|
Name |
Accession |
Description |
Interval |
E-value |
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
12-286 |
1.93e-82 |
|
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: 250.53 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 12 KIWIVNYACAIDYYVDL--------NKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKPYDLNIVS 83
Cdd:cd01164 1 MIYTVTLNPAIDLTIELdqlqpgevNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 84 FISETKTRINLKLLKDEK-TTEINDLSPLITDANLTELLTFLKANVKNNDLVIINGRFKF----EALEKVLNLVFTLTEN 158
Cdd:cd01164 81 VEVAGETRINVKIKEEDGtETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPgvpaDFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 159 VVIDVDESKMLTLLNqSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFHY--CKLLLLSDGDKGAYLFDQNKLLFVSS 236
Cdd:cd01164 161 VILDTSGEALLAALA-AKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIErgAENVLVSLGADGALLVTKDGVYRASP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499171726 237 ITPKqVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:cd01164 240 PKVK-VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
21-286 |
2.41e-48 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 163.38 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 21 AIDYYVDL--------NKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKPYDLNiVSFIS-ETKTR 91
Cdd:COG1105 9 ALDRTYEVdelepgevNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIP-TDFVPiEGETR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 92 INLKLL--KDEKTTEINDLSPLITDANLTELLTFLKANVKNNDLVIINGR----FKFEALEKvlnLVFTLTEN---VVID 162
Cdd:COG1105 88 INIKIVdpSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSlppgVPPDFYAE---LIRLARARgakVVLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 163 VDESKMLTLLnQSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSSitPK 240
Cdd:COG1105 165 TSGEALKAAL-EAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLerGAENVVVSLGADGALLVTEDGVYRAKP--PK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499171726 241 -QVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:COG1105 242 vEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGT 288
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
12-286 |
4.36e-44 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 152.11 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 12 KIWIVNYACAIDYY---VDLNKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTK-NLFLELVKPYDLNIVSFISE 87
Cdd:pfam00294 4 VIGEANIDLIGNVEglpGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFgEFLLQELKKEGVDTDYVVID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 88 TKTRINLKL--LKDEKTTEINDLSPLITDANLTELLTFLKAnVKNNDLVIINGRFKFEALEKVLNLVFTLTEN------V 159
Cdd:pfam00294 84 EDTRTGTALieVDGDGERTIVFNRGAAADLTPEELEENEDL-LENADLLYISGSLPLGLPEATLEELIEAAKNggtfdpN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 160 VIDVDESKMLTLLN-QSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSS 236
Cdd:pfam00294 163 LLDPLGAAREALLElLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLakGIKTVIVTLGADGALVVEGDGEVHVPA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499171726 237 ITPKQVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:pfam00294 243 VPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGA 292
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
13-286 |
1.24e-42 |
|
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: 148.49 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 13 IWIVNYACAIDYYVDL--------NKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKpyDLNIVSF 84
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVdgltpgevNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLA--EEGIKND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 85 ISETK--TRINLKLLKDEKT-TEINDLSPLITDANLTELLTFLKANVKNNDLVIINGRF----KFEALEKVLNLVFTLTE 157
Cdd:TIGR03168 79 FVEVKgeTRINVKIKESSGEeTELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLppgvPPDFYAQLIAIARKKGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 158 NVVIDVDESKMLTLLnQSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFHY--CKLLLLSDGDKGAYLFDQNKLLFVS 235
