNFIEV 83
Cdd:cd01174 10 VDLVTRVDRLPKPGeTVLGSSFETGPGGKGANqavaAAR----LGARVAMIGAVGddAF-GDELLENLREEGIDVSYVEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 84 DEDTR-----INVKlKTGQETEINAPGP--HITSAQFEQLLQQIKNTtseDIVIVAGSvpssIPSDAYAQIAQITAQTGA 156
Cdd:cd01174 85 VVGAPtgtavITVD-ESGENRIVVVPGAngELTPADVDAALELIAAA---DVLLLQLE----IPLETVLAALRAARRAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 157 KLVVDAE--KELAESVLPYHPLFIkPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKA 234
Cdd:cd01174 157 TVILNPApaRPLPAELLALVDILV-PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 586063391 235 VNPQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGTAT 279
Cdd:cd01174 236 PAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALS 280
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
35-279 |
2.49e-17 |
|
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: 80.44 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 35 AGGKGINVSRVLKTLDVESTALGFAGG-FPGKFIIDTLKNSAIQSNFIeVDEDTRinvklkTGQETEINAPG-------- 105
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESEKAGLNVRGI-VFEGRS------TASYTAILDKDgdlvvala 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 106 -PHITSAQFEQLLQQIKNTTSEDIVIVagsVPSSIPSDAYAQIAQITAQTGAKLVVDAEKE--LAESVLPYHPL-FIKPN 181
Cdd:cd01941 107 dMDIYELLTPDFLRKIREALKEAKPIV---VDANLPEEALEYLLALAAKHGVPVAFEPTSApkLKKLFYLLHAIdLLTPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 182 KDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEIS----IKAVNPQGKVVNTVGSGDSTVAGMVA 257
Cdd:cd01941 184 RAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGvetkLFPAPQPETVVNVTGAGDAFVAGLVA 263
|
250 260
....*....|....*....|..
gi 586063391 258 GIASGLTIEKAFQQAVACGTAT 279
Cdd:cd01941 264 GLLEGMSLDDSLRFAQAAAALT 285
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
33-276 |
8.88e-16 |
|
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: 76.08 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 33 KFAGGKGINVSRVLKTLDVES---TALGfAGGFpGKFIIDTLKNSAIQSNFIEVDEDTRINVKLKT---GQETEI----- 101
Cdd:cd01166 28 KFFGGAEANVAVGLARLGHRValvTAVG-DDPF-GRFILAELRREGVDTSHVRVDPGRPTGLYFLEigaGGERRVlyyra 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 102 NAPGPHITSAQF-EQLLQQIknttseDIVIVAGSVPSSIPS--DAYAQIAQITAQTGAKLVVD---------AE--KELA 167
Cdd:cd01166 106 GSAASRLTPEDLdEAALAGA------DHLHLSGITLALSESarEALLEALEAAKARGVTVSFDlnyrpklwsAEeaREAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 168 ESVLPYHPLFIkPNKDELEVMFNTTvnSDEDVIKYGRLLvDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGS 247
Cdd:cd01166 180 EELLPYVDIVL-PSEEEAEALLGDE--DPTDAAERALAL-ALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGA 255
|
250 260
....*....|....*....|....*....
