|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
1-298 |
6.01e-100 |
|
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: 295.31 E-value: 6.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLPRQTTLGEAgFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLS- 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPET-FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 80 RPTTIAFVKLV-DGHATYAFYDENTAGRMITEAELPALGADCEALHFGAISLIPEPCGSTYEALMTREQES-RVISLDPN 157
Cdd:cd01167 80 APTTLAFVTLDaDGERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAgVLISFDPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 158 IRPGFIKDKQSHMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHWLHHGAKLVVVTRGAKGAVGYTTGLKVEVASE 237
Cdd:cd01167 160 LRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739226067 238 RVEVVDTVGAGDTFDAGILASLKMQGLLTkaqvasLTEEQIRKALALGAKAAAVTVSRAGA 298
Cdd:cd01167 240 PVEVVDTTGAGDAFVAGLLAQLLSRGLLA------LDEDELAEALRFANAVGALTCTKAGA 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
1-268 |
5.34e-67 |
|
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: 211.67 E-value: 5.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLPRQTTLGEAG-------FAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFS 73
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGetvlagsFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 74 YCATLS-RPTTIAFVKL-VDGHATYAFYDenTAGRMITEAELP-ALGADCEALHFGAISLIPEPCGSTYEALMTREQESR 150
Cdd:COG0524 81 GVRRDPgAPTGLAFILVdPDGERTIVFYR--GANAELTPEDLDeALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 151 V-ISLDPNIRPGFIKDkqsHMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHWLHHGAKLVVVTRGAKGAVGYTTG 229
Cdd:COG0524 159 VpVSLDPNYRPALWEP---ARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 739226067 230 LKVEVASERVEVVDTVGAGDTFDAGILASLKMQGLLTKA 268
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEA 274
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-259 |
3.58e-46 |
|
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: 157.74 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 2 ILCCGEALIDMLPRQTTLGE--AGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSY-CATL 78
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEqaDSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHvRVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 79 SRPTTIAFVKLVDGHATYAFYD-ENTAGRMITEAELPALG-ADCEALHFGAISL-IPEPCGSTYEALMTREQESRV-ISL 154
Cdd:cd01166 82 GRPTGLYFLEIGAGGERRVLYYrAGSAASRLTPEDLDEAAlAGADHLHLSGITLaLSESAREALLEALEAAKARGVtVSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 155 DPNIRPGFIKDKQSHmARIRRMAAMSDIVKFSDEDL-AWFGLEGDEDTLAR-HWLHHGAKLVVVTRGAKGAVGYTTGLKV 232
Cdd:cd01166 162 DLNYRPKLWSAEEAR-EALEELLPYVDIVLPSEEEAeALLGDEDPTDAAERaLALALGVKAVVVKLGAEGALVYTGGGRV 240
|
250 260
....*....|....*....|....*..
gi 739226067 233 EVASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01166 241 FVPAYPVEVVDTTGAGDAFAAGFLAGL 267
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-279 |
6.51e-41 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 144.76 E-value: 6.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLPRQT--TLGEA-GFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCA- 76
Cdd:PLN02323 12 LVVCFGEMLIDFVPTVSgvSLAEApAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 77 -TLSRpTTIAFVKL-VDGHATYAFYDENTAGRMITEAELPA-LGADCEALHFGAISLIPEPCGSTYEALMTREQESRVI- 152
Cdd:PLN02323 92 dPGAR-TALAFVTLrSDGEREFMFYRNPSADMLLRESELDLdLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 153 SLDPNIRPGFIKDKQSHMARIRRMAAMSDIVKFSDEDLAWF--GLEGDEDTLARHWlHHGAKLVVVTRGAKGAVGYTTGL 230
Cdd:PLN02323 171 SYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLtgGDDPDDDTVVKLW-HPNLKLLLVTEGEEGCRYYTKDF 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 739226067 231 KVEVASERVEVVDTVGAGDTFDAGILASLkmqglltkAQVASLTEEQIR 279
Cdd:PLN02323 250 KGRVEGFKVKAVDTTGAGDAFVGGLLSQL--------AKDLSLLEDEER 290
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
6-266 |
4.37e-38 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 136.60 E-value: 4.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 6 GEALIDMLPRqttlGEAGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCA--TLSRPTT 83
Cdd:PRK09434 9 GDAVVDLIPE----GENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRldPAHRTST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 84 IAfVKLVD-GHATYAFYDENTAGRMITEAELPALGADcEALHFGAISLIPEPC-GSTYEALMTREQESRVISLDPNIRPG 161
Cdd:PRK09434 85 VV-VDLDDqGERSFTFMVRPSADLFLQPQDLPPFRQG-EWLHLCSIALSAEPSrSTTFEAMRRIKAAGGFVSFDPNLRED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 162 FIKDKQSHMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTlARHWL--HHGAKLVVVTRGAKGAVGYTTGLKVEVASERV 239
Cdd:PRK09434 163 LWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLED-AIYALadRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSV 241
|
250 260
....*....|....*....|....*..
