|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
3-304 |
2.07e-175 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 487.52 E-value: 2.07e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 3 AMNKVWVIGDASVDLVPEKQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADL 82
Cdd:PRK09434 1 MMNKVWVLGDAVVDLIPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 83 TSAVLIVNLTADGERSFTYLVHPGADTYVSPQDLPPFRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDVNLR 162
Cdd:PRK09434 81 RTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 163 SKMWGNTDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDL-GCDTTIISLGADGALLITAEGEFHFPAPR 241
Cdd:PRK09434 161 EDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRyPIALLLVTLGAEGVLVHTRGQVQHFPAPS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446569164 242 VDVVDTTGAGDAFVGGLLFTLSRANCWNHI-LLAEAISNANACGAMAVTAKGAMTALPFPDQLN 304
Cdd:PRK09434 241 VDPVDTTGAGDAFVAGLLAGLSQAGLWTDEaELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-294 |
1.84e-107 |
|
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: 314.96 E-value: 1.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEKQNS---YLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADL 82
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGApetFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 83 TSAVLIVNLTADGERSFTYLVHPGADTYVSPQDLPP-FRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDVNL 161
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDlLSEADILHFGSIALASEPSRSALLELLEAAKKAGVLISFDPNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 162 RSKMWGNTDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPR 241
Cdd:cd01167 161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446569164 242 VDVVDTTGAGDAFVGGLLFTLSRANCW--NHILLAEAISNANACGAMAVTAKGAM 294
Cdd:cd01167 241 VEVVDTTGAGDAFVAGLLAQLLSRGLLalDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-303 |
3.54e-87 |
|
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: 263.67 E-value: 3.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEKQ-----------NSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVT 74
Cdd:COG0524 1 DVLVIGEALVDLVARVDrlpkggetvlaGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 75 FLRLDADLTSAVLIVNLTADGERSFTYlvHPGADTYVSPQDLPP--FRQYEWFYFSSIGLTDRPAREACLEGARRMREAG 152
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVF--YRGANAELTPEDLDEalLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 153 GYVLFDVNLRSKMWgntDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAE 232
Cdd:COG0524 159 VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446569164 233 GEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRancwnHILLAEAISNANACGAMAVTAKGAMTALPFPDQL 303
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLE-----GLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-294 |
1.73e-66 |
|
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: 210.51 E-value: 1.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEK------QNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLD 79
Cdd:cd01166 1 DVVTIGEVMVDLSPPGggrleqADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 80 ADLTSAVLIVNLTADGERSFTYLVHPGADTYVSPQDLPP--FRQYEWFYFSSIGL-TDRPAREACLEGARRMREAGGYVL 156
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEaaLAGADHLHLSGITLaLSESAREALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 157 FDVNLRSKMWGNtDEIPELIARSAALASICKVSADELCQLSGASHWQDA--RYYLRDLGCDTTIISLGADGALLITAEGE 234
Cdd:cd01166 161 FDLNYRPKLWSA-EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAaeRALALALGVKAVVVKLGAEGALVYTGGGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 235 FHFPAPRVDVVDTTGAGDAFVGGLLFTLSRAncWNhilLAEAISNANACGAMAVTAKGAM 294
Cdd:cd01166 240 VFVPAYPVEVVDTTGAGDAFAAGFLAGLLEG--WD---LEEALRFANAAAALVVTRPGDI 294
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
25-309 |
1.03e-62 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 201.77 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 25 YLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADGERSFTYLVH 104
Cdd:PLN02323 38 FKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 105 PGADTYVSPQ--DLPPFRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDVNLRSKMWGNTDEIPELIARSAAL 182
Cdd:PLN02323 118 PSADMLLRESelDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 183 ASICKVSADELCQLSGA-SHWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFT 261
Cdd:PLN02323 198 ADIIKVSDEEVEFLTGGdDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQ 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446569164 262 L--SRANCWNHILLAEAISNANACGAMAVTAKGAMTALPFPDQLNTFLSS 309
Cdd:PLN02323 278 LakDLSLLEDEERLREALRFANACGAITTTERGAIPALPTKEAVLKLLKK 327
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-295 |
3.38e-57 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 186.39 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPE---------KQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFL 76
Cdd:pfam00294 1 KVVVIGEANIDLIGNveglpgelvRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 77 RLDADLTSAVLIVNLTADGERSFTYlvHPGADTYVSPQDL----PPFRQYEWFYFSsiGLTDRPAREACLEGARRMREAG 152
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVF--NRGAAADLTPEELeeneDLLENADLLYIS--GSLPLGLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 153 GYvlFDVNLRSKMWGNTDEIPELIarsaALASICKVSADELCQLSGASHW--QDARYYLRDL---GCDTTIISLGADGAL 227