Cdd:TIGR03168 159 KVILDTSGEALREAL-AAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDrgAENVLVSLGADGALLVTKEGALKAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499171726 236 SitPK-QVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:TIGR03168 238 P--PKvEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGT 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
21-286 |
2.01e-41 |
|
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: 145.42 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 21 AIDYYVDL--------NKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKpyDLNIVS-FIS-ETKT 90
Cdd:TIGR03828 9 AIDLTIELdgltlgevNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLR--EEGIKTdFVRvPGET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 91 RINLKL-LKDEKTTEINDLSPLITDANLTELLTFLKANVKNNDLVIINGRF----KFEALEKVLNLVFTLTENVVIDVDE 165
Cdd:TIGR03828 87 RINVKIkEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLppgvPPDFYAELIALAREKGAKVILDTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 166 SKMLTLLnQSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFHY--CKLLLLSDGDKGAYLFDQNKLLFVSSITPKqVV 243
Cdd:TIGR03828 167 EALRDGL-KAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDlgAENVLISLGADGALLVTKEGALFAQPPKGE-VV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499171726 244 STTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:TIGR03828 245 STVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGT 287
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
36-288 |
6.90e-17 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 79.35 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 36 LIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKpyDLNIVS--FISETKTRINLKLL-KDEKTTEINDLSPLI 112
Cdd:PRK09513 36 LHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFS--ELGIANrfQVVQGRTRINVKLTeKDGEVTDFNFSGFEV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 113 TDANLTELLTFLKANVKNNDLVIINGRF-------KFEALEKVLNlvftlTENVVIDVDESK-MLTLLNQSKPLVMKPNI 184
Cdd:PRK09513 114 TPADWERFVTDSLSWLGQFDMVAVSGSLprgvspeAFTDWMTRLR-----SQCPCIIFDSSReALVAGLKAAPWLVKPNR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 185 DEFQTMINTFFHDQQSLIAAIKKF------HycklLLLSDGDKGAylfdqnklLFVSSIT------PK-QVVSTTGAGDT 251
Cdd:PRK09513 189 RELEIWAGRKLPELKDVIEAAHALreqgiaH----VVISLGAEGA--------LWVNASGewiakpPAcDVVSTVGAGDS 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 499171726 252 LLAVFLANLILKVDLKTALIKATNYASATISK--LGVVD 288
Cdd:PRK09513 257 MVGGLIYGLLMRESSEHTLRLATAVSALAVSQsnVGITD 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
38-285 |
1.79e-16 |
|
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: 78.00 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 38 PGGKGINVAIVMKSLGFDPTVITFLGQ-PTKNLFLELVKPYDLNI--VSFISETKTRINLKLLKDEKTTEIndlsplITD 114
Cdd:COG0524 35 PGGAAANVAVALARLGARVALVGAVGDdPFGDFLLAELRAEGVDTsgVRRDPGAPTGLAFILVDPDGERTI------VFY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 115 ANLTELLT---FLKANVKNNDLVIINGRFKF-----EALEKVLNLVFTLTENVVIDVDESKMLTLLNQSKPL-------V 179
Cdd:COG0524 109 RGANAELTpedLDEALLAGADILHLGGITLAsepprEALLAALEAARAAGVPVSLDPNYRPALWEPARELLRellalvdI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 180 MKPNIDEFQTMINTffhdqQSLIAAIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSSItPKQVVSTTGAGDTLLAVFL 257
Cdd:COG0524 189 LFPNEEEAELLTGE-----TDPEEAAAALLarGVKLVVVTLGAEGALLYTGGEVVHVPAF-PVEVVDTTGAGDAFAAGFL 262
|
250 260
....*....|....*....|....*...
gi 499171726 258 ANLILKVDLKTALIKATNYASATISKLG 285
Cdd:COG0524 263 AGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
38-282 |
1.64e-14 |
|
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: 72.35 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 38 PGGKGINVAIVMKSLGFDPTVITFLGQP-TKNLFLELVKPYDLNIVSFISETK-TRINLKLLkdektTEINDLSPLITDA 115
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDDsEGESILEESEKAGLNVRGIVFEGRsTASYTAIL-----DKDGDLVVALADM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 116 NLTELLT-----FLKANVKNNDLVIINGRFKFEALEKVLNLvfTLTENVVIDVDESKMLTLLNQSKPL----VMKPNIDE 186
Cdd:cd01941 109 DIYELLTpdflrKIREALKEAKPIVVDANLPEEALEYLLAL--AAKHGVPVAFEPTSAPKLKKLFYLLhaidLLTPNRAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 187 FQTMINTFFHDQQSLIAAIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSS---ITPKQVVSTTGAGDTLLAVFLANLI 261
Cdd:cd01941 187 LEALAGALIENNEDENKAAKILLlpGIKNVIVTLGAKGVLLSSREGGVETKLfpaPQPETVVNVTGAGDAFVAGLVAGLL 266
|
250 260
....*....|....*....|.
