|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
12-344 |
0e+00 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 538.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 12 MGNPLLDISAVVDKDFLDKYGLKPNDQILAEEKHKALFDEIVNKSKVEYHAGGSTQNSVKIAQWMIQEPHkVATFFGCIG 91
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 92 TDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAACITGDNRSLVANLAAANCYnKEKHLDIDRNWSLVEKARVYYIAGFF 171
Cdd:PLN02548 80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCY-KVEHLKKPENWALVEKAKFYYIAGFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 172 LTVSPDSILKVAKHASDNNKIFGLNLSAPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEQGFETEDIAEIAHRVQNL 251
Cdd:PLN02548 159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 252 PKVNKNRQRIVVFTQGREDTVATVGDKVKMFPVLDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVII 331
Cdd:PLN02548 239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318
|
330
....*....|...
gi 38488696 332 RRSGCTFPEKPDF 344
Cdd:PLN02548 319 QRSGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
2-344 |
1.01e-167 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 470.66 E-value: 1.01e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 2 PTVSQNSLFGMGNPLLDISAVVDKDFLDKYGLKPNDQILAEEKHKALFDEIVNKSKVEYHAGGSTQNSVKIAQWMIQEPH 81
Cdd:PTZ00247 1 TSSAPKKLLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 82 KVATFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAACITGDNRSLVANLAAANCYnKEKHLDIDRNWSLVEK 161
Cdd:PTZ00247 81 GFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHL-SAEHMQSHAVQEAIKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 162 ARVYYIAGFFLTVSPDSILKVAKHASDNNKIFGLNLSAPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEQGFETEDI 241
Cdd:PTZ00247 160 AQLYYLEGFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 242 AEIAHRVQNLPKVNKNRQRIVVFTQGREDTVATVGDKVKMFPVLDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIR 321
Cdd:PTZ00247 240 KEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVE 319
|
330 340
....*....|....*....|...
gi 38488696 322 AGHYAAHVIIRRSGCTFPEKPDF 344
Cdd:PTZ00247 320 AGHYSAQVIIQHNGCTYPEKPPF 342
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-339 |
3.98e-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: 394.29 E-value: 3.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 9 LFGMGNPLLDISAVVDKDFLDKYGLKPNDQILAeekHKALFDEIVNKSKVEYHAGGSTQNSVKIAQWMIQEphkvATFFG 88
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGS----AAFIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 89 CIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAACITGD-NRSLVANLAAANCYNKEkhldiDRNWSLVEKARVYYI 167
Cdd:cd01168 77 RVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPD-----DLDWSLLAKAKYLYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 168 AGFFLTVSPDSILKVAKHASDNNKIFGLNLSAPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEqgfETEDIAEIAHR 247
Cdd:cd01168 152 EGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 248 VQNLpkvnknRQRIVVFTQGREDTVatVGDKVKMFPVLDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAA 327
Cdd:cd01168 229 LLAL------RCRIVVITQGAKGAV--VVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300
|
330
....*....|..
