|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
4-290 |
3.32e-100 |
|
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: 295.76 E-value: 3.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 4 LICGSIAYDSImtfegrFREHILPDqvhlINLSFLVPTMRREFGGCAGNIGYALHLLGGDARIMGTMGALDA-QPYLDRL 82
Cdd:cd01942 3 AVVGHLNYDII------LKVESFPG----PFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHgRLYLEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 83 DQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAAFHPGAMMQSHLNHAGDaPDIKLAIVGPDGFDGMVQHVEELAKAGVP 162
Cdd:cd01942 73 REEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEAD-PDGLADIVHLSSGPGLIELARELAAGGIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 163 FVFDPGQGLPLFDGATLRRSIELATYVAVNDYEAKLVSDKTGWSEDEIASRVDALVITRGEHGATIRHKQGAEQIPVVPA 242
Cdd:cd01942 152 VSFDPGQELPRLSGEELEEILERADILFVNDYEAELLKERTGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 757910752 243 ERIADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGPQ 290
Cdd:cd01942 232 VKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-299 |
2.56e-60 |
|
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: 194.33 E-value: 2.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 4 LICGSIAYDSIMTFEGrfrehiLPDQVHLInlsfLVPTMRREFGGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRL 82
Cdd:COG0524 3 LVIGEALVDLVARVDR------LPKGGETV----LAGSFRRSPGGAAANVAVALARLGARVALVGAVGDdPFGDFLLAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 83 DQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAAFHPGAMmqSHLNhAGDAPDIKLA-----------IVGPDGFDGMVQ 151
Cdd:COG0524 73 RAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGAN--AELT-PEDLDEALLAgadilhlggitLASEPPREALLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 152 HVEELAKAGVPFVFDPGQGLPLFDGA--TLRRSIELATYVAVNDYEAKLVSDKTGWSE--DEIASR-VDALVITRGEHGA 226
Cdd:COG0524 150 ALEAARAAGVPVSLDPNYRPALWEPAreLLRELLALVDILFPNEEEAELLTGETDPEEaaAALLARgVKLVVVTLGAEGA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757910752 227 TIRHKQGAEQIPVVPAErIADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGPQTYVLTRAEI 299
Cdd:COG0524 230 LLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
38-291 |
1.05e-33 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 125.15 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 38 LVPTMRREFGGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAA 116
Cdd:pfam00294 25 RVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDGERTIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 117 FHPGAMM---QSHLNHAGDAPD----IKLAIVGPDGFDG-MVQHVEELAKAGVpfVFDPGQGLPLFDGA-TLRRSIELAT 187
Cdd:pfam00294 105 FNRGAAAdltPEELEENEDLLEnadlLYISGSLPLGLPEaTLEELIEAAKNGG--TFDPNLLDPLGAAReALLELLPLAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 188 YVAVNDYEAKLVSDKTGWSEDE--------IASRVDALVITRGEHGATIRHKQGAEQIPVVPAERIADPTGCGDAFRGGL 259
Cdd:pfam00294 183 LLKPNEEELEALTGAKLDDIEEalaalhklLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGF 262
|
250 260 270
....*....|....*....|....*....|..