gi 499171726 262 LKVDLKTALIKATNYASATIS 282
Cdd:cd01941 267 EGMSLDDSLRFAQAAAALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
26-285 |
4.21e-14 |
|
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: 71.05 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 26 VDLNKQKNsvlIPGGKGiNVAIVMKSLGFDPTVITFLGQ-PTKNLFLELVKPYDLNiVSFISE------TKTRI---NLK 95
Cdd:cd01172 30 VKVEREEI---RLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGID-TDGIVDegrpttTKTRViarNQQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 96 LLK-DEKtteinDLSPlITDANLTELLTFLKANVKNNDLVII----NGRFKFEALEKVLNLVFTLTENVVID---VDESK 167
Cdd:cd01172 105 LLRvDRE-----DDSP-LSAEEEQRLIERIAERLPEADVVILsdygKGVLTPRVIEALIAAARELGIPVLVDpkgRDYSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 168 ML--TLLnqskplvmKPNIDEFQTMINTFFHDQQSLIAA---IKKFHYCKLLLLSDGDKGAYLFDQNKLLFVSSITPKQV 242
Cdd:cd01172 179 YRgaTLL--------TPNEKEAREALGDEINDDDELEAAgekLLELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKEV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499171726 243 VSTTGAGDTLLAVFLANLILKVDLKTALIKAtNYASAT-ISKLG 285
Cdd:cd01172 251 YDVTGAGDTVIATLALALAAGADLEEAAFLA-NAAAGVvVGKVG 293
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
38-287 |
1.91e-13 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 69.45 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 38 PGGKGiNVAIVMKSLGFDPTVITFLGQ-PTKNLFLELVKpyDLNI-VSFISE-------TKTRI---NLKLLK-DEKTTE 104
Cdd:COG2870 55 PGGAA-NVAANLAALGAQVTLVGVVGDdEAGRELRRLLE--EAGIdTDGLVVdprrpttTKTRViagGQQLLRlDFEDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 105 indlspLITDANLTELLTFLKANVKNNDLVIINGRFKFealekvlnlvfTLTENVVidvdeSKMLTLLNQSKPLV----- 179
Cdd:COG2870 132 ------PLSAELEARLLAALEAALPEVDAVILSDYGKG-----------VLTPELI-----QALIALARAAGKPVlvdpk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 180 ------------MKPNIDEFQTMINTFFHDQQSLIAA----IKKFHyCKLLLLSDGDKGAYLFDQNKLLFVSSITPKQVV 243
Cdd:COG2870 190 grdfsryrgatlLTPNLKEAEAAVGIPIADEEELVAAaaelLERLG-LEALLVTRGEEGMTLFDADGPPHHLPAQAREVF 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499171726 244 STTGAGDTLLAVFLANLILKVDLKTALIKAtNYASA-TISKLGVV 287
Cdd:COG2870 269 DVTGAGDTVIATLALALAAGASLEEAAELA-NLAAGiVVGKLGTA 312
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
182-289 |
1.25e-11 |
|
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: 63.72 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 182 PNIDEFQTMINTFFHDQQSLIAAIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSSITPKqVVSTTGAGDTLLAVFLAN 259
Cdd:cd01174 181 PNETEAALLTGIEVTDEEDAEKAARLLLakGVKNVIVTLGAKGALLASGGEVEHVPAFKVK-AVDTTGAGDTFIGALAAA 259
|
90 100 110
....*....|....*....|....*....|
gi 499171726 260 LILKVDLKTALIKATNYASATISKLGVVDS 289
Cdd:cd01174 260 LARGLSLEEAIRFANAAAALSVTRPGAQPS 289
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
26-284 |
1.61e-10 |
|
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: 60.11 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 26 VDLNKQKNS-VLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKPYDLNIVSFISETkTRINLKLLKDEKTTE 104
Cdd:cd01937 10 IDEIVTNGSgVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLLSTET-TTFELNYTNEGRTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 105 INDLSPLITDanltellTFLKANVKNNDLVIINGRFK--FEALEKVLNLVFTLTENVVIDVDESKMLTLLNQSKPLVMKP 182
Cdd:cd01937 89 LLAKCAAIPD-------TESPLSTITAEIVILGPVPEeiSPSLFRKFAFISLDAQGFLRRANQEKLIKCVILKLHDVLKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 183 NIDEFQTMintffHDQQSLIAAIKKFhYCKLLLLSDGDKGAYLFDQNKLLFVSSiTPKQVVSTTGAGDTLLAVFLANLIL 262
Cdd:cd01937 162 SRVEAEVI-----STPTELARLIKET-GVKEIIVTDGEEGGYIFDGNGKYTIPA-SKKDVVDPTGAGDVFLAAFLYSRLS 234
|
250 260
....*....|....*....|..
