|
Name |
Accession |
Description |
Interval |
E-value |
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
1-312 |
0e+00 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 668.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 1 MSRRVATITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIA 80
Cdd:PRK09513 1 MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 81 NRFQVVQGRTRINVKLTEKDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQ 160
Cdd:PRK09513 81 NRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 161 CPCIIFDSSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIA 240
Cdd:PRK09513 161 CPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864600 241 KPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRTQLAAMMARVDLKPFN 312
Cdd:PRK09513 241 KPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTPFN 312
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
5-306 |
4.55e-125 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 359.45 E-value: 4.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 5 VATITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQ 84
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 85 VVQGRTRINVKLTE-KDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPC 163
Cdd:COG1105 81 PIEGETRINIKIVDpSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 164 IIFDSSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPP 243
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864600 244 SMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRTQLAAMMARV 306
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQV 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
4-276 |
6.13e-124 |
|
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: 356.07 E-value: 6.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 4 RVATITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRF 83
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 84 QVVQGRTRINVKLTEKDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPC 163
Cdd:cd01164 81 VEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 164 IIFDSSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPP 243
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270
....*....|....*....|....*....|...
gi 493864600 244 SMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALR 273
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
5-306 |
1.59e-117 |
|
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: 340.72 E-value: 1.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 5 VATITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQ 84
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 85 VVQGRTRINVKLTEKDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCI 164
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 165 IFDSSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPS 244
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864600 245 MEVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRTQLAAMMARV 306
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQV 302
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
5-306 |
5.04e-115 |
|
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: 334.16 E-value: 5.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 5 VATITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQ 84
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 85 VVQGRTRINVKLTEKDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCI 164
Cdd:TIGR03168 81 EVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 165 IFDSSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPS 244
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864600 245 MEVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRTQLAAMMARV 306
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQV 302
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
14-276 |
1.23e-68 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 215.67 E-value: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 14 YDLVGFCPEIErGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDN-QDGFQQLFSELGIANRFQVVQGRTRI 92
Cdd:pfam00294 10 IDLIGNVEGLP-GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNfGEFLLQELKKEGVDTDYVVIDEDTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 93 NVKLTEKDGEV-TDLNFSGFEVTPADWERFVaDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCI--IFDSS 169
Cdd:pfam00294 89 GTALIEVDGDGeRTIVFNRGAAADLTPEELE-ENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGTFDpnLLDPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 170 RDALVAGLKASP--WLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP-PSME 246
Cdd:pfam00294 168 GAAREALLELLPlaDLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKVK 247
|
250 260 270
....*....|....*....|....*....|
gi 493864600 247 VVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:pfam00294 248 VVDTTGAGDSFVGGFLAGLLAGKSLEEALR 277
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-276 |
2.34e-33 |
|
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: 124.23 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 13 AYDLVGFCPEIER-GEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKD-NQDGFQQLFSELGIANRFQVV--QG 88
Cdd:COG0524 9 LVDLVARVDRLPKgGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDpFGDFLLAELRAEGVDTSGVRRdpGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 89 RTRINVKLTEKDGEVTdlnfsgFEVTPADWERFVADSL--SWLGQFDMVCVSG-SLPSGVSPEAFTDWMTRLRSQCPCII 165
Cdd:COG0524 89 PTGLAFILVDPDGERT------IVFYRGANAELTPEDLdeALLAGADILHLGGiTLASEPPREALLAALEAARAAGVPVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 166 FD-SSRDALVAGLKASPW-------LVKPNRRELEIWAGRKlpelkDVIDAAHALREQGIAHVVISLGAEGALWVNASGE 237
Cdd:COG0524 163 LDpNYRPALWEPARELLRellalvdILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGGEV 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 493864600 238 WIAKPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:COG0524 238 VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALR 276
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
4-261 |
2.95e-33 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 124.13 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 4 RVATITLNPAYDLVGFCPEI-ERGEVnlvRTTG--LHAAGKGINVAKVLKDLGIDVT----VGGFLGKDnqdgFQQLFSE 76
Cdd:PRK10294 3 RIYTLTLAPSLDSATITPQIyPEGKL---RCSApvFEPGGGGINVARAIAHLGGSATaifpAGGATGEH----LVSLLAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 77 LGIANRFQVVQGRTRINVKL-TEKDGEVTDLNFSGFEVTPADWeRFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMT 155
Cdd:PRK10294 76 ENVPVATVEAKDWTRQNLHVhVEASGEQYRFVMPGAALNEDEF-RQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 156 RLRSQCPCIIFDSSRDALVAGLKASPW-LVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAH-VVISLGAEGALWVN 233
Cdd:PRK10294 155 AAQKQGIRCIIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKrVVVSLGPQGALGVD 234
|
250 260
....*....|....*....|....*...
