|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-297 |
1.92e-78 |
|
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: 240.94 E-value: 1.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 5 EVICIGAAIVDipLQPVSKNIFDvdsyPLERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDI 84
Cdd:cd01166 1 DVVTIGEVMVD--LSPPGGGRLE----QADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 QSLKQDADIDTSINVGLVTADGERTFVTNRNGS-LWKLNINDVDLDRFSQAKVLSLASIFNSPLLDGKALT-EIFTQAKA 162
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSaASRLTPEDLDEAALAGADHLHLSGITLALSESAREALlEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 163 YRLIICAD-MIKPRLN---ETLEDIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFL--DCGVKTVVIKTGKRGCFIK 236
Cdd:cd01166 155 RGVTVSFDlNYRPKLWsaeEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKLGAEGALVY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134370524 237 RADMKMEVPAVSgITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGAT 297
Cdd:cd01166 235 TGGGRVFVPAYP-VEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-306 |
4.78e-78 |
|
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: 240.17 E-value: 4.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpvsknIFDVDSYP-------LERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCR 78
Cdd:COG0524 2 VLVIGEALVDL--------VARVDRLPkggetvlAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 79 RENIDIQSLKQDADIDTSINVGLVTADGERTFVTNRnGSLWKLNINDVDLDRFSQAKVLSLASIFNSPLLDGKALTEIFT 158
Cdd:COG0524 74 AEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYR-GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 159 QAKAYRLIICAD-MIKPRL-NETLEDIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFLDCGVKTVVIKTGKRGCFIK 236
Cdd:COG0524 153 AARAAGVPVSLDpNYRPALwEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLY 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 237 RADMKMEVPAVSgITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGATTGVKNRKLV 306
Cdd:COG0524 233 TGGEVVHVPAFP-VEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-298 |
3.04e-70 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 219.91 E-value: 3.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 5 EVICIGAAIVDipLQPVSKNIFDVDSYPlERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDI 84
Cdd:pfam00294 1 KVVVIGEANID--LIGNVEGLPGELVRV-STVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 QSLKQDADIDTSINVGLVTADGERTFVTNRNGSLWKLNI-NDVDLDRFSQAKVLSLASIFNSPLLD--GKALTEIFTQAK 161
Cdd:pfam00294 78 DYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEeLEENEDLLENADLLYISGSLPLGLPEatLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 162 AYRLIICadmikPRLNETLEDIRHALSYVDYLFPNFEEARLLTGKEtLDEIAD------SFLDCGVKTVVIKTGKRGCFI 235
Cdd:pfam00294 158 TFDPNLL-----DPLGAAREALLELLPLADLLKPNEEELEALTGAK-LDDIEEalaalhKLLAKGIKTVIVTLGADGALV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134370524 236 KRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGATT 298
Cdd:pfam00294 232 VEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-296 |
3.51e-42 |
|
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: 147.31 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 37 AMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVTADGERTFVTNR-- 114
Cdd:cd01174 32 ETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPga 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 115 NGSLWKLNInDVDLDRFSQAKVLSLAsiFNSPLldgKALTEIFTQAKAYRLIICADM--IKPRLNEtledirhALSYVDY 192
Cdd:cd01174 112 NGELTPADV-DAALELIAAADVLLLQ--LEIPL---ETVLAALRAARRAGVTVILNPapARPLPAE-------LLALVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 193 LFPNFEEARLLTGKETLDE-----IADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFASGFI 267
Cdd:cd01174 179 LVPNETEAALLTGIEVTDEedaekAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK-VKAVDTTGAGDTFIGALA 257
|
250 260
....*....|....*....|....*....
gi 1134370524 268 SALLEGKPLRECALFANATAAISVLSVGA 296
Cdd:cd01174 258 AALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-296 |
9.56e-42 |
|
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: 146.24 E-value: 9.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVD-IPLQPVSKNIFDvdSYPleriamttGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDI 84
Cdd:cd01167 2 VVCFGEALIDfIPEGSGAPETFT--KAP--------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 QSLKQDADIDTSINVGLVTADGERTFVTNRNGSLWKLNINDVDLDRFSQAKVLSLASIfnsPLLDG---KALTEIFTQAK 161
Cdd:cd01167 72 RGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSI---ALASEpsrSALLELLEAAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 162 AYRLIICAD------MIKPRlNETLEDIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFLDCGVKTVVIKTGKRGCFI 235
Cdd:cd01167 149 KAGVLISFDpnlrppLWRDE-EEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134370524 236 KRADMKMEVPAVSgITAIDTIGAGDNFASGFISALLEGK-------PLRECALFANATAAISVLSVGA 296
Cdd:cd01167 228 YTKGGVGEVPGIP-VEVVDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAGA 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
6-299 |
2.98e-41 |
|
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: 145.45 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpvsknIFDVDSYPLERIAMT------------------------TGGDAINEATIISRLGHRTALI 61
Cdd:cd01168 4 VLGLGNALVDI--------LAQVDDAFLEKLGLKkgdmiladmeeqeellaklpvkyiAGGSAANTIRGAAALGGSAAFI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 62 SRVGDDAPGHFIVDHCRRENIDIqSLKQDADIDTSINVGLVTADGERTFVTNRnGSLWKLNINDVDLDRFSQAKVLSLAS 141
Cdd:cd01168 76 GRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAERTMCTYL-GAANELSPDDLDWSLLAKAKYLYLEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 142 IFNspLLDGKALTEIFTQAKAYRLIICADM----IKPRLNEtleDIRHALSYVDYLFPNFEEARLLTGKETLD--EIADS 215
Cdd:cd01168 154 YLL--TVPPEAILLAAEHAKENGVKIALNLsapfIVQRFKE---ALLELLPYVDILFGNEEEAEALAEAETTDdlEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 216 FLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVG 295
Cdd:cd01168 229 LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
|
....