gi 38488696 328 HVIIRRSGCTFP 339
Cdd:cd01168 301 AEVIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
27-338 |
8.54e-72 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 224.91 E-value: 8.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 27 FLDKYGLKPNDQILAEEKHkalFDEIVNKSKVEYHAGGSTQNSVKIAQWMIQEphkvATFFGCIGTDHFGEILKQKAAEA 106
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 107 HVDAHYYEQN-QEPTGTCAACITGD-NRSLVANLAAANCYNKEKHLDidrNWSLVEKARVYYIAGFFLTVSPDSILKVAK 184
Cdd:pfam00294 74 GVDTDYVVIDeDTRTGTALIEVDGDgERTIVFNRGAAADLTPEELEE---NEDLLENADLLYISGSLPLGLPEATLEELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 185 HASDNNKIFGLNLSAPFISQfsKEPLMKVLPYVDIIFGNETEAATFAKEQGFETEDIAEIAHrvqnlpKVNKNRQRIVVF 264
Cdd:pfam00294 151 EAAKNGGTFDPNLLDPLGAA--REALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH------KLLAKGIKTVIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38488696 265 TQGREDTVATVGDKVkmFPVLDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVIIRRSGCTF 338
Cdd:pfam00294 223 TLGADGALVVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
84-337 |
2.50e-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: 140.79 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVDAHYYEQ-NQEPTGTCAACITGD-NRSLVANLAAANCYNKEkhlDIDRnwSLVEK 161
Cdd:COG0524 53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE---DLDE--ALLAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 162 ARVYYIAGFFLT--VSPDSILKVAKHASDNNK--IFGLNLSAPFISQFSKEpLMKVLPYVDIIFGNETEAATFakeqgFE 237
Cdd:COG0524 128 ADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEPAREL-LRELLALVDILFPNEEEAELL-----TG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 238 TEDIAEIAHRVQNLPKvnknrqRIVVFTQGREDTVATVGDKVKMFPVLDIDqndIVDTNGAGDAFVGGFLSALVQDQPLE 317
Cdd:COG0524 202 ETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEVVHVPAFPVE---VVDTTGAGDAFAAGFLAGLLEGLDLE 272
|
250 260
....*....|....*....|
gi 38488696 318 ECIRAGHYAAHVIIRRSGCT 337
Cdd:COG0524 273 EALRFANAAAALVVTRPGAQ 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
85-335 |
6.26e-34 |
|
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: 126.51 E-value: 6.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQ-EPTGTcaACIT----GDNRSLVAnlAAANcynkeKHL---DIDRNW 156
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVVVgAPTGT--AVITvdesGENRIVVV--PGAN-----GELtpaDVDAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 157 SLVEKARVyyiagfFLT---VSPDSILKVAKHASDNNKIFGLNlSAPFisqfsKEPLMKVLPYVDIIFGNETEAATFAKE 233
Cdd:cd01174 125 ELIAAADV------LLLqleIPLETVLAALRAARRAGVTVILN-PAPA-----RPLPAELLALVDILVPNETEAALLTGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 234 QGFETEDIAEIAHRVQNLPKvnknrqRIVVFTQGREDTVATVGDKVKMFPVLdidQNDIVDTNGAGDAFVGGFLSALVQD 313
Cdd:cd01174 193 EVTDEEDAEKAARLLLAKGV------KNVIVTLGAKGALLASGGEVEHVPAF---KVKAVDTTGAGDTFIGALAAALARG 263
|
250 260
....*....|....*....|..
gi 38488696 314 QPLEECIRAGHYAAHVIIRRSG 335
Cdd:cd01174 264 LSLEEAIRFANAAAALSVTRPG 285
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
85-335 |
1.29e-29 |
|
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: 115.01 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAAEAHVDAHYYEQ-NQEPTGTcaACI----TGDNRSLVAnlAAANcynkeKHL---DIDRNW 156
Cdd:TIGR02152 49 SMIGKVGDDAFGDELLENLKSNGIDTEYVGTvKDTPTGT--AFItvddTGENRIVVV--AGAN-----AELtpeDIDAAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 157 SLVEKARVYYIAgffLTVSPDSILKVAKHASDNNKIFGLNlSAPFISQFSKEplmkVLPYVDIIFGNETEAATFAKEQGF 236
Cdd:TIGR02152 120 ALIAESDIVLLQ---LEIPLETVLEAAKIAKKHGVKVILN-PAPAIKDLDDE----LLSLVDIITPNETEAEILTGIEVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 237 ETEDIAEIAHRVQNLPKvnknrqRIVVFTQGREDTVATVGDKVKMFPVLDIDqndIVDTNGAGDAFVGGFLSALVQDQPL 316
Cdd:TIGR02152 192 DEEDAEKAAEKLLEKGV------KNVIITLGSKGALLVSKDESKLIPAFKVK---AVDTTAAGDTFNGAFAVALAEGKSL 262
|
250
....*....|....*....
