|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
1-251 |
3.92e-118 |
|
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: 339.19 E-value: 3.92e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 1 MTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAK 80
Cdd:TIGR02152 47 EVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 81 VMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:TIGR02152 127 IVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPAIKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 161 GCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:TIGR02152 207 GVKNVIITLGSKGALLVSKDES--KLIPAFKVKAVDTTAAGDTFNGAFAVALAEGK--SLEDAIRFANAAAAISVTRKGA 282
|
250
....*....|.
gi 567316250 241 QSSYPYKKDLP 251
Cdd:TIGR02152 283 QSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
2-246 |
1.09e-102 |
|
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: 300.24 E-value: 1.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:cd01174 53 VAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 82 MVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPqFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRG 161
Cdd:cd01174 133 LLLQLEIPLETVLAALRAARRAGVTVILNPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 162 CQVVIITLGAEGCVVLSqtEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPnlSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:cd01174 212 VKNVIVTLGAKGALLAS--GGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL--SLEEAIRFANAAAALSVTRPGAQ 287
|
....*
gi 567316250 242 SSYPY 246
Cdd:cd01174 288 PSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-251 |
3.67e-84 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 254.28 E-value: 3.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNE-GQNIIVIVAGANLLLNTEDLRAAANVI-SRA 79
Cdd:PTZ00292 69 VAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNIC 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 80 KVMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQ----FYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:PTZ00292 149 KYLICQNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 VLLKRGCQVVIITLGAEGCVvLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSV 235
Cdd:PTZ00292 229 ELQQLGVENVIITLGANGCL-IVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSR--GKDLKESCKRANRIAAISV 305
|
250
....*....|....*.
gi 567316250 236 QAAGTQSSYPYKKDLP 251
Cdd:PTZ00292 306 TRHGTQSSYPHPSELP 321
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-250 |
2.25e-61 |
|
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: 195.10 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAAnvISRAKV 81
Cdd:COG0524 53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 82 MVCQL-----EITPATSLEALTMARRSGVKTLFNPAPAIADLDP------QFYTLSDVFCCNESEAEILTGLTvgsaaDA 150
Cdd:COG0524 131 LHLGGitlasEPPREALLAALEAARAAGVPVSLDPNYRPALWEParellrELLALVDILFPNEEEAELLTGET-----DP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 151 GEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFI 230
Cdd:COG0524 206 EEAAAALLARGVKLVVVTLGAEGALLYTGGEVV--HVPAFPVEVVDTTGAGDAFAAGFLAGLLE--GLDLEEALRFANAA 281
|
250 260
....*....|....*....|
gi 567316250 231 AAVSVQAAGTQSSYPYKKDL 250
Cdd:COG0524 282 AALVVTRPGAQPALPTREEV 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
2-251 |
1.34e-58 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 188.15 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:PRK11142 56 IAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 82 MVCQLEiTPATS-LEALTMARRSGVKTLFNPAPAiADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:PRK11142 136 LLMQLE-TPLETvLAAAKIAKQHGTKVILNPAPA-RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 161 GCQVVIITLGAEGcVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAfyLAYYPNLSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:PRK11142 214 GIETVLITLGSRG-VWLSENG-EGQRVPGFRVQAVDTIAAGDTFNGALV--TALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
250
....*....|.
gi 567316250 241 QSSYPYKKDLP 251
Cdd:PRK11142 290 QPSIPWREEID 300
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-242 |
2.64e-46 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 155.96 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKV 81
Cdd:pfam00294 51 VAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 82 MV----CQLEITPATSLEALTMARRSG--VKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAAL 155
Cdd:pfam00294 131 LYisgsLPLGLPEATLEELIEAAKNGGtfDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 VLLKRGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEDMLNRSNFIAAVS 234
Cdd:pfam00294 211 KLLAKGIKTVIVTLGADGALVVEGDG-EVHVPAVPKVKVVDTTGAGDSFVGGfLAGLLA---GKSLEEALRFANAAAALV 286
|
....*...