gi 1134370524 296 ATTG 299
Cdd:cd01168 309 PRLP 312
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-296 |
2.87e-39 |
|
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: 139.37 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpvsknIFDVDSYPLERIAMTT-------GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCR 78
Cdd:cd01942 2 VAVVGHLNYDI--------ILKVESFPGPFESVLVkdlrrefGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 79 RENIDIQSLKQDADIDTSINVGLVTADGERTFVTNRnGSLWKLNINDVDlDRFSQAKVLSLASifnsplldGKALTEIFT 158
Cdd:cd01942 74 EEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYP-GAMDELEPNDEA-DPDGLADIVHLSS--------GPGLIELAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 159 QAKAYRLIICAD---MIKPRLNETLEDIrhaLSYVDYLFPNFEEARLLTGKETLDEIAdsfLDCGVKTVVIKTGKRGCFI 235
Cdd:cd01942 144 ELAAGGITVSFDpgqELPRLSGEELEEI---LERADILFVNDYEAELLKERTGLSEAE---LASGVRVVVVTLGPKGAIV 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134370524 236 KRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGA 296
Cdd:cd01942 218 FEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
41-312 |
4.79e-30 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 115.74 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVTADGERTFVTNRnGSLWK 120
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHA-GANAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 121 LNINDVD--LDRFSQAKVLSLAsiFNSPLldgKALTEIFTQAKAYRliicadmIKPRLN----ETLEDirHALSYVDYLF 194
Cdd:PRK11142 118 LTPALVEahRELIANADALLMQ--LETPL---ETVLAAAKIAKQHG-------TKVILNpapaRELPD--ELLALVDIIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 195 PNFEEARLLTGKETLDE-----IADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFASGFISA 269
Cdd:PRK11142 184 PNETEAEKLTGIRVEDDddaakAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFR-VQAVDTIAAGDTFNGALVTA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1134370524 270 LLEGKPLRECALFANATAAISVLSVGATTGVKNRKLVEQLLDE 312
Cdd:PRK11142 263 LLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQE 305
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
6-299 |
1.27e-28 |
|
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: 111.23 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpvsknIFDVDSYPL--ERIAMTT-----GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCR 78
Cdd:cd01945 2 VLGVGLAVLDL--------IYLVASFPGgdGKIVATDyavigGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 79 RENIDIQSLKQDADIDTSIN-VGLVTADGERTFVTNRNGSLWKLNINDVDLDRFSqakVLslasifnspLLDGK---ALT 154
Cdd:cd01945 74 AEGVDTSFIVVAPGARSPISsITDITGDRATISITAIDTQAAPDSLPDAILGGAD---AV---------LVDGRqpeAAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 155 EIFTQAKA--YRLIICADMIKPRLNETLedirhaLSYVDYLFPNFEEARLLTGkETLDEIADSFLDCGVKTVVIKTGKRG 232
Cdd:cd01945 142 HLAQEARArgIPIPLDLDGGGLRVLEEL------LPLADHAICSENFLRPNTG-SADDEALELLASLGIPFVAVTLGEAG 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134370524 233 C-FIKRADMKMEVPAVSgITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGATTG 299
Cdd:cd01945 215 ClWLERDGELFHVPAFP-VEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAG 281
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
41-298 |
1.13e-24 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 101.35 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTS---INVGLVTADGERTFVTNRNGS 117
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGlamIFVDTKTGNNEIVIIPGANNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 118 LWKLNINDVDLDRFSQAKVLSLASifNSPLLDGKALTEIFTQAKAYRLIICADMIKPrlnETLEDIRHALSYVDYLFPNF 197
Cdd:PTZ00292 132 LTPQMVDAQTDNIQNICKYLICQN--EIPLETTLDALKEAKERGCYTVFNPAPAPKL---AEVEIIKPFLKYVSLFCVNE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 198 EEARLLTGKETLDE-----IADSFLDCGVKTVVIKTGKRGCFI-KRADMKMEVPAVSgITAIDTIGAGDNFASGFISALL 271
Cdd:PTZ00292 207 VEAALITGMEVTDTesafkASKELQQLGVENVIITLGANGCLIvEKENEPVHVPGKR-VKAVDTTGAGDCFVGSMAYFMS 285
|
250 260
....*....|....*....|....*..