gi 739226067 240 EVVDTVGAGDTFDAGILASLKMQGLLT 266
Cdd:PRK09434 242 DPVDTTGAGDAFVAGLLAGLSQAGLWT 268
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
1-259 |
1.30e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 127.46 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLPRQTTLGE-----AGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYC 75
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGelvrvSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 76 -ATLSRPTTIAFVkLVDGHATYAFYDENTAGRMITEAELPALGADCEA---LHFGAiSLIPEPCGSTYEALMTREQESRV 151
Cdd:pfam00294 81 vIDEDTRTGTALI-EVDGDGERTIVFNRGAAADLTPEELEENEDLLENadlLYISG-SLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 152 isLDPNIRPGFIKDKQshmaRIRRMAAMSDIVKFSDEDL-AWFGLEGDEDTLARHWLH----HGAKLVVVTRGAKGAVGY 226
Cdd:pfam00294 159 --FDPNLLDPLGAARE----ALLELLPLADLLKPNEEELeALTGAKLDDIEEALAALHkllaKGIKTVIVTLGADGALVV 232
|
250 260 270
....*....|....*....|....*....|....
gi 739226067 227 TTGLKVEVASER-VEVVDTVGAGDTFDAGILASL 259
Cdd:pfam00294 233 EGDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGL 266
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
27-259 |
1.92e-21 |
|
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: 91.26 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 27 YAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSRPTTIAFVKLVDGHATYAFYDEN-TAG 105
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVDGDRIFGLSNKGgVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 106 RMITEAELPALGAdCEALHFGAISLIpepcGSTYEALMTREQESRVISLDPNIRpgfikdkqSHMARIRRMAAMSDIVKF 185
Cdd:cd01940 100 EHPFEADLEYLSQ-FDLVHTGIYSHE----GHLEKALQALVGAGALISFDFSDR--------WDDDYLQLVCPYVDFAFF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739226067 186 SDEDLawfGLEGDEDTLARHwLHHGAKLVVVTRGAKGAVGYTTGLKVEVASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01940 167 SASDL---SDEEVKAKLKEA-VSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSL 236
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
2-274 |
9.00e-19 |
|
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: 84.28 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 2 ILCCGEALIDMLPRQTTL---GEAGFAP----YAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSY 74
Cdd:cd01942 2 VAVVGHLNYDIILKVESFpgpFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 75 CATLSR-PTTIAFVkLVDGHATYAFYDENTAGRMITEAELPALGADCEALHFGAISLIPEpcgstyealMTREQESRV-- 151
Cdd:cd01942 82 VRVVDEdSTGVAFI-LTDGDDNQIAYFYPGAMDELEPNDEADPDGLADIVHLSSGPGLIE---------LARELAAGGit 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 152 ISLDPNIR-PGFIKDkqshmaRIRRMAAMSDIVkFSDEDLAWFGLE---GDEDTLARHwlhhgAKLVVVTRGAKGAVGYT 227
Cdd:cd01942 152 VSFDPGQElPRLSGE------ELEEILERADIL-FVNDYEAELLKErtgLSEAELASG-----VRVVVVTLGPKGAIVFE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 739226067 228 TGLKVEVASE-RVEVVDTVGAGDTFDAG-ILASLKMQGLLTKAQVASLT 274
Cdd:cd01942 220 DGEEVEVPAVpAVKVVDTTGAGDAFRAGfLYGLLRGYDLEESLRLGNLA 268
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-264 |
6.78e-18 |
|
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: 82.28 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 9 LIDMlPRQTTLGEAGFAPY-AGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSRPTTIAFV 87
Cdd:cd01168 35 LADM-EEQEELLAKLPVKYiAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 88 kLV--DGHATYAFYDEnTAGRMITEAELPALGADCEALHFGAISLIPEPCGSTYEALMTREqESRVISL---DPNIrpgf 162
Cdd:cd01168 114 -LVtpDAERTMCTYLG-AANELSPDDLDWSLLAKAKYLYLEGYLLTVPPEAILLAAEHAKE-NGVKIALnlsAPFI---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 163 ikdKQSHMARIRRMAAMSDIVkFSDED--LAWFGLEGDED-TLARHWLHHGAKLVVVTRGAKGAVGYTTGLKVEVASERV 239
Cdd:cd01168 187 ---VQRFKEALLELLPYVDIL-FGNEEeaEALAEAETTDDlEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPV 262
|
250 260
....*....|....*....|....*.
