|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
1-333 |
0e+00 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 542.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 1 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 80
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 81 IDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLERNWMLVEKARVCYIAGFF 160
Cdd:PLN02548 80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAGFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 161 LTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQAL 240
Cdd:PLN02548 159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 241 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQREIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 320
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318
|
330
....*....|...
gi 1353386 321 RRTGCTFPEKPDF 333
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
1-333 |
1.96e-166 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 467.20 E-value: 1.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 1 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIG 80
Cdd:PTZ00247 11 FGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVGCVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 81 IDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLERNWMLVEKARVCYIAGFF 160
Cdd:PTZ00247 91 DDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTAQLYYLEGFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 161 LTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQAL 240
Cdd:PTZ00247 170 LTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARIAML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 241 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQREIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 320
Cdd:PTZ00247 250 PKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVII 329
|
330
....*....|...
gi 1353386 321 RRTGCTFPEKPDF 333
Cdd:PTZ00247 330 QHNGCTYPEKPPF 342
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-328 |
9.89e-138 |
|
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: 393.13 E-value: 9.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 1 MGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAATFFGCIG 80
Cdd:cd01168 7 LGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAAFIGRVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 81 IDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlerNWMLVEKARVCYIAGF 159
Cdd:cd01168 80 DDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKYLYLEGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 160 FLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREqgfETKDIKEIAKKTQA 239
Cdd:cd01168 155 LLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 240 LpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqrEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASII 319
Cdd:cd01168 232 L------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEV 303
|
....*....
gi 1353386 320 IRRTGCTFP 328
Cdd:cd01168 304 IQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
16-327 |
6.73e-74 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 229.92 E-value: 6.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 16 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 95
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 96 HVDAHYYEQDEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKHLDlerNWMLVEKARVCYIAGFFLTVSPESVLKVAH 173
Cdd:pfam00294 74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEELEE---NEDLLENADLLYISGSLPLGLPEATLEELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 174 HASENNRIFTLNLSAPFISqfYKESLMKVMPYVDILFGNETEAATFAREQgfetkdIKEIAKKTQALPKMNSKRQRIVIF 253
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------LDDIEEALAALHKLLAKGIKTVIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353386 254 TQGRDDTIMATESEVtaFAVLDQDQREIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTF 327
Cdd:pfam00294 223 TLGADGALVVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
73-326 |
2.78e-39 |
|
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: 140.40 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 73 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLErnwmLVEK 150
Cdd:COG0524 53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGaPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 151 ARVCYIAGFFLT--VSPESVLKVAHHASENNR--IFTLNLSAPFISQfYKESLMKVMPYVDILFGNETEAATFareqgFE 226
Cdd:COG0524 128 ADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEP-ARELLRELLALVDILFPNEEEAELL-----TG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 227 TKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDK 303
Cdd:COG0524 202 ETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGL 269
|
250 260
....*....|....*....|...
gi 1353386 304 PLTECIRAGHYAASIIIRRTGCT 326
Cdd:COG0524 270 DLEEALRFANAAAALVVTRPGAQ 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
74-324 |
9.98e-32 |
|
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: 120.35 E-value: 9.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 74 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-DEQPTGTcaACIT----GDNRslIANLAAANcykkeKHL---DLERNW 145
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENR--IVVVPGAN-----GELtpaDVDAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 146 MLVEKARVCYIAgffLTVSPESVLKVAHHASENNRIFTLNlSAPFISQFYKeslmkVMPYVDILFGNETEAATFAREQGF 225
Cdd:cd01174 125 ELIAAADVLLLQ---LEIPLETVLAALRAARRAGVTVILN-PAPARPLPAE-----LLALVDILVPNETEAALLTGIEVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 226 ETKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATESEVT---AFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSD 302
Cdd:cd01174 196 DEEDAEKAARLLLAKGV------KNVIVTLGAKGALLASGGEVEhvpAFKV------KAVDTTGAGDTFIGALAAALARG 263
|
250 260
....*....|....*....|..