gi 1134370524 272 EGKPLRECALFANATAAISVLSVGATT 298
Cdd:PTZ00292 286 RGKDLKESCKRANRIAAISVTRHGTQS 312
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
5-293 |
1.56e-24 |
|
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: 100.47 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 5 EVICIGAAIVDIPLQpVSKNIFDVDSYPlERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDI 84
Cdd:cd01941 1 EIVVIGAANIDLRGK-VSGSLVPGTSNP-GHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 qslkqDADIDTSINVGLVTAdgertfVTNRNGSLwKLNINDVDL-------------DRFSQAKVLslasifnspLLDG- 150
Cdd:cd01941 79 -----RGIVFEGRSTASYTA------ILDKDGDL-VVALADMDIyelltpdflrkirEALKEAKPI---------VVDAn 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 151 ---KALTEIFTQAKAYRLIIC---ADMIKprlnetLEDIRHALSYVDYLFPNFEEARLLTG---KETLDEI--ADSFLDC 219
Cdd:cd01941 138 lpeEALEYLLALAAKHGVPVAfepTSAPK------LKKLFYLLHAIDLLTPNRAELEALAGaliENNEDENkaAKILLLP 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134370524 220 GVKTVVIKTGKRGCFI---KRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLS 293
Cdd:cd01941 212 GIKNVIVTLGAKGVLLssrEGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
41-303 |
4.09e-22 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 94.23 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVTADGER--TFVTNRNGSL 118
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 119 WklnINDVDLDRFSQAKVLSLASIfnsplldgkALT---------EIFTQAKAYRLIICADmikPRLNETL--------E 181
Cdd:PRK09434 108 F---LQPQDLPPFRQGEWLHLCSI---------ALSaepsrsttfEAMRRIKAAGGFVSFD---PNLREDLwqdeaelrE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 182 DIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFLD-CGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGD 260
Cdd:PRK09434 173 CLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADrYPIALLLVTLGAEGVLVHTRGQVQHFPAPS-VDPVDTTGAGD 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1134370524 261 NFASGFISALLEGKPLRECALF------ANATAAISVLSVGATTGVKNR 303
Cdd:PRK09434 252 AFVAGLLAGLSQAGLWTDEAELaeiiaqAQACGALATTAKGAMTALPNR 300
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-291 |
1.32e-21 |
|
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: 92.49 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpvsknIFDVDSYP-------LERIAMTTGGdAINEATIISRLGHRTALISRVGDDAPGHFIVDHCR 78
Cdd:cd01944 2 VLVIGAAVVDI--------VLDVDKLPasggdieAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 79 RENIDIqSLKQDADIDTSINVGLVTADGERTFVTnrngslWKLNINDVDLDRFSQAKV-------LSLASIFNSPLLDG- 150
Cdd:cd01944 73 DEGIEI-LLPPRGGDDGGCLVALVEPDGERSFIS------ISGAEQDWSTEWFATLTVapydyvyLSGYTLASENASKVi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 151 --KALTEIftqAKAYRLIICADMIKPRLNET-LEDIRHALSYVDYlfpNFEEARLLTGKETLdEIADSFLDCGVKT---V 224
Cdd:cd01944 146 llEWLEAL---PAGTTLVFDPGPRISDIPDTiLQALMAKRPIWSC---NREEAAIFAERGDP-AAEASALRIYAKTaapV 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134370524 225 VIKTGKRGCFIKRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISV 291
Cdd:cd01944 219 VVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVV 285
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
41-310 |
1.02e-20 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 90.45 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVTADGERTFVTNRNGS--- 117
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSadm 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 118 LwkLNINDVDLDRFSQAKVLSLASIfnsplldgKALTEI--FTQAKAYRLIICADMI---KPRLNETL--------EDIR 184
Cdd:PLN02323 123 L--LRESELDLDLIRKAKIFHYGSI--------SLITEPcrSAHLAAMKIAKEAGALlsyDPNLRLPLwpsaeaarEGIM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 185 HALSYVDYLFPNFEEARLLTGKETL-DEIADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFA 263
Cdd:PLN02323 193 SIWDEADIIKVSDEEVEFLTGGDDPdDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFK-VKAVDTTGAGDAFV 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1134370524 264 SGFIS------ALLEGKP-LRECALFANATAAISVLSVGATTGVKNRKLVEQLL 310
Cdd:PLN02323 272 GGLLSqlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
41-312 |
1.72e-20 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 89.42 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDApGHFIVDHCRRENIDIQSLKQDADidTSINVGLVTADGERTFVTNRNGslwk 120
Cdd:COG1105 35 GGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGE--TRINIKIVDPSDGTETEINEPG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 121 LNINDVDLDRF--------SQAKVLSLA-SIfnSPLLDGKALTEIFTQAKAYRLIICADMIKPRLnetlediRHALSY-V 190
Cdd:COG1105 108 PEISEEELEALlerleellKEGDWVVLSgSL--PPGVPPDFYAELIRLARARGAKVVLDTSGEAL-------KAALEAgP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 191 DYLFPNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFASG 265