gi 38488696 317 EECIRAGHYAAHVIIRRSG 335
Cdd:TIGR02152 263 EDAIRFANAAAAISVTRKG 281
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
61-337 |
5.91e-29 |
|
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: 113.05 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 61 HAGGSTQNsvkIAQWMIQEPHKVAtFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQE-PTGTcAACITGDN--RSLVAN 137
Cdd:cd01166 29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGgeRRVLYY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 138 LA-AANCYNKEKHLDIDrnwsLVEKARVYYIAGFFLTVSPDS---ILKVAKHASDNNK--IFGLNLSAPFIS-QFSKEPL 210
Cdd:cd01166 104 RAgSAASRLTPEDLDEA----ALAGADHLHLSGITLALSESAreaLLEALEAAKARGVtvSFDLNYRPKLWSaEEAREAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 211 MKVLPYVDIIFGNETEAATFAKEQGfeTEDIAEIAHRVQNLPKVnknrqriVVFTQGREDTVATVGDK---VKMFPVldi 287
Cdd:cd01166 180 EELLPYVDIVLPSEEEAEALLGDED--PTDAAERALALALGVKA-------VVVKLGAEGALVYTGGGrvfVPAYPV--- 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 38488696 288 dqnDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGH-YAAHVIIRRsGCT 337
Cdd:cd01166 248 ---EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANaAAALVVTRP-GDI 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
84-336 |
1.25e-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: 92.76 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVD-AHYYEQNQEPTGTcaACIT--GDNRSLVANLAAANcynkekhldidRNWSLVE 160
Cdd:cd01942 53 PGLVAAVGEDFHGRLYLEELREEGVDtSHVRVVDEDSTGV--AFILtdGDDNQIAYFYPGAM-----------DELEPND 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 161 KARVYYIAGFfltVSPDS-----ILKVAKHASDNNKIFGLnlsAPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEQG 235
Cdd:cd01942 120 EADPDGLADI---VHLSSgpgliELARELAAGGITVSFDP---GQELPRLSGEELEEILERADILFVNDYEAELLKERTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 236 FETEDIAEiahrvqnlpkvnknRQRIVVFTQGREDTVATVGDKVKMFPVLDIDqnDIVDTNGAGDAFVGGFLSALVQDQP 315
Cdd:cd01942 194 LSEAELAS--------------GVRVVVVTLGPKGAIVFEDGEEVEVPAVPAV--KVVDTTGAGDAFRAGFLYGLLRGYD 257
|
250 260
....*....|....*....|.
gi 38488696 316 LEECIRAGHYAAHVIIRRSGC 336
Cdd:cd01942 258 LEESLRLGNLAASLKVERRGA 278
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
172-311 |
3.40e-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: 87.15 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 172 LTVSPDSILKVAKHASDNNKIFGLNLSAPFISQFsKEPLMKVLPYVDIIFGNETEAATFAKEQGFETEDIAEIAHRVQNl 251
Cdd:cd00287 66 LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLD-GEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLS- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38488696 252 pkvnkNRQRIVVFTQGRE-DTVATVGDKVKMFPVLDIdqnDIVDTNGAGDAFVGGFLSALV 311
Cdd:cd00287 144 -----KGPKVVIVTLGEKgAIVATRGGTEVHVPAFPV---KVVDTTGAGDAFLAALAAGLA 196
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
84-323 |
4.30e-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: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVD-AHYYEQNQEPTGTCAACITGDNR---SLVANLAAANcynkekHLDIDRNWSLV 159
Cdd:cd01167 45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDADGErsfEFYRGPAADL------LLDTELNPDLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 160 EKARVYYIAGFFLTVSP--DSILKVAKHASDNNKI--FGLNLSAPFISQF--SKEPLMKVLPYVDIIFGNETEAATFake 233
Cdd:cd01167 119 SEADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWRDEeeARERIAELLELADIVKLSDEELELL--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 234 qgFETEDIAEIAHRVQNLpkvnkNRQRIVVfTQGREDTVATVGDKVKMFPVLDIDQndiVDTNGAGDAFVGGFLSALVQD 313
Cdd:cd01167 196 --FGEEDPEEIAALLLLF-----GLKLVLV-TRGADGALLYTKGGVGEVPGIPVEV---VDTTGAGDAFVAGLLAQLLSR 264
|
250
....*....|....*..