Cdd:pfam00294 157 GT--FDPNLLDPLGAAREALLELL----PLADLLKPNEEELEALTGAKLDdiEEALAALHKLlakGIKTVIVTLGADGAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446569164 228 LITAEGEFHFPA-PRVDVVDTTGAGDAFVGGLLFTLSRANCwnhilLAEAISNANACGAMAVTAKGAMT 295
Cdd:pfam00294 231 VVEGDGEVHVPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKS-----LEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-298 |
3.00e-54 |
|
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: 178.90 E-value: 3.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLV------PE-----KQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVT 74
Cdd:cd01174 1 KVVVVGSINVDLVtrvdrlPKpgetvLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 75 FLRLDADLTSAVLIVNLTADGERSFtyLVHPGADTYVSPQDLPPFRqyEWFYFSSIGLTDR--PArEACLEGARRMREAG 152
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRI--VVVPGANGELTPADVDAAL--ELIAAADVLLLQLeiPL-ETVLAALRAARRAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 153 GYVLFdvnlrskmwgN----TDEIPELIArsaaLASICKVSADELCQLSGAS-----HWQDARYYLRDLGCDTTIISLGA 223
Cdd:cd01174 156 VTVIL----------NpapaRPLPAELLA----LVDILVPNETEAALLTGIEvtdeeDAEKAARLLLAKGVKNVIVTLGA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446569164 224 DGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRancwnHILLAEAISNANACGAMAVTAKGAMTALP 298
Cdd:cd01174 222 KGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALAR-----GLSLEEAIRFANAAAALSVTRPGAQPSIP 291
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
9-307 |
5.80e-49 |
|
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: 165.46 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 9 VIGDASVDLVPEKQN-------SYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDAD 81
Cdd:TIGR04382 6 TIGRVGVDLYPQQIGvpledvtSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 82 LTSAVLIVNLTADGERSFTYLVHPGADTYVSPQDLP--PFRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDV 159
Cdd:TIGR04382 86 RRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDedYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 160 NLRSKMWGNTDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAEGE-FHFP 238
Cdd:TIGR04382 166 DYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEgVEVP 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446569164 239 APRVDVVDTTGAGDAFVGGLLFTLSRAncWNhilLAEAISNANACGAMAVTAKGAMTALPFPDQLNTFL 307
Cdd:TIGR04382 246 GFPVEVLNVLGAGDAFASGFLYGLLAG--WD---LEKALRYGNACGAIVVSRHSCSPAMPTLEELEAFL 309
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
29-304 |
5.78e-46 |
|
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: 157.38 E-value: 5.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADGERSFtyLVHPGAD 108
Cdd:TIGR02152 30 PGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRI--VVVAGAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 109 TYVSPQDLPpfRQYEWFYFSSIGLTDRPAR-EACLEGARRMREAGGYVLFD---VNLRSKmwgntdeiPELIArsaaLAS 184
Cdd:TIGR02152 108 AELTPEDID--AAEALIAESDIVLLQLEIPlETVLEAAKIAKKHGVKVILNpapAIKDLD--------DELLS----LVD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 185 ICKVSADELCQLSG--ASHWQDARY---YLRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLL 259
Cdd:TIGR02152 174 IITPNETEAEILTGieVTDEEDAEKaaeKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAGDTFNGAFA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446569164 260 FTLSRANCwnhilLAEAISNANACGAMAVTAKGAMTALPFPDQLN 304
Cdd:TIGR02152 254 VALAEGKS-----LEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-308 |
1.55e-34 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 128.32 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 3 AMNKVWVIGDASVDLV------PE-----KQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGV 71
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIgyvdrmPQvgetlHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 72 DVTFLRLDADLTS--AVLIVNL-TADGErsftYLVHPGADTYVSPQDLPPFR-QYEWFYFSSIGLTDRPArEACLEGARR 147
Cdd:PTZ00292 94 NTSFVSRTENSSTglAMIFVDTkTGNNE----IVIIPGANNALTPQMVDAQTdNIQNICKYLICQNEIPL-ETTLDALKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 148 MREAGGYVLFdvNLRSkmwGNTDEIPELIARSAALASICKVSADELCQLSG------ASHWQDARYyLRDLGCDTTIISL 221
Cdd:PTZ00292 169 AKERGCYTVF--NPAP---APKLAEVEIIKPFLKYVSLFCVNEVEAALITGmevtdtESAFKASKE-LQQLGVENVIITL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 222 GADGALLITAE-GEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRAncwnhILLAEAISNANACGAMAVTAKGAMTALPFP 300
Cdd:PTZ00292 243 GANGCLIVEKEnEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRG-----KDLKESCKRANRIAAISVTRHGTQSSYPHP 317
|
....*...
gi 446569164 301 DQLNTFLS 308
Cdd:PTZ00292 318 SELPADVK 325
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
29-293 |
2.55e-34 |
|
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: 126.27 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVnlTADGERSFTYLVHPGAD 108
Cdd:cd01942 35 FGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFI--LTDGDDNQIAYFYPGAM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 109 TYVSP-QDLPPFRQYEWFYFSSigltdrpaREACLEGARRMREAGGYVLFDVNLRSKMWGNtDEIPELIARSAALAsick 187
Cdd:cd01942 113 DELEPnDEADPDGLADIVHLSS--------GPGLIELARELAAGGITVSFDPGQELPRLSG-EELEEILERADILF---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 188 VSADELCQLSGASHWQDARyylRDLGCDTTIISLGADGALLITAEGEFHFPA-PRVDVVDTTGAGDAFVGGLLFTLSRAn 266
Cdd:cd01942 180 VNDYEAELLKERTGLSEAE---LASGVRVVVVTLGPKGAIVFEDGEEVEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRG- 255
|
250 260
....*....|....*....|....*..