gi 499171726 263 KVDLKtaliKATNYASATISKL 284
Cdd:cd01937 235 GKDIK----EAAEFAAAAAAKF 252
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
38-273 |
2.81e-10 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 60.12 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 38 PGGKGINVAIVMKSLGfDPTVITFLGQPTKNLFLElvKPYDLNIVSFISETK--TRINLKLLKDEKTTEINDLSPLITDA 115
Cdd:PRK13508 35 AGGKGLNVTRVLSEFG-ENVLATGLIGGELGQFIA--EHLDDQIKHAFYKIKgeTRNCIAILHEGQQTEILEKGPEISVQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 116 NLTELLTFLKANVKNNDLVIINGrfkfeALEKVLN------LVFTLTEN---VVIDVD-ESKMLTLLNQSKPLVMKPNID 185
Cdd:PRK13508 112 EADGFLHHFKQLLESVEVVAISG-----SLPAGLPvdyyaqLIELANQAgkpVVLDCSgAALQAVLESPYKPTVIKPNIE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 186 EFQTMIN-TFFHDQQSLIAAIKK--FHYCKLLLLSDGDKGAylFDQNKLLFVSSITPK-QVVSTTGAGDTLLAVFLANLI 261
Cdd:PRK13508 187 ELSQLLGkEVSEDLDELKEVLQQplFEGIEWIIVSLGADGA--FAKHNDTFYKVDIPKiEVVNPVGSGDSTVAGIASGLL 264
|
250
....*....|..
gi 499171726 262 LKVDLKTALIKA 273
Cdd:PRK13508 265 HQEDDADLLKKA 276
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
202-285 |
3.69e-10 |
|
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: 59.57 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 202 IAAIKKFHYCKLLLLSDGDKGAYLFDQNKLLFVSSITPKqVVSTTGAGDTLLAVFLANL-------ILKVDLKTALIKAT 274
Cdd:cd01167 204 IAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVE-VVDTTGAGDAFVAGLLAQLlsrgllaLDEDELAEALRFAN 282
|
90
....*....|.