gi 757910752 260 LYGIEHGLDWATTGRLASLMGSLKIAHQGPQT 291
Cdd:pfam00294 263 LAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
39-289 |
2.13e-21 |
|
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: 91.87 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 39 VPTMRREFGGCAGNIGYALHLLGGDARIMGTMGAlDA--QPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTD-------- 108
Cdd:cd01166 23 ADSFRKFFGGAEANVAVGLARLGHRVALVTAVGD-DPfgRFILAELRREGVDTSHVRVDPGRPTGLYFLEIGaggerrvl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 109 LDNNQIAAfhpGAMMQSHLNHAGDAPD-------IKLAIvGPDGFDGMVQHVEELAKAGVPFVFDPG--QGLPLFDGA-- 177
Cdd:cd01166 102 YYRAGSAA---SRLTPEDLDEAALAGAdhlhlsgITLAL-SESAREALLEALEAAKARGVTVSFDLNyrPKLWSAEEAre 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 178 TLRRSIELATYVAVNDYEAKLVSDKTGWSEDEIASR-----VDALVITRGEHGATIRHKQGAEQIPVVPAErIADPTGCG 252
Cdd:cd01166 178 ALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalalgVKAVVVKLGAEGALVYTGGGRVFVPAYPVE-VVDTTGAG 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 757910752 253 DAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGP 289
Cdd:cd01166 257 DAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
47-289 |
1.02e-19 |
|
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: 87.28 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 47 GGCAGNIGYALHLLGGDARIMGTMGALD-AQPYLDRLDQLGLRRdHVRVLPDTYTAQAMITTDLDNNQIAAFHPGAmmQS 125
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKlGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAERTMCTYLGA--AN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 126 HLNHAgdapDIKLAIVG------------PDGFDGMVQHVEELAKAGVPFVF---DPGqgLPLFDGATLRRSIELATYVA 190
Cdd:cd01168 132 ELSPD----DLDWSLLAkakylylegyllTVPPEAILLAAEHAKENGVKIALnlsAPF--IVQRFKEALLELLPYVDILF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 191 VNDYEAKLVSDKTGWSEDEIA-----SRVDALVITRGEHGATIRHKQGAEQIPVVPAERIADPTGCGDAFRGGLLYGIEH 265
Cdd:cd01168 206 GNEEEAEALAEAETTDDLEAAlkllaLRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQ 285
|
250 260
....*....|....*....|....
gi 757910752 266 GLDWATTGRLASLMGSLKIAHQGP 289
Cdd:cd01168 286 GEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
47-288 |
2.82e-19 |
|
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: 86.15 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 47 GGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAAFHPGAMMQS 125
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDdEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 126 HLNHAGDAPDIK---------LAIVGPDGFDGMVQHVEELAKAGVPFVFDPGQGLPLFDGATLRRS-----IELATYVAV 191
Cdd:cd01167 108 LLDTELNPDLLSeadilhfgsIALASEPSRSALLELLEAAKKAGVLISFDPNLRPPLWRDEEEAREriaelLELADIVKL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 192 NDYEAKLVSDKTGWSE---DEIASRVDALVITRGEHGATIRHKQGAEQIPVVPAErIADPTGCGDAFRGGLLYGI-EHGL 267
Cdd:cd01167 188 SDEELELLFGEEDPEEiaaLLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVE-VVDTTGAGDAFVAGLLAQLlSRGL 266
|
250 260
....*....|....*....|....*..
gi 757910752 268 D------WATTGRLASLMGSLKIAHQG 288
Cdd:cd01167 267 LaldedeLAEALRFANAVGALTCTKAG 293
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
23-304 |
2.09e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 80.95 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 23 EHILPDQVHLINlsflvpTMRREFGGCAGNIGYALHLLGGDARIMGTMGALDAQPYLDRLDQLGLRRDHVRVLPDTYTAQ 102
Cdd:COG1105 17 DELEPGEVNRAS------EVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFVPIEGETRINI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 103 AmITTDLDNNQIAAFHPG--------AMMQSHLNHAGDAPDIkLAI-------VGPDGFDGMVqhvEELAKAGVPFVFDp 167
Cdd:COG1105 91 K-IVDPSDGTETEINEPGpeiseeelEALLERLEELLKEGDW-VVLsgslppgVPPDFYAELI---RLARARGAKVVLD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 168 gqglplFDGATLRRSIE-LATYVAVNDYEAKLVSDKTGWSEDEI--------ASRVDALVITRGEHGATIRHKQGAEQIP 238
Cdd:COG1105 165 ------TSGEALKAALEaGPDLIKPNLEELEELLGRPLETLEDIiaaarellERGAENVVVSLGADGALLVTEDGVYRAK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757910752 239 VvPAERIADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGpqTYVLTRAEIDARFE 304
Cdd:COG1105 239 P-PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLA 301
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
60-282 |
5.74e-15 |
|
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: 73.74 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 60 LGGDARIMGTMGALD-AQPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLD-NNQIAaFHPGAmmqshlNHAGDAPDIK 137
Cdd:cd01174 49 LGARVAMIGAVGDDAfGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESgENRIV-VVPGA------NGELTPADVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 138 LA---IVGPDGFdgMVQH------VEELAK----AGVPFVFDPGQGLPLFDGAtlrrsIELATYVAVNDYEAKLVSDKTG 204
Cdd:cd01174 122 AAlelIAAADVL--LLQLeipletVLAALRaarrAGVTVILNPAPARPLPAEL-----LALVDILVPNETEAALLTGIEV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 205 WSEDEIASRVDAL--------VITRGEHGATIRHKQGAEQIPVVPAErIADPTGCGDAFRGGLLYGIEHGLDWATTGRLA 276
Cdd:cd01174 195 TDEEDAEKAARLLlakgvknvIVTLGAKGALLASGGEVEHVPAFKVK-AVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
....*.