gi 446569164 267 cWNhilLAEAISNANACGAMAVTAKGA 293
Cdd:cd01942 256 -YD---LEESLRLGNLAASLKVERRGA 278
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
30-298 |
1.29e-30 |
|
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: 116.62 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 30 GGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAV-LIVNLTADGERSFTYLVHPGAD 108
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPIsSITDITGDRATISITAIDTQAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 109 tyvsPQDLPPFRQYEwfyfSSIGLTDRPAREACLEGARRMREAGGYVLFDVNlrSKMWGNTDEIPEL----IARSAALAS 184
Cdd:cd01945 116 ----PDSLPDAILGG----ADAVLVDGRQPEAALHLAQEARARGIPIPLDLD--GGGLRVLEELLPLadhaICSENFLRP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 185 ICKVSADELCQlsgashwqdaryYLRDLGCDTTIISLGADGALLITAEGE-FHFPAPRVDVVDTTGAGDAFVGGLLFTLS 263
Cdd:cd01945 186 NTGSADDEALE------------LLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPVEVVDTTGAGDVFHGAFAHALA 253
|
250 260 270
....*....|....*....|....*....|....*
gi 446569164 264 RANcwnhiLLAEAISNANACGAMAVTAKGAMTALP 298
Cdd:cd01945 254 EGM-----PLREALRFASAAAALKCRGLGGRAGLP 283
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
16-307 |
2.07e-30 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 116.77 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 16 DLVPEKQN---SYLKCPGGASANVGVCVARLGGE---CGFIGclgdDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIV 89
Cdd:COG1105 18 ELEPGEVNrasEVRLDPGGKGINVARVLKALGVDvtaLGFLG----GFTGEFIEELLDEEGIPTDFVPIEGETRINIKIV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 90 NLTADGErsfTYLVHPGADtyVSPQDLPPFRQY--------EWFYFS-SI--GLTDrparEACLEGARRMREAGGYVLFD 158
Cdd:COG1105 94 DPSDGTE---TEINEPGPE--ISEEELEALLERleellkegDWVVLSgSLppGVPP----DFYAELIRLARARGAKVVLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 159 VnlrSKmwgntdeiPELIARSAALASICKVSADELCQLSGAS--HWQDARYYLRDL---GCDTTIISLGADGALLITAEG 233
Cdd:COG1105 165 T---SG--------EALKAALEAGPDLIKPNLEELEELLGRPleTLEDIIAAARELlerGAENVVVSLGADGALLVTEDG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446569164 234 EFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRANCWnhillAEAISNANACGAMAVTAKGamTALPFPDQLNTFL 307
Cdd:COG1105 234 VYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDL-----EEALRLAVAAGAAAALSPG--TGLPDREDVEELL 300
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
24-293 |
2.29e-30 |
|
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: 116.56 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 24 SYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDaDLTSAVLIVNLTADGERSF-TYL 102
Cdd:cd01168 49 PVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVTPDAERTMcTYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 103 vhpGADTYVSPQDLPP--FRQYEWFYFSSIGLTDRParEACLEGARRMREAGgyVLFDVNLRSkmwgntdeiPELIARS- 179
Cdd:cd01168 128 ---GAANELSPDDLDWslLAKAKYLYLEGYLLTVPP--EAILLAAEHAKENG--VKIALNLSA---------PFIVQRFk 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 180 ---AALASICKVSA---DELCQLSGASHWQD---ARYYLRdLGCDTTIISLGADGALLITAEGEFHFPAPRVD-VVDTTG 249
Cdd:cd01168 192 ealLELLPYVDILFgneEEAEALAEAETTDDleaALKLLA-LRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNG 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446569164 250 AGDAFVGGLLFTLSRANCwnhilLAEAISNANACGAMAVTAKGA 293
Cdd:cd01168 271 AGDAFAGGFLYGLVQGEP-----LEECIRLGSYAAAEVIQQLGP 309
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
4-310 |
4.44e-30 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 115.74 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 4 MNKVWVIGDASVDLV------PE-----KQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVD 72
Cdd:PRK11142 2 MGKLVVLGSINADHVlnlesfPRpgetlTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 73 VTFLRLDADLTSAVLIVNLTADGERSFTylVHPGADTYVSPQDLPpfRQYEWFYFSSIGLT--DRPArEACLEGARRMRE 150
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIG--IHAGANAALTPALVE--AHRELIANADALLMqlETPL-ETVLAAAKIAKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 151 AGGYVLFD----VNLRSKMWGNTDEIPELIARSAALASIcKVSADELCQLsgASHWqdaryyLRDLGCDTTIISLGADGA 226
Cdd:PRK11142 157 HGTKVILNpapaRELPDELLALVDIITPNETEAEKLTGI-RVEDDDDAAK--AAQV------LHQKGIETVLITLGSRGV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 227 LLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRANCwnhilLAEAISNANACGAMAVTAKGAMTALPFPDQLNTF 306
Cdd:PRK11142 228 WLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKP-----LPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAF 302
|
....
