|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-310 |
1.20e-90 |
|
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: 272.14 E-value: 1.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 9 IVFFGECMVEISGSP---------LTKKFGGDTLNTALYLSRLTqhqnLSVHYATGLGSDELSQNMIDGWQLEGIQTHFV 79
Cdd:cd01166 2 VVTIGEVMVDLSPPGggrleqadsFRKFFGGAEANVAVGLARLG----HRVALVTAVGDDPFGRFILAELRREGVDTSHV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 80 ERIPNKLPGLYMVETDETGERHFHYWRSDAAVKFYfqidnlnkQADDLNKLEIAliekQVDAVYISGISIAILDDAsRER 159
Cdd:cd01166 78 RVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRL--------TPEDLDEAALA----GADHLHLSGITLALSESA-REA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 160 LFKAISVFSNQGGKVIFDNNYRPQLWSTEQAQHWYAKLLPLVDIALITEDDDLLVWGNSESVQQ----RCLRLGCQEIVI 235
Cdd:cd01166 145 LLEALEAAKARGVTVSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAaeraLALALGVKAVVV 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327222203 236 KRGCEPCKIVqveqDDVVESYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:cd01166 225 KLGAEGALVY----TGGGRVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-310 |
3.42e-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: 3.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 8 NIVFFGECMVEIS--------------GSPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEG 73
Cdd:COG0524 1 DVLVIGEALVDLVarvdrlpkggetvlAGSFRRSPGGAAANVAVALARL----GARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 74 IQTHFVERIPNKLPGLYMVETDETGERHFHYWRSdAAVKFyfqidnlnkQADDLNKLEIAliekQVDAVYISGISIAilD 153
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRG-ANAEL---------TPEDLDEALLA----GADILHLGGITLA--S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 154 DASRERLFKAISVFSNQGGKVIFDNNYRPQLWstEQAQHWYAKLLPLVDIALITEDDDLLVWGNS--ESVQQRCLRLGCQ 231
Cdd:COG0524 141 EPPREALLAALEAARAAGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEEAELLTGETdpEEAAAALLARGVK 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327222203 232 EIVIKRGCEPCKIvqVEQDDVVEsyVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:COG0524 219 LVVVTLGAEGALL--YTGGEVVH--VPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
8-311 |
4.51e-45 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 155.19 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 8 NIVFFGECMVEISG------------SPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEGIQ 75
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvrvSTVEKGPGGKGANVAVALARL----GGDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 76 THFVERIPNKLPGLYMVETDETGERHFHYWRSDAAvkfyfqidNLNKQADDLNKLEIAliekQVDAVYISGIsiaiLDDA 155
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAA--------DLTPEELEENEDLLE----NADLLYISGS----LPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 156 SRERLFKAISVFSNQGGKviFDNNYRPQLWSTEQAqhwYAKLLPLVDIALITEDDDLLVWG----NSESVQQRCLRL--- 228
Cdd:pfam00294 141 LPEATLEELIEAAKNGGT--FDPNLLDPLGAAREA---LLELLPLADLLKPNEEELEALTGakldDIEEALAALHKLlak 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 229 GCQEIVIKRGCEPCKIVqveqDDVVESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSG 308
Cdd:pfam00294 216 GIKTVIVTLGADGALVV----EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
...
gi 1327222203 309 AII 311
Cdd:pfam00294 292 AQT 294
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
104-292 |
7.32e-13 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 68.01 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 104 YWRSDAAVKfyfqidnlNKQADDLNKLEIalieKQVDAVYISGISIAiLDDASRERLFKAISVFSNQGGKVIFDNNYRPQ 183
Cdd:NF041332 104 YDRADAAVT--------TATPEELPLDRI----RDAEVFYTSGITPA-LSETLAETTAALLEAAQEAGTTTAFDLNYRSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 184 LWSTEQAQHWYAKLLPLVDIALITEDDDLLVWGNSESVQQRCLRL----GCQEIVIKRGCEPCkiVQVEQDDVVESYVSA 259
Cdd:NF041332 171 LWSPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHGLaseyDFETVVVTRGEEGA--LALHDGEVHEQPAYE 248
|
170 180 190
....*....|....*....|....*....|...