gi 567316250 235 VQAAGTQS 242
Cdd:pfam00294 287 VQKSGAQT 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
2-240 |
1.57e-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: 115.40 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDIstEFTYQT-KDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAAnvISRAK 80
Cdd:cd01168 72 AAFIGRVGDDKLGDFLLKDLRAAGV--DTRYQVqPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSL--LAKAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 81 VMVC---QLEITPATSLEALTMARRSGVKTLFN-PAPAIAD-----LDPQFYTLSDVFCcNESEAEILTGLTVGSAAdag 151
Cdd:cd01168 148 YLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFIVQrfkeaLLELLPYVDILFG-NEEEAEALAEAETTDDL--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 152 EAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEK-VKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFI 230
Cdd:cd01168 224 EAALKLLALRCRIVVITQGAKGAVVVEGGEVY--PVPAIPvEKIVDTNGAGDAFAG--GFLYGLVQGEPLEECIRLGSYA 299
|
250
....*....|
gi 567316250 231 AAVSVQAAGT 240
Cdd:cd01168 300 AAEVIQQLGP 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-239 |
8.35e-28 |
|
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: 107.66 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIV--NNEGQNIIVIVAGANLLLNTEDLRAAAnvISRA 79
Cdd:cd01166 48 VALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIgaGGERRVLYYRAGSAASRLTPEDLDEAA--LAGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 80 KvMVCQLEITPATS-------LEALTMARRSGVKTLF--NPAPAIADLD------PQFYTLSDVFCCNESEAEILTGLTV 144
Cdd:cd01166 126 D-HLHLSGITLALSesarealLEALEAAKARGVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDED 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 145 GSAAdagEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGA-LAFYLAyypNLSLEDM 223
Cdd:cd01166 205 PTDA---AERALALALGVKAVVVKLGAEGALVYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGfLAGLLE---GWDLEEA 276
|
250
....*....|....*.
gi 567316250 224 LNRSNFIAAVSVQAAG 239
Cdd:cd01166 277 LRFANAAAALVVTRPG 292
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
2-239 |
1.22e-27 |
|
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: 107.34 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAG--ANLLLNTEDLraaANVISRA 79
Cdd:cd01167 45 AAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADLLLDTELN---PDLLSEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 80 K-VMVCQL----EITPATSLEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVFCCNESEAEILTGLTvg 145
Cdd:cd01167 122 DiLHFGSIalasEPSRSALLELLEAAKKAGVLISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFGEE-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 146 saaDAGEAALVLLKRGCQVVIITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLS-----L 220
Cdd:cd01167 200 ---DPEEIAALLLLFGLKLVLVTRGADGALLY--TKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedeL 274
|
250
....*....|....*....
gi 567316250 221 EDMLNRSNFIAAVSVQAAG 239
Cdd:cd01167 275 AEALRFANAVGALTCTKAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-241 |
9.71e-27 |
|
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: 104.70 E-value: 9.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 5 VCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLnteDLRAAANVISRAKVmvc 84
Cdd:cd01942 56 VAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDEL---EPNDEADPDGLADI--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 85 qLEITPATSLEALTMARRSGVKTL-FNPAPAIADLD----PQFYTLSDVFCCNESEAEILTGLTVGSAADageaalvlLK 159
Cdd:cd01942 130 -VHLSSGPGLIELARELAAGGITVsFDPGQELPRLSgeelEEILERADILFVNDYEAELLKERTGLSEAE--------LA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFvgALAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:cd01942 201 SGVRVVVVTLGPKGAIVFEDGE-EVEVPAVPAVKVVDTTGAGDAF--RAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
..
gi 567316250 240 TQ 241
Cdd:cd01942 278 AQ 279
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
8-236 |
4.88e-23 |
|
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: 94.69 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 8 VGKDSFGNDYIENLKQNDISTEFTyQTKDAATGTASIIVNNEGqNIIVIVAGANL--LLNTEDLRAAANVISRAKVMVCQ 85
Cdd:cd01941 58 VGDDSEGESILEESEKAGLNVRGI-VFEGRSTASYTAILDKDG-DLVVALADMDIyeLLTPDFLRKIREALKEAKPIVVD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 86 LEITPATSLEALTMARRSGVKTLFNPA-----PAIADLDPQFYTLSdvfcCNESEAEILTGLTVGSAADAGEAALVLLKR 160
Cdd:cd01941 136 ANLPEEALEYLLALAAKHGVPVAFEPTsapklKKLFYLLHAIDLLT----PNRAELEALAGALIENNEDENKAAKILLLP 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567316250 161 GCQVVIITLGAEGcVVLSQTEP--EPKHIPTEKV-KAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSVQ 236
Cdd:cd01941 212 GIKNVIVTLGAKG-VLLSSREGgvETKLFPAPQPeTVVNVTGAGDAFVAGLVAGLLE--GMSLDDSLRFAQAAAALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
8-245 |
2.75e-22 |
|
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: 93.01 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 8 VGKDSFGNDYIENLKQNDISTEFTYQtKDAATGTASIIVNnEGQNIIVIVAGANLLLNTED----LRAAANVISRAKVMV 83
Cdd:cd01172 62 VGDDEAGDLLRKLLEKEGIDTDGIVD-EGRPTTTKTRVIA-RNQQLLRVDREDDSPLSAEEeqrlIERIAERLPEADVVI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 84 cqLE------ITPATSLEALTMARRSGVKTLFNPAPaiadLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVL 157
Cdd:cd01172 140 --LSdygkgvLTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 158 LKR-GCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQ 236
Cdd:cd01172 214 LELlNLEALLVTLGEEGMTLFERDG-EVQHIPALAKEVYDVTGAGDTVIATLALALA--AGADLEEAAFLANAAAGVVVG 290
|
....*....