gi 739226067 240 E-VVDTVGAGDTFDAGILASLkMQGL 264
Cdd:cd01168 263 EkIVDTNGAGDAFAGGFLYGL-VQGE 287
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
4-256 |
8.90e-18 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 80.94 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 4 CCGEALIDMLPRqttLGEAgfapYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSRPTT 83
Cdd:PRK09813 5 TIGDNCVDIYPQ---LGKA----FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 84 IAFVKLVDGHATYAFYDENT-AGRMITEAELPALgADCEALHFGAislipepCGSTYEALMTREQESRVISLDPNIRPGf 162
Cdd:PRK09813 78 QTQVELHDNDRVFGDYTEGVmADFALSEEDYAWL-AQYDIVHAAI-------WGHAEDAFPQLHAAGKLTAFDFSDKWD- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 163 ikdkqshmarirrmaamSDIVKFSDEDLAW-FGLEGDEDTLARHWLHH----GAKLVVVTRGAKGAVGYTTGLKVEVASE 237
Cdd:PRK09813 149 -----------------SPLWQTLVPHLDYaFASAPQEDEFLRLKMKAivarGAGVVIVTLGENGSIAWDGAQFWRQAPE 211
|
250
....*....|....*....
gi 739226067 238 RVEVVDTVGAGDTFDAGIL 256
Cdd:PRK09813 212 PVTVVDTMGAGDSFIAGFL 230
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
10-274 |
1.15e-17 |
|
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: 81.44 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 10 IDMLPR--QTTLGEaGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSR-PTTIAF 86
Cdd:cd01174 16 VDRLPKpgETVLGS-SFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGaPTGTAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 87 VkLVDGHAtyafydENT------AGRMITEAELPALGADCEALHFgaISL---IPEPcgSTYEAL-MTREQESRVIsLDP 156
Cdd:cd01174 95 I-TVDESG------ENRivvvpgANGELTPADVDAALELIAAADV--LLLqleIPLE--TVLAALrAARRAGVTVI-LNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 157 nirpgfikdkqshmARIRRMAAmsDIVKFSD-------EDLAWFGLEGDE----DTLARHWLHHGAKLVVVTRGAKGAVG 225
Cdd:cd01174 163 --------------APARPLPA--ELLALVDilvpnetEAALLTGIEVTDeedaEKAARLLLAKGVKNVIVTLGAKGALL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 739226067 226 YTTGLKVEVASERVEVVDTVGAGDTFDAGILASLkMQGLLTK------AQVASLT 274
Cdd:cd01174 227 ASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAAL-ARGLSLEeairfaNAAAALS 280
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-259 |
2.48e-14 |
|
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: 71.68 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 29 GGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRaSHVDFSYCATLSRPTTIAFVkLVDGHATYAFYDENTAgrmi 108
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SGGDKHTVAWRDKPTRKTLS-FIDPNGERTITVPGER---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 109 TEAELPAlgadCEALHFGAISLIPEPCGStyEALMTREQESRVIsLDPNIRPGFIKDKQSHMarirrmaaMSDIVKFSDE 188
Cdd:cd01947 110 LEDDLKW----PILDEGDGVFITAAAVDK--EAIRKCRETKLVI-LQVTPRVRVDELNQALI--------PLDILIGSRL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739226067 189 DlawFGLEGDEDTLARHwlhhGAKLVVVTRGAKGAVGYTTGLKVEVASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01947 175 D---PGELVVAEKIAGP----FPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGL 238
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
102-259 |
3.39e-14 |
|
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: 69.82 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 102 NTAGRMITEAELpaLGADceALHFGAISLIPEPCGstyEALMTREQESRVISLDPNIRPGFIKDKQshmarIRRMAAMSD 181
Cdd:cd00287 44 VALARLGVSVTL--VGAD--AVVISGLSPAPEAVL---DALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 182 IVKFSDEDL-AWFGLEGDEDT----LARHWLHHGAKLVVVTRGAKGAVGYTTG-LKVEVASERVEVVDTVGAGDTFDAGI 255
Cdd:cd00287 112 ILTPNEEEAeALTGRRDLEVKeaaeAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHVPAFPVKVVDTTGAGDAFLAAL 191
|
....