gi 446569164 307 LSSH 310
Cdd:PRK11142 303 LQEQ 306
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
27-308 |
3.48e-29 |
|
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: 113.44 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 27 KCPGGASANVGVCVARLGGEC---GFIGclgdDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNltADGERsfTYLV 103
Cdd:TIGR03168 32 KDAGGKGINVARVLARLGAEVvatGFLG----GFTGEFIEALLAEEGIKNDFVEVKGETRINVKIKE--SSGEE--TELN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 104 HPGAdtYVSPQDLPPF--------RQYEWFYFS-SI--GLTDrparEACLEGARRMREAGGYVLFDVnlrSKmwgntdei 172
Cdd:TIGR03168 104 EPGP--EISEEELEQLleklrellASGDIVVISgSLppGVPP----DFYAQLIAIARKKGAKVILDT---SG-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 173 PELIARSAALASICKVSADELCQLSGAS-----HWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVDT 247
Cdd:TIGR03168 167 EALREALAAKPFLIKPNHEELEELFGRElktleEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNT 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446569164 248 TGAGDAFVGGLLFTLSRANCWnhillAEAISNANACGAMAVTAKGamTALPFPDQLNTFLS 308
Cdd:TIGR03168 247 VGAGDSMVAGFLAGLARGLSL-----EEALRFAVAAGSAAAFSPG--TGLPDPEDVEELLD 300
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
22-292 |
4.68e-26 |
|
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: 104.54 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 22 QNSYLKCPGGASANVGVCVARLGGEC---GFIGclgdDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVnltaDGERS 98
Cdd:cd01164 28 VSSTRKDAGGKGINVARVLKDLGVEVtalGFLG----GFTGDFFEALLKEEGIPDDFVEVAGETRINVKIK----EEDGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 99 FTYLVHPGADtyVSPQDLPPFRQY--------EWFYFS-SI--GLTDrparEACLEGARRMREAGGYVLFDVnlrSKmwg 167
Cdd:cd01164 100 ETEINEPGPE--ISEEELEALLEKlkallkkgDIVVLSgSLppGVPA----DFYAELVRLAREKGARVILDT---SG--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 168 ntdeiPELIARSAALASICKVSADELCQLSGASHWQDARYY-----LRDLGCDTTIISLGADGALLITAEGEFHFPAPRV 242
Cdd:cd01164 168 -----EALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIaaarkLIERGAENVLVSLGADGALLVTKDGVYRASPPKV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446569164 243 DVVDTTGAGDAFVGGLLFTLSRANCwnhilLAEAISNANACGAMAVTAKG 292
Cdd:cd01164 243 KVVSTVGAGDSMVAGFVAGLAQGLS-----LEEALRLAVAAGSATAFSPG 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
27-308 |
2.11e-25 |
|
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: 103.05 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 27 KCPGGASANVGVCVARLGGEC---GFIGclgdDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADgersFTYLV 103
Cdd:TIGR03828 32 IDAGGKGINVSRVLKNLGVDVvalGFLG----GFTGDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGT----ETKLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 104 HPGAdtYVSPQDLPPF--------RQYEWFYFS-SI--GLTDrparEACLEGARRMREAGGYVLFDVnlrskmwgntdEI 172
Cdd:TIGR03828 104 GPGP--EISEEELEALleklraqlAEGDWLVLSgSLppGVPP----DFYAELIALAREKGAKVILDT-----------SG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 173 PELIARSAALASICKVSADELCQLSGA--SHWQDARYY---LRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVDT 247
Cdd:TIGR03828 167 EALRDGLKAKPFLIKPNDEELEELFGRelKTLEEIIEAareLLDLGAENVLISLGADGALLVTKEGALFAQPPKGEVVST 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446569164 248 TGAGDAFVGGLLFTLSRancwnHILLAEAISNANACGAMAVTAKGamTALPFPDQLNTFLS 308
Cdd:TIGR03828 247 VGAGDSMVAGFLAGLES-----GLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLP 300
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
6-293 |
2.25e-22 |
|
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: 93.96 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEKQNSYlkcPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLdADLTSA 85
Cdd:cd01940 1 RLAAIGDNVVDKYLHLGKMY---PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV-KEGENA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 86 VLIVnLTADGERSFT-YLVHPGADTYVSPQDLPPFRQYEWFYfssIGLTDRP--AREAClegaRRMREAGGYVLFDVNLR 162
Cdd:cd01940 77 VADV-ELVDGDRIFGlSNKGGVAREHPFEADLEYLSQFDLVH---TGIYSHEghLEKAL----QALVGAGALISFDFSDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 163 SKMWGNTDEIPELiarSAALASICKVSADELCQLSGAshwqdaryyLRDLGCDTTIISLGADGALLITAEGEFHFPAPRV 242
Cdd:cd01940 149 WDDDYLQLVCPYV---DFAFFSASDLSDEEVKAKLKE---------AVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPV 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446569164 243 DVVDTTGAGDAFVGGLLFTLSrANCWNhilLAEAISNANACGAMAVTAKGA 293
Cdd:cd01940 217 EVVDTLGAGDSFIAGFLLSLL-AGGTA---IAEAMRQGAQFAAKTCGHEGA 263
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
25-263 |
1.12e-19 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 89.20 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 25 YLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLT-ADGERSFTYLV 103
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAETV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 104 HPGA-DTYVSPQ-DLPPFRQYEWFYFSSIGLTDrPAREACLEGARRM-REAGGYVLFDVNLRSKMWGNTDEIPELIARSA 180
Cdd:PLN02543 247 KEAAeDSLLASElNLAVLKEARMFHFNSEVLTS-PSMQSTLFRAIELsKKFGGLIFFDLNLPLPLWRSRDETRELIKKAW 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 181 ALASICKVSADELCQLSGASHWQDAR-----YYLRDLgcDTT-------------IISLGADG-ALLITAEG--EFHFPA 239
Cdd:PLN02543 326 NEADIIEVSRQELEFLLDEDYYERKRnyppqYYAESF--EQTknwrdyyhytpeeIAPLWHDGlKLLLVTDGtlRIHYYT 403
|
250 260 270
....*....|....*....|....*....|....*...