gi 567316250 237 AAGTQSSYP 245
Cdd:cd01172 291 KVGTAPVTP 299
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
2-246 |
1.20e-21 |
|
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: 91.20 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAG----ANLLLNTEDLRAAANVI- 76
Cdd:cd01945 53 ARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGGADAVLv 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 77 -SRAkvmvcqleitPATSLEALTMARRSGVktlfnpaPAIADLDPQF-------YTLSDVFCCNESEAEILTGLtvgsaa 148
Cdd:cd01945 133 dGRQ----------PEAALHLAQEARARGI-------PIPLDLDGGGlrvleelLPLADHAICSENFLRPNTGS------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 149 dAGEAALVLLK-RGCQVVIITLGAEGCVVLSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRS 227
Cdd:cd01945 190 -ADDEALELLAsLGIPFVAVTLGEAGCLWLERDG-ELFHVPAFPVEVVDTTGAGDVFHGAFAHALA--EGMPLREALRFA 265
|
250
....*....|....*....
gi 567316250 228 NFIAAVSVQAAGTQSSYPY 246
Cdd:cd01945 266 SAAAALKCRGLGGRAGLPT 284
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
8-240 |
1.62e-21 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 91.41 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 8 VGKDSFGNDYIENLKQNDISTEFTYQTKDAATgTASIIVNNEGQNIIVIVAGANLLLNTED----LRAAANVISRAKVMV 83
Cdd:COG2870 78 VGDDEAGRELRRLLEEAGIDTDGLVVDPRRPT-TTKTRVIAGGQQLLRLDFEDRFPLSAELearlLAALEAALPEVDAVI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 84 cqLE------ITPATSLEALTMARRSGVKTLFNPAPAiadlDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVL 157
Cdd:COG2870 157 --LSdygkgvLTPELIQALIALARAAGKPVLVDPKGR----DFSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAAAEL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 158 LKR-GCQVVIITLGAEGCVVLSQTEPePKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAVSVQ 236
Cdd:COG2870 231 LERlGLEALLVTRGEEGMTLFDADGP-PHHLPAQAREVFDVTGAGDTVIATLALALAA--GASLEEAAELANLAAGIVVG 307
|
....
gi 567316250 237 AAGT 240
Cdd:COG2870 308 KLGT 311
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
89-213 |
2.92e-20 |
|
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: 85.22 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 89 TPATSLEALTMARRSGVKTLFNPAPAIADLDPQ----FYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQV 164
Cdd:cd00287 69 APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKV 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 567316250 165 VIITLGAEGCVVLSQTEPEpKHIPTEKVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd00287 149 VIVTLGEKGAIVATRGGTE-VHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
7-250 |
1.44e-19 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 85.76 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 7 KVGKDSFGNDYIENLKQNDISTEFTYQtkDAATGTASIIV--NNEGQN--IIVIVAGANLLLNTEDLR------------ 70
Cdd:PRK09434 50 RVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVdlDDQGERsfTFMVRPSADLFLQPQDLPpfrqgewlhlcs 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 71 -AAANVISRAkvmvcqleitpaTSLEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVfcCNESEAEiLT 140
Cdd:PRK09434 128 iALSAEPSRS------------TTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALADV--VKLSEEE-LC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 141 GLTVGSAADAGEAALVLLkRGCQVVIITLGAEGcvVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLS- 219
Cdd:PRK09434 193 FLSGTSQLEDAIYALADR-YPIALLLVTLGAEG--VLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTd 269
|
250 260 270
....*....|....*....|....*....|....