gi 739226067 256 LASL 259
Cdd:cd00287 192 AAGL 195
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
27-259 |
9.66e-14 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 70.16 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 27 YAGGAVFNTAIALGRLGVPS-AffTGLSDDMMGDILRETLRASHV--DFSYCATLSRpTTIAFVKLVDGHaTYAFydeNT 103
Cdd:COG1105 33 DPGGKGINVARVLKALGVDVtA--LGFLGGFTGEFIEELLDEEGIptDFVPIEGETR-INIKIVDPSDGT-ETEI---NE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 104 AGRMITEAELPALgadCEALHfgaiSLIPEP-----CGS--------TYEALMT--REQESRVIsLD---PNIRPGfikd 165
Cdd:COG1105 106 PGPEISEEELEAL---LERLE----ELLKEGdwvvlSGSlppgvppdFYAELIRlaRARGAKVV-LDtsgEALKAA---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 166 kqshmarirrMAAMSDIVKFSDEDLA-WFG--LEGDEDTL--ARHWLHHGAKLVVVTRGAKGAVGYTTGLKVEVASERVE 240
Cdd:COG1105 174 ----------LEAGPDLIKPNLEELEeLLGrpLETLEDIIaaARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVE 243
|
250
....*....|....*....
gi 739226067 241 VVDTVGAGDTFDAGILASL 259
Cdd:COG1105 244 VVSTVGAGDSMVAGFLAGL 262
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
2-259 |
2.22e-13 |
|
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: 68.88 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 2 ILCCGEALID--------MLPRQTTLGEAGFAPyaGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFS 73
Cdd:cd01941 2 IVVIGAANIDlrgkvsgsLVPGTSNPGHVKQSP--GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 74 YCATLSRPTtiafvklvdghATY-AFYDENtagrmiteAELPALGADcealhFGAISLIPEPCGSTYEALMTREQES--- 149
Cdd:cd01941 80 GIVFEGRST-----------ASYtAILDKD--------GDLVVALAD-----MDIYELLTPDFLRKIREALKEAKPIvvd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 150 ---------RVISL--DPNIRPGFIKDKQSHMARIRRMAAMSDIVKFS-DEDLAWFG--LEGDEDTLARH--WLHHGAKL 213
Cdd:cd01941 136 anlpeealeYLLALaaKHGVPVAFEPTSAPKLKKLFYLLHAIDLLTPNrAELEALAGalIENNEDENKAAkiLLLPGIKN 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 739226067 214 VVVTRGAKGAvgYTTGLKVEV------ASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01941 216 VIVTLGAKGV--LLSSREGGVetklfpAPQPETVVNVTGAGDAFVAGLVAGL 265
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
28-259 |
6.51e-13 |
|
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: 67.99 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 28 AGGAVFNTAIALGRLGVPSAFfTGLSDDMMGDILRETLRASHV--DFSYCATLSRPTtiafVKLVDGHATYafYDENTAG 105
Cdd:TIGR03168 34 AGGKGINVARVLARLGAEVVA-TGFLGGFTGEFIEALLAEEGIknDFVEVKGETRIN----VKIKESSGEE--TELNEPG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 106 RMITEAELPALGADCEALhfgaislIPEP-----CGS--------TYEALM--TREQESRVIsLDpnirpgfikdkQSHM 170
Cdd:TIGR03168 107 PEISEEELEQLLEKLREL-------LASGdivviSGSlppgvppdFYAQLIaiARKKGAKVI-LD-----------TSGE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 171 ARIRRMAAMSDIVKFSDEDLA-WFG--LEGDEDTL--ARHWLHHGAKLVVVTRGAKGAVGYT--TGLKVEVAseRVEVVD 243
Cdd:TIGR03168 168 ALREALAAKPFLIKPNHEELEeLFGreLKTLEEIIeaARELLDRGAENVLVSLGADGALLVTkeGALKATPP--KVEVVN 245
|
250
....*....|....*.