gi 757910752 277 SLMGSL 282
Cdd:cd01174 274 NAAAAL 279
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
144-263 |
7.27e-14 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 69.05 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 144 DGFDGMVQHVEELAKAGVPFVFDPGQGLPLFDGATLRRSIELATYVAVNDYEAKLVSDKTGWSEDEIAS--------RVD 215
Cdd:cd00287 68 PAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEaaalllskGPK 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 757910752 216 ALVITRGEHGATIRHKQGAEQ-IPVVPAErIADPTGCGDAFRGGLLYGI 263
Cdd:cd00287 148 VVIVTLGEKGAIVATRGGTEVhVPAFPVK-VVDTTGAGDAFLAALAAGL 195
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
46-291 |
2.55e-12 |
|
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: 66.16 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 46 FGGCAGNIGYALHLLGGDARIMGTMG-ALDAQPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAAFHPGammq 124
Cdd:cd01945 35 GGGNAANAAVAVARLGGQARLIGVVGdDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAI---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 125 shlNHAGDAPDIKLAIVGpdGFD---------GMVQHVEELAKA-GVPFVFDpgqglplFDGATLRRSIELATYVAVNDY 194
Cdd:cd01945 111 ---DTQAAPDSLPDAILG--GADavlvdgrqpEAALHLAQEARArGIPIPLD-------LDGGGLRVLEELLPLADHAIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 195 EAKLVSDKTGWSEDE----IASRVDALV-ITRGEHGATIRHKQGAEQIPVVPAERIADPTGCGDAFRGGLLYGIEHGLDW 269
Cdd:cd01945 179 SENFLRPNTGSADDEalelLASLGIPFVaVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPL 258
|
250 260
....*....|....*....|..
gi 757910752 270 ATTGRLASLMGSLKIAHQGPQT 291
Cdd:cd01945 259 REALRFASAAAALKCRGLGGRA 280
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
41-286 |
4.45e-11 |
|
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: 62.33 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 41 TMRREFGGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRLDQLGLRrDHVRVLPDTYTAQAMITTDLDNNQIAAFHP 119
Cdd:cd01941 29 HVKQSPGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESEKAGLN-VRGIVFEGRSTASYTAILDKDGDLVVALAD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 120 GAMMQSH----LNHAGDAPDIKLAIVgpdgFDG-----MVQHVEELA-KAGVPFVFDPgqglplFDGATLRRSIELATYV 189
Cdd:cd01941 108 MDIYELLtpdfLRKIREALKEAKPIV----VDAnlpeeALEYLLALAaKHGVPVAFEP------TSAPKLKKLFYLLHAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 190 AV---NDYEAK-----LVSDKTGWSEDEIA---SRVDALVITRGEHGATIRHKQGAEQIPVVPA---ERIADPTGCGDAF 255
Cdd:cd01941 178 DLltpNRAELEalagaLIENNEDENKAAKIlllPGIKNVIVTLGAKGVLLSSREGGVETKLFPApqpETVVNVTGAGDAF 257
|
250 260 270
....*....|....*....|....*....|.