gi 1353386 303 KPLTECIRAGHYAASIIIRRTG 324
Cdd:cd01174 264 LSLEEAIRFANAAAALSVTRPG 285
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
151-300 |
1.29e-28 |
|
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: 109.49 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 151 ARVCYIAGffLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKEsLMKVMPYVDILFGNETEAATFAREQGFETKDI 230
Cdd:cd00287 58 ADAVVISG--LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-LEKLLPGVDILTPNEEEAEALTGRRDLEVKEA 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 231 keiakkTQALPKMNSKRQRIVIFTQGRDDTIMATEsEVTAFAVLDQDqREIIDTNGAGDAFVGGFLSQLV 300
Cdd:cd00287 135 ------AEAAALLLSKGPKVVIVTLGEKGAIVATR-GGTEVHVPAFP-VKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
50-326 |
2.80e-27 |
|
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: 108.43 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 50 HAGGSTQNsikVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQ-PTGTcAACITGDNRS---LIA 125
Cdd:cd01166 29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGGErrvLYY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 126 NLAAANCYKKEKHLDLErnwmLVEKARVCYIAGFFLTVSP---ESVLKVAHHASENN--RIFTLNLSAPFIS-QFYKESL 199
Cdd:cd01166 104 RAGSAASRLTPEDLDEA----ALAGADHLHLSGITLALSEsarEALLEALEAAKARGvtVSFDLNYRPKLWSaEEAREAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 200 MKVMPYVDILFGNETEAATFAREQGfeTKDIKEIAKKTQALPKmnskrqrIVIFTQGRDDTIMATESEVTAFAVLdqdQR 279
Cdd:cd01166 180 EELLPYVDIVLPSEEEAEALLGDED--PTDAAERALALALGVK-------AVVVKLGAEGALVYTGGGRVFVPAY---PV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1353386 280 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 326
Cdd:cd01166 248 EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
73-325 |
2.03e-21 |
|
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: 91.99 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 73 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQDEQPTGTcaACIT--GDNRSLIANLAAANCYKKE------------K 137
Cdd:cd01942 53 PGLVAAVGEDFHGRLYLEELREEGVDtSHVRVVDEDSTGV--AFILtdGDDNQIAYFYPGAMDELEPndeadpdgladiV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 138 HLDLERNwmLVEKARVCYIAGFFLTVSPesvlkvahhasennriftlnlsAPFISQFYKESLMKVMPYVDILFGNETEAA 217
Cdd:cd01942 131 HLSSGPG--LIELARELAAGGITVSFDP----------------------GQELPRLSGEELEEILERADILFVNDYEAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 218 TFAREQGFETKDIkeiakktqalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQdqREIIDTNGAGDAFVGGFLS 297
Cdd:cd01942 187 LLKERTGLSEAEL--------------ASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPA--VKVVDTTGAGDAFRAGFLY 250
|
250 260
....*....|....*....|....*...
gi 1353386 298 QLVSDKPLTECIRAGHYAASIIIRRTGC 325
Cdd:cd01942 251 GLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
73-324 |
2.74e-21 |
|
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: 91.93 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 73 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQ-PTGTCAACITGD-NRS-LIANLAAANCykkekHLDLERNWMLVE 149
Cdd:cd01167 45 AAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAaPTTLAFVTLDADgERSfEFYRGPAADL-----LLDTELNPDLLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 150 KARVCYIAGFFLTVSP--ESVLKVAHHASENNRI--FTLNLSAPFISQFY--KESLMKVMPYVDILFGNETEAATFareq 223
Cdd:cd01167 120 EADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWRDEEeaRERIAELLELADIVKLSDEELELL---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 224 gFETKDIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMAT---ESEVTAFAVldqdqrEIIDTNGAGDAFVGGFLSQLV 300
Cdd:cd01167 196 -FGEEDPEEIAALLLLFG------LKLVLVTRGADGALLYTkggVGEVPGIPV------EVVDTTGAGDAFVAGLLAQLL 262
|
250 260 270
....*....|....*....|....*....|.