gi 446569164 240 PRVD--VV------------DTTGAGDAFVGGLLFTLS 263
Cdd:PLN02543 404 PKFDgvVVgtedvlitpftcDRTGSGDAVVAAIMRKLT 441
|
|
| PLN02967 |
PLN02967 |
kinase |
19-198 |
2.68e-19 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 88.18 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 19 PEKqnsYLKCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADGeRS 98
Cdd:PLN02967 235 PEK---FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRG-RL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 99 FTYLVHPGADTYVSPQDLPP--FRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDVNLRSKMWGNTDEIPELI 176
Cdd:PLN02967 311 KTTCVKPCAEDSLSKSEINIdvLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSFI 390
|
170 180
....*....|....*....|..
gi 446569164 177 ARSAALASICKVSADELCQLSG 198
Cdd:PLN02967 391 QEAWNLADIIEVTKQELEFLCG 412
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-292 |
2.98e-19 |
|
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: 85.94 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLV-------------PEKQNSYLkcpGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVD 72
Cdd:cd01944 1 KVLVIGAAVVDIVldvdklpasggdiEAKSKSYV---IGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 73 VTFL-RLDADltSAVLIVNLTADGERSFtyLVHPGADTYVSPQDLPPFR--QYEWFYFSSIGLTDRPAREACLEGARRMR 149
Cdd:cd01944 78 ILLPpRGGDD--GGCLVALVEPDGERSF--ISISGAEQDWSTEWFATLTvaPYDYVYLSGYTLASENASKVILLEWLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 150 EAGGYVLFDVNLRskmwgnTDEIPE-LIARSAALASICKVSADELCQLSGASHWQDARYyLRDLGCDT---TIISLGADG 225
Cdd:cd01944 154 PAGTTLVFDPGPR------ISDIPDtILQALMAKRPIWSCNREEAAIFAERGDPAAEAS-ALRIYAKTaapVVVRLGSNG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446569164 226 ALLITAEGE-FHFPAPRVDVVDTTGAGDAFVGGLLFTLSRAncwnhILLAEAISNANACGAMAVTAKG 292
Cdd:cd01944 227 AWIRLPDGNtHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKG-----MSLADAVLLANAAAAIVVTRSG 289
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
29-296 |
2.67e-18 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 83.71 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGAsANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTF----------------------LRLD------- 79
Cdd:COG2870 55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGlvvdprrptttktrviaggqqlLRLDfedrfpl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 80 ADLTSAVLIVNLTAdgersftylVHPGADTYVspqdlppfrqyewfyFS---SIGLTDRPAREACLEGarrmREAGGYVL 156
Cdd:COG2870 134 SAELEARLLAALEA---------ALPEVDAVI---------------LSdygKGVLTPELIQALIALA----RAAGKPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 157 FDVNLR--SKMWGN---TDEIPELiarSAALASICKvSADELCQLsgashwqdARYYLRDLGCDTTIISLGADGALLITA 231
Cdd:COG2870 186 VDPKGRdfSRYRGAtllTPNLKEA---EAAVGIPIA-DEEELVAA--------AAELLERLGLEALLVTRGEEGMTLFDA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446569164 232 EGE-FHFPAPRVDVVDTTGAGDAFVGGLlfTLSRAncwNHILLAEAISNANACGAMAVTAKGAMTA 296
Cdd:COG2870 254 DGPpHHLPAQAREVFDVTGAGDTVIATL--ALALA---AGASLEEAAELANLAAGIVVGKLGTATV 314
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-293 |
8.72e-18 |
|
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: 81.31 E-value: 8.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADlTSAVLIVnLTADGERSFTylVHPGAD 108
Cdd:cd01947 35 PGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKP-TRKTLSF-IDPNGERTIT--VPGERL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 109 tyVSPQDLPPFRQYEWFYFSSiGLTDRPAREACLEGarrmreagGYVLFDVNLRSKMwgntDEIPELIARSAALasICkv 188
Cdd:cd01947 111 --EDDLKWPILDEGDGVFITA-AAVDKEAIRKCRET--------KLVILQVTPRVRV----DELNQALIPLDIL--IG-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 189 SADELCQLSGAShwQDARYYLRdlgcdTTIISLGADGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRancw 268
Cdd:cd01947 172 SRLDPGELVVAE--KIAGPFPR-----YLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLK---- 240
|
250 260
....*....|....*....|....*
gi 446569164 269 NHIlLAEAISNANACGAMAVTAKGA 293
Cdd:cd01947 241 GWS-IEEALELGAQCGAICVSHFGP 264
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
31-293 |
1.85e-17 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 82.57 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 31 GASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLrldADLTSAVLIVNLTADGERSFTyLVHP-GADT 109
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGL---IEGTDAGDSSSASYETLLCWV-LVDPlQRHG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 110 YVSPQDLPPfrqyeWFYFSSIGLTDRPAREA------------------------CLEGARrmrEAGGYVLFDVNLRSK- 164