gi 757910752 256 RGGLLYGIEHGLDWATTGRLASLMGSLKIAH 286
Cdd:cd01941 258 VAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
159-288 |
1.28e-10 |
|
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: 60.90 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 159 AGVPFVFDPGQGLPLFDGATLRRSIELATYVAVNDYEAKLVSDKTGWSEDEIASRVDA-----LVITRGEHGATIRHKQG 233
Cdd:cd01944 155 AGTTLVFDPGPRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAktaapVVVRLGSNGAWIRLPDG 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 757910752 234 AEQIpvVPAE--RIADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQG 288
Cdd:cd01944 235 NTHI--IPGFkvKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
39-299 |
5.88e-10 |
|
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: 59.11 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 39 VPTMRREF--GGcAGNIgyALHL--LGGDARIMGTMGA-LDAQPYLDRLDQLGLRRDHV-----------RVLPDTytaQ 102
Cdd:cd01172 30 VKVEREEIrlGG-AANV--ANNLasLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGIvdegrptttktRVIARN---Q 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 103 AMITTDLDNNQIAAFHPGAMMQSHLNHAGDAPDiklAIVGPD---GF--DGMVQHVEELAKA-GVPFVFDP-GQGLPLFD 175
Cdd:cd01172 104 QLLRVDREDDSPLSAEEEQRLIERIAERLPEAD---VVILSDygkGVltPRVIEALIAAARElGIPVLVDPkGRDYSKYR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 176 GATLrrsielatyVAVNDYEAKLVSDKTGWSEDEIA---------SRVDALVITRGEHGATIRHKQGAEQ-IPVVPAErI 245
Cdd:cd01172 181 GATL---------LTPNEKEAREALGDEINDDDELEaagekllelLNLEALLVTLGEEGMTLFERDGEVQhIPALAKE-V 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757910752 246 ADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGpqTYVLTRAEI 299
Cdd:cd01172 251 YDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG--TAPVTPKEL 302
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
178-288 |
1.04e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 58.66 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 178 TLRRSIELATYVAVN--------DYEAKLVS----DKTGWSE--DEI----ASRVDAL-------------VITRGEHGA 226
Cdd:PLN02630 136 TLERMVEICDVVVVDiqalirvfDPVDGTVKlvklEETGFYDmlPRIgflkASSEEALfidveevrqkccvIVTNGKKGC 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757910752 227 TIRHKQGAEQIPVVPAERIaDPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQG 288
Cdd:PLN02630 216 RIYWKDGEMRVPPFPAIQV-DPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
41-289 |
2.30e-09 |
|
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: 57.04 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 41 TMRREFGGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRLDQLGLRrdHVRVLPDTYTAQAMITTDlDNNQIAAFHP 119
Cdd:cd01947 30 DSRESPGGGGANVAVQLAKLGNDVRFFSNLGRdEIGIQSLEELESGGDK--HTVAWRDKPTRKTLSFID-PNGERTITVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 120 GAmmqshlnhaGDAPDIKLAIvgPDGFDGM----------VQHVEELAKAGVpfvFDPGQGLPLfdgATLRRSIELATYV 189
Cdd:cd01947 107 GE---------RLEDDLKWPI--LDEGDGVfitaaavdkeAIRKCRETKLVI---LQVTPRVRV---DELNQALIPLDIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 190 AVNDYEAKLVSDktgwSEDEIASRVDALVITRGEHGATIRHKQGAEQIPVVPAeRIADPTGCGDAFRGGLLYGIEHGLDW 269
Cdd:cd01947 170 IGSRLDPGELVV----AEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKA-KVPDSTGAGDSFAAGFIYGLLKGWSI 244
|
250 260
....*....|....*....|
gi 757910752 270 ATTGRLASLMGSLKIAHQGP 289
Cdd:cd01947 245 EEALELGAQCGAICVSHFGP 264
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
179-260 |
3.83e-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: 56.70 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 179 LRRSIELATYVAVNDYEAKLVsdkTGWSEDEIASR------VDALVITRGEHGATIRHKQGAEQIPVVPAERIADPTGCG 252
Cdd:cd01946 157 LKKVLAKVDVVIINDGEARQL---TGAANLVKAARlilamgPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAG 233
|
....*...