gi 493864600 234 ASGEWIAKPPSMEVVSTVGAGDSMVGGL 261
Cdd:PRK10294 235 SENCIQVVPPPVKSQSTVGAGDSMVGAM 262
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
7-276 |
1.74e-31 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 119.44 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 7 TITLNPAYDLVGFCPEIERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDgF--QQLFSElgIANRFQ 84
Cdd:PRK13508 4 TVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQ-FiaEHLDDQ--IKHAFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 85 VVQGRTRiNVKLTEKDGEVTDLNFSGFEVTPADWERFVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCI 164
Cdd:PRK13508 81 KIKGETR-NCIAILHEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 165 IFDSSRDALVAGLKAS--PWLVKPNRRELEIWAGRKLPelKDVIDAAHALRE---QGIAHVVISLGAEGALWVNASGEWI 239
Cdd:PRK13508 160 VLDCSGAALQAVLESPykPTVIKPNIEELSQLLGKEVS--EDLDELKEVLQQplfEGIEWIIVSLGADGAFAKHNDTFYK 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 493864600 240 AKPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLK 274
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
37-276 |
5.56e-23 |
|
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: 96.17 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 37 HAAGKGINVAKVLKDLGIDVtvgGFLGKDNQDGF----QQLFSELGIANRFQVVQG--RTRI-NVKLTEkDGEvtdLNFS 109
Cdd:cd01167 26 APGGAPANVAVALARLGGKA---AFIGKVGDDEFgdflLETLKEAGVDTRGIQFDPaaPTTLaFVTLDA-DGE---RSFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 110 GFEVTPADWERFVADSLSWLGQFDMVCVsGSLP--SGVSPEAFTDWMTRLRSQCPCIIFD--------SSRDALVAGLKA 179
Cdd:cd01167 99 FYRGPAADLLLDTELNPDLLSEADILHF-GSIAlaSEPSRSALLELLEAAKKAGVLISFDpnlrpplwRDEEEARERIAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 180 SpW----LVKPNRRELEIWAGRKLPElkdviDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGD 255
Cdd:cd01167 178 L-LeladIVKLSDEELELLFGEEDPE-----EIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGD 251
|
250 260
....*....|....*....|.
gi 493864600 256 SMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01167 252 AFVAGLLAQLLSRGLLALDED 272
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
40-276 |
1.24e-19 |
|
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: 86.98 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 40 GKGINVAKVLKDLGIDVTVGGFLGKDNQ-DGFQQLFSELGIANRFQVVQGR-TRINVKLTEKDGEV------TDLnfsgF 111
Cdd:cd01941 36 GVGRNIAENLARLGVSVALLSAVGDDSEgESILEESEKAGLNVRGIVFEGRsTASYTAILDKDGDLvvaladMDI----Y 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 112 EVTPADWERFVADSLSwlgQFDMVCVSGSLPSGVspeaftdwMTRLRSQC-------PCIIFDSSRDALVAGLKASPWLV 184
Cdd:cd01941 112 ELLTPDFLRKIREALK---EAKPIVVDANLPEEA--------LEYLLALAakhgvpvAFEPTSAPKLKKLFYLLHAIDLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 185 KPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGE---WIAKPPSME-VVSTVGAGDSMVGG 260
Cdd:cd01941 181 TPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGvetKLFPAPQPEtVVNVTGAGDAFVAG 260
|
250
....*....|....*.