Cdd:COG1105 179 DLIKPNLEELEELLGRPleTLEDIiaaARELLERGAENVVVSLGADGALLVTEDGVYRAKPPK-VEVVSTVGAGDSMVAG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1134370524 266 FISALLEGKPLRECALFANATAAISVLSVGatTGVKNRKLVEQLLDE 312
Cdd:COG1105 258 FLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
2-312 |
8.59e-20 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 89.51 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 2 ENIEVICIGAAIVDI-----PLQPVSKNifDVDSYpLERIAMT--------TGGDAiNEATIISRLGHRTALISRVGDDA 68
Cdd:PLN02341 71 KEIDVATLGNLCVDIvlpvpELPPPSRE--ERKAY-MEELAASppdkksweAGGNC-NFAIAAARLGLRCSTIGHVGDEI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 69 PGHFIVDHCRRENIDIQSLKQDADIDTSINVG--------LVTADGERTFVTNRNGSLWKLNINDVDLDRFSQAKVLSLA 140
Cdd:PLN02341 147 YGKFLLDVLAEEGISVVGLIEGTDAGDSSSASyetllcwvLVDPLQRHGFCSRADFGPEPAFSWISKLSAEAKMAIRQSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 141 SIFnsplLDGKALTEIFTQAkayrLIICADMIK-----------PR----LNETLED---IRHALSYVDYLFPNFEEARL 202
Cdd:PLN02341 227 ALF----CNGYVFDELSPSA----IASAVDYAIdvgtavffdpgPRgkslLVGTPDErraLEHLLRMSDVLLLTSEEAEA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 203 LTGKETLDEIADSFL--DCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFASGFISALLEGKPLRECA 280
Cdd:PLN02341 299 LTGIRNPILAGQELLrpGIRTKWVVVKMGSKGSILVTRSSVSCAPAFK-VNVVDTVGCGDSFAAAIALGYIHNLPLVNTL 377
|
330 340 350
....*....|....*....|....*....|..
gi 1134370524 281 LFANATAAISVLSVGATTGVKNRKLVEQLLDE 312
Cdd:PLN02341 378 TLANAVGAATAMGCGAGRNVATLEKVLELLRA 409
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
41-312 |
3.72e-19 |
|
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: 85.70 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDaPGHFIVDHCRRENIDIQSLKQDADidTSINVGLVTADGERTfvtnrngslwK 120
Cdd:TIGR03168 35 GGKGINVARVLARLGAEVVATGFLGGF-TGEFIEALLAEEGIKNDFVEVKGE--TRINVKIKESSGEET----------E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 121 LN-----INDVDLDRF--------SQAKVLSLA-SIfnSPLLDGKALTEIFTQAKAYRLIICADMIKPRLNETLEdirha 186
Cdd:TIGR03168 102 LNepgpeISEEELEQLleklrellASGDIVVISgSL--PPGVPPDFYAQLIAIARKKGAKVILDTSGEALREALA----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 187 lSYVDYLFPNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRGCFIKRAD--MKMEVPAVsgiTAIDTIGAG 259
Cdd:TIGR03168 175 -AKPFLIKPNHEELEELFGRElkTLEEIieaARELLDRGAENVLVSLGADGALLVTKEgaLKATPPKV---EVVNTVGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1134370524 260 DNFASGFISALLEGKPLRECALFANATAAISVLSVGatTGVKNRKLVEQLLDE 312
Cdd:TIGR03168 251 DSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDVEELLDQ 301
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
29-310 |
3.65e-18 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 83.69 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 29 DSYPLERIAmttGGDAINEATIISR-LGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIdTSINVGLVTADGE 107
Cdd:PLN02379 77 DLSPIKTMA---GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGP-TAQCVCLVDALGN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 108 RTFVTNRNGSLwKLNINDVDLDRFSQAKVLSLA-SIFNSPLLDgkaltEIFTQAKAYRLIICADM--------IKPRLNE 178
Cdd:PLN02379 153 RTMRPCLSSAV-KLQADELTKEDFKGSKWLVLRyGFYNLEVIE-----AAIRLAKQEGLSVSLDLasfemvrnFRSPLLQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 179 TLEDirhalSYVDYLFPNFEEAR-LLTGKETLD-EIADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSGITAIDTI 256
Cdd:PLN02379 227 LLES-----GKIDLCFANEDEAReLLRGEQESDpEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDAT 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1134370524 257 GAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGATTGVKNRKLVEQLL 310
Cdd:PLN02379 302 GAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGEVTPENWQWMYKQM 355
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
28-296 |
2.54e-17 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 79.78 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 28 VDSYPLERIAMTtGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVtaDGE 107
Cdd:PRK09813 11 VDIYPQLGKAFS-GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELH--DND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 108 RTFVTNRNGSLWKLNINDVDLdRFSQAKVLSLASIFnsplldGKAlTEIFTQAKAYRLIICADMiKPRLNETLedIRHAL 187
Cdd:PRK09813 88 RVFGDYTEGVMADFALSEEDY-AWLAQYDIVHAAIW------GHA-EDAFPQLHAAGKLTAFDF-SDKWDSPL--WQTLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 188 SYVDYLFpNFEEARLLTGKETLDEIadsfLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDNFASGFI 267
Cdd:PRK09813 157 PHLDYAF-ASAPQEDEFLRLKMKAI----VARGAGVVIVTLGENGSIAWDGAQFWRQAPEP-VTVVDTMGAGDSFIAGFL 230
|
250 260
....*....|....*....|....*....