gi 586063391 248 GDSTVAGMVAGIASGLTIEKAFQQAVACG 276
Cdd:cd01166 256 GDAFAAGFLAGLLEGWDLEEALRFANAAA 284
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
33-280 |
6.66e-15 |
|
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: 73.44 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 33 KFAGGKGINVSRVLKTLDVEStalGFAGG----FPGKFIIDTLKNSAIQSNFIEVDED--TRI-NVKLK-TGQET-EINA 103
Cdd:cd01167 25 KAPGGAPANVAVALARLGGKA---AFIGKvgddEFGDFLLETLKEAGVDTRGIQFDPAapTTLaFVTLDaDGERSfEFYR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 104 PGP---HITSAQFEQLLQQIKnttsediVIVAGSVP--SSIPSDAYAQIAQITAQTGAKLVVD------------AEKEL 166
Cdd:cd01167 102 GPAadlLLDTELNPDLLSEAD-------ILHFGSIAlaSEPSRSALLELLEAAKKAGVLISFDpnlrpplwrdeeEARER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 167 AESVLPY-HplFIKPNKDELEVMFNTtvnSDEDVIkyGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTV 245
Cdd:cd01167 175 IAELLELaD--IVKLSDEELELLFGE---EDPEEI--AALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTT 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 586063391 246 GSGDSTVAGMVAGIASGL-------TIEKAFQQAVACGTATA 280
Cdd:cd01167 248 GAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTC 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
1-260 |
6.61e-13 |
|
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: 66.35 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 1 MIYTVTFNPSIDYVIFTNDFKIDGLNRATATYKFAGGKGINVSRVLKTLDVESTALGFaggfpgkfiidtlknsaiqsnf 80
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 81 ievdedtrinvklktgqeteinapgphitsaqfeqllqqiknttseDIVIVAGSVPSSipsDAYAQIAQITAQTGAKLVV 160
Cdd:cd00287 59 ----------------------------------------------DAVVISGLSPAP---EAVLDALEEARRRGVPVVL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 161 D-------AEKELAESVLPyHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDK---EI 230
Cdd:cd00287 90 DpgpravrLDGEELEKLLP-GVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRggtEV 168
|
250 260 270
....*....|....*....|....*....|
gi 586063391 231 SIKAVNPqgKVVNTVGSGDSTVAGMVAGIA 260
Cdd:cd00287 169 HVPAFPV--KVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
33-279 |
3.96e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 65.14 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 33 KFAGGKGINVSRVLKTLDVESTALGFAGGFP-GKFIIDTLKNSAIQSNFIEVDEdtriNVKLKTGQETEinaPGPHITSA 111
Cdd:PRK09813 20 AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKH----GVTAQTQVELH---DNDRVFGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 112 QFEQLLQQIKnTTSEDIVIVAGS--VPSSIPSDAYAQIAQITAqTGAKLVVDA----EKELAESVLPYhplfikpnkdeL 185
Cdd:PRK09813 93 YTEGVMADFA-LSEEDYAWLAQYdiVHAAIWGHAEDAFPQLHA-AGKLTAFDFsdkwDSPLWQTLVPH-----------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 186 EVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTI 265
Cdd:PRK09813 160 DYAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTL 239
|
250
....*....|....
gi 586063391 266 EKAFQQAVACGTAT 279
Cdd:PRK09813 240 PQAMAQGTACAAKT 253
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
36-275 |
2.28e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 63.60 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 36 GGKGINVSRVLKTLDVESTALGFAG--GFpGKFIIDTLKNSAIQSNFIEVDEDTR-----INVKLKTGQETEINAPGP-- 106
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGtdGF-GSDTIKNFKRNGVNTSFVSRTENSStglamIFVDTKTGNNEIVIIPGAnn 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 107 HITSAQFEQLLQQIKNTTseDIVIVAGSVPSSIPSDAYAQIAQ---ITAQTGAKLVVDAEKELAESVLPYHPLFIkPNKD 183
Cdd:PTZ00292 131 ALTPQMVDAQTDNIQNIC--KYLICQNEIPLETTLDALKEAKErgcYTVFNPAPAPKLAEVEIIKPFLKYVSLFC-VNEV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 184 ELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKE-ISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASG 262
Cdd:PTZ00292 208 EAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKEnEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRG 287
|
250
....*....|...
gi 586063391 263 LTIEKAFQQAVAC 275
Cdd:PTZ00292 288 KDLKESCKRANRI 300
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
180-276 |
2.40e-09 |
|
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: 56.94 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 180 PNKDELEVMFNTTVNSDEDVIKYGRLlvdkgaqsVIVSLGGDGAIYID--KEISIKAVNPQgKVVNTVGSGDSTVAGMVA 257
Cdd:cd01942 180 VNDYEAELLKERTGLSEAELASGVRV--------VVVTLGPKGAIVFEdgEEVEVPAVPAV-KVVDTTGAGDAFRAGFLY 250
|
90
....*....|....*....