Cdd:PLN02341 196 FCSRADFGP-----EPAFSWISKLSAEAKMAirqskalfcngyvfdelspsaiasAVDYAI---DVGTAVFFDPGPRGKs 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 165 MWGNTDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDT--TIISLGADGALLITAEGEFHFPAPRV 242
Cdd:PLN02341 268 LLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKV 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446569164 243 DVVDTTGAGDAFVGGLLFTLsrancWNHILLAEAISNANACGAMAVTAKGA 293
Cdd:PLN02341 348 NVVDTVGCGDSFAAAIALGY-----IHNLPLVNTLTLANAVGAATAMGCGA 393
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
6-293 |
1.95e-16 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 77.47 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEKQNSYlkcPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRldadltsa 85
Cdd:PRK09813 2 KLATIGDNCVDIYPQLGKAF---SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 86 vlivnlTADGersftylvhPGADTYVSPQDLPP-FRQYEWFYFSSIGLTDRPAREACLegarrmreaggyvlFDVnLRSK 164
Cdd:PRK09813 71 ------TKHG---------VTAQTQVELHDNDRvFGDYTEGVMADFALSEEDYAWLAQ--------------YDI-VHAA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 165 MWGNTDE-IPELIARSAALA--------SICKVSADELCQLSGASHWQDA---RYYLRDL---GCDTTIISLGADGALLI 229
Cdd:PRK09813 121 IWGHAEDaFPQLHAAGKLTAfdfsdkwdSPLWQTLVPHLDYAFASAPQEDeflRLKMKAIvarGAGVVIVTLGENGSIAW 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446569164 230 TAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSrancwNHILLAEAISNANACGAMAVTAKGA 293
Cdd:PRK09813 201 DGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWL-----AGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-288 |
2.09e-16 |
|
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: 77.74 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVDLVPEKQNSYL----------KCPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTF 75
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVpgtsnpghvkQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 76 LRLDADLTSAVLIVNlTADGErsftyLVHPGADTYVSpQDLPPFRqyewfyfssigltdrpareacLEGARRMREAGGYV 155
Cdd:cd01941 81 IVFEGRSTASYTAIL-DKDGD-----LVVALADMDIY-ELLTPDF---------------------LRKIREALKEAKPI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 156 LFDVNLRskmwgntdeiPELIARSAALA------------SICKVSA---------------DELCQLSGASH-----WQ 203
Cdd:cd01941 133 VVDANLP----------EEALEYLLALAakhgvpvafeptSAPKLKKlfyllhaidlltpnrAELEALAGALIennedEN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 204 DARYYLRDLGCDTTIISLGADGALLITAEGE---FHFPAPRVD-VVDTTGAGDAFVGGLLFTLsrANCWNhilLAEAISN 279
Cdd:cd01941 203 KAAKILLLPGIKNVIVTLGAKGVLLSSREGGvetKLFPAPQPEtVVNVTGAGDAFVAGLVAGL--LEGMS---LDDSLRF 277
|
....*....
gi 446569164 280 ANACGAMAV 288
Cdd:cd01941 278 AQAAAALTL 286
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
6-288 |
1.31e-15 |
|
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: 75.67 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 6 KVWVIGDASVD---------LVPEKQNSYLKC------PGGAsANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNG 70
Cdd:cd01172 1 KVLVVGDVILDeylygdverISPEAPVPVVKVereeirLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 71 VDVTFLRldadltsavlivnltaDGERSFTYLVHPGADTYvspQDlppFRQYEwfyfssigLTDRPAREACLEG-----A 145
Cdd:cd01172 80 IDTDGIV----------------DEGRPTTTKTRVIARNQ---QL---LRVDR--------EDDSPLSAEEEQRlieriA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 146 RRMREAGGYVLFDVNLrskmwG--NTDEIPELIARSAALASICKVS-----------ADELC-------QLSGASHWQD- 204
Cdd:cd01172 130 ERLPEADVVILSDYGK-----GvlTPRVIEALIAAARELGIPVLVDpkgrdyskyrgATLLTpnekearEALGDEINDDd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 205 -----ARYYLRDLGCDTTIISLGADGALLITAEGEF-HFPAPRVDVVDTTGAGDAFVGglLFTLSRANCWNhilLAEAIS 278
Cdd:cd01172 205 eleaaGEKLLELLNLEALLVTLGEEGMTLFERDGEVqHIPALAKEVYDVTGAGDTVIA--TLALALAAGAD---LEEAAF 279
|
330
....*....|
gi 446569164 279 NANACGAMAV 288
Cdd:cd01172 280 LANAAAGVVV 289
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
9-291 |
5.91e-14 |
|
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: 70.51 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 9 VIGDASVDLVPEKQNSYLKcPGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRqvFQDNGVDVTFLrLDADLTSAVLi 88
Cdd:cd01937 4 IIGHVTIDEIVTNGSGVVK-PGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSD--LFDNGIEVISL-LSTETTTFEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 89 vNLTADGeRSFTYLVHPGADTYVSPQDlpPFRQYEWFYFSSIgltdrpareaCLEGARRMREAGGYVLFDVN--LRSkmW 166
Cdd:cd01937 79 -NYTNEG-RTRTLLAKCAAIPDTESPL--STITAEIVILGPV----------PEEISPSLFRKFAFISLDAQgfLRR--A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 167 GNTDEIPEliaRSAALASICKVSADELCQLSGAShwqDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVD 246