gi 1353386 301 SDK-------PLTECIRAGHYAASIIIRRTG 324
Cdd:cd01167 263 SRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
52-326 |
6.51e-14 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 71.09 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 52 GGSTQNsikVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDA-HYYEQDEQPTGtcaACITG----DNRSLIan 126
Cdd:TIGR04382 34 GGSPAN---IAVGAARLGLKTA-FITRVGDDQFGRFVRDYLRREGVDTsHVVTDPGRRTS---LVFLEikppDEFPLL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 127 laaancYKKEKHLDL-----ERNWMLVEKARVCYIAGFFLTVSP--ESVLKVAHHASENNRIFTLNLSapFISQFYKES- 198
Cdd:TIGR04382 105 ------FYRENAADLaltpdDVDEDYIASARALLVSGTALSQEPsrEAVLKALEYARAAGVRVVLDID--YRPYLWKSPe 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 199 -----LMKVMPYVDILFGNETEAATFAREqgfetKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATES----EVT 269
Cdd:TIGR04382 177 eagiyLRLVLPLVDVIIGTREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDgegvEVP 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353386 270 AFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 326
Cdd:TIGR04382 246 GFPV------EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
168-324 |
2.38e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 168 VLKVAHHASennrIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAreqGFETKDIKEIAKKTQALPKMNSkr 247
Cdd:PTZ00292 165 ALKEAKERG----CYTVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALIT---GMEVTDTESAFKASKELQQLGV-- 235
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353386 248 qRIVIFTQG-RDDTIMATESEVTAfavLDQDQREIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 324
Cdd:PTZ00292 236 -ENVIITLGaNGCLIVEKENEPVH---VPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
73-318 |
5.00e-12 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 65.41 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 73 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGDNRSLIAnLAAANCYK-------KEKHLDLER-- 143
Cdd:cd01941 52 VALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGDLVVA-LADMDIYElltpdflRKIREALKEak 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 144 ------NWMLVEKARV---CYIAGFFLTVSPESVLKVAHhasennrIFTLNlsapfisqfykeslmkvmPYVDILFGNET 214
Cdd:cd01941 131 pivvdaNLPEEALEYLlalAAKHGVPVAFEPTSAPKLKK-------LFYLL------------------HAIDLLTPNRA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 215 EAATFAREQGFETKDIKeIAKKTQALPKMNskrqrIVIFTQGRDDTI---MATESEVTAFAVLDQDqrEIIDTNGAGDAF 291
Cdd:cd01941 186 ELEALAGALIENNEDEN-KAAKILLLPGIK-----NVIVTLGAKGVLlssREGGVETKLFPAPQPE--TVVNVTGAGDAF 257
|
250 260
....*....|....*....|....*..
gi 1353386 292 VGGFLSQLVSDKPLTECIRAGHYAASI 318
Cdd:cd01941 258 VAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
74-324 |
9.40e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 64.89 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 74 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDE-QPTGTcaACI----TGDNRSLIAnlAAANCYKKEKHLdlERNWMLV 148
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKgESTGV--ALIfvndEGENSIGIH--AGANAALTPALV--EAHRELI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 149 EKARVCYIAgffLTVSPESVLKVAHHASENNRIFTLNlSAPfiSQFYKESLMKVmpyVDILFGNETEAATFAreqGFETK 228
Cdd:PRK11142 131 ANADALLMQ---LETPLETVLAAAKIAKQHGTKVILN-PAP--ARELPDELLAL---VDIITPNETEAEKLT---GIRVE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 229 DIKEIAKKTQALpkmNSKRQRIVIFTQGRDDTIMATESE---VTAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKPL 305
Cdd:PRK11142 199 DDDDAAKAAQVL---HQKGIETVLITLGSRGVWLSENGEgqrVPGFRV------QAVDTIAAGDTFNGALVTALLEGKPL 269
|
250
....*....|....*....