gi 586063391 258 GIASGLTIEKAFQQAVACG 276
Cdd:cd01942 251 GLLRGYDLEESLRLGNLAA 269
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
33-268 |
1.17e-08 |
|
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: 55.26 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 33 KFAGGKGiNVSRVLKTLDVESTALGFAGG-FPGKFIIDTLKNSAIQSNFIeVDEDTRINVKLK----TGQETEINAPGPH 107
Cdd:cd01172 37 IRLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGI-VDEGRPTTTKTRviarNQQLLRVDREDDS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 108 ITSAQFEQLLQQI--KNTTSEDIVIVA-----GSVPSSIpsdayAQIAQITAQTGAKLVVDAeKELAESVLPyHPLFIKP 180
Cdd:cd01172 115 PLSAEEEQRLIERiaERLPEADVVILSdygkgVLTPRVI-----EALIAAARELGIPVLVDP-KGRDYSKYR-GATLLTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 181 NKDELEVMFNTTVNSDEDVIKYGRLLVDK-GAQSVIVSLGGDGAIYIDKE---ISIKAVNPQgkVVNTVGSGDSTVAGMV 256
Cdd:cd01172 188 NEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDgevQHIPALAKE--VYDVTGAGDTVIATLA 265
|
250
....*....|..
gi 586063391 257 AGIASGLTIEKA 268
Cdd:cd01172 266 LALAAGADLEEA 277
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
183-280 |
6.85e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 53.30 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 183 DELEVMfnTTVnsdEDVIKYGRLLV--DKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMVAGIA 260
Cdd:PLN02341 294 EEAEAL--TGI---RNPILAGQELLrpGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYI 368
|
90 100
....*....|....*....|
gi 586063391 261 SGLTIEKAFQQAVACGTATA 280
Cdd:PLN02341 369 HNLPLVNTLTLANAVGAATA 388
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
152-274 |
8.98e-08 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 52.10 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 152 AQTGAKLVV-DAEKELAESVLPyHPLFIKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIV---SLGGDGAIYID 227
Cdd:pfam08543 97 AKSGDSLLDdEAIEALKEELLP-LATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIkggHLEGEEAVVTD 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 586063391 228 ----KEISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVA 274
Cdd:pfam08543 176 vlydGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKE 226
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
214-276 |
1.98e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 51.48 E-value: 1.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586063391 214 VIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASG------LTIEKAFQQAVACG 276
Cdd:PRK09434 216 LLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQACG 284
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
12-277 |
2.05e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 51.53 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 12 DYVIFTNDFKID--GLNRATATY--------KFA-GGKGINVSRVLKTLDVESTALGFAGG-FPGKFIIDTLKNSAIQSN 79
Cdd:PRK09850 5 DYVVIIGSANIDvaGYSHESLNYadsnpgkiKFTpGGVGRNIAQNLALLGNKAWLLSAVGSdFYGQSLLTQTNQSGVYVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 80 --FIEVDEDTRINVKL--KTGQE-TEIN--APGPHITS---AQFEQLLQQIK------NTTSEDIVIV---AGSVPSSI- 139
Cdd:PRK09850 85 kcLIVPGENTSSYLSLldNTGEMlVAINdmNISNAITAeylAQHREFIQRAKvivadcNISEEALAWIldnAANVPVFVd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 140 PSDAYAQIaqitaqtgaklvvdaekELAESVLPYHPLfiKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLG 219
Cdd:PRK09850 165 PVSAWKCV-----------------KVRDRLNQIHTL--KPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMG 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 586063391 220 GDGAIYIDKEISIKAVNP-QGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACGT 277
Cdd:PRK09850 226 GDGVYYSDISGESGWSAPiKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSS 284
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
178-274 |
3.37e-07 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 50.53 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 178 IKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIV-SLGGDGaiYIDKEISIKAVNPQGKV--------VNTVGSG 248
Cdd:COG2240 142 ITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVtSVPLDD--TPADKIGNLAVTADGAWlvetpllpFSPNGTG 219
|
90 100
....*....|....*....|....*.