Cdd:cd01937 143 NQEKLIKC---VILKLHDVLKLSRVEAEVISTPT---ELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446569164 247 TTGAGDAFVGGLLFTLSRAncwNHILLAeaisnanACGAMAVTAK 291
Cdd:cd01937 217 PTGAGDVFLAAFLYSRLSG---KDIKEA-------AEFAAAAAAK 251
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
29-289 |
1.69e-13 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 69.72 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASANVGVCVARLGGECGFIGCLGDDDVGRFlRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADgersFTYLVHPGAD 108
Cdd:PRK09513 38 AAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGF-QQLFSELGIANRFQVVQGRTRINVKLTEKDGE----VTDFNFSGFE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 109 tyVSPQDlppfrqyeWFYFSSIGLT------------DRPA---REACLEGARRMREAGGYVLFDVN-------LRSKMW 166
Cdd:PRK09513 113 --VTPAD--------WERFVTDSLSwlgqfdmvavsgSLPRgvsPEAFTDWMTRLRSQCPCIIFDSSrealvagLKAAPW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 167 ---GNTDEIPELIARS-AALASICkvsadelcqlsgashwqDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPRV 242
Cdd:PRK09513 183 lvkPNRRELEIWAGRKlPELKDVI-----------------EAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPAC 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446569164 243 DVVDTTGAGDAFVGGLLFTLSRANCWNHIL-LAEAISnanacgAMAVT 289
Cdd:PRK09513 246 DVVSTVGAGDSMVGGLIYGLLMRESSEHTLrLATAVS------ALAVS 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
136-259 |
4.94e-12 |
|
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: 64.04 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 136 PAREACLEGARRMREAGGYVLFDVNLRSKMWgntdeIPELIARSAALASICKVSADELCQLSGASHW--QDARYYLRDL- 212
Cdd:cd00287 68 PAPEAVLDALEEARRRGVPVVLDPGPRAVRL-----DGEELEKLLPGVDILTPNEEEAEALTGRRDLevKEAAEAAALLl 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446569164 213 --GCDTTIISLGADGALLITAEG-EFHFPAPRVDVVDTTGAGDAFVGGLL 259
Cdd:cd00287 143 skGPKVVIVTLGEKGAIVATRGGtEVHVPAFPVKVVDTTGAGDAFLAALA 192
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
15-292 |
1.39e-11 |
|
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: 63.96 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 15 VDLVPEkQNSYLKCP------GGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFL-RLDADLTSAVL 87
Cdd:cd01939 16 VDKYPF-EDSDQRTTngrwqrGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCyRKDIDEPASSY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 88 IVNLTADGErsfTYLVHPGADTYVSPQDlppFR-----QYEWFYFSSigltdRPAREAC-----LEGARRMREAGGYVL- 156
Cdd:cd01939 95 IIRSRAGGR---TTIVNDNNLPEVTYDD---FSkidltQYGWIHFEG-----RNPDETLrmmqhIEEHNNRRPEIRITIs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 157 FDV-NLRSKMWGNTDEIPELIARSAALASICKVSADELCQLsgashwqdaRYYLRDLGCdTTIISLGADGALLITAEGE- 234
Cdd:cd01939 164 VEVeKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRG---------EGPRAKKAA-LLVCTWGDQGAGALGPDGEy 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446569164 235 FHFPA-PRVDVVDTTGAGDAFVGGLLFTLSRANcwnhILLAEAISNANACGAMAVTAKG 292
Cdd:cd01939 234 VHSPAhKPIRVVDTLGAGDTFNAAVIYALNKGP----DDLSEALDFGNRVASQKCTGVG 288
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
29-268 |
7.70e-10 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 58.96 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASAN-VGVCVARLG--GECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRlDADL---TSAVLIVnltaDGERSftyL 102
Cdd:PLN02548 51 AGGATQNsIRVAQWMLQipGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTptgTCAVLVV----GGERS---L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 103 VH--PGADTYVS-----PQDLPPFRQYEWFYFSSIGLTDRP------AREACLEG----------------ARRMREAGG 153
Cdd:PLN02548 123 VAnlSAANCYKVehlkkPENWALVEKAKFYYIAGFFLTVSPesimlvAEHAAANNktfmmnlsapficeffKDQLMEALP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 154 YVLFdvnlrskMWGNTDEiPELIARSAALASI-CKVSADELCQLSGASHWQdARYYLRDLGCDTTIISlgADGALLitae 232
Cdd:PLN02548 203 YVDF-------LFGNETE-ARTFAKVQGWETEdVEEIALKISALPKASGTH-KRTVVITQGADPTVVA--EDGKVK---- 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446569164 233 gEFH-FPAPRVDVVDTTGAGDAFVGGLLFTL---------SRANCW 268
Cdd:PLN02548 268 -EFPvIPLPKEKLVDTNGAGDAFVGGFLSQLvqgkdieecVRAGNY 312
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
173-264 |
1.11e-09 |
|
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: 58.25 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 173 PELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPA-PRVDVVDTTGAG 251
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAyPLESVFDPTGAG 233
|
90
....*....|...