gi 567316250 220 ---LEDMLNRSNFIAAVSVQAAGTQSSYPYKKDL 250
Cdd:PRK09434 270 eaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
132-241 |
2.79e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 84.80 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAfy 211
Cdd:COG1105 184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTVGAGDSMVAGFL-- 259
|
90 100 110
....*....|....*....|....*....|
gi 567316250 212 LAYYPNLSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:COG1105 260 AGLARGLDLEEALRLAVAAGAAAALSPGTG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
70-239 |
2.45e-16 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 77.95 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 70 RAAANVISRAKVMVCQL----EITPATSLEALTMARRSGVKTLFNPAP---AIADLDP-------QFYTLSDVFCCNESE 135
Cdd:PLN02341 216 AEAKMAIRQSKALFCNGyvfdELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPderraleHLLRMSDVLLLTSEE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 136 AEILTGLtvGSAADAGEAalvLLKRGC--QVVIITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFylA 213
Cdd:PLN02341 296 AEALTGI--RNPILAGQE---LLRPGIrtKWVVVKMGSKGSILV--TRSSVSCAPAFKVNVVDTVGCGDSFAAAIAL--G 366
|
170 180
....*....|....*....|....*.
gi 567316250 214 YYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PLN02341 367 YIHNLPLVNTLTLANAVGAATAMGCG 392
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
103-239 |
1.96e-15 |
|
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: 74.00 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 103 SGVKTLFNPAPAIADLDPQFytLSDV------FCCNESEAEILTGlTVGSAADAgeAALVLLKRGCQVVIITLGAEGCVV 176
Cdd:cd01944 155 AGTTLVFDPGPRISDIPDTI--LQALmakrpiWSCNREEAAIFAE-RGDPAAEA--SALRIYAKTAAPVVVRLGSNGAWI 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567316250 177 LSQTEpEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:cd01944 230 RLPDG-NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLA--KGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
132-241 |
8.82e-15 |
|
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: 72.18 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALAfy 211
Cdd:cd01164 184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFV-- 259
|
90 100 110
....*....|....*....|....*....|
gi 567316250 212 LAYYPNLSLEDMLNRSNFIAAVSVQAAGTQ 241
Cdd:cd01164 260 AGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
5-222 |
3.80e-14 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 70.81 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 5 VCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIV--AGANLLLNTEDLRAaaNVISRAKVM 82
Cdd:PLN02323 63 IGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADMLLRESELDL--DLIRKAKIF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 83 ---VCQLEITPATS--LEALTMARRSGVKTLFNP---------APAIADLDPQFYTLSDVFCCNESEAEILTGltvgSAA 148
Cdd:PLN02323 141 hygSISLITEPCRSahLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGIMSIWDEADIIKVSDEEVEFLTG----GDD 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567316250 149 DAGEAALVLLKRGCQVVIITLGAEGCVVLSqtePEPK-HIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLsLED 222
Cdd:PLN02323 217 PDDDTVVKLWHPNLKLLLVTEGEEGCRYYT---KDFKgRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSL-LED 287
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
8-244 |
6.54e-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: 66.67 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 8 VGKDSFGNDYIENLKQNDIstEFTYQTKDAATGTASIIVNNEGQNIIVIVAGanlllNTEDLRAAANVISRAKVMvcqle 87
Cdd:cd01947 59 LGRDEIGIQSLEELESGGD--KHTVAWRDKPTRKTLSFIDPNGERTITVPGE-----RLEDDLKWPILDEGDGVF----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 88 ITPATSL-EALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTgltvgsaadageAALVLLKRGCQVVI 166
Cdd:cd01947 127 ITAAAVDkEAIRKCRETKLVILQVTPRVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLI 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567316250 167 ITLGAEGCVVLsqTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNRSNFIAAvsvQAAGTQSSY 244
Cdd:cd01947 195 VTEGELGAILY--PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLK--GWSIEEALELGAQCGA---ICVSHFGPY 265
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
8-250 |
1.02e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 66.59 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 8 VGKDSFGNDYIENLKQNDISTEFTYqTKDAATGTASIIVNNEGQNIIVIVAGANLL----LNTEDLRAAanvISRAKVMV 83
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTCAVLVCGKERSLVANLGAANHLsaehMQSHAVQEA---IKTAQLYY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 84 CQ---LEITPATSLEALTMARRSGVKTLFN-PAP-AIADLDPQFYTL---SDVFCCNESEAEiltglTVGSAADAGEAAL 155
Cdd:PTZ00247 165 LEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyVDILFGNEEEAK-----TFAKAMKWDTEDL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 156 V-LLKRGCQ----------VVIITLGAEGCVVLSQTE----PEPkhiPTEKVKAVDTTGAGDSFVGAlafYLAYYPN-LS 219
Cdd:PTZ00247 240 KeIAARIAMlpkysgtrprLVVFTQGPEPTLIATKDGvtsvPVP---PLDQEKIVDTNGAGDAFVGG---FLAQYANgKD 313
|
250 260 270
....*....|....*....|....*....|.