gi 586063391 249 DSTVAGMVAGIASGLTIEKAFQQAVA 274
Cdd:COG2240 220 DLFAALLLAHLLRGKSLEEALERAAA 245
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
34-279 |
3.42e-07 |
|
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: 50.43 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 34 FAGGKGINVSRVLKTLDVESTALGFAGGFP-GKFIIDTLKNSAIQSNFIEVDEdtRIN----VKLKTGQ-----ETEINA 103
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHESAYIGAVGNDDaGAHVRSTLKRLGVDISHCRVKE--GENavadVELVDGDrifglSNKGGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 104 PGPHITSAQFEQLLQQiknttseDIV-IVAGSVPSSIPsdayaQIAQITAQTGAKLVVD----AEKELAESVLPYHPLFI 178
Cdd:cd01940 98 AREHPFEADLEYLSQF-------DLVhTGIYSHEGHLE-----KALQALVGAGALISFDfsdrWDDDYLQLVCPYVDFAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 179 KPNKDElevmfnttvnSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDK----EISIKAVNpqgkVVNTVGSGDSTVAG 254
Cdd:cd01940 166 FSASDL----------SDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGavfySVAPRPVE----VVDTLGAGDSFIAG 231
|
250 260
....*....|....*....|....*.
gi 586063391 255 MVAG-IASGLTIEKAFQQAVACGTAT 279
Cdd:cd01940 232 FLLSlLAGGTAIAEAMRQGAQFAAKT 257
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
35-275 |
1.70e-06 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 48.77 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 35 AGGKGINVSRVLKTLDVESTALGFAGG-FPGKFIIDTLKNSAIQ-SNFIEVD-EDTRINVKLKTGQETEINAPG-PHIts 110
Cdd:PRK09954 92 AGGVGRNIAHNLALLGRDVHLLSAIGDdFYGETLLEETRRAGVNvSGCIRLHgQSTSTYLAIANRQDETVLAINdTHI-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 111 aqFEQLLQQIKNTtSEDIVIVAGSVPSSIPSDAYAQIAQITAQTGAKLVVDAEKEL-AESVLPYHPLF--IKPNKDELEV 187
Cdd:PRK09954 170 --LQQLTPQLLNG-SRDLIRHAGVVLADCNLTAEALEWVFTLADEIPVFVDTVSEFkAGKIKHWLAHIhtLKPTQPELEI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 188 MFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKE-ISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTIE 266
Cdd:PRK09954 247 LWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDgEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFR 326
|
....*....
gi 586063391 267 KAFQQAVAC 275
Cdd:PRK09954 327 DSARFAMAC 335
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
140-276 |
1.78e-06 |
|
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: 48.76 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 140 PSDAYAQIAQITAQTGAKL--------VVDAEKELAESVLPY-HPLFIkpNKDELEVMFNTTVNSDEDVIKYgrlLVDKG 210
Cdd:cd01168 159 PPEAILLAAEHAKENGVKIalnlsapfIVQRFKEALLELLPYvDILFG--NEEEAEALAEAETTDDLEAALK---LLALR 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586063391 211 AQSVIVSLGGDGAIYIDK--EISIKAVnPQGKVVNTVGSGDSTVAGMVAGIASGLTIEKAFQQAVACG 276
Cdd:cd01168 234 CRIVVITQGAKGAVVVEGgeVYPVPAI-PVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
178-274 |
3.91e-05 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 44.11 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 178 IKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVS---LGGDGAIYidkeiSIKAVNPQGKVVNT---------V 245
Cdd:cd01173 140 ITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveLADDDRIE-----MLGSTATEAWLVQRpkipfpayfN 214
|
90 100
....*....|....*....|....*....
