|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
1-298 |
1.13e-92 |
|
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: 276.82 E-value: 1.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDMLPRETTGGETaFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAI-SN 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPET-FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 80 RPTTLAFVRLV-DGQARYAFYDENTAGRMLSRNDMPYVDETISAMLFGCISLISEPCGSVYETLLAREAPNRVM-FLDPN 157
Cdd:cd01167 80 APTTLAFVTLDaDGERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLiSFDPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 158 IRANLITVRETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGV 237
Cdd:cd01167 160 LRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490822568 238 KVDVVDTVGAGDTVNAGILASLHSQGLLtkdalaNLSEDQIHSAVALGVRAATVTVSRAGA 298
Cdd:cd01167 240 PVEVVDTTGAGDAFVAGLLAQLLSRGLL------ALDEDELAEALRFANAVGALTCTKAGA 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
1-302 |
6.63e-68 |
|
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: 213.98 E-value: 6.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDMLPRET---TGGETA----FQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYS 73
Cdd:COG0524 1 DVLVIGEALVDLVARVDrlpKGGETVlagsFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 74 FAAISN-RPTTLAFVRL-VDGQARYAFYDenTAGRMLSRNDMPYVD-ETISAMLFGCISLISEPCGSVYETLL--AREAP 148
Cdd:COG0524 81 GVRRDPgAPTGLAFILVdPDGERTIVFYR--GANAELTPEDLDEALlAGADILHLGGITLASEPPREALLAALeaARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 149 NRVMFlDPNIRANLItvrETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLKLGPKLVVITKGAHGAVAYTN 228
Cdd:COG0524 159 VPVSL-DPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490822568 229 HATVPVPGVKVDVVDTVGAGDTVNAGILASLHSQGLLTKdalanlsedqihsAVALGVRAATVTVSRAGANPPW 302
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEE-------------ALRFANAAAALVVTRPGAQPAL 295
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-299 |
1.15e-47 |
|
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: 161.59 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 2 ILCCGEALIDMLPRETTGGETA--FQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSF-AAIS 78
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQAdsFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHvRVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 79 NRPTTLAFVRLVDGQARYAFYD-ENTAGRMLSRNDMPYVD-ETISAMLFGCISL-ISEPCGSVYETLL--AREAPNRVMF 153
Cdd:cd01166 82 GRPTGLYFLEIGAGGERRVLYYrAGSAASRLTPEDLDEAAlAGADHLHLSGITLaLSESAREALLEALeaAKARGVTVSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 154 lDPNIRANLITVRETHLTrVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLK--LGPKLVVITKGAHGAVAYTNHAT 231
Cdd:cd01166 162 -DLNYRPKLWSAEEAREA-LEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490822568 232 VPVPGVKVDVVDTVGAGDTVNAGILASLhsqglltkdaLANLSEDQihsAVALGVRAATVTVSRAGAN 299
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGL----------LEGWDLEE---ALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
1-299 |
1.50e-38 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 137.86 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDMLPRET-TGGETA----FQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFA 75
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEgLPGELVrvstVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 76 AIS-NRPTTLAFVRLVDGQARYAFYDENTAGRMLSRNDMPYVDETISAMLFGCISLISEPCGSVYETLLAREAPNRVMFl 154
Cdd:pfam00294 81 VIDeDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGTF- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 155 DPNIRANLITVREThltrVKRMIALADIVKLSDEDLD-WFGEKG-SHDEIAA---EWLKLGPKLVVITKGAHGAVAYTNH 229
Cdd:pfam00294 160 DPNLLDPLGAAREA----LLELLPLADLLKPNEEELEaLTGAKLdDIEEALAalhKLLAKGIKTVIVTLGADGALVVEGD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490822568 230 ATVPVPGV-KVDVVDTVGAGDTVNAGILASLhsqglltkdaLANLSedqIHSAVALGVRAATVTVSRAGAN 299
Cdd:pfam00294 236 GEVHVPAVpKVKVVDTTGAGDSFVGGFLAGL----------LAGKS---LEEALRFANAAAALVVQKSGAQ 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-300 |