gi 499171726 275 NYASATISKLG 285
Cdd:cd01167 283 AVGALTCTKAG 293
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
132-261 |
1.38e-08 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 53.64 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 132 DLVIINGRF-KFEALEKVLNLVFTLTENVVIDV-------DESKMLTLLNQskPLVMKPNIDEFQTMINTFFHDQQSLIA 203
Cdd:cd00287 59 DAVVISGLSpAPEAVLDALEEARRRGVPVVLDPgpravrlDGEELEKLLPG--VDILTPNEEEAEALTGRRDLEVKEAAE 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 204 AIKKFH--YCKLLLLSDGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANLI 261
Cdd:cd00287 137 AAALLLskGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
182-285 |
4.23e-08 |
|
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: 53.35 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 182 PNIDEFQTMinTFFHDQQSLIAAIKKFHY-CKLLLLSDGDKGAYLFDQNKLLFVSSiTPKQVVSTTGAGDTLLAVFLANL 260
Cdd:cd01166 191 PSEEEAEAL--LGDEDPTDAAERALALALgVKAVVVKLGAEGALVYTGGGRVFVPA-YPVEVVDTTGAGDAFAAGFLAGL 267
|
90 100
....*....|....*....|....*
gi 499171726 261 ILKVDLKTALIKATNYASATISKLG 285
Cdd:cd01166 268 LEGWDLEEALRFANAAAALVVTRPG 292
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
32-286 |
8.93e-08 |
|
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: 52.42 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 32 KNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQP-TKNLFLELVKPYDLNIVSFISETKTRINLKLLKdektteiNDLSP 110
Cdd:cd01947 29 SDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDeIGIQSLEELESGGDKHTVAWRDKPTRKTLSFID-------PNGER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 111 LITDA--NLTELLTFlkANVKNNDLVIINGR------FKFEALEKVLNLVFTLTENVVIDVDESKMLTLLNQSKplvmkp 182
Cdd:cd01947 102 TITVPgeRLEDDLKW--PILDEGDGVFITAAavdkeaIRKCRETKLVILQVTPRVRVDELNQALIPLDILIGSR------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 183 niDEFQTmintffHDQQSLIAAIKKfhycKLLLLSDGDKGAYLFDQNKLlFVSSITPKQVVSTTGAGDTLLAVFLANLIL 262
Cdd:cd01947 174 --LDPGE------LVVAEKIAGPFP----RYLIVTEGELGAILYPGGRY-NHVPAKKAKVPDSTGAGDSFAAGFIYGLLK 240
|
250 260
....*....|....*....|....
gi 499171726 263 KVDLKTALIKATNYASATISKLGV 286
Cdd:cd01947 241 GWSIEEALELGAQCGAICVSHFGP 264
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
183-281 |
1.39e-07 |
|
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: 51.85 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 183 NIDEFQTMINTFFHDqqSLIAAIKKFH-YCKLLLLSDGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANLI 261
Cdd:cd01168 207 NEEEAEALAEAETTD--DLEAALKLLAlRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLV 284
|
90 100
....*....|....*....|
gi 499171726 262 LKVDLKTAlIKATNYASATI 281
Cdd:cd01168 285 QGEPLEEC-IRLGSYAAAEV 303
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
164-260 |
2.22e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 51.48 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 164 DESKMLTLLNQSKPL--VMKPNIDEFQTMINTffHDQQSLIAAIKKFHYCKLLLLSDGDKGAYLFDQNKLLFVSSiTPKQ 241
Cdd:PRK09434 166 DEAELRECLRQALALadVVKLSEEELCFLSGT--SQLEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPA-PSVD 242
|
90
....*....|....*....
gi 499171726 242 VVSTTGAGDTLLAVFLANL 260
Cdd:PRK09434 243 PVDTTGAGDAFVAGLLAGL 261
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
201-285 |
7.75e-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: 49.27 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 201 LIAAIKKFHY--CKLLLLSDGDKGAYLFDQNKLlFVSSITPKQVVSTTGAGDTLLAVFLANLILKVD-LKTALIKATNYA 277
Cdd:cd01940 176 VKAKLKEAVSrgAKLVIVTRGEDGAIAYDGAVF-YSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTaIAEAMRQGAQFA 254
|
....*...
gi 499171726 278 SATISKLG 285
Cdd:cd01940 255 AKTCGHEG 262
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
219-285 |
1.77e-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: 1.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499171726 219 GDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLG 285
Cdd:cd01942 211 GPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
182-275 |
7.84e-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: 43.34 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 182 PNIDEFQTMINTFFHDQQSLIAAIKKFH--YCKLLLLS------DGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLL 253
Cdd:cd01173 142 PNQFELELLTGKKINDLEDAKAAARALHakGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFPAYFNGTGDLFA 221
|
90 100
....*....|....*....|..
gi 499171726 254 AVFLANLILKVDLKTALIKATN 275
Cdd:cd01173 222 ALLLARLLKGKSLAEALEKALN 243
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
182-283 |
4.42e-04 |
|
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: 40.93 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 182 PNIDEFQTMINTFFHDQQSLIAAIKKFH--YCKLLLL----SDGDKGA---YLFDQNKLLFVSSitpkQVVSTT---GAG 249
Cdd:pfam08543 125 PNLPEAEALTGRKIKTLEDMKEAAKKLLalGAKAVLIkgghLEGEEAVvtdVLYDGGGFYTLEA----PRIPTKnthGTG 200
|
90 100 110
....*....|....*....|....*....|....