gi 493864600 261 LIYGLLMRESSEHTLR 276
Cdd:cd01941 261 LVAGLLEGMSLDDSLR 276
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
103-266 |
3.71e-19 |
|
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: 83.68 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 103 VTDLNFSGFEVTPADWE-------RFVADSLSWLGQ------FDMVCVSGSLPSgvsPEAFTDWMTRLRSQCPCIIFD-- 167
Cdd:cd00287 16 VDALPLPGGLVRPGDTEeragggaANVAVALARLGVsvtlvgADAVVISGLSPA---PEAVLDALEEARRRGVPVVLDpg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 168 ----SSRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNaSGEWI--AK 241
Cdd:cd00287 93 pravRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVAT-RGGTEvhVP 171
|
170 180
....*....|....*....|....*
gi 493864600 242 PPSMEVVSTVGAGDSMVGGLIYGLL 266
Cdd:cd00287 172 AFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
24-276 |
1.14e-18 |
|
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: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 24 ERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDN-QDGFQQLFSELGIANRF--QVVQGRTRINVKLTEKD 100
Cdd:cd01166 16 GGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPfGRFILAELRREGVDTSHvrVDPGRPTGLYFLEIGAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 101 GEVTDLNF----SGFEVTPADWERFVadslswLGQFDMVCVSGSLP--SGVSPEAFTDWMTRLRSQCPCIIFDSS----- 169
Cdd:cd01166 96 GERRVLYYragsAASRLTPEDLDEAA------LAGADHLHLSGITLalSESAREALLEALEAAKARGVTVSFDLNyrpkl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 170 ------RDALVAGLKASPWLVkPNRRELEIWAGRKLPElkDVIDAAHALREqGIAHVVISLGAEGALWVNASGEWIAKPP 243
Cdd:cd01166 170 wsaeeaREALEELLPYVDIVL-PSEEEAEALLGDEDPT--DAAERALALAL-GVKAVVVKLGAEGALVYTGGGRVFVPAY 245
|
250 260 270
....*....|....*....|....*....|...
gi 493864600 244 SMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01166 246 PVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALR 278
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
14-276 |
5.82e-16 |
|
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: 76.43 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 14 YDLVGFCPEIER-GEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDnQDGFQQL--FSELGI--ANRFQVVQG 88
Cdd:cd01174 10 VDLVTRVDRLPKpGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDD-AFGDELLenLREEGIdvSYVEVVVGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 89 RT---RINVkltEKDGEVTDLNFSG--FEVTPADWERFvadsLSWLGQFDMVCVSGSLPsgvsPEAFTDWMTRLRSQCPC 163
Cdd:cd01174 89 PTgtaVITV---DESGENRIVVVPGanGELTPADVDAA----LELIAAADVLLLQLEIP----LETVLAALRAARRAGVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 164 IIFDSS--RDALVAGLKASPWLVkPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAK 241
Cdd:cd01174 158 VILNPApaRPLPAELLALVDILV-PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVP 236
|