1.33e-35 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 130.90 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDMLPreTTGG-----ETAFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYS-- 73
Cdd:PLN02323 12 LVVCFGEMLIDFVP--TVSGvslaeAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEgv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 74 -FAaiSNRPTTLAFVRL-VDGQARYAFYdENTAGRMLSRNDMPYVDETISAMLF--GCISLISEPCGSVYETLL--AREA 147
Cdd:PLN02323 90 rFD--PGARTALAFVTLrSDGEREFMFY-RNPSADMLLRESELDLDLIRKAKIFhyGSISLITEPCRSAHLAAMkiAKEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 148 pNRVMFLDPNIRANLITVRETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAewLKL---GPKLVVITKGAHGAV 224
Cdd:PLN02323 167 -GALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTV--VKLwhpNLKLLLVTEGEEGCR 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490822568 225 AYTNHATVPVPGVKVDVVDTVGAGDTVNAGILASLHSQGLLTKDalanlsEDQIHSAVALGVRAATVTVSRAGANP 300
Cdd:PLN02323 244 YYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLED------EERLREALRFANACGAITTTERGAIP 313
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
6-269 |
5.33e-34 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 125.82 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 6 GEALIDMLPRettgGETAFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAI--SNRPTT 83
Cdd:PRK09434 9 GDAVVDLIPE----GENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLdpAHRTST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 84 LAfVRLVD-GQARYAFYDENTAGRMLSRNDMPYVDEtiSAMLFGC-ISLISEPCGSVyeTLLA----REAPNRVMFlDPN 157
Cdd:PRK09434 85 VV-VDLDDqGERSFTFMVRPSADLFLQPQDLPPFRQ--GEWLHLCsIALSAEPSRST--TFEAmrriKAAGGFVSF-DPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 158 IRANLItvRETHLTR--VKRMIALADIVKLSDEDLDWFGEKgSHDEIAAEWLK--LGPKLVVITKGAHGAVAYTNHATVP 233
Cdd:PRK09434 159 LREDLW--QDEAELRecLRQALALADVVKLSEEELCFLSGT-SQLEDAIYALAdrYPIALLLVTLGAEGVLVHTRGQVQH 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 490822568 234 VPGVKVDVVDTVGAGDTVNAGILASLHSQGLLTKDA 269
Cdd:PRK09434 236 FPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTDEA 271
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
10-300 |
1.01e-24 |
|
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: 100.70 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 10 IDMLPREttgGET----AFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSF-AAISNRPTTL 84
Cdd:cd01174 16 VDRLPKP---GETvlgsSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYvEVVVGAPTGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 85 AFVrLVDGQAryafydENT------AGRMLSRndmpyvdETISAMLfgciSLISE----------PCGSVYETL-LAREA 147
Cdd:cd01174 93 AVI-TVDESG------ENRivvvpgANGELTP-------ADVDAAL----ELIAAadvlllqleiPLETVLAALrAARRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 148 PNRVMF-------LDPNIRAN--LITVREThltrvkrmiALADIVKLSDEDLDwfgekgSHDEIAAEWLKLGPKLVVITK 218
Cdd:cd01174 155 GVTVILnpaparpLPAELLALvdILVPNET---------EAALLTGIEVTDEE------DAEKAARLLLAKGVKNVIVTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 219 GAHGAVAYTNHATVPVPGVKVDVVDTVGAGDTVNAGILASLhSQGLLtkdalanlsedqIHSAVALGVRAATVTVSRAGA 298
Cdd:cd01174 220 GAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAAL-ARGLS------------LEEAIRFANAAAALSVTRPGA 286
|
..
gi 490822568 299 NP 300
Cdd:cd01174 287 QP 288
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
2-259 |
1.15e-24 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 101.14 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 2 ILCCGEALIDMLPRETTGG---ETAFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAIS 78
Cdd:TIGR04382 4 VITIGRVGVDLYPQQIGVPledVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 79 N-RPTTLAF--VRLVDGQARYaFYDENTAGRMLSRNDMPYVD-ETISAMLFGCISLISEPCGSVyeTLLARE---APNRV 151
Cdd:TIGR04382 84 PgRRTSLVFleIKPPDEFPLL-FYRENAADLALTPDDVDEDYiASARALLVSGTALSQEPSREA--VLKALEyarAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 152 MFLDPNIRANLITVRETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLKLGPKLVVITKGAHGAVAYT-NHA 230
Cdd:TIGR04382 161 VVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTgDGE 240
|
250 260
....*....|....*....|....*....