gi 567316250 220 LEDMLNRSNFIAAVSVQAAGtqSSYPYKKDL 250
Cdd:PTZ00247 314 IDRCVEAGHYSAQVIIQHNG--CTYPEKPPF 342
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
2-250 |
1.81e-11 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 63.20 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 2 TSMVCKVGKDSFGNDYIENLKQNDISTEFtYQTKDAATGTASIIVNNEGQNIIVIVAGANLLlNTEDLRAAAN--VISRA 79
Cdd:PLN02548 72 TSYMGCIGKDKFGEEMKKCATAAGVNVHY-YEDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENwaLVEKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 80 KVMVCQ---LEITPATSLEALTMARRSGVKTLFN-PAPAIADL--DPQFYTLS--DVFCCNESEAEILTGLTVGSAADAG 151
Cdd:PLN02548 150 KFYYIAgffLTVSPESIMLVAEHAAANNKTFMMNlSAPFICEFfkDQLMEALPyvDFLFGNETEARTFAKVQGWETEDVE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 152 EAALVL----LKRGCQ--VVIITLGAEGCVVL--SQTEPEPKhIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDM 223
Cdd:PLN02548 230 EIALKIsalpKASGTHkrTVVITQGADPTVVAedGKVKEFPV-IPLPKEKLVDTNGAGDAFVG--GFLSQLVQGKDIEEC 306
|
250 260
....*....|....*....|....*..
gi 567316250 224 LNRSNFIAAVSVQAAGTqsSYPYKKDL 250
Cdd:PLN02548 307 VRAGNYAANVIIQRSGC--TYPEKPDF 331
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
127-223 |
6.50e-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: 55.16 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 127 DVFCCNESEAEILTGltvgsAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTE----PEpkhIPTEKVkaVDTTGAGD 202
Cdd:cd01946 165 DVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGyfaaPA---YPLESV--FDPTGAGD 234
|
90 100
....*....|....*....|.
gi 567316250 203 SFVGALAFYLAYYPNLSLEDM 223
Cdd:cd01946 235 TFAGGFIGYLASQKDTSEANM 255
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
132-222 |
9.20e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 55.18 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGltvGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTepEPKHIP-TEKVKAVDTTGAGDSFVGalAF 210
Cdd:PLN02379 239 NEDEARELLR---GEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGK--EVVRVPaIGETNAVDATGAGDLFAS--GF 311
|
90
....*....|..
gi 567316250 211 YLAYYPNLSLED 222
Cdd:PLN02379 312 LYGLIKGLSLEE 323
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
4-241 |
1.29e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.81 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 4 MVCKVGKDSFGNDYIENLKQNDIstEFTYQ-TKDAATGTASIIVNNEGQNIIVIVAGANLLLN-TEDLRAAanvISRAKV 81
Cdd:PLN02813 153 MAGSVGSDPLGDFYRTKLRRANV--HFLSQpVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNyDSCLASA---ISKSRV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 82 MVCQ-----LEITPATSLEALTMARRSGVK---TLFNPApAIADLDPQFYTL----SDVFCCNESEAEILTGLtvgSAAD 149
Cdd:PLN02813 228 LVVEgylweLPQTIEAIAQACEEAHRAGALvavTASDVS-CIERHRDDFWDVmgnyADILFANSDEARALCGL---GSEE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 150 AGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFV-GALAFYLAYYPNL-SLEDMLNRs 227
Cdd:PLN02813 304 SPESATRYLSHFCPLVSVTDGARGSYIGVKGEAV--YIPPSPCVPVDTCGAGDAYAaGILYGLLRGVSDLrGMGELAAR- 380
|
250
....*....|....