250 260 270
....*....|....*....|....*....|....*
gi 493864600 242 PPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01174 237 AFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIR 271
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
39-265 |
2.12e-15 |
|
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: 74.77 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 39 AGKGINVAKVLKDLGIDVTVGGFLGKDNQDGF-QQLFSELGIANRFQVVQGRTRIN-VKLTEKDGEVTDLNFSGFEvtpA 116
Cdd:cd01944 35 IGGGFNVMVAASRLGIPTVNAGPLGNGNWADQiRQAMRDEGIEILLPPRGGDDGGClVALVEPDGERSFISISGAE---Q 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 117 DWERFVADSLSwLGQFDMVCVSG-SLPS-GVSPEAFTDWMTRLRSQCPCIIFDSSR-----DALVAGLKASPWLVKPNRR 189
Cdd:cd01944 112 DWSTEWFATLT-VAPYDYVYLSGyTLASeNASKVILLEWLEALPAGTTLVFDPGPRisdipDTILQALMAKRPIWSCNRE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864600 190 ELEIWAGRKLPELKDVIDAAHALREqgiAHVVISLGAEGALWVNASGEWIAKPP-SMEVVSTVGAGDSMVGGLIYGL 265
Cdd:cd01944 191 EAAIFAERGDPAAEASALRIYAKTA---APVVVRLGSNGAWIRLPDGNTHIIPGfKVKAVDTIGAGDTHAGGMLAGL 264
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
111-274 |
1.56e-11 |
|
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: 63.63 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 111 FEVTPADW-ERFVAD--SLSWLGQFDMVcVSGSLpsgVSPE---AFTDWMTRLRSQCP----------------CIIFDS 168
Cdd:COG2240 51 GRDLPTDDiADILDGwkELGVLLEFDAV-LSGYL---GSAEqgdIIADFVARVKAANPdalylcdpvmgdngkgYYVFPG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 169 SRDALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVI-SLGAE-------GALWVNASGEWIA 240
Cdd:COG2240 127 IAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVtSVPLDdtpadkiGNLAVTADGAWLV 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 493864600 241 KPPSMEvVSTVGAGD----SMVGGLIYGLLMRESSEHT 274
Cdd:COG2240 207 ETPLLP-FSPNGTGDlfaaLLLAHLLRGKSLEEALERA 243
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
37-265 |
5.00e-11 |
|
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: 62.19 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 37 HAAGKGINVAKVLKDLGIDVTVGGFLGKD-NQDGFQQLFSELGIANRFQVVQGR-----TRI---NVKLTEKDGEvTDLN 107
Cdd:cd01172 37 IRLGGAANVANNLASLGAKVTLLGVVGDDeAGDLLRKLLEKEGIDTDGIVDEGRptttkTRViarNQQLLRVDRE-DDSP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 108 FSGFEVTPAdWERFVADslswLGQFDMVCVS----GSLPSGVspeaftdwMTRLRSQC-----PCIIfDS-SRD-ALVAG 176
Cdd:cd01172 116 LSAEEEQRL-IERIAER----LPEADVVILSdygkGVLTPRV--------IEALIAAArelgiPVLV-DPkGRDySKYRG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 177 lkASpwLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAH-VVISLGAEGALWVNASGEWIAKPP-SMEVVSTVGAG 254
Cdd:cd01172 182 --AT--LLTPNEKEAREALGDEINDDDELEAAGEKLLELLNLEaLLVTLGEEGMTLFERDGEVQHIPAlAKEVYDVTGAG 257
|
250
....*....|.