gi 38488696 314 Q-------PLEECIRAG 323
Cdd:cd01167 265 GllaldedELAEALRFA 281
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
63-337 |
5.97e-18 |
|
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: 83.03 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 63 GGSTQNsvkIAQWMIQEPHKVAtFFGCIGTDHFGE-ILKQKAAEAHVDAHYYEQNQEPTGtcaACITG----DNRSLV-- 135
Cdd:TIGR04382 34 GGSPAN---IAVGAARLGLKTA-FITRVGDDQFGRfVRDYLRREGVDTSHVVTDPGRRTS---LVFLEikppDEFPLLfy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 136 ----ANLAaancynkekhLDIDR-NWSLVEKARVYYIAGFFLTVSP--DSILKVAKHASDNNKIFGLNLSapFISQFSKE 208
Cdd:TIGR04382 107 renaADLA----------LTPDDvDEDYIASARALLVSGTALSQEPsrEAVLKALEYARAAGVRVVLDID--YRPYLWKS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 209 P------LMKVLPYVDIIFGNETEAATFAKEqgfetEDIAEIAHRVQNLPKvnknrqRIVVFTQGREDTVATVGD----K 278
Cdd:TIGR04382 175 PeeagiyLRLVLPLVDVIIGTREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDgegvE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 38488696 279 VKMFPVldidqnDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVIIRRSGCT 337
Cdd:TIGR04382 244 VPGFPV------EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
84-327 |
4.18e-14 |
|
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: 71.58 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAAcITGDNRSLVANLAAANCYN---------------KEK 148
Cdd:cd01941 52 VALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTA-ILDKDGDLVVALADMDIYElltpdflrkirealkEAK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 149 HLDIDRNWS------LVEKARvyyIAGFFLTVSPDSILKVAKhasdnnkifglnlsapfisqfskepLMKVLPYVDIIFG 222
Cdd:cd01941 131 PIVVDANLPeealeyLLALAA---KHGVPVAFEPTSAPKLKK-------------------------LFYLLHAIDLLTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 223 NETEAATFAKEQGFETED--IAEIAHRVQNLPkvnknrqrIVVFTQGREDTVAT---VGDKVKMFPVldIDQNDIVDTNG 297
Cdd:cd01941 183 NRAELEALAGALIENNEDenKAAKILLLPGIK--------NVIVTLGAKGVLLSsreGGVETKLFPA--PQPETVVNVTG 252
|
250 260 270
....*....|....*....|....*....|
gi 38488696 298 AGDAFVGGFLSALVQDQPLEECIRAGHYAA 327
Cdd:cd01941 253 AGDAFVAGLVAGLLEGMSLDDSLRFAQAAA 282
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
85-335 |
2.70e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 66.43 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAAEAHVD-AHYYEQNQEPTGTcaACI----TGDNRSLVAnlAAANCYNKEKHLDidRNWSLV 159
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDtAPVSVIKGESTGV--ALIfvndEGENSIGIH--AGANAALTPALVE--AHRELI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 160 EKARVYYIAgffLTVSPDSILKVAKHASDNNKIFGLNlSAPfISQFSKEplmkVLPYVDIIFGNETEAATFAkeqGFETE 239
Cdd:PRK11142 131 ANADALLMQ---LETPLETVLAAAKIAKQHGTKVILN-PAP-ARELPDE----LLALVDIITPNETEAEKLT---GIRVE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 240 DIAEIAHRVQNLpkvNKNRQRIVVFTQGREDTVATVGDKVKMFPVLDIDqndIVDTNGAGDAFVGGFLSALVQDQPLEEC 319
Cdd:PRK11142 199 DDDDAAKAAQVL---HQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQ---AVDTIAAGDTFNGALVTALLEGKPLPEA 272
|
250
....*....|....*.