gi 739226067 244 TVGAGDTFDAGILASL 259
Cdd:TIGR03168 246 TVGAGDSMVAGFLAGL 261
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
10-306 |
9.02e-13 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 67.24 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 10 IDMLPR--QTTLGEaGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSR-PTTIAF 86
Cdd:TIGR02152 11 TDRLPKpgETVHGH-SFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDtPTGTAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 87 VKLVDGhatyafyDENT------AGRMITEAELPALGADCEALHFGAISL-IPEPcgSTYEAL-MTREQESRVIsLDPni 158
Cdd:TIGR02152 90 ITVDDT-------GENRivvvagANAELTPEDIDAAEALIAESDIVLLQLeIPLE--TVLEAAkIAKKHGVKVI-LNP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 159 RPGFIKDKQShmarirrMAAMSD-IVKFSDEDLAWFGLE-GDEDTL---ARHWLHHGAKLVVVTRGAKGAVGYTTGLKVE 233
Cdd:TIGR02152 158 APAIKDLDDE-------LLSLVDiITPNETEAEILTGIEvTDEEDAekaAEKLLEKGVKNVIITLGSKGALLVSKDESKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 234 VASERVEVVDTVGAGDTFDAGiLASLKMQGL-----LTKAQVASlteeqirkalalgakaaAVTVSRAGANP--PFAHEI 306
Cdd:TIGR02152 231 IPAFKVKAVDTTAAGDTFNGA-FAVALAEGKsledaIRFANAAA-----------------AISVTRKGAQSsiPYLEEV 292
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
28-268 |
9.86e-13 |
|
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: 67.17 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 28 AGGAVFNTAIALGRLGVPSA--FFTGlsdDMMGDILRETLRASHV--DFSYCATLSRPTtiafVKLVDGHATYafYDENT 103
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTalGFLG---GFTGDFFEALLKEEGIpdDFVEVAGETRIN----VKIKEEDGTE--TEINE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 104 AGRMITEAELPALGADCEAL--HFGAISLipepCGS--------TYEALMT--REQESRVIsLDpnirpgfikdkQSHMA 171
Cdd:cd01164 106 PGPEISEEELEALLEKLKALlkKGDIVVL----SGSlppgvpadFYAELVRlaREKGARVI-LD-----------TSGEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 172 RIRRMAAMSDIVKFSDEDL-AWFGLE-GDEDTL---ARHWLHHGAKLVVVTRGAKGAVGYTTGLKVEVASERVEVVDTVG 246
Cdd:cd01164 170 LLAALAAKPFLIKPNREELeELFGRPlGDEEDViaaARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVG 249
|
250 260
....*....|....*....|..
gi 739226067 247 AGDTFDAGILASLKMQGLLTKA 268
Cdd:cd01164 250 AGDSMVAGFVAGLAQGLSLEEA 271
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
11-255 |
1.01e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 68.32 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 11 DMLPRQTTLGEAGFAP------YAGGAVfNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRA---SHV------DFSYC 75
Cdd:PLN02341 96 SREERKAYMEELAASPpdkkswEAGGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEegiSVVgliegtDAGDS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 76 ATLSRPTTIAFVkLVDGHATYAF---YD--ENTAGRMITE--AELPALGADCEALH---FGAISLIPEPCGStyeALMTR 145
Cdd:PLN02341 175 SSASYETLLCWV-LVDPLQRHGFcsrADfgPEPAFSWISKlsAEAKMAIRQSKALFcngYVFDELSPSAIAS---AVDYA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 146 EQESRVISLDPNIR-PGFIKDKQSHMARIRRMAAMSDIVKFSDEDLAwfGLEGDED-TLARHWLHH---GAKLVVVTRGA 220
Cdd:PLN02341 251 IDVGTAVFFDPGPRgKSLLVGTPDERRALEHLLRMSDVLLLTSEEAE--ALTGIRNpILAGQELLRpgiRTKWVVVKMGS 328
|
250 260 270
....*....|....*....|....*....|....*
gi 739226067 221 KGAVGYTTGLKVEVASERVEVVDTVGAGDTFDAGI 255
Cdd:PLN02341 329 KGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAI 363
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
27-259 |
2.98e-12 |
|
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: 66.07 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 27 YAGGAVFNTAIALGRLGVPSAFfTGLSDDMMGDILRETLRASHVDfSYCATLSRPTTIAfVKLVDGHATYafYDENTAGR 106
Cdd:TIGR03828 33 DAGGKGINVSRVLKNLGVDVVA-LGFLGGFTGDFIEALLREEGIK-TDFVRVPGETRIN-VKIKEPSGTE--TKLNGPGP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 107 MITEAELPALGADCEA-LHFGAISLIpepCGS--------TYEALMTREQESRVisldpnirpGFIKDKqSHMARIRRMA 177
Cdd:TIGR03828 108 EISEEELEALLEKLRAqLAEGDWLVL---SGSlppgvppdFYAELIALAREKGA---------KVILDT-SGEALRDGLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 178 AMSDIVKFSDEDLA-WFG--LEGDEDTL--ARHWLHHGAKLVVVTRGAKGAVgYTTGLKVEVASE-RVEVVDTVGAGDTF 251
Cdd:TIGR03828 175 AKPFLIKPNDEELEeLFGreLKTLEEIIeaARELLDLGAENVLISLGADGAL-LVTKEGALFAQPpKGEVVSTVGAGDSM 253
|
....*...