gi 1353386 306 TECIRAGHYAASIIIRRTG 324
Cdd:PRK11142 270 PEAIRFAHAAAAIAVTRKG 288
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
75-324 |
1.85e-11 |
|
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: 63.60 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 75 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGD-NRSLIANLAAancykkEKHLDLErnWML---VEK 150
Cdd:cd01944 54 NAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDgERSFISISGA------EQDWSTE--WFAtltVAP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 151 ARVCYIAGFFLTVSPESV--LKVAHHASENNRIFTLNLSaPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETK 228
Cdd:cd01944 126 YDYVYLSGYTLASENASKviLLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 229 D-IKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMAtesevtAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKPLTE 307
Cdd:cd01944 205 AsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIP------GFKV------KAVDTIGAGDTHAGGMLAGLAKGMSLAD 272
|
250
....*....|....*..
gi 1353386 308 CIRAGHYAASIIIRRTG 324
Cdd:cd01944 273 AVLLANAAAAIVVTRSG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
57-319 |
5.27e-11 |
|
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: 61.99 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 57 NSIKVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQPTG-TCAACITGDNRSLIANLAAAncyKK 135
Cdd:cd01940 24 NALNVAVYAKRLGHESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAvADVELVDGDRIFGLSNKGGV---AR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 136 EKHLDLERNWmlVEKARVCYIAGFFLTVSPESVLKVAHHASennriftLNLSAPFISQFYKESLMKVMPYVDILFgnete 215
Cdd:cd01940 100 EHPFEADLEY--LSQFDLVHTGIYSHEGHLEKALQALVGAG-------ALISFDFSDRWDDDYLQLVCPYVDFAF----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 216 aatFAREqGFETKDIKEIAKKTQalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQREIIDTNGAGDAFVGGF 295
Cdd:cd01940 166 ---FSAS-DLSDEEVKAKLKEAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEVVDTLGAGDSFIAGF 232
|
250 260
....*....|....*....|....*.
gi 1353386 296 L-SQLVSDKPLTECIRAG-HYAASII 319
Cdd:cd01940 233 LlSLLAGGTAIAEAMRQGaQFAAKTC 258
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
1-324 |
3.38e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.43 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 1 MGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELV-KKFKVEyhAGGSTQNSI----KVAQWMIQQPHKAAT 74
Cdd:PLN02813 75 LGQAMVDFSGMVDDEFLERLGLeKGTRKVINHEERGKVLRALDgCSYKAS--AGGSLSNTLvalaRLGSQSAAGPALNVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 75 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAACITGD-NRSLIANLAAANCYKkekhLDlERNWMLVEKARV 153
Cdd:PLN02813 153 MAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDaQRTMLSYQGTSSTVN----YD-SCLASAISKSRV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 154 CYIAGFF--LTVSPESVLKVAHHASENNRIFTLNLSAP-FISQFYKESLMKVMPYVDILFGNETEAATFAreqGFETKDI 230
Cdd:PLN02813 228 LVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVsCIERHRDDFWDVMGNYADILFANSDEARALC---GLGSEES 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 231 KEIAkkTQALpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQdqrEIIDTNGAGDAFVGGFLSQL---VSDkplte 307
Cdd:PLN02813 305 PESA--TRYL----SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPC---VPVDTCGAGDAYAAGILYGLlrgVSD----- 370
|
330 340
....*....|....*....|.
gi 1353386 308 cIR-AGHYA---ASIIIRRTG 324
Cdd:PLN02813 371 -LRgMGELAarvAATVVGQQG 390
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
196-307 |
1.09e-06 |
|
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: 49.39 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 196 KESLMKVMPYVDILFGNETEAatfareqgfetKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVtaFAVLD 275
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEA-----------RQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGY--FAAPA 220
|
90 100 110
....*....|....*....|....*....|..