gi 757910752 253 DAFRGGLL 260
Cdd:cd01946 234 DTFAGGFI 241
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
46-301 |
1.64e-08 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 46 FGGCAGNIGYALHLLGGDARIMGTMGA-LDAQPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLD--NNQIAaFHPGAm 122
Cdd:PTZ00292 51 FGGKGANQAVMASKLGAKVAMVGMVGTdGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKtgNNEIV-IIPGA- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 123 mQSHLNHA---GDAPDI--KLAIVgpdgfdgMVQ---------HVEELAK-AGVPFVFDPGQGLPLFDGATLRRSIELAT 187
Cdd:PTZ00292 129 -NNALTPQmvdAQTDNIqnICKYL-------ICQneiplettlDALKEAKeRGCYTVFNPAPAPKLAEVEIIKPFLKYVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 188 YVAVNDYEAKLVSDKTgWSEDEIASR---------VDALVITRGEHGATIRHKqgaEQIPV-VPAERI--ADPTGCGDAF 255
Cdd:PTZ00292 201 LFCVNEVEAALITGME-VTDTESAFKaskelqqlgVENVIITLGANGCLIVEK---ENEPVhVPGKRVkaVDTTGAGDCF 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 757910752 256 RGGLLYGIEHGLDWATTGRLASLMGSLKIAHQGPQTYVLTRAEIDA 301
Cdd:PTZ00292 277 VGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPA 322
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
178-276 |
3.11e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 54.17 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 178 TLRRSIELATYVAVNDYEAKLVSDKTGWSED--EIASR--VDALVITRGEHGATIRHkqgAEQIPVVPAERIA--DPTGC 251
Cdd:PRK09434 173 CLRQALALADVVKLSEEELCFLSGTSQLEDAiyALADRypIALLLVTLGAEGVLVHT---RGQVQHFPAPSVDpvDTTGA 249
|
90 100
....*....|....*....|....*
gi 757910752 252 GDAFRGGLLYGIEHGLDWATTGRLA 276
Cdd:PRK09434 250 GDAFVAGLLAGLSQAGLWTDEAELA 274
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
47-284 |
2.42e-07 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 50.86 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 47 GGCAGNIGYALHLLGGDARIMGTMGAldaqPYLDRLDQLGLRRDHVRVLPDTYTAQAMITTDLDNNQIAAFHPGAmmqsh 126
Cdd:cd01937 24 GGPATYASLTLSRLGLTVKLVTKVGR----DYPDKWSDLFDNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCA----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 127 lnhagdaPDIKLA-----------IVGPdgfdgmVQH--VEELAKAGVPFVFDPgQGL---PLFDGATLRRSIELATYVA 190
Cdd:cd01937 95 -------AIPDTEsplstitaeivILGP------VPEeiSPSLFRKFAFISLDA-QGFlrrANQEKLIKCVILKLHDVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 191 VNDYEAKLVSDKTgwsedEIASR-----VDALVITRGEHGATIRHKQGAEQIPVVPAErIADPTGCGDAFRGGLLYGIEH 265
Cdd:cd01937 161 LSRVEAEVISTPT-----ELARLiketgVKEIIVTDGEEGGYIFDGNGKYTIPASKKD-VVDPTGAGDVFLAAFLYSRLS 234
|
250
....*....|....*....
gi 757910752 266 GLDWATTGRLASLMGSLKI 284
Cdd:cd01937 235 GKDIKEAAEFAAAAAAKFI 253
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
48-253 |
1.68e-06 |
|
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: 49.06 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 48 GCAGNIGYALHLLGGDARIMGTMGALDAQPYL-DRLDQLGLRRDHVRVlPD--TYTA-------QAMITTDLDNNqIAAF 117
Cdd:PRK11316 51 GGAANVAMNIASLGAQARLVGLTGIDEAARALsKLLAAVGVKCDFVSV-PThpTITKlrvlsrnQQLIRLDFEEG-FEGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 118 HPGAM---MQSHLNHAGdapdiklAIVGPDGFDGMVQHVEEL----AKAGVPFVFDP-GQGLPLFDGATLrrsielatyV 189
Cdd:PRK11316 129 DPQPLlerIEQALPSIG-------ALVLSDYAKGALASVQAMiqlaRKAGVPVLIDPkGTDFERYRGATL---------L 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757910752 190 AVNDYEAKLVSDKTGwSEDEIASR---------VDALVITRGEHGAT-IRHKQGAEQIPVVpAERIADPTGCGD 253
Cdd:PRK11316 193 TPNLSEFEAVVGKCK-DEAELVEKgmkliadydLSALLVTRSEQGMTlLQPGKAPLHLPTQ-AREVYDVTGAGD 264
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
47-268 |