gi 490822568 231 TVPVPGVKVDVVDTVGAGDTVNAGILASL 259
Cdd:TIGR04382 241 GVEVPGFPVEVLNVLGAGDAFASGFLYGL 269
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
2-299 |
2.92e-24 |
|
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: 99.31 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 2 ILCCGEALID------MLPRE-----TTGGETAFqpfaGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNV 70
Cdd:cd01942 2 VAVVGHLNYDiilkveSFPGPfesvlVKDLRREF----GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 71 DYSFAAISNR-PTTLAFVrLVDGQARYAFYDENTAGRMLSRNdmpyvDETISAMLFGCISLISEPcgsvYETLLAREAPN 149
Cdd:cd01942 78 DTSHVRVVDEdSTGVAFI-LTDGDDNQIAYFYPGAMDELEPN-----DEADPDGLADIVHLSSGP----GLIELARELAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 150 RVMFL--DPNIRANLITVREthltrVKRMIALADIVKLSDEDLDWFGEK-GSHDEIAAEwlklGPKLVVITKGAHGAVAY 226
Cdd:cd01942 148 GGITVsfDPGQELPRLSGEE-----LEEILERADILFVNDYEAELLKERtGLSEAELAS----GVRVVVVTLGPKGAIVF 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490822568 227 TNHATVPVPGVK-VDVVDTVGAGDTVNAG-ILASLHSQGLLTkdalanlsedqihsAVALGVRAATVTVSRAGAN 299
Cdd:cd01942 219 EDGEEVEVPAVPaVKVVDTTGAGDAFRAGfLYGLLRGYDLEE--------------SLRLGNLAASLKVERRGAQ 279
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
27-298 |
1.32e-17 |
|
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: 80.86 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTTLAFVRLVDGQARYAFYDEN-TAG 105
Cdd:cd01940 20 YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVDGDRIFGLSNKGgVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 106 RMLSRNDMPYVD--ETISAMLFGCISLISEPCGSVYET--LLAREAPNRvmFLDPNIranlitvrethltrvKRMIALAD 181
Cdd:cd01940 100 EHPFEADLEYLSqfDLVHTGIYSHEGHLEKALQALVGAgaLISFDFSDR--WDDDYL---------------QLVCPYVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 182 IVKLSDEDLDWFGEKGSHDEIAAEwlklGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVDTVGAGDTVNAGILASLhs 261
Cdd:cd01940 163 FAFFSASDLSDEEVKAKLKEAVSR----GAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSL-- 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 490822568 262 qgLLTKDALAnlsedqihSAVALGVRAATVTVSRAGA 298
Cdd:cd01940 237 --LAGGTAIA--------EAMRQGAQFAAKTCGHEGA 263
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
4-298 |
3.99e-17 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 79.40 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 4 CCGEALIDMLPRETTGgetafqpFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTT 83
Cdd:PRK09813 5 TIGDNCVDIYPQLGKA-------FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 84 LAFVRLVDGQARYAFYDENT-AGRMLSRNDMPYV---DETISAMLfgcislisepcGSVYETLlareapnrvmfldPNIR 159
Cdd:PRK09813 78 QTQVELHDNDRVFGDYTEGVmADFALSEEDYAWLaqyDIVHAAIW-----------GHAEDAF-------------PQLH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 160 ANLITVRETHLTRVKrmialADIVKLSDEDLDW-FGEKGSHDEIAAEWLK----LGPKLVVITKGAHGAVAYTNHATVPV 234
Cdd:PRK09813 134 AAGKLTAFDFSDKWD-----SPLWQTLVPHLDYaFASAPQEDEFLRLKMKaivaRGAGVVIVTLGENGSIAWDGAQFWRQ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490822568 235 PGVKVDVVDTVGAGDTVNAGILASLhSQGLLTKDALANlsedqihsavalGVRAATVTVSRAGA 298
Cdd:PRK09813 209 APEPVTVVDTMGAGDSFIAGFLCGW-LAGMTLPQAMAQ------------GTACAAKTIQYHGA 259
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-301 |
4.43e-17 |
|
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: 79.97 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGE---ALIDMLPRETTggetafqpfAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAI 77
Cdd:cd01168 33 MILADMEeqeELLAKLPVKYI---------AGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 78 SNRPTTLAFVRLVDGqaryafydentAGRMLSRNDMPYVDETISAMLFGCIS----LISEPcgsvYetllareapnrvmF 153
Cdd:cd01168 104 PDGPTGTCAVLVTPD-----------AERTMCTYLGAANELSPDDLDWSLLAkakyLYLEG----Y-------------L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 154 LDPNIRANLITVRETHLTRVKRMIALAD--IVKLSDEDLD------------------WFGEKGSHD-EIAAEWLKLGPK 212
Cdd:cd01168 156 LTVPPEAILLAAEHAKENGVKIALNLSApfIVQRFKEALLellpyvdilfgneeeaeaLAEAETTDDlEAALKLLALRCR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 213 LVVITKGAHGAVAYTNHATVPVPGVKVD-VVDTVGAGDTVNAGILASLHsqglltkdalANLSEDQihsAVALGVRAATV 291
Cdd:cd01168 236 IVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLV----------QGEPLEE---CIRLGSYAAAE 302
|
330
....*....|
gi 490822568 292 TVSRAGANPP 301
Cdd:cd01168 303 VIQQLGPRLP 312
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
14-305 |
5.27e-17 |
|
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: 79.57 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 14 PRETTGGET----AFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFA-AISNRPTTLAFVr 88
Cdd:TIGR02152 12 DRLPKPGETvhghSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVgTVKDTPTGTAFI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 89 LVDGQaryafyDENT------AGRMLSRNDMPYVDETISAMLFgCISLISEPCGSVYETL-LAREAPNRVMF-------- 153
Cdd:TIGR02152 91 TVDDT------GENRivvvagANAELTPEDIDAAEALIAESDI-VLLQLEIPLETVLEAAkIAKKHGVKVILnpapaikd 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 154 LDPNI--RANLITVRETHLtrvkrmialADIVKLSDEDLDWFGEkgshdeiAAEWL-KLGPKLVVITKGAHGAVAYTNHA 230