gi 1327222203 260 TrvsNVVDTCAAGDSFAAGYLAARLTGESAIEA 292
Cdd:NF041332 249 A---DTVDPIGTGDAFVGGFLARRLAGGDVPTA 278
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
196-312 |
5.55e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 65.82 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 196 KLLPLVDIALITEDD-----DLLVWGnSESVQQRCLRLGCQE---------IVIKRGCEPCKIVQveqDDVVESY-VSAT 260
Cdd:PTZ00247 210 QVLPYVDILFGNEEEaktfaKAMKWD-TEDLKEIAARIAMLPkysgtrprlVVFTQGPEPTLIAT---KDGVTSVpVPPL 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1327222203 261 RVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAIIP 312
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
56-309 |
2.72e-07 |
|
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: 51.06 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 56 LGSDELSQNMIDGWQLEGIQTHFVERIPNKLPGLYMVETDETGERhfhywrsdaavkfyfQI-----DNLNKQADDLNKL 130
Cdd:TIGR02152 54 VGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGEN---------------RIvvvagANAELTPEDIDAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 131 EIALIEKQVdavYISGISIAIldDASRErlfkAISVFSNQGGKVIFdnNYRPQLWSTEQAqhwyakLLPLVDI------- 203
Cdd:TIGR02152 119 EALIAESDI---VLLQLEIPL--ETVLE----AAKIAKKHGVKVIL--NPAPAIKDLDDE------LLSLVDIitpnete 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 204 -ALITEDDdllvWGNSESVQ---QRCLRLGCQEIVIKRGCEPCKIVqvEQDDVVesYVSATRVsNVVDTCAAGDSFAAGY 279
Cdd:TIGR02152 182 aEILTGIE----VTDEEDAEkaaEKLLEKGVKNVIITLGSKGALLV--SKDESK--LIPAFKV-KAVDTTAAGDTFNGAF 252
|
250 260 270
....*....|....*....|....*....|
gi 1327222203 280 LAARLTGESAIEAAKLGHQLASTVIQYSGA 309
Cdd:TIGR02152 253 AVALAEGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-310 |
1.20e-90 |
|
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: 272.14 E-value: 1.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 9 IVFFGECMVEISGSP---------LTKKFGGDTLNTALYLSRLTqhqnLSVHYATGLGSDELSQNMIDGWQLEGIQTHFV 79
Cdd:cd01166 2 VVTIGEVMVDLSPPGggrleqadsFRKFFGGAEANVAVGLARLG----HRVALVTAVGDDPFGRFILAELRREGVDTSHV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 80 ERIPNKLPGLYMVETDETGERHFHYWRSDAAVKFYfqidnlnkQADDLNKLEIAliekQVDAVYISGISIAILDDAsRER 159
Cdd:cd01166 78 RVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRL--------TPEDLDEAALA----GADHLHLSGITLALSESA-REA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 160 LFKAISVFSNQGGKVIFDNNYRPQLWSTEQAQHWYAKLLPLVDIALITEDDDLLVWGNSESVQQ----RCLRLGCQEIVI 235
Cdd:cd01166 145 LLEALEAAKARGVTVSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAaeraLALALGVKAVVV 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327222203 236 KRGCEPCKIVqveqDDVVESYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:cd01166 225 KLGAEGALVY----TGGGRVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-310 |
3.42e-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: 3.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 8 NIVFFGECMVEIS--------------GSPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEG 73