gi 739226067 252 DAGILASL 259
Cdd:TIGR03828 254 VAGFLAGL 261
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
2-251 |
4.34e-11 |
|
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: 62.31 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 2 ILCCGEALIDMLPR---QTTLGE----AGFAPYAGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSY 74
Cdd:cd01945 2 VLGVGLAVLDLIYLvasFPGGDGkivaTDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 75 CATLSRPTTIAFVKLVD--GHATYAFYDENTAGrmiTEAELP-ALGADCEALHFGaislipepcGSTYEALMTREQESR- 150
Cdd:cd01945 82 IVVAPGARSPISSITDItgDRATISITAIDTQA---APDSLPdAILGGADAVLVD---------GRQPEAALHLAQEARa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 151 -----VISLDPNIrpgfikdkqshMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHWLHhGAKLVVVTRGAKGAVG 225
Cdd:cd01945 150 rgipiPLDLDGGG-----------LRVLEELLPLADHAICSENFLRPNTGSADDEALELLASL-GIPFVAVTLGEAGCLW 217
|
250 260
....*....|....*....|....*..
gi 739226067 226 YT-TGLKVEVASERVEVVDTVGAGDTF 251
Cdd:cd01945 218 LErDGELFHVPAFPVEVVDTTGAGDVF 244
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
8-251 |
2.28e-10 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 60.52 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 8 ALIDMLPR--QTTLGEA---GFapyaGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDfsyCATLSRpt 82
Cdd:PTZ00292 30 GYVDRMPQvgETLHGTSfhkGF----GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN---TSFVSR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 83 tiaFVKLVDGHATYaFYDENTAGRMI------TEAELPALGADCEALHFGAISLI----PEPCGSTYEALmTREQESRVI 152
Cdd:PTZ00292 101 ---TENSSTGLAMI-FVDTKTGNNEIviipgaNNALTPQMVDAQTDNIQNICKYLicqnEIPLETTLDAL-KEAKERGCY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 153 SLdPNIRPGfikDKQSHMARIRRMAAMSDIVKFSDEDLAwfGLEGDEDT-------LARHWLHHGAKLVVVTRGAKG-AV 224
Cdd:PTZ00292 176 TV-FNPAPA---PKLAEVEIIKPFLKYVSLFCVNEVEAA--LITGMEVTdtesafkASKELQQLGVENVIITLGANGcLI 249
|
250 260
....*....|....*....|....*..
gi 739226067 225 GYTTGLKVEVASERVEVVDTVGAGDTF 251
Cdd:PTZ00292 250 VEKENEPVHVPGKRVKAVDTTGAGDCF 276
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
1-268 |
2.33e-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: 59.72 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLPrqtTLGEAGFAPyaGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILretlrashvdfsycatLSR 80
Cdd:cd01937 1 KIVIIGHVTIDEIV---TNGSGVVKP--GGPATYASLTLSRLGLTVKLVTKVGRDYPDKWS----------------DLF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 81 PTTIAFVKLVDGHATYAFYDENTAGRMITEAELPALGADC---------EALHFGAIS--LIPEPCGSTYealmtreqes 149
Cdd:cd01937 60 DNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCAAIPDTesplstitaEIVILGPVPeeISPSLFRKFA---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 150 rVISLDPNirpGFIKDKQSHMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHWlhhGAKLVVVTRGAKGAVGYTTG 229
Cdd:cd01937 130 -FISLDAQ---GFLRRANQEKLIKCVILKLHDVLKLSRVEAEVISTPTELARLIKET---GVKEIIVTDGEEGGYIFDGN 202
|
250 260 270
....*....|....*....|....*....|....*....