Cdd:TIGR02152 164 LDDELlsLVDIITPNETEA---------EILTGIEVTDEEDAEK-------AAEKLlEKGVKNVIITLGSKGALLVSKDE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490822568 231 TVPVPGVKVDVVDTVGAGDTVNAgilaslhsqglltkdALAN-LSEDQ-IHSAVALGVRAATVTVSRAGANP--PWAHE 305
Cdd:TIGR02152 228 SKLIPAFKVKAVDTTAAGDTFNG---------------AFAVaLAEGKsLEDAIRFANAAAAISVTRKGAQSsiPYLEE 291
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
29-305 |
3.14e-16 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 77.60 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 29 GGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVD-YSFAAISNRPTTLAFVrLVDGQAryafydENTAGRM 107
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDtAPVSVIKGESTGVALI-FVNDEG------ENSIGIH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 108 LSRNDM---PYVD---ETI---SAMLfgcISLISePCGSVYETL-LAREAPNRVMfLDPNIRANL----------ITVRE 167
Cdd:PRK11142 112 AGANAAltpALVEahrELIanaDALL---MQLET-PLETVLAAAkIAKQHGTKVI-LNPAPARELpdellalvdiITPNE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 168 THltrvkrmialADI---VKLSDEDldwfgekgsHDEIAAEWL-KLGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVD 243
Cdd:PRK11142 187 TE----------AEKltgIRVEDDD---------DAAKAAQVLhQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVD 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490822568 244 TVGAGDTVNAGILASLhsqglltkdalanLSEDQIHSAVALGVRAATVTVSRAGANP--PWAHE 305
Cdd:PRK11142 248 TIAAGDTFNGALVTAL-------------LEGKPLPEAIRFAHAAAAIAVTRKGAQPsiPWREE 298
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
27-298 |
6.04e-16 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 76.71 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVFNTAIALGRLGVP---TGFFSGissdFFGDVLRDTLARSNVDYSFAAISNR-PTTLAFVRLVDGQaryaFYDEN 102
Cdd:COG1105 33 DPGGKGINVARVLKALGVDvtaLGFLGG----FTGEFIEELLDEEGIPTDFVPIEGEtRINIKIVDPSDGT----ETEIN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 103 TAGrmlsrndmPYVDETISAMLFGCISLISEP------CGSV--------YETL--LAREAPNRVmFLD---PNIRANLI 163
Cdd:COG1105 105 EPG--------PEISEEELEALLERLEELLKEgdwvvlSGSLppgvppdfYAELirLARARGAKV-VLDtsgEALKAALE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 164 tvrethltrvkrmiALADIVKLSDEDL-DWFGEK-GSHDEI---AAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVK 238
Cdd:COG1105 176 --------------AGPDLIKPNLEELeELLGRPlETLEDIiaaARELLERGAENVVVSLGADGALLVTEDGVYRAKPPK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 239 VDVVDTVGAGDTVNAGILASLhSQGLLTKDALanlsedqihsavALGVRAATVTVSRAGA 298
Cdd:COG1105 242 VEVVSTVGAGDSMVAGFLAGL-ARGLDLEEAL------------RLAVAAGAAAALSPGT 288
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
27-301 |
2.75e-15 |
|
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: 74.53 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVFNTAIALGRLGVP---TGFFSGISSDFFgdvlRDTLARSNVDYSFAAISnrPTTLAFVRLVDGQARYafYDENT 103
Cdd:TIGR03168 33 DAGGKGINVARVLARLGAEvvaTGFLGGFTGEFI----EALLAEEGIKNDFVEVK--GETRINVKIKESSGEE--TELNE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 104 AGRMLSRNDMPYVDETISAMLFGCISLISepCGSV--------YETL--LAREAPNRVmFLDPNiRANLITVRETHLtrv 173
Cdd:TIGR03168 105 PGPEISEEELEQLLEKLRELLASGDIVVI--SGSLppgvppdfYAQLiaIARKKGAKV-ILDTS-GEALREALAAKP--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 174 krmialaDIVKLSDEDL-DWFG-EKGSHDEI---AAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVDTVGAG 248
Cdd:TIGR03168 178 -------FLIKPNHEELeELFGrELKTLEEIieaARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490822568 249 DTVNAGILASLhSQGLLTKDALanlsedqihsavALGVRAATVTVSRAGANPP 301
Cdd:TIGR03168 251 DSMVAGFLAGL-ARGLSLEEAL------------RFAVAAGSAAAFSPGTGLP 290
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
119-260 |
4.83e-15 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 72.13 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 119 TISAMLFGCISLISEPCGSVYEtlLAREAPNRVmFLDPNIRAnlitvRETHLTRVKRMIALADIVKLSDEDLDW-FGEKG 197
Cdd:cd00287 57 GADAVVISGLSPAPEAVLDALE--EARRRGVPV-VLDPGPRA-----VRLDGEELEKLLPGVDILTPNEEEAEAlTGRRD 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490822568 198 SH----DEIAAEWLKLGPKLVVITKGAHGAVAYTNHAT-VPVPGVKVDVVDTVGAGDTVNAGILASLH 260
Cdd:cd00287 129 LEvkeaAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTeVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-270 |
1.09e-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: 72.45 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 29 GGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLaRSNVDYSFAAISNRPTTLAFVrLVDGQARYAFYDENTAGR-- 106
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGGDKHTVAWRDKPTRKTLS-FIDPNGERTITVPGERLEdd 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 107 ----MLSRNDMPYVDETIsamlfgcislisepcgsVYETLLAREAPNRVMFLDPNIRANLITVRETHLtrvkrmiaLADI 182
Cdd:cd01947 114 lkwpILDEGDGVFITAAA-----------------VDKEAIRKCRETKLVILQVTPRVRVDELNQALI--------PLDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 183 VKLSDEDldwFGEKGSHDEIAaewlKLGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVDTVGAGDTVNAGILASLhSQ 262
Cdd:cd01947 169 LIGSRLD---PGELVVAEKIA----GPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGL-LK 240
|
....*...