gi 1353386 276 QDQREIIDTNGAGDAFVGGFLSQLVSDKPLTE 307
Cdd:cd01946 221 YPLESVFDPTGAGDTFAGGFIGYLASQKDTSE 252
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
201-320 |
4.88e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 47.04 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 201 KVMPYVDILFGNETEAATFAREQgfeTKDIKEIAKKTqalpkmnskrqriVIFTQGRDDTIMATESEVTAFAVldqDQRE 280
Cdd:PRK09813 154 TLVPHLDYAFASAPQEDEFLRLK---MKAIVARGAGV-------------VIVTLGENGSIAWDGAQFWRQAP---EPVT 214
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1353386 281 IIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 320
Cdd:PRK09813 215 VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
212-312 |
1.01e-05 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 46.67 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 212 NETEAATFAreqGFETKDIKEIAKKTQALPKMNSkrqRIVIFTQGRDDTIMATESEVTAFAVLdqdQREIIDTNGAGDAF 291
Cdd:COG1105 184 NLEELEELL---GRPLETLEDIIAAARELLERGA---ENVVVSLGADGALLVTEDGVYRAKPP---KVEVVSTVGAGDSM 254
|
90 100
....*....|....*....|.
gi 1353386 292 VGGFLSQLVSDKPLTECIRAG 312
Cdd:COG1105 255 VAGFLAGLARGLDLEEALRLA 275
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
196-324 |
1.08e-05 |
|
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: 46.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 196 KESLMKVMPYVDILFGNETEAATFAREQGFETKDIKE------IAKKTQALPKMNSkrqrIVIFTQGRDDTIMATESEVT 269
Cdd:cd01943 171 LEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEkeavlqALLFSGILQDPGG----GVVLRCGKLGCYVGSADSGP 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1353386 270 AF---AVlDQDQREIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 324
Cdd:cd01943 247 ELwlpAY-HTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
51-324 |
1.15e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 46.71 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 51 AGGSTQNSIK-------VAQWMIqqphkaatffGCIGIDKFGEILKRKAAEAHVDAHYYEQDEQPTGTCAaCITGD--NR 121
Cdd:PLN02379 85 AGGSVANTIRglsagfgVSTGII----------GACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCV-CLVDAlgNR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 122 SLIANLAAA-----NCYKKEkhlDLE-RNWMLVEkarvcYiaGFFltvSPESVLKVAHHASENNRIFTLNLSAPFISQFY 195
Cdd:PLN02379 154 TMRPCLSSAvklqaDELTKE---DFKgSKWLVLR-----Y--GFY---NLEVIEAAIRLAKQEGLSVSLDLASFEMVRNF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 196 KESLMKVMPY--VDILFGNETEAATFAReqGFETKDIKEiakktqALpKMNSKRQRIVIFTQGRDDTIMATESEVTAFAV 273
Cdd:PLN02379 221 RSPLLQLLESgkIDLCFANEDEARELLR--GEQESDPEA------AL-EFLAKYCNWAVVTLGSKGCIARHGKEVVRVPA 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1353386 274 LDQDQreIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 324
Cdd:PLN02379 292 IGETN--AVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
282-307 |
1.61e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 46.15 E-value: 1.61e-05
10 20
....*....|....*....|....*.
gi 1353386 282 IDTNGAGDAFVGGFLSQLVSDKPLTE 307
Cdd:PLN02323 261 VDTTGAGDAFVGGLLSQLAKDLSLLE 286
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
158-326 |
5.54e-05 |
|
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: 43.95 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 158 GFFLTvsPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMkvmpYVDILFGNETEAAtfarEQGFETKDIKeiakkt 237
Cdd:cd01947 124 GVFIT--AAAVDKEAIRKCRETKLVILQVTPRVRVDELNQALI----PLDILIGSRLDPG----ELVVAEKIAG------ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 238 qalpkmnsKRQRIVIFTQGRDDTIMATESE---VTAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHY 314
Cdd:cd01947 188 --------PFPRYLIVTEGELGAILYPGGRynhVPAKKA------KVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQ 253
|
170
....*....|..
gi 1353386 315 AASIIIRRTGCT 326
Cdd:cd01947 254 CGAICVSHFGPY 265
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
228-312 |
1.08e-04 |
|
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: 43.29 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 228 KDIKEIAKKtqalpkMNSKRQRIVIFTQGRDDTIMATESEV---TAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKP 304
Cdd:cd01164 200 EDVIAAARK------LIERGAENVLVSLGADGALLVTKDGVyraSPPKV------KVVSTVGAGDSMVAGFVAGLAQGLS 267
|
....*...