gi 739226067 230 LKVEVASERVEVVDTVGAGDTFDAGILASLKMQGLLTKA 268
Cdd:cd01937 203 GKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEA 241
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
1-259 |
9.00e-10 |
|
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: 58.57 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 1 MILCCGEALIDMLprqTTLGEAGFAPYA----------GGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHV 70
Cdd:cd01939 1 AVLCVGLTVLDFI---TTVDKYPFEDSDqrttngrwqrGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 71 DFSYCATLSRPTTIAFVKLVdghatyafydENTAGRMITE--AELPAL------GADCEA---LHF-GAISLIPEPCGST 138
Cdd:cd01939 78 DISHCYRKDIDEPASSYIIR----------SRAGGRTTIVndNNLPEVtyddfsKIDLTQygwIHFeGRNPDETLRMMQH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 139 YEALMTREQESR-VISLDpnirpgFIKDKQSHMarirRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHW-LHHGAKLVVV 216
Cdd:cd01939 148 IEEHNNRRPEIRiTISVE------VEKPREELL----ELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGpRAKKAALLVC 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 739226067 217 TRGAKGAVGYTT-GLKVEVASERVE-VVDTVGAGDTFDAGILASL 259
Cdd:cd01939 218 TWGDQGAGALGPdGEYVHSPAHKPIrVVDTLGAGDTFNAAVIYAL 262
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
25-259 |
4.55e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.04 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 25 APY---AGGAVFNTAIALGRLGVPSA-------FFTG-LSDDMMGDILRETLRASHVDFsycatLSRPT------TIAFV 87
Cdd:PLN02813 119 CSYkasAGGSLSNTLVALARLGSQSAagpalnvAMAGsVGSDPLGDFYRTKLRRANVHF-----LSQPVkdgttgTVIVL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 88 KLVDGHATYAFYdENTAGRMITEAELPALGADCEALHF-GAISLIPEPCGSTYEALMTREQESRVISLDPNiRPGFIKDK 166
Cdd:PLN02813 194 TTPDAQRTMLSY-QGTSSTVNYDSCLASAISKSRVLVVeGYLWELPQTIEAIAQACEEAHRAGALVAVTAS-DVSCIERH 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 167 QSHMARIrrMAAMSDIVkFSDED----LAWFGLEGDEDTLARHwLHHGAKLVVVTRGAKGAVGYTTGLKVEVASERVEVV 242
Cdd:PLN02813 272 RDDFWDV--MGNYADIL-FANSDearaLCGLGSEESPESATRY-LSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPV 347
|
250
....*....|....*..
gi 739226067 243 DTVGAGDTFDAGILASL 259
Cdd:PLN02813 348 DTCGAGDAYAAGILYGL 364
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
10-259 |
6.27e-08 |
|
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: 52.81 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 10 IDMLPRQTTLGEAG-FAPYAGGAvFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHV---------DFSYCAtls 79
Cdd:cd01944 16 VDKLPASGGDIEAKsKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIeillpprggDDGGCL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 80 rpttiafVKLVDGHATYAFYDENTAGRMITEAELPALGADCEALHFGAISLIPEPCGST--YEALMTREQESRVISLDPN 157
Cdd:cd01944 92 -------VALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKviLLEWLEALPAGTTLVFDPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 158 IRPGFIKDkqshmARIRRMAAMSDIVKFSDEDLAWFGLEGD--EDTLARHWLHHGAKLVVVTRGAKGAVGYTTGLKVE-V 234
Cdd:cd01944 165 PRISDIPD-----TILQALMAKRPIWSCNREEAAIFAERGDpaAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHiI 239
|
250 260
....*....|....*....|....*
gi 739226067 235 ASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01944 240 PGFKVKAVDTIGAGDTHAGGMLAGL 264
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
27-259 |
3.10e-07 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 50.97 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 27 YAGGAVfNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSRPTTIafVKL--VDGHATYAFYDEnta 104
Cdd:COG2870 54 RPGGAA-NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTT--TKTrvIAGGQQLLRLDF--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 105 grmitEAELPALGADCEALHFGAISLIPEpcgstYEALmtreqesrVIS------LDPNIRPGFIK------------DK 166
Cdd:COG2870 128 -----EDRFPLSAELEARLLAALEAALPE-----VDAV--------ILSdygkgvLTPELIQALIAlaraagkpvlvdPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 167 QSHMARIRR-------MAAMSDIVKFSDEDlawfglEGDEDTLARHWLHH-GAKLVVVTRGAKGAVGYT-TGLKVEVASE 237
Cdd:COG2870 190 GRDFSRYRGatlltpnLKEAEAAVGIPIAD------EEELVAAAAELLERlGLEALLVTRGEEGMTLFDaDGPPHHLPAQ 263
|
250 260
....*....|....*....|..
gi 739226067 238 RVEVVDTVGAGDTFDAGILASL 259
Cdd:COG2870 264 AREVFDVTGAGDTVIATLALAL 285
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
198-306 |
3.53e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 47.56 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 198 DEDT--LARHWLH-HGAKLVVVTRGAKGAVGYTTGLKVEVASERVEVVDTVGAGDTFD----AGILASLKMQGLLTKAQV 270
Cdd:PRK11142 199 DDDDaaKAAQVLHqKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNgalvTALLEGKPLPEAIRFAHA 278
|
90 100 110
....*....|....*....|....*....|....*...