gi 490822568 263 GLLTKDAL 270
Cdd:cd01947 241 GWSIEEAL 248
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
28-308 |
1.21e-14 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 74.10 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 28 AGGSVfNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLAR---------SNVDYSFAAISNRPTTLAFVrLVDGQARYAF 98
Cdd:PLN02341 119 AGGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEegisvvgliEGTDAGDSSSASYETLLCWV-LVDPLQRHGF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 99 YDENTAGRMLSRNDMPYVDETISAMLFGCISLISEpcGSVYETL----------LAREAPNRVMFlDPNIRA-NLITVRE 167
Cdd:PLN02341 197 CSRADFGPEPAFSWISKLSAEAKMAIRQSKALFCN--GYVFDELspsaiasavdYAIDVGTAVFF-DPGPRGkSLLVGTP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 168 THLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLK--LGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVDTV 245
Cdd:PLN02341 274 DERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRpgIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTV 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490822568 246 GAGDTVNAGI-LASLHSQGLLTKDALANlsedqihsavalGVRAATVTVSRAGANPPWAHEMRD 308
Cdd:PLN02341 354 GCGDSFAAAIaLGYIHNLPLVNTLTLAN------------AVGAATAMGCGAGRNVATLEKVLE 405
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
10-297 |
2.27e-14 |
|
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: 72.07 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 10 IDMLPRetTGGE---TAFQPFAGGSvFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTTLAf 86
Cdd:cd01944 16 VDKLPA--SGGDieaKSKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 87 VRLVDGQARYAFYDENTAGRMLSRNDMPYVDETISAMLFGCISLISEPCGSVyETLLA--REAPNRVMFL-DPNIRanli 163
Cdd:cd01944 92 VALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASK-VILLEwlEALPAGTTLVfDPGPR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 164 tVRETHLTRVKRMIALADIVKLSDEDLDWFGEKGsHDEIAAEWLKLGPKL---VVITKGAHGAVAY-TNHATVPVPGVKV 239
Cdd:cd01944 167 -ISDIPDTILQALMAKRPIWSCNREEAAIFAERG-DPAAEASALRIYAKTaapVVVRLGSNGAWIRlPDGNTHIIPGFKV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490822568 240 DVVDTVGAGDTVNAGILASLhSQGLLTKDalanlsedqihsAVALGVRAATVTVSRAG 297
Cdd:cd01944 245 KAVDTIGAGDTHAGGMLAGL-AKGMSLAD------------AVLLANAAAAIVVTRSG 289
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
27-298 |
3.23e-14 |
|
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: 71.47 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVFNTAIALGRLGVP---TGFFSGISSDFFgdvlRDTLARSNVDYSFAAISnrPTTLAFVRLVDGQARYafYDENT 103
Cdd:TIGR03828 33 DAGGKGINVSRVLKNLGVDvvaLGFLGGFTGDFI----EALLREEGIKTDFVRVP--GETRINVKIKEPSGTE--TKLNG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 104 AGRMLSRNDMPYVDETISAMLFGCISLI---SEPCG---SVYETLLAREAPNRVMFL----DPNIRANLitvrETHltrv 173
Cdd:TIGR03828 105 PGPEISEEELEALLEKLRAQLAEGDWLVlsgSLPPGvppDFYAELIALAREKGAKVIldtsGEALRDGL----KAK---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 174 krmialADIVKLSDEDL-DWFG-EKGSHDEI---AAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVDTVGAG 248
Cdd:TIGR03828 177 ------PFLIKPNDEELeELFGrELKTLEEIieaARELLDLGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490822568 249 DTVNAGILASLhSQGLLTKDALanlsedqihsavALGVRAATVTVSRAGA 298
Cdd:TIGR03828 251 DSMVAGFLAGL-ESGLSLEEAL------------RLAVAAGSAAAFSEGT 287
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
27-297 |
5.73e-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: 67.94 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVFNTAIALGRLGVP---TGFFSGissdFFGDVLRDTLARSNVDYSFAAISNrpTTLAFVRLVDGQARYafYDENT 103
Cdd:cd01164 34 DAGGKGINVARVLKDLGVEvtaLGFLGG----FTGDFFEALLKEEGIPDDFVEVAG--ETRINVKIKEEDGTE--TEINE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 104 AGrmlsrndmPYVDETISAMLFGCISLISEP------CGSV--------YETLLAREAPNRVMF-LDPNIRANLITVRet 168
Cdd:cd01164 106 PG--------PEISEEELEALLEKLKALLKKgdivvlSGSLppgvpadfYAELVRLAREKGARViLDTSGEALLAALA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 169 hltrvkrmiALADIVKLSDEDL-DWFG-EKGSHDEI---AAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVKVDVVD 243