gi 38488696 320 IRAGHYAAHVIIRRSG 335
Cdd:PRK11142 273 IRFAHAAAAIAVTRKG 288
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
84-330 |
3.31e-12 |
|
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: 65.84 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAACITGDNRSLVAnlaaancYNKEKHLDidrnwSLVEKAR 163
Cdd:cd01940 39 SAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVDGDRIFGL-------SNKGGVAR-----EHPFEAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 164 VYYIAGFFLTVSpdSILKVAKHASDNNK---IFGLNLSAPFISQFSKEPLMKVLPYVDIIFGNETEaatfakeqgFETED 240
Cdd:cd01940 107 LEYLSQFDLVHT--GIYSHEGHLEKALQalvGAGALISFDFSDRWDDDYLQLVCPYVDFAFFSASD---------LSDEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 241 IAEIAHRVQNlpkvnkNRQRIVVFTQGREDTVATVGDKVkmFPVLdIDQNDIVDTNGAGDAFVGGFLSALVQ-DQPLEEC 319
Cdd:cd01940 176 VKAKLKEAVS------RGAKLVIVTRGEDGAIAYDGAVF--YSVA-PRPVEVVDTLGAGDSFIAGFLLSLLAgGTAIAEA 246
|
250
....*....|..
gi 38488696 320 IRAG-HYAAHVI 330
Cdd:cd01940 247 MRQGaQFAAKTC 258
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
11-335 |
5.27e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 66.37 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 11 GMGNPLLDISAVVDKDFLDKYGLKPNDQ--ILAEEKHKALfdEIVNKSKVEYHAGGSTQNSV----KIAQWMIQEPHKVA 84
Cdd:PLN02813 74 GLGQAMVDFSGMVDDEFLERLGLEKGTRkvINHEERGKVL--RALDGCSYKASAGGSLSNTLvalaRLGSQSAAGPALNV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAAEAHVdahyyEQNQEP-----TGTCAACITGD-NRSLVANLAAANCYNKEKHLDidrnwSL 158
Cdd:PLN02813 152 AMAGSVGSDPLGDFYRTKLRRANV-----HFLSQPvkdgtTGTVIVLTTPDaQRTMLSYQGTSSTVNYDSCLA-----SA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 159 VEKARVYYIAGFF--LTVSPDSILKVAKHASDNNKIFGLNLSAPFISQFSKEPLMKVLP-YVDIIFGNETEAATFAkeqG 235
Cdd:PLN02813 222 ISKSRVLVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGnYADILFANSDEARALC---G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 236 FETEDIAEIAHRVQN--LPkvnknrqrIVVFTQG-REDTVATVGDKVKMFPVLDIDqndiVDTNGAGDAFVGGFLSALVQ 312
Cdd:PLN02813 299 LGSEESPESATRYLShfCP--------LVSVTDGaRGSYIGVKGEAVYIPPSPCVP----VDTCGAGDAYAAGILYGLLR 366
|
330 340
....*....|....*....|....*.
gi 38488696 313 DQPleECIRAGHYAAHV---IIRRSG 335
Cdd:PLN02813 367 GVS--DLRGMGELAARVaatVVGQQG 390
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
85-335 |
8.73e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 65.14 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAAEAHVDAHY-YEQNQEPTGtCAACI----TGDNRSLVanlaaanCYNKEKHL---DIDRNW 156
Cdd:PTZ00292 70 AMVGMVGTDGFGSDTIKNFKRNGVNTSFvSRTENSSTG-LAMIFvdtkTGNNEIVI-------IPGANNALtpqMVDAQT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 157 SLVEKARVYYIAGffLTVSPDSILKVAKHASDNNKIFGLNlSAPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEQgF 236
Cdd:PTZ00292 142 DNIQNICKYLICQ--NEIPLETTLDALKEAKERGCYTVFN-PAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALITGME-V 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 237 ETEDIAEIAHR-VQNLPKVNknrqriVVFTQGREDTVATVGDKVKMFpvLDIDQNDIVDTNGAGDAFVGGFLSALVQDQP 315
Cdd:PTZ00292 218 TDTESAFKASKeLQQLGVEN------VIITLGANGCLIVEKENEPVH--VPGKRVKAVDTTGAGDCFVGSMAYFMSRGKD 289
|
250 260
....*....|....*....|
gi 38488696 316 LEECIRAGHYAAHVIIRRSG 335
Cdd:PTZ00292 290 LKESCKRANRIAAISVTRHG 309
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
86-335 |
1.94e-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: 63.98 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 86 FFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTGTCAACITGD-NRSLVANLAAancynkEKHLDIDRNWSL-VEKAR 163
Cdd:cd01944 54 NAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDgERSFISISGA------EQDWSTEWFATLtVAPYD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 164 VYYIAGFFLTVS--PDSILKVAKHASDNNKIFGLNLSaPFISQFSKEPLMKVLPYVDIIFGNETEAATFAKEQGFETEDI 241
Cdd:cd01944 128 YVYLSGYTLASEnaSKVILLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEAS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 242 AEIAHRVQNLPkvnknrqriVVFTQGREDT-VATVGDK---VKMFPVldidqnDIVDTNGAGDAFVGGFLSALVQDQPLE 317
Cdd:cd01944 207 ALRIYAKTAAP---------VVVRLGSNGAwIRLPDGNthiIPGFKV------KAVDTIGAGDTHAGGMLAGLAKGMSLA 271
|
250
....*....|....*...