gi 1134370524 268 SALLEGKPLRECALFANATAAISVLSVGA 296
Cdd:PRK09813 231 CGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
28-296 |
9.03e-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: 78.55 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 28 VDSYPLERIaMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQD------ADIDTSinvgl 101
Cdd:cd01940 10 VDKYLHLGK-MYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKegenavADVELV----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 102 vtaDGERTFVTNRNGSLWKLNINDVDLDRFSQAKVlslasIFNSPLLDGKALTEIFTQAKAYRLIICADMikpRLNETLE 181
Cdd:cd01940 84 ---DGDRIFGLSNKGGVAREHPFEADLEYLSQFDL-----VHTGIYSHEGHLEKALQALVGAGALISFDF---SDRWDDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 182 DIRHALSYVDYLFPNFEEArlltGKETLDEIADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSgITAIDTIGAGDN 261
Cdd:cd01940 153 YLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRP-VEVVDTLGAGDS 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1134370524 262 FASGFISALLEGK-PLRECALFANATAAISVLSVGA 296
Cdd:cd01940 228 FIAGFLLSLLAGGtAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
41-297 |
1.62e-14 |
|
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: 72.56 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDaPGHFIVDHCRRENIDIQSLKQDADidTSINVGLVTADGERTfvtnrngslwK 120
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGE--TRINVKIKEEDGTET----------E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 121 LN-----INDVDLDRFsQAKVLSLASIFN--------SPLLDGKALTEIFTQAKAY--RLIIcaDMIKPRLNETLEdirh 185
Cdd:cd01164 103 INepgpeISEEELEAL-LEKLKALLKKGDivvlsgslPPGVPADFYAELVRLAREKgaRVIL--DTSGEALLAALA---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 186 alSYVDYLFPNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVsGITAIDTIGAGD 260
Cdd:cd01164 176 --AKPFLIKPNREELEELFGRPlgDEEDViaaARKLIERGAENVLVSLGADGALLVTKDGVYRASPP-KVKVVSTVGAGD 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1134370524 261 NFASGFISALLEGKPLRECALFANATAAISVLSVGAT 297
Cdd:cd01164 253 SMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
155-291 |
1.54e-13 |
|
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: 69.42 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 155 EIFTQAKAYRLIICADM-----IKPrlnetlEDIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFLDCGVKTVVIKTG 229
Cdd:cd01946 130 EVLEQVKDPKLVVMDTMnfwisIKP------EKLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRG 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134370524 230 KRGCFIKRADMKMEVPAVSGITAIDTIGAGDNFASGFISALLEGKP-----LRECALFANATAAISV 291
Cdd:cd01946 204 EYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDtseanMRRAIIYGSAMASFCV 270
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
14-297 |
2.25e-13 |
|
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: 68.98 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 14 VDIPLQPVSKNIFDvdsypleRIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDhcRRENIDIQSLKQDADI 93
Cdd:cd01947 16 LDAPPQPGGISHSS-------DSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLE--ELESGGDKHTVAWRDK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 94 DTSINVGLVTADGERTFVtnrngslwklNINDVDLDRFSQAKVLSLASIFNSPLLDGKALTEIFTQAKAyrLIICAdmiK 173
Cdd:cd01947 87 PTRKTLSFIDPNGERTIT----------VPGERLEDDLKWPILDEGDGVFITAAAVDKEAIRKCRETKL--VILQV---T 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 174 PRlnETLEDIRHALSYVDYLFPNFEEARLLTgkeTLDEIADSFLDCgvktVVIKTGKRGCFIKRADMKMEVPAVSgITAI 253
Cdd:cd01947 152 PR--VRVDELNQALIPLDILIGSRLDPGELV---VAEKIAGPFPRY----LIVTEGELGAILYPGGRYNHVPAKK-AKVP 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1134370524 254 DTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGAT 297
Cdd:cd01947 222 DSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
41-312 |
3.75e-13 |
|
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: 68.77 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGHRTALISRVGDDaPGHFIVDHCRRENIDIQSLKQDADidTSINVGLVTADGERTfvtnrngslwK 120
Cdd:TIGR03828 35 GGKGINVSRVLKNLGVDVVALGFLGGF-TGDFIEALLREEGIKTDFVRVPGE--TRINVKIKEPSGTET----------K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 121 LN-----INDVDLDRF--------SQAKVLSLA-SIfnSPLLDGKALTEIFTQAKAYRLIICADMIKPRLNETLEdirha 186
Cdd:TIGR03828 102 LNgpgpeISEEELEALleklraqlAEGDWLVLSgSL--PPGVPPDFYAELIALAREKGAKVILDTSGEALRDGLK----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 187 lsYVDYLF-PNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRGCFIKRAD--MKMEVPAvsgITAIDTIGA 258
Cdd:TIGR03828 175 --AKPFLIkPNDEELEELFGRElkTLEEIieaARELLDLGAENVLISLGADGALLVTKEgaLFAQPPK---GEVVSTVGA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1134370524 259 GDNFASGFISALLEGKPLRECALFANATAAISVLSVGatTGVKNRKLVEQLLDE 312