gi 567316250 228 nfIAAVSVQAAGTQ 241
Cdd:PLN02813 381 --VAATVVGQQGTR 392
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
125-233 |
2.27e-07 |
|
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: 50.28 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT----LGAEGCVVLSQTEPEPKHIPTEKVKAVDT-TG 199
Cdd:cd01173 136 LADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsvelADDDRIEMLGSTATEAWLVQRPKIPFPAYfNG 215
|
90 100 110
....*....|....*....|....*....|....*
gi 567316250 200 AGDSFVGALAFYLAYYPnlSLEDMLNRS-NFIAAV 233
Cdd:cd01173 216 TGDLFAALLLARLLKGK--SLAEALEKAlNFVHEV 248
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-209 |
2.71e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 50.76 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 4 MVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIvagaNLLLNTEDLRAA-----ANVISR 78
Cdd:PRK09850 59 LLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAI----NDMNISNAITAEylaqhREFIQR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 79 AKVMVCQLEITPATSLEALTMArrSGVKTLFNPAPA-----IADLDPQFYTLSDvfccNESEAEILTGLTVGSAADAGEA 153
Cdd:PRK09850 135 AKVIVADCNISEEALAWILDNA--ANVPVFVDPVSAwkcvkVRDRLNQIHTLKP----NRLEAETLSGIALSGREDVAKV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 567316250 154 ALVLLKRGCQVVIITLGAEGcVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALA 209
Cdd:PRK09850 209 AAWFHQHGLNRLVLSMGGDG-VYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLA 263
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
132-213 |
4.66e-07 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 49.65 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT---LGAEGCV-VLsQTEPEPKHIPTEKVKAVDTTGAGDSFVGA 207
Cdd:COG0351 133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghLPGDEAVdVL-YDGDGVREFSAPRIDTGNTHGTGCTLSSA 211
|
....*.
gi 567316250 208 LAFYLA 213
Cdd:COG0351 212 IAALLA 217
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
132-234 |
8.19e-07 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 48.94 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADageaalvLLKR-GCQVVIITLGAEGCVVLSQTEPEpkHIPTEKVKAVDTTGAGDSFVGALaF 210
Cdd:cd01937 160 KLSRVEAEVISTPTELAR-------LIKEtGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPTGAGDVFLAAF-L 229
|
90 100
....*....|....*....|....
gi 567316250 211 YLAYYPNLSLEdmlnRSNFIAAVS 234
Cdd:cd01937 230 YSRLSGKDIKE----AAEFAAAAA 249
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
164-213 |
1.36e-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: 48.49 E-value: 1.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 567316250 164 VVIITLGAEGCVVLSQTEPEPKHIP---TEKVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd01943 227 GVVLRCGKLGCYVGSADSGPELWLPayhTKSTKVVDPTGGGNSFLGGFAAGLA 279
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
145-213 |
2.10e-06 |
|
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: 47.73 E-value: 2.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567316250 145 GSAADAG-EAALVLLK----RGCQVVIITLGAEGCVVLS-----QTEPEPkhiptekVKAVDTTGAGDSFVGALAFYLA 213
Cdd:cd01940 166 FSASDLSdEEVKAKLKeavsRGAKLVIVTRGEDGAIAYDgavfySVAPRP-------VEVVDTLGAGDSFIAGFLLSLL 237
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
132-235 |
2.65e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 47.38 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLS-----QTEPepkhiptEKVKAVDTTGAGDSFVG 206
Cdd:PRK09513 187 NRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNasgewIAKP-------PACDVVSTVGAGDSMVG 259
|
90 100
....*....|....*....|....*....
gi 567316250 207 ALAFYLAYypNLSLEDMLNRSNFIAAVSV 235
Cdd:PRK09513 260 GLIYGLLM--RESSEHTLRLATAVSALAV 286
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
132-223 |
3.91e-06 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 47.09 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEILTGLTVGSAADAGEAALVLLKRG-CQVVIITLGAEGCVVLS-----QTEPEPkhiptekVKAVDTTGAGDSFV 205
Cdd:PRK10294 187 NQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDsenciQVVPPP-------VKSQSTVGAGDSMV 259
|
90
....*....|....*...