gi 586063391 246 GSGDSTVAGMVAGIASGLTIEKAFQQAVA 274
Cdd:cd01173 215 GTGDLFAALLLARLLKGKSLAEALEKALN 243
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
121-268 |
4.73e-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: 43.93 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 121 KNTTSEDIVIVagsvpSSIPSDAYAQIAQITAqtgaKLVVDA---------EKELAESVLPYHpLFIKPNKDELEVMFNT 191
Cdd:cd01937 103 LSTITAEIVIL-----GPVPEEISPSLFRKFA----FISLDAqgflrranqEKLIKCVILKLH-DVLKLSRVEAEVISTP 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586063391 192 TVNSdedvikygRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMVAGIASGLTIEKA 268
Cdd:cd01937 173 TELA--------RLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEA 241
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
177-279 |
5.24e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 44.23 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 177 FIKPNKDELEVMFNTTVNSDEDVIKygrlLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMV 256
Cdd:PLN02323 200 IIKVSDEEVEFLTGGDDPDDDTVVK----LWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLL 275
|
90 100 110
....*....|....*....|....*....|
gi 586063391 257 AGIASGLTI---EKAFQQAV----ACGTAT 279
Cdd:PLN02323 276 SQLAKDLSLledEERLREALrfanACGAIT 305
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
178-274 |
6.66e-04 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 40.62 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 178 IKPNKDELEVMFNTTVNSDEDVIKYGRLLVDKGAQSVIVSLGGDGAIYIDKEISIKAVNPQGKVVNTVGSGDSTVAGMVA 257
Cdd:PRK11142 182 ITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVT 261
|
90
....*....|....*....
gi 586063391 258 GIASGLTIEKA--FQQAVA 274
Cdd:PRK11142 262 ALLEGKPLPEAirFAHAAA 280
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
214-268 |
1.95e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 39.40 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 586063391 214 VIVSLGGDGA-IYI-DKEISIKAVnpQGKVVNTVGSGDSTVAGMVAGIASGLTIEKA 268
Cdd:PLN02630 206 VIVTNGKKGCrIYWkDGEMRVPPF--PAIQVDPTGAGDSFLGGFVAGLVQGLAVPDA 260
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
163-294 |
3.27e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 38.48 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 163 EKELAESVLPYHPLFiKPNKDELEVMFNTTVN---SDEDVIKYGRLLVDKGAQ-----SVIVSLGGDGAIYI----DKEI 230
Cdd:cd01943 170 NLEDLLQALPRVDVF-SPNLEEAARLLGLPTSepsSDEEKEAVLQALLFSGILqdpggGVVLRCGKLGCYVGsadsGPEL 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586063391 231 SIKAVN-PQGKVVNTVGSGDSTVAGMVAGIASGLTIEkafqQAVACGT-ATAFdedlatrdAIEKI 294
Cdd:cd01943 249 WLPAYHtKSTKVVDPTGGGNSFLGGFAAGLALTKSID----EACIYGSvAASF--------AIEQV 302
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
33-268 |
3.48e-03 |
|
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: 38.56 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 33 KFAGGKGINVSRVLKTLDVESTALGFAG-GFPGKFIidtlkNSAIQSNFIEV------DEDTRINVKL--KTGQETEINA 103
Cdd:cd01944 32 SYVIGGGFNVMVAASRLGIPTVNAGPLGnGNWADQI-----RQAMRDEGIEIllpprgGDDGGCLVALvePDGERSFISI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 104 PG--PHITSAQFEQLlqqikNTTSEDIVIVAG-SVPSSIPSDAYAQIAQITAQTGAKLVVDA-------EKELAESVLPY 173
Cdd:cd01944 107 SGaeQDWSTEWFATL-----TVAPYDYVYLSGyTLASENASKVILLEWLEALPAGTTLVFDPgprisdiPDTILQALMAK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063391 174 HPLfIKPNKDELEVMFNTTVNSDEDvikYGRLLVDKGAQSVIVSLGGDGAIYID---KEISIKAVnpQGKVVNTVGSGDS 250
Cdd:cd01944 182 RPI-WSCNREEAAIFAERGDPAAEA---SALRIYAKTAAPVVVRLGSNGAWIRLpdgNTHIIPGF--KVKAVDTIGAGDT 255
|
250
....*....|....*...
gi 586063391 251 TVAGMVAGIASGLTIEKA 268
Cdd:cd01944 256 HAGGMLAGLAKGMSLADA 273
|
|
| |