Cdd:TIGR03828 250 GDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLPQ 301
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
32-298 |
5.54e-13 |
|
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: 67.97 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 32 PLERIAMTTGGdAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQslkqdadidtsinvgLVTADGERTFV 111
Cdd:cd01172 31 KVEREEIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTD---------------GIVDEGRPTTT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 112 TNRngsLWKLNINDVDLDRFSQAKVlslasifnSPLLDGKALTEIFTQAKAYRLIICAD----MIKPRLNETLEDIRHAL 187
Cdd:cd01172 95 KTR---VIARNQQLLRVDREDDSPL--------SAEEEQRLIERIAERLPEADVVILSDygkgVLTPRVIEALIAAAREL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 188 S--------------Y--VDYLFPNFEEARLLTG-----KETLDEIADSFL-DCGVKTVVIKTGKRGC-FIKRADMKMEV 244
Cdd:cd01172 164 GipvlvdpkgrdyskYrgATLLTPNEKEAREALGdeindDDELEAAGEKLLeLLNLEALLVTLGEEGMtLFERDGEVQHI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1134370524 245 PAVSgITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGATT 298
Cdd:cd01172 244 PALA-KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAP 296
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
5-289 |
1.66e-12 |
|
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: 66.27 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 5 EVICIGAAIVDIPLQPVSKNIfdvdsypleriamTTGGDAINEATIISRLGHRTALISRVGDDapghfivdhcrreNIDI 84
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSGVV-------------KPGGPATYASLTLSRLGLTVKLVTKVGRD-------------YPDK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 QSLKQDADIDTSINVGLVTAdGERTFVTNRNGSLWKLNINDVDLDRFSQAKVLSLASIFNSPLLD--GKALTEIFTqaka 162
Cdd:cd01937 55 WSDLFDNGIEVISLLSTETT-TFELNYTNEGRTRTLLAKCAAIPDTESPLSTITAEIVILGPVPEeiSPSLFRKFA---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 163 yrlIICADM--IKPRLNETLEDIRHALSYVDYLFPNFEEARLLTgkeTLDEIADSFLDCGVKTVVIKTGKRGCFIKRADM 240
Cdd:cd01937 130 ---FISLDAqgFLRRANQEKLIKCVILKLHDVLKLSRVEAEVIS---TPTELARLIKETGVKEIIVTDGEEGGYIFDGNG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1134370524 241 KMEVPAvSGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAI 289
Cdd:cd01937 204 KYTIPA-SKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
181-297 |
4.85e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 65.82 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 181 EDIRHALSYVDYLFPNFEEARLLT-----GKETLDEIAD---SFLDCGVK---TVVIKTGKRG--CFIKRADMKMEVPAV 247
Cdd:PTZ00247 206 ERLLQVLPYVDILFGNEEEAKTFAkamkwDTEDLKEIAAriaMLPKYSGTrprLVVFTQGPEPtlIATKDGVTSVPVPPL 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1134370524 248 SGITAIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVGAT 297
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCT 335
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
6-295 |
1.06e-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: 64.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIplqpVSKnifdVDSYPLE-RIAMTT------GGDAINEATIISRLGHRTALisrVGDDAPGH---FIVD 75
Cdd:cd01939 2 VLCVGLTVLDF----ITT----VDKYPFEdSDQRTTngrwqrGGNASNSCTVLRLLGLSCEF---LGVLSRGPvfeSLLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 76 HCRRENIDIQS---LKQDADIDTSInvgLVTADGERTFVTNRNgslwklNINDVDLDRFSQAkVLSLAS-------IFNS 145
Cdd:cd01939 71 DFQSRGIDISHcyrKDIDEPASSYI---IRSRAGGRTTIVNDN------NLPEVTYDDFSKI-DLTQYGwihfegrNPDE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 146 PLLDGKALTEIFTQAKAYRLIICADMIKPRlnetlEDIRHALSYVDYLFPNFEEARLLTGKETLDEIADSFLDCGVKTVV 225
Cdd:cd01939 141 TLRMMQHIEEHNNRRPEIRITISVEVEKPR-----EELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134370524 226 IKT-GKRGCFIKRADMK-MEVPAVSGITAIDTIGAGDNFASGFISALLEGK-PLRECALFANATAAISVLSVG 295
Cdd:cd01939 216 VCTwGDQGAGALGPDGEyVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPdDLSEALDFGNRVASQKCTGVG 288
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
36-294 |
1.10e-11 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 64.95 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 36 IAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKQDADIDTSINVGLVTADGERTFVTNRN 115
Cdd:PRK09954 88 IHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAINDT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 116 GSLWKLN--INDVDLDRFSQAKVLsLASIFNSPlldgKALTEIFTqakayrliiCADMIkPRLNETL-----EDIRHALS 188
Cdd:PRK09954 168 HILQQLTpqLLNGSRDLIRHAGVV-LADCNLTA----EALEWVFT---------LADEI-PVFVDTVsefkaGKIKHWLA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 189 YVDYLFPNFEEARLLTGKETLDE-----IADSFLDCGVKTVVIKTGKRGCFIKRADMKMEVPAVSGITAIDTIGAGDNFA 263
Cdd:PRK09954 233 HIHTLKPTQPELEILWGQAITSDadrnaAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFM 312
|
250 260 270
....*....|....*....|....*....|.