Cdd:cd01164 176 ---------AKPFLIKPNREELeELFGrPLGDEEDViaaARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVS 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490822568 244 TVGAGDTVNAGILASLHSQGLLTKdalanlsedqihsAVALGVRAATVTVSRAG 297
Cdd:cd01164 247 TVGAGDSMVAGFVAGLAQGLSLEE-------------ALRLAVAAGSATAFSPG 287
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
2-294 |
1.86e-12 |
|
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: 66.18 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 2 ILCCGEALID--------MLPRETTGGETAFQPfaGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYS 73
Cdd:cd01941 2 IVVIGAANIDlrgkvsgsLVPGTSNPGHVKQSP--GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 74 FAAISNRPTtlafvrlvdgqARY-AFYDENtaGRMLSR-NDMpyvdetisamlfGCISLISEPCGSVYETLLAREAPnrV 151
Cdd:cd01941 80 GIVFEGRST-----------ASYtAILDKD--GDLVVAlADM------------DIYELLTPDFLRKIREALKEAKP--I 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 152 MFlDPNIR----ANLITVRETHL-------TRVKRMIALADIVKL-------SDEDLDWFGEKGSHDE----IAAEWLKL 209
Cdd:cd01941 133 VV-DANLPeealEYLLALAAKHGvpvafepTSAPKLKKLFYLLHAidlltpnRAELEALAGALIENNEdenkAAKILLLP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 210 GPKLVVITKGAHGAVaYTNHAT------VPVPGVKvDVVDTVGAGDTVNAGILASLhsqglltkdaLANLSEDQihsAVA 283
Cdd:cd01941 212 GIKNVIVTLGAKGVL-LSSREGgvetklFPAPQPE-TVVNVTGAGDAFVAGLVAGL----------LEGMSLDD---SLR 276
|
330
....*....|.
gi 490822568 284 LGVRAATVTVS 294
Cdd:cd01941 277 FAQAAAALTLE 287
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
8-298 |
2.82e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 8 ALIDMLPR--ETTGGETAFQPFaGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAA-ISNRPTTL 84
Cdd:PTZ00292 30 GYVDRMPQvgETLHGTSFHKGF-GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSrTENSSTGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 85 AFVrLVD-----------GQARYAFYDEntagrMLSRNDMPYvdETISAMLFgCISLIsePCGSVYETL-LAREAPNRVM 152
Cdd:PTZ00292 109 AMI-FVDtktgnneiviiPGANNALTPQ-----MVDAQTDNI--QNICKYLI-CQNEI--PLETTLDALkEAKERGCYTV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 153 FlDPNIRANLITVREthltrVKRMIALADIVKLSD-EDLDWFGEKGSHDEIAA----EWLKLGPKLVVITKGAHG-AVAY 226
Cdd:PTZ00292 178 F-NPAPAPKLAEVEI-----IKPFLKYVSLFCVNEvEAALITGMEVTDTESAFkaskELQQLGVENVIITLGANGcLIVE 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490822568 227 TNHATVPVPGVKVDVVDTVGAGDTVnAGILASLHSQGLltkdalaNLSEdqihsAVALGVRAATVTVSRAGA 298
Cdd:PTZ00292 252 KENEPVHVPGKRVKAVDTTGAGDCF-VGSMAYFMSRGK-------DLKE-----SCKRANRIAAISVTRHGT 310
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
2-289 |
9.11e-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: 61.54 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 2 ILCCGEALIDMLPR-ET--TGGE----TAFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSF 74
Cdd:cd01945 2 VLGVGLAVLDLIYLvASfpGGDGkivaTDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 75 aAISNRPTTLAFVRLVDGQARyafydeNTAGRMLSRNDMPYVDETISAMLFGCISLISEPCGSVYETLLAREAPNRvmfl 154
Cdd:cd01945 82 -IVVAPGARSPISSITDITGD------RATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQEARAR---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 155 dpNIRAnLITVRETHLTRVKRMIALADIVKLSdedlDWFGEK--GSHDEIAAEWLK-LGPKLVVITKGAHGAVAYT-NHA 230
Cdd:cd01945 151 --GIPI-PLDLDGGGLRVLEELLPLADHAICS----ENFLRPntGSADDEALELLAsLGIPFVAVTLGEAGCLWLErDGE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490822568 231 TVPVPGVKVDVVDTVGAGDTVNAGILASLhSQGLLTKDALANLSEDQIHSAVALGVRAA 289
Cdd:cd01945 224 LFHVPAFPVEVVDTTGAGDVFHGAFAHAL-AEGMPLREALRFASAAAALKCRGLGGRAG 281
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
167-299 |
6.68e-10 |
|
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: 58.63 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 167 ETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVKV-DVVDTV 245
Cdd:cd01946 151 SIKPEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLeSVFDPT 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490822568 246 GAGDTVNAGILASLHSQGlltkdalaNLSEDQIHSAVALGVRAATVTVSRAGAN 299
Cdd:cd01946 231 GAGDTFAGGFIGYLASQK--------DTSEANMRRAIIYGSAMASFCVEDFGTK 276
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