gi 493864600 255 DSMVGGLIYGL 265
Cdd:cd01172 258 DTVIATLALAL 268
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
187-270 |
1.48e-09 |
|
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: 58.01 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 187 NRRELEIWAGrklPELKDVIDAAHALREQGIAHVVISLGAEGA-LWVNASGEWIAKPPSMEVVSTVGAGDSMVGGLIYGL 265
Cdd:cd01168 207 NEEEAEALAE---AETTDDLEAALKLLALRCRIVVITQGAKGAvVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGL 283
|
....*
gi 493864600 266 LMRES 270
Cdd:cd01168 284 VQGEP 288
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
145-271 |
1.66e-09 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 58.02 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 145 VSPEAFtDWMTRLRSQCPCIIfDSsrdalVAGLKASP---WL-----VKPNRRELEIWAGRKLPELKDVIDAAHALREQG 216
Cdd:PRK09954 197 LTAEAL-EWVFTLADEIPVFV-DT-----VSEFKAGKikhWLahihtLKPTQPELEILWGQAITSDADRNAAVNALHQQG 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 217 IAHVVISLGAEGALWVNASGE-WIAKPPSMEVVSTVGAGDSMVGGLIYGLL----MRESS 271
Cdd:PRK09954 270 VQQIFVYLPDESVFCSEKDGEqFLLTAPAHTTVDSFGADDGFMAGLVYSFLegysFRDSA 329
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
107-275 |
6.70e-09 |
|
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: 55.67 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 107 NFSGFeVTPADW-ERFVAD--SLSWLGQFDMVcVSGSLPSGVSPEAFTDWMTRLRSQCPCIIF-------DSSR------ 170
Cdd:cd01173 46 TWTGF-VLSAEElEDLLEGleALGLLLEYDAV-LTGYLGSAEQVEAVAEIVKRLKEKNPNLLYvcdpvmgDNGKlyvvae 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 171 ---DALVAGLKASPWLVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVIS---LGAEG---ALWVNASGEWIAK 241
Cdd:cd01173 124 eivPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveLADDDrieMLGSTATEAWLVQ 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 493864600 242 PPSMEVVST-VGAGD----SMVGGLIYGLLMRESSEHTL 275
Cdd:cd01173 204 RPKIPFPAYfNGTGDlfaaLLLARLLKGKSLAEALEKAL 242
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
206-276 |
7.65e-09 |
|
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: 55.76 E-value: 7.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864600 206 IDAAHALREQGIAHVVISLGAEGALWVNASGE-WIAKPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01945 192 DEALELLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALR 263
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
184-261 |
8.13e-09 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 55.76 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 184 VKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGE--WIAkPPSMEVVSTVGAGDSMVGGL 261
Cdd:PRK09850 184 LKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGEsgWSA-PIKTNVINVTGAGDAMMAGL 262
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
40-266 |
1.26e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 54.74 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 40 GKGINVAKVLKDLGIDVTVGGFLGKDNQ-DGFQQLFSELGI-ANRFQVVQGRTRIN-VKLTEKD---GEVTDLNFSGFEV 113
Cdd:PRK09813 24 GNAVNVAVYCTRYGIQPGCITWVGDDDYgTKLKQDLARMGVdISHVHTKHGVTAQTqVELHDNDrvfGDYTEGVMADFAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 114 TPADwerfvadsLSWLGQFDMVcVSGSLpsGVSPEAFTdwmtRLRSQCPCIIFDSSrdalvaglkaspwlvkpNRRELEI 193
Cdd:PRK09813 104 SEED--------YAWLAQYDIV-HAAIW--GHAEDAFP----QLHAAGKLTAFDFS-----------------DKWDSPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 194 WagRKLPELKDVIDAAH------------ALREQGIAHVVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGDSMVGGL 261
Cdd:PRK09813 152 W--QTLVPHLDYAFASApqedeflrlkmkAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGF 229
|
....*
gi 493864600 262 IYGLL 266
Cdd:PRK09813 230 LCGWL 234
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
186-266 |
6.13e-08 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 52.95 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 186 PNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGAlWVNASGEW-IAKPPSMEVVSTVGAGDSMVGGLIYG 264
Cdd:PRK11142 184 PNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGV-WLSENGEGqRVPGFRVQAVDTIAAGDTFNGALVTA 262
|
..
gi 493864600 265 LL 266
Cdd:PRK11142 263 LL 264
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
186-265 |
1.80e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 51.86 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 186 PNRRElEIWagRKLPELKDVIDAAHAL----------------------------REQGIAHVVISLGAEGALWVNASGE 237
Cdd:PRK09434 157 PNLRE-DLW--QDEAELRECLRQALALadvvklseeelcflsgtsqledaiyalaDRYPIALLLVTLGAEGVLVHTRGQV 233
|
90 100
....*....|....*....|....*...