gi 38488696 318 ECIRAGHYAAHVIIRRSG 335
Cdd:cd01944 272 DAVLLANAAAAIVVTRSG 289
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
37-335 |
4.98e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 60.19 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 37 DQILAE-EKHKALFDEivNKSKVEYHAGGSTQNSVK-------IAQWMIqephkvatffGCIGTDHFGEILKQKAAEAHV 108
Cdd:PLN02379 61 EHILREvNAHILPSPD--DLSPIKTMAGGSVANTIRglsagfgVSTGII----------GACGDDEQGKLFVSNMGFSGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 109 DAHYYEQNQEPTGTCAaCITGD--NRSLVANLAAA-----NCYNKEKHLDIdrNWSLVEkarvYYIAGffltvspdsiLK 181
Cdd:PLN02379 129 DLSRLRAKKGPTAQCV-CLVDAlgNRTMRPCLSSAvklqaDELTKEDFKGS--KWLVLR----YGFYN----------LE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 182 VAKHASDNNKIFGLNLS---APF-ISQFSKEPLMKVLPY--VDIIFGNETEAATFAK-EQGFETEDIAEIahrvqnlpkV 254
Cdd:PLN02379 192 VIEAAIRLAKQEGLSVSldlASFeMVRNFRSPLLQLLESgkIDLCFANEDEARELLRgEQESDPEAALEF---------L 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 255 NKNRQRIVVfTQGREDTVATVGDKVKMFPVldIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVIIRRS 334
Cdd:PLN02379 263 AKYCNWAVV-TLGSKGCIARHGKEVVRVPA--IGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRAL 339
|
.
gi 38488696 335 G 335
Cdd:PLN02379 340 G 340
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
206-323 |
4.75e-09 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 56.68 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 206 SKEPLMKVLPY-VDIIFGNETEAATFAKEQGFETEDIAEIAHRVqnlpkVNKNRQRIVVfTQGREDTVATVGDKVKMFPV 284
Cdd:COG1105 166 SGEALKAALEAgPDLIKPNLEELEELLGRPLETLEDIIAAAREL-----LERGAENVVV-SLGADGALLVTEDGVYRAKP 239
|
90 100 110
....*....|....*....|....*....|....*....
gi 38488696 285 LDIDqndIVDTNGAGDAFVGGFLSALVQDQPLEECIRAG 323
Cdd:COG1105 240 PKVE---VVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
194-331 |
7.25e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 52.82 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 194 GLNLSAPFISQFSKEPLMKVLPYVDIIFGNETEaatfakeqgfETEDIAEIAHRVQNL-PKVnknrqriVVFTQGREDTV 272
Cdd:PRK09813 136 GKLTAFDFSDKWDSPLWQTLVPHLDYAFASAPQ----------EDEFLRLKMKAIVARgAGV-------VIVTLGENGSI 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 38488696 273 ATVGDKVKMFPvldIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVII 331
Cdd:PRK09813 199 AWDGAQFWRQA---PEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
84-335 |
3.32e-07 |
|
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: 51.14 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 84 ATFFGCIGTDHFGEILKQKAAEAHVDAHYYEQNQEPTG--TCAACITGDNRSlVANLAAancynkekHLDIDRNW---SL 158
Cdd:cd01945 53 ARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSpiSSITDITGDRAT-ISITAI--------DTQAAPDSlpdAI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 159 VEKARVYYIAGffltVSPDSILKVAKHASDNNKIFGLNLSAPfisqfSKEPLMKVLPYVD-IIFgneteAATFAKEQGFE 237
Cdd:cd01945 124 LGGADAVLVDG----RQPEAALHLAQEARARGIPIPLDLDGG-----GLRVLEELLPLADhAIC-----SENFLRPNTGS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 238 TEDIAEIAHRVQNLPkvnknrqrIVVFTQG------REDTVATVgdKVKMFPVldidqnDIVDTNGAGDAFVGGFLSALV 311
Cdd:cd01945 190 ADDEALELLASLGIP--------FVAVTLGeagclwLERDGELF--HVPAFPV------EVVDTTGAGDVFHGAFAHALA 253
|
250 260
....*....|....*....|....