Cdd:COG0524 1 DVLVIGEALVDLVarvdrlpkggetvlAGSFRRSPGGAAANVAVALARL----GARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 74 IQTHFVERIPNKLPGLYMVETDETGERHFHYWRSdAAVKFyfqidnlnkQADDLNKLEIAliekQVDAVYISGISIAilD 153
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRG-ANAEL---------TPEDLDEALLA----GADILHLGGITLA--S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 154 DASRERLFKAISVFSNQGGKVIFDNNYRPQLWstEQAQHWYAKLLPLVDIALITEDDDLLVWGNS--ESVQQRCLRLGCQ 231
Cdd:COG0524 141 EPPREALLAALEAARAAGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEEAELLTGETdpEEAAAALLARGVK 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327222203 232 EIVIKRGCEPCKIvqVEQDDVVEsyVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:COG0524 219 LVVVTLGAEGALL--YTGGEVVH--VPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
8-311 |
4.51e-45 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 155.19 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 8 NIVFFGECMVEISG------------SPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEGIQ 75
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvrvSTVEKGPGGKGANVAVALARL----GGDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 76 THFVERIPNKLPGLYMVETDETGERHFHYWRSDAAvkfyfqidNLNKQADDLNKLEIAliekQVDAVYISGIsiaiLDDA 155
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAA--------DLTPEELEENEDLLE----NADLLYISGS----LPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 156 SRERLFKAISVFSNQGGKviFDNNYRPQLWSTEQAqhwYAKLLPLVDIALITEDDDLLVWG----NSESVQQRCLRL--- 228
Cdd:pfam00294 141 LPEATLEELIEAAKNGGT--FDPNLLDPLGAAREA---LLELLPLADLLKPNEEELEALTGakldDIEEALAALHKLlak 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 229 GCQEIVIKRGCEPCKIVqveqDDVVESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSG 308
Cdd:pfam00294 216 GIKTVIVTLGADGALVV----EGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
...
gi 1327222203 309 AII 311
Cdd:pfam00294 292 AQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
8-310 |
1.29e-33 |
|
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: 125.06 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 8 NIVFFGECMVEI------SGSPLTKKFGGDTLNTALYLSRLTQHqnlsVHYATGLGSDELSQNMIDGWQLEGIQTHFVER 81
Cdd:cd01167 1 KVVCFGEALIDFipegsgAPETFTKAPGGAPANVAVALARLGGK----AAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 82 IPNKLPGLYMVETDETGERHFHYWRSDAAvkfyfqiDNLNKQADDLNKLEialiekQVDAVYISgiSIAILDDASRERLF 161
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAA-------DLLLDTELNPDLLS------EADILHFG--SIALASEPSRSALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 162 KAISVFSNQGGKVIFDNNYRPQLW-STEQAQHWYAKLLPLVDIALITEDDdlLVW----GNSESVQQRCLRLGCQEIVIK 236
Cdd:cd01167 142 ELLEAAKKAGVLISFDPNLRPPLWrDEEEARERIAELLELADIVKLSDEE--LELlfgeEDPEEIAALLLLFGLKLVLVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 237 RGCEPCKIVqveqDDVVESYVSATRVsNVVDTCAAGDSFAAGYLAA-------RLTGESAIEAAKLGHQLASTVIQYSGA 309
Cdd:cd01167 220 RGADGALLY----TKGGVGEVPGIPV-EVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTKAGA 294
|
.