34-297 |
1.35e-09 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 58.28 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 34 NTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTTLAFVRLVDGQ---ARYAFYDentagrmlsr 110
Cdd:COG2870 60 NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGGqqlLRLDFED---------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 111 nDMPYVDETISAMLFGCISLISEP---------CGSVYETL------LAREAPNRVMFlDPNIR-------ANLIT--VR 166
Cdd:COG2870 130 -RFPLSAELEARLLAALEAALPEVdavilsdygKGVLTPELiqaliaLARAAGKPVLV-DPKGRdfsryrgATLLTpnLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 167 EthltrvkrMIALADIVKLSDEDLdwfgekgshdEIAAEWL--KLGPKLVVITKGAHGAVAYT-NHATVPVPGVKVDVVD 243
Cdd:COG2870 208 E--------AEAAVGIPIADEEEL----------VAAAAELleRLGLEALLVTRGEEGMTLFDaDGPPHHLPAQAREVFD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490822568 244 TVGAGDTVNAGILASLhsqglltkdaLANLSedqIHSAVALGVRAATVTVSRAG 297
Cdd:COG2870 270 VTGAGDTVIATLALAL----------AAGAS---LEEAAELANLAAGIVVGKLG 310
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
1-290 |
2.57e-09 |
|
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: 57.03 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDML------PRETTGGE-TAFQPFAGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDys 73
Cdd:cd01939 1 AVLCVGLTVLDFIttvdkyPFEDSDQRtTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGID-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 74 faaISNRPTTlafvrlvDGQARYAFY--DENTAGR--MLSRNDMPYV--DETISAML--FGCISLisePCGSVYETLlar 145
Cdd:cd01939 79 ---ISHCYRK-------DIDEPASSYiiRSRAGGRttIVNDNNLPEVtyDDFSKIDLtqYGWIHF---EGRNPDETL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 146 eapnRVM--FLDPNIRANLITVR-----ETHLTRVKRMIALADIVKLSDEDLDWFGEKGSHDEIAAEWLKLG-PKLVVIT 217
Cdd:cd01939 143 ----RMMqhIEEHNNRRPEIRITisvevEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKkAALLVCT 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490822568 218 KGAHGAVAYT---NHATVPV-PGVKVdvVDTVGAGDTVNAGILASLhsqglltkdalaNLSEDQIHSAVALGVRAAT 290
Cdd:cd01939 219 WGDQGAGALGpdgEYVHSPAhKPIRV--VDTLGAGDTFNAAVIYAL------------NKGPDDLSEALDFGNRVAS 281
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
20-270 |
1.22e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 52.30 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 20 GETAFQPfaGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTTLAFVRLVDgqaryafy 99
Cdd:PRK09850 33 GKIKFTP--GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLD-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 100 deNTAGRMLSRNDMPyVDETISAMLFG-------CISLISEPCGSVYETL--LAREAPNRVMFLDPNIRANLITVREtHL 170
Cdd:PRK09850 103 --NTGEMLVAINDMN-ISNAITAEYLAqhrefiqRAKVIVADCNISEEALawILDNAANVPVFVDPVSAWKCVKVRD-RL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 171 TRVKRMialaDIVKLSDEDLDWFGEKGSHD--EIAAEWLKLGPKLVVITKGAHGaVAYT--NHATVPVPGVKVDVVDTVG 246
Cdd:PRK09850 179 NQIHTL----KPNRLEAETLSGIALSGREDvaKVAAWFHQHGLNRLVLSMGGDG-VYYSdiSGESGWSAPIKTNVINVTG 253
|
250 260
....*....|....*....|....
gi 490822568 247 AGDTVNAGiLASLHSQGLLTKDAL 270
Cdd:PRK09850 254 AGDAMMAG-LASCWVDGMPFAESV 276
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
1-265 |
3.17e-07 |
|
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: 50.48 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 1 MILCCGEALIDMLPRETTGgETAFqpfaGGSVFNTAIALGRLGVPTGFFSGISSDFFGDVlrDTLARSNVDysFAAISNR 80
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSG-VVKP----GGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLFDNGIE--VISLLST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 81 PTTLAFVRLVDgqaryafyDENTAgRMLSRNDMPYVDETISAMLFGCISLISEPCGSVYETLlaREAPNRVMfLDPN--I 158
Cdd:cd01937 72 ETTTFELNYTN--------EGRTR-TLLAKCAAIPDTESPLSTITAEIVILGPVPEEISPSL--FRKFAFIS-LDAQgfL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 159 RAnlitVRETHLTRvKRMIALADIVKLSDEDLDWFGEKGshdEIAAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVK 238
Cdd:cd01937 140 RR----ANQEKLIK-CVILKLHDVLKLSRVEAEVISTPT---ELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASK 211
|
250 260
....*....|....*....|....*..