gi 38488696 312 QDQPLEECIRAGHYAAHVIIRRSG 335
Cdd:cd01945 254 EGMPLREALRFASAAAALKCRGLG 277
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
199-323 |
1.50e-06 |
|
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: 49.07 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 199 APFISQFSKEPLMKVLPY-VDIIFGNETEAATFAKEQGFETEDIAEIAHRVQNLpkvnknRQRIVVFTQGREDTVATVGD 277
Cdd:cd01164 159 ARVILDTSGEALLAALAAkPFLIKPNREELEELFGRPLGDEEDVIAAARKLIER------GAENVLVSLGADGALLVTKD 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 38488696 278 KVKMFPVLDIDqndIVDTNGAGDAFVGGFLSALVQDQPLEECIRAG 323
Cdd:cd01164 233 GVYRASPPKVK---VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
85-334 |
2.68e-06 |
|
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: 48.18 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 85 TFFGCIGTDHFGEILKQKAaEAHVDAHYYEQNQEPTGTCAACITGDNRSLVANLAAANcyNKEKHLDIDRNWSLVekarv 164
Cdd:cd01947 54 RFFSNLGRDEIGIQSLEEL-ESGGDKHTVAWRDKPTRKTLSFIDPNGERTITVPGERL--EDDLKWPILDEGDGV----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 165 yyiagfFLTVSPDSILKVAKHASDNNKIFGLNLSAPFISqfskepLMKVLPYVDIIFGNETEaatfakeqgFETEDIAEi 244
Cdd:cd01947 126 ------FITAAAVDKEAIRKCRETKLVILQVTPRVRVDE------LNQALIPLDILIGSRLD---------PGELVVAE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 245 ahrvqnlpKVNKNRQRIVVFTQGreDTVATVGDKVKMFPVlDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAG- 323
Cdd:cd01947 184 --------KIAGPFPRYLIVTEG--ELGAILYPGGRYNHV-PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGa 252
|
250
....*....|.
gi 38488696 324 HYAAHVIIRRS 334
Cdd:cd01947 253 QCGAICVSHFG 263
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
205-335 |
1.79e-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: 45.79 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 205 FSKEPLMKVLPYVDIIFGNETEAATFA--KEQGFETEDIAEIAHRVQNLPKVNKNRQRIVVFTQGRED--TVATVGDKVK 280
Cdd:cd01943 169 ENLEDLLQALPRVDVFSPNLEEAARLLglPTSEPSSDEEKEAVLQALLFSGILQDPGGGVVLRCGKLGcyVGSADSGPEL 248
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 38488696 281 MFPVLDIDQNDIVDTNGAGDAFVGGFLSALVQDQPLEECIRAGHYAAHVIIRRSG 335
Cdd:cd01943 249 WLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
278-316 |
1.97e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.77 E-value: 1.97e-05
10 20 30
....*....|....*....|....*....|....*....