gi 1327222203 310 I 310
Cdd:cd01167 295 I 295
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
29-312 |
1.70e-18 |
|
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: 84.20 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 29 GGDTLNTALYLSRLTQhqnlSVHYATGLGSDELSQNMIDGWQLEGIQTHFVerIPNKLP-GLYMVETDETGERhfhywrS 107
Cdd:cd01168 55 GGSAANTIRGAAALGG----SAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQ--VQPDGPtGTCAVLVTPDAER------T 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 108 -----DAAVKFyfqidnlnkQADDLNKLEIalieKQVDAVYISGIsiaiLDDASRERLFKAISVFSNQGGKVIFD----- 177
Cdd:cd01168 123 mctylGAANEL---------SPDDLDWSLL----AKAKYLYLEGY----LLTVPPEAILLAAEHAKENGVKIALNlsapf 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 178 --NNYRPQLWsteqaqhwyaKLLPLVDIALITEDD--DLLVWGNSESVQQ--RCLRLGCQEIVIKRGCEPCKIVQVEQdd 251
Cdd:cd01168 186 ivQRFKEALL----------ELLPYVDILFGNEEEaeALAEAETTDDLEAalKLLALRCRIVVITQGAKGAVVVEGGE-- 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327222203 252 vvESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAIIP 312
Cdd:cd01168 254 --VYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-310 |
1.90e-17 |
|
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: 80.82 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 6 NFNIVFFGECMVEISGSPLTK----KFGGDTLNTALYLSRLTQHqnlSVHYATgLGSDELSQNMIDGWQLEGIQTHFVER 81
Cdd:cd01942 9 NYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLS---PGLVAA-VGEDFHGRLYLEELREEGVDTSHVRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 82 IPNKLPGLYMVETDETGERhfhywrsdaAVKFYfQIDNLNKQADDLNKLEIALiekqvDAVYISGISIAILDDasRErlf 161
Cdd:cd01942 85 VDEDSTGVAFILTDGDDNQ---------IAYFY-PGAMDELEPNDEADPDGLA-----DIVHLSSGPGLIELA--RE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 162 kaisvFSNQGGKVIFDNNYRPQLWSTEQAQHWyaklLPLVDIALITEDD-DLLV--WGNSESVqqrcLRLGCQEIVIKRG 238
Cdd:cd01942 145 -----LAAGGITVSFDPGQELPRLSGEELEEI----LERADILFVNDYEaELLKerTGLSEAE----LASGVRVVVVTLG 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327222203 239 CEPCKIVqvEQDDVVEsyVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:cd01942 212 PKGAIVF--EDGEEVE--VPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
29-309 |
3.18e-17 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 79.71 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 29 GGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEGIQTHFVeRIPNKLPGLYMVETDEtGERHFHYWRSd 108
Cdd:cd01940 22 GGNALNVAVYAKRL----GHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGLSNK- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 109 AAVKFYFQIDNlnkqadDLNKLeialieKQVDAVYISGISiailDDASRERLFKAISVfsnQGGKVIFDNNYRpqlWSTE 188
Cdd:cd01940 95 GGVAREHPFEA------DLEYL------SQFDLVHTGIYS----HEGHLEKALQALVG---AGALISFDFSDR---WDDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 189 QAQhwyaKLLPLVDIALITEDDDllvwgNSESVQQRCLRL---GCQEIVIKRGCEPckiVQVEQDDVVesYVSATRVSNV 265
Cdd:cd01940 153 YLQ----LVCPYVDFAFFSASDL-----SDEEVKAKLKEAvsrGAKLVIVTRGEDG---AIAYDGAVF--YSVAPRPVEV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1327222203 266 VDTCAAGDSFAAGYLAARLTGESAI-EAAKLGHQLASTVIQYSGA 309
Cdd:cd01940 219 VDTLGAGDSFIAGFLLSLLAGGTAIaEAMRQGAQFAAKTCGHEGA 263
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
104-292 |
7.32e-13 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 68.01 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 104 YWRSDAAVKfyfqidnlNKQADDLNKLEIalieKQVDAVYISGISIAiLDDASRERLFKAISVFSNQGGKVIFDNNYRPQ 183
Cdd:NF041332 104 YDRADAAVT--------TATPEELPLDRI----RDAEVFYTSGITPA-LSETLAETTAALLEAAQEAGTTTAFDLNYRSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 184 LWSTEQAQHWYAKLLPLVDIALITEDDDLLVWGNSESVQQRCLRL----GCQEIVIKRGCEPCkiVQVEQDDVVESYVSA 259
Cdd:NF041332 171 LWSPEEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHGLaseyDFETVVVTRGEEGA--LALHDGEVHEQPAYE 248
|
170 180 190
....*....|....*....|....*....|...