gi 490822568 239 VDVVDTVGAGDTVNAGILASLHSQGLL 265
Cdd:cd01937 212 KDVVDPTGAGDVFLAAFLYSRLSGKDI 238
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
27-273 |
3.35e-06 |
|
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: 47.94 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 27 FAGGSVfNTAIALGRLGVPTGFFSGISSDFFGDVLRDTLARSNVDYSFAAISNRPTTLAfVRLVDGQ---ARYAFYD--- 100
Cdd:cd01172 38 RLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTTTK-TRVIARNqqlLRVDREDdsp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 101 --ENTAGRMLSR--NDMPYVDetisAMLF-----GCIS--LISEPCGsvyetlLAREAPNRVmFLDPNIRANLITVRETH 169
Cdd:cd01172 116 lsAEEEQRLIERiaERLPEAD----VVILsdygkGVLTprVIEALIA------AARELGIPV-LVDPKGRDYSKYRGATL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 170 LTRVKRMIALA-DIVKLSDEDLDWFGEKGSHdeiaaewlKLGPKLVVITKGAHGAVAYTNH-ATVPVPGVKVDVVDTVGA 247
Cdd:cd01172 185 LTPNEKEAREAlGDEINDDDELEAAGEKLLE--------LLNLEALLVTLGEEGMTLFERDgEVQHIPALAKEVYDVTGA 256
|
250 260
....*....|....*....|....*...
gi 490822568 248 GDTVNAgILASLHSQGLLTKDA--LANL 273
Cdd:cd01172 257 GDTVIA-TLALALAAGADLEEAafLANA 283
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
28-298 |
6.85e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 47.11 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 28 AGGSVFNTAIALGRLGVPTGFFS--------GISSDFFGDVLRDTLARSNVDYSFAAISNRPT-TLAFVRLVDGQARyaf 98
Cdd:PLN02813 125 AGGSLSNTLVALARLGSQSAAGPalnvamagSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTgTVIVLTTPDAQRT--- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 99 ydentagrMLSRNDMPYV---DETISAMLFGCISLISEpcGSVYETLLAREAPNRVMFLdpnIRAN--LITVRETHLTRV 173
Cdd:PLN02813 202 --------MLSYQGTSSTvnyDSCLASAISKSRVLVVE--GYLWELPQTIEAIAQACEE---AHRAgaLVAVTASDVSCI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 174 KR--------MIALADIV-KLSDE--DLDWFGEKGShDEIAAEWLKLGPKLVVITKGAHG---AVAYTNHATVPVPGVKV 239
Cdd:PLN02813 269 ERhrddfwdvMGNYADILfANSDEarALCGLGSEES-PESATRYLSHFCPLVSVTDGARGsyiGVKGEAVYIPPSPCVPV 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490822568 240 DvvdTVGAGDTVNAGILASLhsqglltkdaLANLSEdqIHSAVALGVRAATVTVSRAGA 298
Cdd:PLN02813 348 D---TCGAGDAYAAGILYGL----------LRGVSD--LRGMGELAARVAATVVGQQGT 391
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
180-301 |
8.27e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 46.56 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 180 ADIVKLSDEDLDWFGEK-----GSHDEIAAEWLKLGPK------LVVITKGAHGAVAYTNHA--TVPVPGVKVD-VVDTV 245
Cdd:PTZ00247 215 VDILFGNEEEAKTFAKAmkwdtEDLKEIAARIAMLPKYsgtrprLVVFTQGPEPTLIATKDGvtSVPVPPLDQEkIVDTN 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490822568 246 GAGDTVNAGILAslhsqglltkdALANlSEDQIHSAVAlGVRAATVTVSRAGANPP 301
Cdd:PTZ00247 295 GAGDAFVGGFLA-----------QYAN-GKDIDRCVEA-GHYSAQVIIQHNGCTYP 337
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
214-297 |
1.75e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 39.29 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822568 214 VVITKGAHGAVAYTNHATVPVPGVKVDVVDTVGAGDTVNAGILaslhsQGLLTKdalanlsEDQIHS-AVALGVRAATVT 292
Cdd:PRK09513 220 VVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLI-----YGLLMR-------ESSEHTlRLATAVSALAVS 287
|
....*
gi 490822568 293 VSRAG 297
Cdd:PRK09513 288 QSNVG 292
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
194-259 |
5.96e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 37.85 E-value: 5.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490822568 194 GEKGSHDEIAAEWLKLGPKLVVITKGAHGAVAYTNHATVPVPGVK-VDVVDTVGAGDTVNAGILASL 259
Cdd:PLN02379 249 GEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGFLYGL 315
|
|
| |