gi 38488696 278 KVKMFPVldidqnDIVDTNGAGDAFVGGFLSALVQDQPL 316
Cdd:PLN02323 252 RVEGFKV------KAVDTTGAGDAFVGGLLSQLAKDLSL 284
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
2-70 |
2.56e-05 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 45.77 E-value: 2.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38488696 2 PTVSQNSLFGMGNPLLDISAVVDKDFLDKYGL-KPNDQILAEEKHKALFDEIVNKSKVEYH-AGGSTQNSV 70
Cdd:PRK15074 29 NETSRTYIVGIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
260-312 |
2.64e-05 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 45.31 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 38488696 260 RIVVFTQGREDTVATVGDKVKMFPVLDIDqndIVDTNGAGDAFVGGFLSALVQ 312
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPAPSVD---PVDTTGAGDAFVAGLLAGLSQ 263
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
165-329 |
1.39e-04 |
|
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: 42.77 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 165 YYIAGFFLTVSPDSILKVAKHASDnnkifglnlSAPFISQFSKEPLMK--VLPYVDIIFGNETEAAtfakeqgfETEDIA 242
Cdd:cd01937 111 VILGPVPEEISPSLFRKFAFISLD---------AQGFLRRANQEKLIKcvILKLHDVLKLSRVEAE--------VISTPT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 243 EIAHRVQNLPkvnknrQRIVVFTQGRED-TVATVGDKVKMFPVldidQNDIVDTNGAGDAFVGGFLSALVQDQPLEEcir 321
Cdd:cd01937 174 ELARLIKETG------VKEIIVTDGEEGgYIFDGNGKYTIPAS----KKDVVDPTGAGDVFLAAFLYSRLSGKDIKE--- 240
|
....*...
gi 38488696 322 AGHYAAHV 329
Cdd:cd01937 241 AAEFAAAA 248
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
212-332 |
4.98e-04 |
|
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: 41.29 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 212 KVLPYVDIIFGNETEAATFAKEQGFETEDIAEIAHRVQNLpkvnkNRQRIVV----FTQGREDTVATV---GDKVK--MF 282
Cdd:COG2240 134 RLVPLADIITPNLTELALLTGRPYETLEEALAAARALLAL-----GPKIVVVtsvpLDDTPADKIGNLavtADGAWlvET 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 38488696 283 PVLDidqndiVDTNGAGDAFVGGFLSALVQDQPLEECI-RAGHYAAHVIIR 332
Cdd:COG2240 209 PLLP------FSPNGTGDLFAALLLAHLLRGKSLEEALeRAAAFVYEVLER 253
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
170-310 |
1.16e-03 |
|
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: 40.14 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 170 FFLTVSPDSILKVAKHAsDNNKIFGLNLSAPFISqFSKEPLMKVLPYVDIIFGNETEAatfakeqgfetEDIAEIAHRVQ 249
Cdd:cd01946 119 FLGNIAPELQREVLEQV-KDPKLVVMDTMNFWIS-IKPEKLKKVLAKVDVVIINDGEA-----------RQLTGAANLVK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38488696 250 NLPKVNKNRQRIVVFTQGREDTVATVGDKVKMFPVLDIDqnDIVDTNGAGDAFVGGFLSAL 310
Cdd:cd01946 186 AARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLE--SVFDPTGAGDTFAGGFIGYL 244
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
209-334 |
2.57e-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: 39.10 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38488696 209 PLMK--VLPYVDIIFGNETEAATFAkeqGFETEDIAEIAHRVQNLpkVNKNRQRIVV-----FTQGREDTVATVGDKVKM 281
Cdd:cd01173 127 PVYRdlLVPLADIITPNQFELELLT---GKKINDLEDAKAAARAL--HAKGPKTVVVtsvelADDDRIEMLGSTATEAWL 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 38488696 282 F--PVLDIDQNdivdTNGAGDAFVGGFLSALVQDQPLEEciRAGHYAAHV--IIRRS 334
Cdd:cd01173 202 VqrPKIPFPAY----FNGTGDLFAALLLARLLKGKSLAE--ALEKALNFVheVLEAT 252
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
293-325 |
6.23e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.25 E-value: 6.23e-03
10 20 30
....*....|....*....|....*....|...
gi 38488696 293 VDTNGAGDAFVGGFLSALVQDQPLEECIRAGHY 325
Cdd:PLN02630 234 VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNY 266
|
|
| |