gi 446569164 252 DAFVGGLLFTLSR 264
Cdd:cd01946 234 DTFAGGFIGYLAS 246
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
16-259 |
4.50e-09 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 56.96 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 16 DLVPEKQNSYLkcPGGASANVgvcvARLG--------GECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTS--A 85
Cdd:PTZ00247 50 ELESIPNVSYV--PGGSALNT----ARVAqwmlqapkGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGtcA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 86 VLIVNltadGERSFTYL----VHPGADTYVSPQDLPPFRQYEWFYFSSIGLTDRP------AREACLEGA---------- 145
Cdd:PTZ00247 124 VLVCG----KERSLVANlgaaNHLSAEHMQSHAVQEAIKTAQLYYLEGFFLTVSPnnvlqvAKHARESGKlfclnlsapf 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 146 ------RRMREAGGYV--LF--DVNLR----SKMWGNTDeIPELIARSAALAsicKVSAdelcqlsgashwQDARyylrd 211
Cdd:PTZ00247 200 isqfffERLLQVLPYVdiLFgnEEEAKtfakAMKWDTED-LKEIAARIAMLP---KYSG------------TRPR----- 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446569164 212 lgcdTTIISLGADGALLITAEGEFHFPAPRVD---VVDTTGAGDAFVGGLL 259
Cdd:PTZ00247 259 ----LVVFTQGPEPTLIATKDGVTSVPVPPLDqekIVDTNGAGDAFVGGFL 305
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
24-264 |
9.16e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 56.36 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 24 SYLKCPGGASANVGVCVARLGGE--------CGFIGCLGDDDVGRFLRQVFQDNGVDvtFLRLD-ADLTSAVLIVNLTAD 94
Cdd:PLN02813 120 SYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVH--FLSQPvKDGTTGTVIVLTTPD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 95 GERSFtyLVHPGAD----------TYVSPQDLPPFRQYEWfyfsSIGLTDRPAREAClEGARRmreAGGYVLF---DVNL 161
Cdd:PLN02813 198 AQRTM--LSYQGTSstvnydsclaSAISKSRVLVVEGYLW----ELPQTIEAIAQAC-EEAHR---AGALVAVtasDVSC 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 162 ----RSKMWgntdeipELIARSAalaSICKVSADE---LCQLSGASHWQDARYYLRDLgCDTTIISLGADGALlITAEGE 234
Cdd:PLN02813 268 ierhRDDFW-------DVMGNYA---DILFANSDEaraLCGLGSEESPESATRYLSHF-CPLVSVTDGARGSY-IGVKGE 335
|
250 260 270
....*....|....*....|....*....|..
gi 446569164 235 FHF--PAPRVDVvDTTGAGDAFVGGLLFTLSR 264
Cdd:PLN02813 336 AVYipPSPCVPV-DTCGAGDAYAAGILYGLLR 366
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
29-291 |
4.20e-08 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 53.84 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 29 PGGASANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVtflrldadltSAVLIVNltadGERSFTYL--VHPG 106
Cdd:PRK09850 39 PGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYV----------DKCLIVP----GENTSSYLslLDNT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 107 ADTYVSPQDLppfrqyewfyfssiGLTDRPAREACLEGARRMREAGgYVLFDVNLRSK--MW--GNTDEIPELIARSAA- 181
Cdd:PRK09850 105 GEMLVAINDM--------------NISNAITAEYLAQHREFIQRAK-VIVADCNISEEalAWilDNAANVPVFVDPVSAw 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 182 --------LASICKVSADEL-------CQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAP-RVDVV 245
Cdd:PRK09850 170 kcvkvrdrLNQIHTLKPNRLeaetlsgIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPiKTNVI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446569164 246 DTTGAGDAFVGGLlftlsrANCW-NHILLAEAISNANACGAMAVTAK 291
Cdd:PRK09850 250 NVTGAGDAMMAGL------ASCWvDGMPFAESVRFAQGCSSMALSCE 290
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
189-287 |
5.54e-06 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 47.34 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 189 SADELCQLSgashwQDARYYLRDLGCDTTIISL--GADGALLITAE--GEFHFPAPRVD---VVDTTGAGDAFVGGLLFT 261
Cdd:cd01943 203 SSDEEKEAV-----LQALLFSGILQDPGGGVVLrcGKLGCYVGSADsgPELWLPAYHTKstkVVDPTGGGNSFLGGFAAG 277
|
90 100
....*....|....*....|....*.
gi 446569164 262 LSRANcwnhillaeAISNANACGAMA 287
Cdd:cd01943 278 LALTK---------SIDEACIYGSVA 294
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
30-262 |
2.58e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 45.55 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 30 GGASANV--GVCvARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLDADLTS-AVLIVNltADGERS----FTYL 102
Cdd:PLN02379 86 GGSVANTirGLS-AGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAqCVCLVD--ALGNRTmrpcLSSA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 103 VHPGADTyVSPQDlppFRQYEW----FYFSSIGLTDRPAREACLEGAR-RMREAGgyvlFDV--NLRSKMW-----GNTD 170
Cdd:PLN02379 163 VKLQADE-LTKED---FKGSKWlvlrYGFYNLEVIEAAIRLAKQEGLSvSLDLAS----FEMvrNFRSPLLqllesGKID 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446569164 171 eipeliarsaalasICKVSADELCQLSGASHWQDARYYLRDLG--CDTTIISLGADGALLITAEGEFHFPA-PRVDVVDT 247
Cdd:PLN02379 235 --------------LCFANEDEARELLRGEQESDPEAALEFLAkyCNWAVVTLGSKGCIARHGKEVVRVPAiGETNAVDA 300
|
250
....*....|....*
gi 446569164 248 TGAGDAFVGGLLFTL 262
Cdd:PLN02379 301 TGAGDLFASGFLYGL 315
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
29-79 |
8.81e-05 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 44.05 E-value: 8.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446569164 29 PGGAsANVGVCVARLGGECGFIGCLGDDDVGRFLRQVFQDNGVDVTFLRLD 79
Cdd:PRK11316 50 PGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVP 99
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
218-292 |
5.55e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 41.33 E-value: 5.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446569164 218 IISLGADGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRAncwnhILLAEAISNANACGAMAVTAKG 292
Cdd:PLN02630 207 IVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQG-----LAVPDAALLGNYFGSLAVEQVG 276
|
|
| |