gi 493864600 238 WIAKPPSMEVVSTVGAGDSMVGGLIYGL 265
Cdd:PRK09434 234 QHFPAPSVDPVDTTGAGDAFVAGLLAGL 261
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
183-267 |
4.62e-07 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 50.25 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 183 LVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHV-VISLGAEGA-------LWVNASGEWIAKPPSMEV-VSTVGA 253
Cdd:PRK05756 141 IITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVlVTSLARAGYpadrfemLLVTADGAWHISRPLVDFmRQPVGV 220
|
90
....*....|....
gi 493864600 254 GDsmvggLIYGLLM 267
Cdd:PRK05756 221 GD-----LTSALFL 229
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
199-275 |
5.94e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 50.60 E-value: 5.94e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864600 199 LPELKDVIDAAHALREQGIAH--VVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTL 275
Cdd:PLN02341 299 LTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTL 377
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-266 |
1.02e-06 |
|
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: 49.27 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 40 GKGINVAKVLKDLGIDVTVGGFLGKD-NQDGFQQLFSELGIANRF-QVVQGRTRI-NVKLTEKDGEVTDLNFSGFevtpA 116
Cdd:cd01940 23 GNALNVAVYAKRLGHESAYIGAVGNDdAGAHVRSTLKRLGVDISHcRVKEGENAVaDVELVDGDRIFGLSNKGGV----A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 117 DWERFVADsLSWLGQFDMVCVSGSLPSGVSPEAftdwMTRLRSQCPCIIFDSSRDALVAGL-KASPWLvkpnrrELEIWA 195
Cdd:cd01940 99 REHPFEAD-LEYLSQFDLVHTGIYSHEGHLEKA----LQALVGAGALISFDFSDRWDDDYLqLVCPYV------DFAFFS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864600 196 GRKLPElKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGDSMVGGLIYGLL 266
Cdd:cd01940 168 ASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLL 237
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-276 |
1.87e-06 |
|
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: 48.46 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 13 AYDLVGFCPEI-ERGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQ-DGFQQLFSELGIANRF--QVVQG 88
Cdd:cd01942 9 NYDIILKVESFpGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHgRLYLEELREEGVDTSHvrVVDED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 89 RTRINVKLTEKDGEVTdlnfSGFEVTPADWERfVADSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRlrsqcpcIIFDS 168
Cdd:cd01942 89 STGVAFILTDGDDNQI----AYFYPGAMDELE-PNDEADPDGLADIVHLSSGPGLIELARELAAGGIT-------VSFDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 169 SRD-ALVAGLKASPWLVK-----PNRRELEIW---AGRKLPELKDVIDAahalreqgiahVVISLGAEGALWVNASGEW- 238
Cdd:cd01942 157 GQElPRLSGEELEEILERadilfVNDYEAELLkerTGLSEAELASGVRV-----------VVVTLGPKGAIVFEDGEEVe 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 493864600 239 IAKPPSMEVVSTVGAGDSMVGGLIYGLLMRESSEHTLR 276
Cdd:cd01942 226 VPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLR 263
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
183-266 |
2.17e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 183 LVKPNRRELEiwagrklpELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGDSMVGGLI 262
Cdd:cd01937 158 VLKLSRVEAE--------VISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFL 229
|
....
gi 493864600 263 YGLL 266
Cdd:cd01937 230 YSRL 233
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
15-272 |
3.03e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 45.11 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 15 DLVGFCPEIER-GEVnlVRTTGLHAA--GKGINVAKVLKDLGIDVTVGGFLGKDnQDGFQQL--FSELGIANRF-----Q 84
Cdd:PTZ00292 27 DLIGYVDRMPQvGET--LHGTSFHKGfgGKGANQAVMASKLGAKVAMVGMVGTD-GFGSDTIknFKRNGVNTSFvsrteN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 85 VVQGRTRINVKLTEKDGEVTDLNFSGFEVTPAdwerFVADSLSWLGQF-DMVCVSGSLPSGVSPEAFtdwmtRLRSQCPC 163
Cdd:PTZ00292 104 SSTGLAMIFVDTKTGNNEIVIIPGANNALTPQ----MVDAQTDNIQNIcKYLICQNEIPLETTLDAL-----KEAKERGC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 164 I-IFDSS---RDALVAGLKASPWLVK---PNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASG 236
Cdd:PTZ00292 175 YtVFNPApapKLAEVEIIKPFLKYVSlfcVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKEN 254
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493864600 237 EWIaKPPSM--EVVSTVGAGDSMVGGLIY----GLLMRESSE 272
Cdd:PTZ00292 255 EPV-HVPGKrvKAVDTTGAGDCFVGSMAYfmsrGKDLKESCK 295
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
197-276 |
4.13e-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: 41.30 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 197 RKLPELKDVIDAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP-PSMEVVSTVGAGDSMVGGLIyGLLMR--ESSEH 273
Cdd:cd01946 175 RQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAyPLESVFDPTGAGDTFAGGFI-GYLASqkDTSEA 253
|
...