gi 739226067 271 ASlteeqirkalalgakaaAVTVSRAGANP--PFAHEI 306
Cdd:PRK11142 279 AA-----------------AIAVTRKGAQPsiPWREEI 299
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
20-264 |
3.56e-05 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 44.59 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 20 GEAGFAPyaGGAVFNTAIALGRLGVPSAFFTGLSDDMMGDILRETLRASHVDFSYCATLSRPTTIAFVKLVD--GHATYA 97
Cdd:PRK09850 33 GKIKFTP--GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDntGEMLVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 98 FYDEN-----TAGRMITEAEL----PALGADC----EALHF-----GAISLIPEPCgSTYEALMTREQESRVISLDPNir 159
Cdd:PRK09850 111 INDMNisnaiTAEYLAQHREFiqraKVIVADCniseEALAWildnaANVPVFVDPV-SAWKCVKVRDRLNQIHTLKPN-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 160 pgfikdkqshmarirRMAAmsdivkfsdEDLAWFGLEGDEDTL-ARHWLH-HGAKLVVVTRGAKGaVGYT--TGLKVEVA 235
Cdd:PRK09850 188 ---------------RLEA---------ETLSGIALSGREDVAkVAAWFHqHGLNRLVLSMGGDG-VYYSdiSGESGWSA 242
|
250 260
....*....|....*....|....*....
gi 739226067 236 SERVEVVDTVGAGDTFDAGiLASLKMQGL 264
Cdd:PRK09850 243 PIKTNVINVTGAGDAMMAG-LASCWVDGM 270
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
208-259 |
8.31e-05 |
|
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: 43.32 E-value: 8.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 739226067 208 HHGAKLVVVTRGAKGAVGYTTGLKVE-VASERVEVVDTVGAGDTFDAGILASL 259
Cdd:cd01172 216 LLNLEALLVTLGEEGMTLFERDGEVQhIPALAKEVYDVTGAGDTVIATLALAL 268
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
99-268 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 99 YDENTAGRMITE--------AELPALGADCEALHFGAISliPEPcgstyeALMTREQ--ESRVISLDP-NIrpgFIKDKq 167
Cdd:cd01946 86 YDLNEADTLDTDlnvfadfdPQLPEHYKDSEFVFLGNIA--PEL------QREVLEQvkDPKLVVMDTmNF---WISIK- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 168 shMARIRRMAAMSDIVKFSDEDLAWFGLEGDEDTLARHWLHHGAKLVVVTRGAKGAVGYT-TGLKVEVASERVEVVDTVG 246
Cdd:cd01946 154 --PEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTdDGYFAAPAYPLESVFDPTG 231
|
170 180
....*....|....*....|..
gi 739226067 247 AGDTFDAGILASLKMQGLLTKA 268
Cdd:cd01946 232 AGDTFAGGFIGYLASQKDTSEA 253
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
28-261 |
9.71e-03 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 37.31 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 28 AGGAVFNTA-IALGRLGVPSAF--FTG-LSDDMMGDILRETLRASHVDFSYCATLSRPTTIAFVKLVD------------ 91
Cdd:PTZ00247 61 PGGSALNTArVAQWMLQAPKGFvcYVGcVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGkerslvanlgaa 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 92 GHATYAFYDENTAGRMITEAELpalgadceaLHFGAISLIPEPCGSTYEALMTREQESR-VISLD-PNIRPGFikdkqsh 169
Cdd:PTZ00247 141 NHLSAEHMQSHAVQEAIKTAQL---------YYLEGFFLTVSPNNVLQVAKHARESGKLfCLNLSaPFISQFF------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226067 170 MARIRRMAAMSDIVKFSDEDLAWF------GLEGDEDTLAR--HWLHHGAK---LVVVTRGAKGAVGYTTGLKVEVASER 238
Cdd:PTZ00247 205 FERLLQVLPYVDILFGNEEEAKTFakamkwDTEDLKEIAARiaMLPKYSGTrprLVVFTQGPEPTLIATKDGVTSVPVPP 284
|
250 260
....*....|....*....|....*.
gi 739226067 239 V---EVVDTVGAGDTFDAGILASLKM 261
Cdd:PTZ00247 285 LdqeKIVDTNGAGDAFVGGFLAQYAN 310
|
|
| |