gi 567316250 206 GALAFYLAyyPNLSLEDM 223
Cdd:PRK10294 260 GAMTLKLA--ENASLEEM 275
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
135-213 |
6.18e-06 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 45.94 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 135 EAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT---LGAEGCVVLSQ--TEPEPKHIPTEKVKAVDTTGAGDSFVGALA 209
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAVVTDVlyDGGGFYTLEAPRIPTKNTHGTGCTLSAAIA 208
|
....
gi 567316250 210 FYLA 213
Cdd:pfam08543 209 ANLA 212
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
125-248 |
1.27e-05 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 45.50 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT-LGAEGCVVLSQTEPEPKHIPTEKVK-AVDT----- 197
Cdd:PLN02978 149 LATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITsIDIDGKLLLVGSHRKEKGARPEQFKiVIPKipayf 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 567316250 198 TGAGDSFVGALAFYLAYYPnlsleDMLNRSNFIAAVSVQAAGTQSSYPYKK 248
Cdd:PLN02978 229 TGTGDLMAALLLGWSHKYP-----DNLDKAAELAVSSLQAVLRRTLADYKR 274
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
135-218 |
1.41e-05 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 45.12 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 135 EAEILTGLTVGSAADAG-EAALVLLKRGCQVVIIT-----LGAEGCVVL-SQTEPEpkHIPTEKVKAVDTTGAGDSFVGA 207
Cdd:PRK06427 143 EAEALTGLPIADTEDEMkAAARALHALGCKAVLIKgghllDGEESVDWLfDGEGEE--RFSAPRIPTKNTHGTGCTLSAA 220
|
90
....*....|.
gi 567316250 208 LAFYLAYYPNL 218
Cdd:PRK06427 221 IAAELAKGASL 231
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
160-239 |
1.42e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 45.57 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCVVLSQTEPepKHIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PLN02630 201 RQKCCVIVTNGKKGCRIYWKDGE--MRVPPFPAIQVDPTGAGDSFLG--GFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
113-233 |
2.45e-05 |
|
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: 44.37 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 113 PAIADLDPQFYTLSDVFCC--------------NESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT-----LGAEG 173
Cdd:COG2240 112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvpldDTPAD 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567316250 174 CV-VLSQTEPEPKHIPTEKVkAVDTTGAGDSFVGALAFYLAYypNLSLEDMLNR-SNFIAAV 233
Cdd:COG2240 192 KIgNLAVTADGAWLVETPLL-PFSPNGTGDLFAALLLAHLLR--GKSLEEALERaAAFVYEV 250
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
160-239 |
1.43e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.03 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 160 RGCQVVIITLGAEGCvvLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGalAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAG 239
Cdd:PRK09813 183 RGAGVVIVTLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIA--GFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
125-168 |
6.51e-04 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 40.06 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 567316250 125 LSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT 168
Cdd:PTZ00344 139 YADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
112-168 |
8.50e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 39.85 E-value: 8.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 567316250 112 APAIAD-LDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIIT 168
Cdd:PRK05756 124 APGVAEfLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
132-240 |
1.12e-03 |
|
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: 39.81 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 132 NESEAEiltgLTVGSAADagEAALVllKRGCQVV--------IITLGAEGCVVLSQTEPePKHIPTEKVKAVDTTGAGDS 203
Cdd:PRK11316 195 NLSEFE----AVVGKCKD--EAELV--EKGMKLIadydlsalLVTRSEQGMTLLQPGKA-PLHLPTQAREVYDVTGAGDT 265
|
90 100 110
....*....|....*....|....*....|....*..
gi 567316250 204 FVGALAFYLAyyPNLSLEDMLNRSNFIAAVSVQAAGT 240
Cdd:PRK11316 266 VISVLAAALA--AGNSLEEACALANAAAGVVVGKLGT 300
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
146-240 |
2.76e-03 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 38.16 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567316250 146 SAADAGEAALVLLKRGCqVVIITLGAEGCVVLSqTEPEPKHIPTEK-VKAVDTTGAGDSFVGALAFYLAYYPNlSLEDML 224
Cdd:cd01939 197 SPEECLRGEGPRAKKAA-LLVCTWGDQGAGALG-PDGEYVHSPAHKpIRVVDTLGAGDTFNAAVIYALNKGPD-DLSEAL 273
|
90
....*....|....*.
gi 567316250 225 NRSNFIAAVSVQAAGT 240
Cdd:cd01939 274 DFGNRVASQKCTGVGF 289
|
|
|