gi 499171726 250 DTLLAVFLANLILKVDLKTALIKATNYASATISK 283
Cdd:pfam08543 201 CTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRD 234
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
209-285 |
5.88e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 40.95 E-value: 5.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499171726 209 HYCKLLLLSDGDKGAYLFDQNKLLFVSSiTPKQVVSTTGAGDTLLAVFLANLILKV-DLKTALIKATNYASATISKLG 285
Cdd:PLN02813 314 HFCPLVSVTDGARGSYIGVKGEAVYIPP-SPCVPVDTCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQG 390
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
15-254 |
1.26e-03 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 39.97 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 15 IVNYACAIDYYVDLNKQKNSvLIPGGKGINVAIVMKSLGFDPTVIT-----FLGQptkNLFLELVKP-YDLNIVSFISET 88
Cdd:PRK09850 17 VAGYSHESLNYADSNPGKIK-FTPGGVGRNIAQNLALLGNKAWLLSavgsdFYGQ---SLLTQTNQSgVYVDKCLIVPGE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 89 KTRINLKLLKD--EKTTEINDLSplITDANLTELLTFLKANVKNNDLVIINGRFKFEALEKVLNLVFTLTenVVID-VDE 165
Cdd:PRK09850 93 NTSSYLSLLDNtgEMLVAINDMN--ISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAANVP--VFVDpVSA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 166 SKMLTLLNQ-SKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFHYCKL--LLLSDGDKGAYLFDQNKLLFVSSITPKQV 242
Cdd:PRK09850 169 WKCVKVRDRlNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLnrLVLSMGGDGVYYSDISGESGWSAPIKTNV 248
|
250
....*....|..
gi 499171726 243 VSTTGAGDTLLA 254
Cdd:PRK09850 249 INVTGAGDAMMA 260
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
179-281 |
1.75e-03 |
|
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: 39.36 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 179 VMKPNIDEFQTMINTFFHDQQSLIAAIKKfhyckllLLSDGDK-----------------GAYLFDQNKLLFVSsiTPKQ 241
Cdd:COG2240 141 IITPNLTELALLTGRPYETLEEALAAARA-------LLALGPKivvvtsvplddtpadkiGNLAVTADGAWLVE--TPLL 211
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499171726 242 VVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATI 281
Cdd:COG2240 212 PFSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVL 251
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
212-286 |
1.79e-03 |
|
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: 39.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 212 KLLLLSDGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANL-----ILKVDLKTALIKATNYASATISKLGV 286
Cdd:cd01946 196 KALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFIGYLasqkdTSEANMRRAIIYGSAMASFCVEDFGT 275
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
203-260 |
3.83e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 38.45 E-value: 3.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499171726 203 AAIKKFH-YCKLLLLSDGDKGAYLFDQNKLLFVSSItPKQVVSTTGAGDTLLAVFLANL 260
Cdd:PLN02323 221 TVVKLWHpNLKLLLVTEGEEGCRYYTKDFKGRVEGF-KVKAVDTTGAGDAFVGGLLSQL 278
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
192-285 |
4.56e-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: 38.17 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171726 192 NTFFHDQQSLIAAIKKFHYCKL---LLLSDGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANLILKVDLKT 268
Cdd:cd01944 193 AIFAERGDPAAEASALRIYAKTaapVVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLAD 272
|
90
....*....|....*..
gi 499171726 269 ALIKATNYASATISKLG 285
Cdd:cd01944 273 AVLLANAAAAIVVTRSG 289
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
239-286 |
6.57e-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: 37.71 E-value: 6.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499171726 239 PKQVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGV 286
Cdd:cd01943 257 STKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGL 304
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
219-285 |
8.43e-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: 37.39 E-value: 8.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499171726 219 GDKGA-YLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFL-ANLILKVDLKTALIKATNYASATISKLG 285
Cdd:cd01939 220 GDQGAgALGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIyALNKGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| |