gi 493864600 274 TLR 276
Cdd:cd01946 254 NMR 256
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
220-266 |
8.94e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 40.56 E-value: 8.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493864600 220 VVISLGAEGAlWVNASGEWIAKPPSMEV-VSTVGAGDSMVGGLIYGLL 266
Cdd:PLN02813 319 VSVTDGARGS-YIGVKGEAVYIPPSPCVpVDTCGAGDAYAAGILYGLL 365
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
218-271 |
2.37e-03 |
|
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: 38.93 E-value: 2.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 493864600 218 AHVVISLGAEGALWVNASGEWI----AKPPSmeVVSTVGAGDSMVGGLIYGLLMRESS 271
Cdd:cd01939 213 ALLVCTWGDQGAGALGPDGEYVhspaHKPIR--VVDTLGAGDTFNAAVIYALNKGPDD 268
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
183-222 |
3.02e-03 |
|
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: 38.62 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 493864600 183 LVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVI 222
Cdd:pfam08543 122 LITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLI 161
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
109-225 |
3.14e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 38.51 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 109 SGFEVTPADWERFvADSLSWLGQFDMVCVS-GSLPSGVSPEAFTDWMTrLRSQCPCI-----IFDSSRDALVAGL----- 177
Cdd:PRK12413 47 KGFEVFPVDKEIF-QQQLDSLKDVPFSAIKiGLLPNVEIAEQALDFIK-GHPGIPVVldpvlVCKETHDVEVSELrqeli 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 493864600 178 KASPW--LVKPNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVISLG 225
Cdd:PRK12413 125 QFFPYvtVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGG 174
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
186-222 |
3.61e-03 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 38.52 E-value: 3.61e-03
10 20 30
....*....|....*....|....*....|....*..
gi 493864600 186 PNRRELEIWAGRKLPELKDVIDAAHALREQGIAHVVI 222
Cdd:PTZ00344 145 PNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVI 181
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
25-276 |
3.64e-03 |
|
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: 38.17 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 25 RGEVNLVRTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDnQDGfQQLFSELGIANRFQVVQGR---TRINVKLTEKDG 101
Cdd:cd01947 22 PGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRD-EIG-IQSLEELESGGDKHTVAWRdkpTRKTLSFIDPNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 102 EVTDLNFSGFEVTPADWERFVadslswlgQFDMVCVSGSLPSGvspeaftdwmtrlrsqcPCIIFDSSRDALV--AGLKA 179
Cdd:cd01947 100 ERTITVPGERLEDDLKWPILD--------EGDGVFITAAAVDK-----------------EAIRKCRETKLVIlqVTPRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864600 180 SPWLVKPNRRELEIWAGRKL-PELKDVIDAAhALReqGIAHVVISLGAEGALWVNASGEWIAKPPSMEVVSTVGAGDSMV 258
Cdd:cd01947 155 RVDELNQALIPLDILIGSRLdPGELVVAEKI-AGP--FPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFA 231
|
250
....*....|....*...
gi 493864600 259 GGLIYGLLMRESSEHTLR 276
Cdd:cd01947 232 AGFIYGLLKGWSIEEALE 249
|
|
| |