gi 1134370524 264 SGFISALLEGKPLRECALFANATAAISVLSV 294
Cdd:PRK09954 313 AGLVYSFLEGYSFRDSARFAMACAAISRASG 343
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
159-271 |
1.40e-11 |
|
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: 62.50 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 159 QAKAYRLIICADMIKPRLNETLEDIRHALSYVDYLFPNFEEARLLTGKETLD-----EIADSFLDCGVKTVVIKTGKRGC 233
Cdd:cd00287 79 EARRRGVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEvkeaaEAAALLLSKGPKVVIVTLGEKGA 158
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1134370524 234 FIkrADMK---MEVPAVSgITAIDTIGAGDNFASGFISALL 271
Cdd:cd00287 159 IV--ATRGgteVHVPAFP-VKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
41-296 |
3.95e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 63.29 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 41 GGDAINEATIISRLGH--------RTALISRVGDDAPGHFIVDHCRRENIDIQSlKQDADIDTSINVGLVTADGERTFVT 112
Cdd:PLN02813 126 GGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLS-QPVKDGTTGTVIVLTTPDAQRTMLS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 113 NRnGSLWKLNINDVDLDRFSQAKVLSLAS-IFNSPLLDgKALTEIFTQAKAYRLIIC---ADM--IKPRLNETLEDIRHa 186
Cdd:PLN02813 205 YQ-GTSSTVNYDSCLASAISKSRVLVVEGyLWELPQTI-EAIAQACEEAHRAGALVAvtaSDVscIERHRDDFWDVMGN- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 187 lsYVDYLFPNFEEARLLTGKETLD--EIADSFLDCGVKTVVIKTGKRGCFIkraDMKMEVPAV--SGITAIDTIGAGDNF 262
Cdd:PLN02813 282 --YADILFANSDEARALCGLGSEEspESATRYLSHFCPLVSVTDGARGSYI---GVKGEAVYIppSPCVPVDTCGAGDAY 356
|
250 260 270
....*....|....*....|....*....|....*
gi 1134370524 263 ASGFISALLEGKP-LRECALFANATAAISVLSVGA 296
Cdd:PLN02813 357 AAGILYGLLRGVSdLRGMGELAARVAATVVGQQGT 391
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
177-313 |
3.96e-11 |
|
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: 62.74 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 177 NETLEDIRHALSYVDYLFPNFEEARLLTG----KETLDEIADSFLDC---------GVKTVVIKTGKRGCFIKRADMKME 243
Cdd:cd01943 168 PENLEDLLQALPRVDVFSPNLEEAARLLGlptsEPSSDEEKEAVLQAllfsgilqdPGGGVVLRCGKLGCYVGSADSGPE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 244 --VPAVSGITA--IDTIGAGDNFASGFISALLEGKPLRECALFAN--ATAAISVLSVGATTGVKNRKL-----VEQLLDE 312
Cdd:cd01943 248 lwLPAYHTKSTkvVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSvaASFAIEQVGLPRLTKVEGEELwngetVEERLKE 327
|
.
gi 1134370524 313 Y 313
Cdd:cd01943 328 Y 328
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
28-279 |
1.19e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 58.57 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 28 VDSYPLERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDIQSLKqDADIDTSiNVGLVTADGE 107
Cdd:PLN02548 42 ASKYNVEYIAGGATQNSIRVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTPTG-TCAVLVVGGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 108 RTFVTNRNGSlwklNINDVD-LDR------FSQAKVLSLASIF--NSPlldgKALTEIFTQAKAYRLIICADMIKPRLNE 178
Cdd:PLN02548 120 RSLVANLSAA----NCYKVEhLKKpenwalVEKAKFYYIAGFFltVSP----ESIMLVAEHAAANNKTFMMNLSAPFICE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 179 TLED-IRHALSYVDYLFPNFEEARLLT---GKETLD------EIADSFLDCGV--KTVVIKTGkRGCFIKRADMKMEVPA 246
Cdd:PLN02548 192 FFKDqLMEALPYVDFLFGNETEARTFAkvqGWETEDveeialKISALPKASGThkRTVVITQG-ADPTVVAEDGKVKEFP 270
|
250 260 270
....*....|....*....|....*....|....*.