gi 1353386 305 LTECIRAG 312
Cdd:cd01164 268 LEEALRLA 275
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
249-301 |
3.69e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 41.85 E-value: 3.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353386 249 RIVIFTQGRDDTIMATESEVTAFA---VldqdqrEIIDTNGAGDAFVGGFLSQLVS 301
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
5-59 |
7.72e-04 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 41.15 E-value: 7.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353386 5 LLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELVKKFKVEYH-AGGSTQNSI 59
Cdd:PRK15074 43 LVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
237-324 |
8.30e-04 |
|
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: 40.35 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 237 TQALPKMNSKRQRIVIFTQGRDDTIMATES----EVTAFAVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 312
Cdd:cd01945 192 DEALELLASLGIPFVAVTLGEAGCLWLERDgelfHVPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFA 265
|
90
....*....|..
gi 1353386 313 HYAASIIIRRTG 324
Cdd:cd01945 266 SAAAALKCRGLG 277
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
196-317 |
2.95e-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: 38.93 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 196 KESLMKVMPYVDILFgnetEAATFAREQGFETkdikeiAKKTQALPKMNSKRQRIVIFTQGrDDTIMATESEVTAFAVLD 275
Cdd:cd01939 170 REELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWG-DQGAGALGPDGEYVHSPA 238
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1353386 276 QDQREIIDTNGAGDAFVGGFLSQL-VSDKPLTECIRAGHYAAS 317
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALnKGPDDLSEALDFGNRVAS 281
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
195-323 |
3.12e-03 |
|
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: 38.72 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 195 YKESLMkvmPYVDILFGNETEAATFAreqGFETKDIKEIakkTQALPKMNSKRQRIVIFT------QGRDDTIMATESEV 268
Cdd:cd01173 129 YRDLLV---PLADIITPNQFELELLT---GKKINDLEDA---KAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEA 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353386 269 TAFavldqdQREIIDT----NGAGDAFVGGFLSQLVSDKPLTEciRAGHYAASI--IIRRT 323
Cdd:cd01173 200 WLV------QRPKIPFpayfNGTGDLFAALLLARLLKGKSLAE--ALEKALNFVheVLEAT 252
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
195-318 |
9.69e-03 |
|
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: 37.00 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 195 YKESLMKVMPYVDILFGNETEAAtfareqgfETKDIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMATESE---VTAF 271
Cdd:cd01937 145 EKLIKCVILKLHDVLKLSRVEAE--------VISTPTELARLIKETG------VKEIIVTDGEEGGYIFDGNGkytIPAS 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1353386 272 AVldqdqrEIIDTNGAGDAFVGGFLSQLVSDKpltECIRAGHYAASI 318
Cdd:cd01937 211 KK------DVVDPTGAGDVFLAAFLYSRLSGK---DIKEAAEFAAAA 248
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
201-323 |
9.72e-03 |
|
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: 37.05 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 201 KVMPYVDILFGNETEAATFAreqGFETKDIKEIAKKTQALPKMNSKrqrIVIFTQGRDDTIMATESEVtafAVLDQDQRE 280
Cdd:COG2240 134 RLVPLADIITPNLTELALLT---GRPYETLEEALAAARALLALGPK---IVVVTSVPLDDTPADKIGN---LAVTADGAW 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1353386 281 IIDT-------NGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRT 323
Cdd:COG2240 205 LVETpllpfspNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLERT 254
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
196-310 |
9.96e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 36.96 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353386 196 KESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMN---------SKRQRIVIFTQGRDDTIMAtes 266
Cdd:PRK12413 120 RQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAvvikggnrlSQKKAIDLFYDGKEFVILE--- 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1353386 267 evtaFAVLDQDQreiidtNGAGDAFVGGFLSQLVSDKPLTECIR 310
Cdd:PRK12413 197 ----SPVLEKNN------IGAGCTFASSIASQLVKGKSPLEAVK 230
|
|
| |