7.96e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 46.27 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 47 GGCAGNIGYALHLLGGDARIMGTMGALDAQPYL-DRLDQLGLRRDHVRVLPDTyTAQAMITTDlDNNQI-AAFHPGAMMQ 124
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLkQDLARMGVDISHVHTKHGV-TAQTQVELH-DNDRVfGDYTEGVMAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 125 SHLnhagDAPDIKLAIvgpdGFD----GMVQHVEE----LAKAGVPFVFDPGQGL--PLFDgatlrrsielaTYVAVNDY 194
Cdd:PRK09813 101 FAL----SEEDYAWLA----QYDivhaAIWGHAEDafpqLHAAGKLTAFDFSDKWdsPLWQ-----------TLVPHLDY 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757910752 195 EAKLVSDKTGWSEDEIASRVD----ALVITRGEHGATIRHKQGAEQIPVVPAErIADPTGCGDAFRGGLLYGIEHGLD 268
Cdd:PRK09813 162 AFASAPQEDEFLRLKMKAIVArgagVVIVTLGENGSIAWDGAQFWRQAPEPVT-VVDTMGAGDSFIAGFLCGWLAGMT 238
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
184-288 |
2.14e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.40 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 184 ELATYVAV---NDYEAKLVSDKTGWSED---EIASRVDAL-----------VITRGEHGATIRHKQGAEQIPVVP--AER 244
Cdd:PTZ00247 210 QVLPYVDIlfgNEEEAKTFAKAMKWDTEdlkEIAARIAMLpkysgtrprlvVFTQGPEPTLIATKDGVTSVPVPPldQEK 289
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 757910752 245 IADPTGCGDAFRGGLLYGIEHGLDWATTGRLASLMGSLKIAHQG 288
Cdd:PTZ00247 290 IVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNG 333
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
47-263 |
3.43e-05 |
|
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: 44.65 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 47 GGCAGNIGYALHLLGGDARIMGTMGALD-AQPYLDRLDQLGLRRDHVRVLPdTYTAQAMITTDlDNNQIAAFHPGAMMQS 125
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDaGAHVRSTLKRLGVDISHCRVKE-GENAVADVELV-DGDRIFGLSNKGGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 126 HLNHAGDAPDIK---LAIVGPDGFDGMV-QHVEELAKAGVPFVFDPGQGlplFDGATLRRSIELATYVAVN--DYEAKLV 199
Cdd:cd01940 100 EHPFEADLEYLSqfdLVHTGIYSHEGHLeKALQALVGAGALISFDFSDR---WDDDYLQLVCPYVDFAFFSasDLSDEEV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757910752 200 SDKTgwseDEIASR-VDALVITRGEHGATIRHkqGAE--QIPVVPAErIADPTGCGDAFRGGLLYGI 263
Cdd:cd01940 177 KAKL----KEAVSRgAKLVIVTRGEDGAIAYD--GAVfySVAPRPVE-VVDTLGAGDSFIAGFLLSL 236
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
218-290 |
8.19e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 44.03 E-value: 8.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757910752 218 VITRGEHGATIRHKQGAEQIPVVPAERIaDPTGCGDAFRGGLLYGIEHGL-DWATTGRLASLMGSLKIAHQGPQ 290
Cdd:PLN02813 320 SVTDGARGSYIGVKGEAVYIPPSPCVPV-DTCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQGTR 392
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
218-267 |
3.79e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 41.70 E-value: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 757910752 218 VITRGEHGATIRHKQGAEQIPVVPAERIADPTGCGDAFRGGLLYGIEHGL 267
Cdd:PLN02379 270 VVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGL 319
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
149-288 |
1.16e-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: 40.08 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757910752 149 MVQHVEEL------AKAGVPF-VFDPG-QGLPLFDgatlrrsieLATYVAVndyeAKLVSDKTGW--------SEDEIAS 212
Cdd:cd01939 144 MMQHIEEHnnrrpeIRITISVeVEKPReELLELAA---------YCDVVFV----SKDWAQSRGYkspeeclrGEGPRAK 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757910752 213 RVDALVITRGEHGATIRHKQG-AEQIPVVPAERIADPTGCGDAFRGGLLYG-IEHGLDWATTGRLASLMGSLKIAHQG 288
Cdd:cd01939 211 KAALLVCTWGDQGAGALGPDGeYVHSPAHKPIRVVDTLGAGDTFNAAVIYAlNKGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| |