gi 1134370524 247 VSGITA---IDTIGAGDNFASGFISALLEGKPLREC 279
Cdd:PLN02548 271 VIPLPKeklVDTNGAGDAFVGGFLSQLVQGKDIEEC 306
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
224-295 |
3.78e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 57.12 E-value: 3.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134370524 224 VVIKTGKRGCFIKRADMKMEVPAVSGITaIDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLSVG 295
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQ-VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
184-290 |
1.89e-08 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 54.38 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 184 RHALSYVDYLFPNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKtgkrGC-FIKRADMKMEVPAVS--GITAIDT 255
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPyeTLEEAlaaARALLALGPKIVVVT----SVpLDDTPADKIGNLAVTadGAWLVET 208
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1134370524 256 -------IGAGDNFASGFISALLEGKPLREcALfANATAAIS 290
Cdd:COG2240 209 pllpfspNGTGDLFAALLLAHLLRGKSLEE-AL-ERAAAFVY 248
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
150-278 |
2.17e-08 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 54.13 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 150 GKALTEIFTQAKAYR---LIIC----ADMIK--PRLNETLEDIRH-ALSYVDYLFPNFEEARLLTGK-----ETLDEIAD 214
Cdd:cd01173 87 VEAVAEIVKRLKEKNpnlLYVCdpvmGDNGKlyVVAEEIVPVYRDlLVPLADIITPNQFELELLTGKkindlEDAKAAAR 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134370524 215 SFLDCGVKTVVIK------TGKRGCFI--KRADMKMEVPAVSGITAIdtIGAGDNFASGFISALLEGKPLRE 278
Cdd:cd01173 167 ALHAKGPKTVVVTsveladDDRIEMLGstATEAWLVQRPKIPFPAYF--NGTGDLFAALLLARLLKGKSLAE 236
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
177-278 |
4.59e-08 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 53.14 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 177 NETLEDIRHALSYVDYLFPNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRgcFIKRA------DMKMEVP 245
Cdd:PRK12413 117 SELRQELIQFFPYVTVITPNLVEAELLSGKEikTLEDMkeaAKKLYDLGAKAVVIKGGNR--LSQKKaidlfyDGKEFVI 194
|
90 100 110
....*....|....*....|....*....|...
gi 1134370524 246 AVSGITAIDTIGAGDNFASGFISALLEGKPLRE 278
Cdd:PRK12413 195 LESPVLEKNNIGAGCTFASSIASQLVKGKSPLE 227
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
6-293 |
7.00e-08 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 53.07 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 6 VICIGAAIVDIP-LQPVSKNIfdVDSYPlERIAMTTGGDAINEATIISRLGHRTALISRVGDDAPGHFIVDHCRRENIDI 84
Cdd:PRK09850 7 VVIIGSANIDVAgYSHESLNY--ADSNP-GKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 85 QSLKQDADIDTSINVGLVTADGERTfvtnrngslwkLNINDVDLDRFSQAKVLSLASIFNSPLLDGKALTEIFTQAKAYR 164
Cdd:PRK09850 84 DKCLIVPGENTSSYLSLLDNTGEML-----------VAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 165 LIICADM---IKPRLNETLEDIRHALSYVDYLFPNFEEARLLTG-----KETLDEIADSFLDCGVKTVVIKTGKRGCFIK 236
Cdd:PRK09850 153 LDNAANVpvfVDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGialsgREDVAKVAAWFHQHGLNRLVLSMGGDGVYYS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134370524 237 radmkmEVPAVSGITA------IDTIGAGDNFASGFISALLEGKPLRECALFANATAAISVLS 293
Cdd:PRK09850 233 ------DISGESGWSApiktnvINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALSC 289
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
178-228 |
1.30e-04 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 42.76 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134370524 178 ETLEDIRHALSYVDYLFPNFEEARLLTGKETLD-----EIADSFLDCGVKTVVIKT 228
Cdd:PTZ00344 128 EVVDAYRELIPYADVITPNQFEASLLSGVEVKDlsdalEAIDWFHEQGIPVVVITS 183
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
195-314 |
2.53e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 38.91 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134370524 195 PNFEEARLLTGKE--TLDEI---ADSFLDCGVKTVVIKTGKRGCFIKRAD--MKMEVPAVsgiTAIDTIGAGDNFASGFI 267
Cdd:PRK09513 186 PNRRELEIWAGRKlpELKDVieaAHALREQGIAHVVISLGAEGALWVNASgeWIAKPPAC---DVVSTVGAGDSMVGGLI 262
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1134370524 268 SALLEGKPLRECALFANATAAISVLSvgATTGVKNRKLVEQLLDEYE 314
Cdd:PRK09513 263 YGLLMRESSEHTLRLATAVSALAVSQ--SNVGITDRPQLAAMMARVD 307
|
|
| |