gi 1327222203 260 TrvsNVVDTCAAGDSFAAGYLAARLTGESAIEA 292
Cdd:NF041332 249 A---DTVDPIGTGDAFVGGFLARRLAGGDVPTA 278
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
19-312 |
3.11e-12 |
|
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: 66.03 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 19 ISGSPLTKKFGGDTLNTALYLSRLTQHqnlsVHYATGLGSDELSQNMIDGWQLEGIQTHFVERIPNKLPGLYMVETDETG 98
Cdd:cd01174 26 VLGSSFETGPGGKGANQAVAAARLGAR----VAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 99 ERhfhywrsdaavkfyfQI-----DNLNKQADDLNKLEiALIEKqvdavyiSGISIA---ILDDASRErlfkAISVFSNQ 170
Cdd:cd01174 102 EN---------------RIvvvpgANGELTPADVDAAL-ELIAA-------ADVLLLqleIPLETVLA----ALRAARRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 171 GGKVIFdnNYRPqlwsteqAQHWYAKLLPLVDI--------ALITEDDDLLVwGNSESVQQRCLRLGCQEIVIKRGCEPC 242
Cdd:cd01174 155 GVTVIL--NPAP-------ARPLPAELLALVDIlvpneteaALLTGIEVTDE-EDAEKAARLLLAKGVKNVIVTLGAKGA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327222203 243 KIVqveqDDVVESYVSATRVsNVVDTCAAGDSFaAGYLAARLT-GESAIEAAKLGHQLASTVIQYSGAI--IP 312
Cdd:cd01174 225 LLA----SGGEVEHVPAFKV-KAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAAAALSVTRPGAQpsIP 291
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
196-312 |
5.55e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 65.82 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 196 KLLPLVDIALITEDD-----DLLVWGnSESVQQRCLRLGCQE---------IVIKRGCEPCKIVQveqDDVVESY-VSAT 260
Cdd:PTZ00247 210 QVLPYVDILFGNEEEaktfaKAMKWD-TEDLKEIAARIAMLPkysgtrprlVVFTQGPEPTLIAT---KDGVTSVpVPPL 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1327222203 261 RVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAIIP 312
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
56-282 |
1.28e-11 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 64.19 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 56 LGSDELSQNMIDGWQLEGIQTHFVERIPNKLPGLYMVETDETGERHFHYWRSDAAVKFYfqidnlnkQADDLNKLeiali 135
Cdd:PRK09434 51 VGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADLFL--------QPQDLPPF----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 136 eKQVDAVYISgiSIAILDDASRERLFKAISVFSNQGGKVIFDNNYRPQLW-STEQAQHWYAKLLPLVDIALITEDDDLLV 214
Cdd:PRK09434 118 -RQGEWLHLC--SIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWqDEAELRECLRQALALADVVKLSEEELCFL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327222203 215 WGNSESVQQRCL---RLGCQEIVIKRGCEPCKIVQVEQddvvESYVSATRVsNVVDTCAAGDSFAAGYLAA 282
Cdd:PRK09434 195 SGTSQLEDAIYAladRYPIALLLVTLGAEGVLVHTRGQ----VQHFPAPSV-DPVDTTGAGDAFVAGLLAG 260
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
19-309 |
1.61e-10 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 61.29 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 19 ISGSPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDGWQLEGIQTHFVERIPNKLPGLYMVETDETg 98
Cdd:PTZ00292 42 LHGTSFHKGFGGKGANQAVMASKL----GAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTK- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 99 erhfhywRSDAAVKF------YFQIDNLNKQADDLNK--------LEIALiEKQVDAVYISgisiailddasRERlfkai 164
Cdd:PTZ00292 117 -------TGNNEIVIipgannALTPQMVDAQTDNIQNickylicqNEIPL-ETTLDALKEA-----------KER----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 165 svfsnqGGKVIFDNNYRPQLWSTEQAqhwyAKLLPLVDIALITEDDDLLVWG----NSESVQQ---RCLRLGCQEIVIKR 237
Cdd:PTZ00292 173 ------GCYTVFNPAPAPKLAEVEII----KPFLKYVSLFCVNEVEAALITGmevtDTESAFKaskELQQLGVENVIITL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327222203 238 GCEPCKIVQVEQDDVvesYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGA 309
Cdd:PTZ00292 243 GANGCLIVEKENEPV---HVPGKRV-KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGT 310
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
16-280 |
3.45e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 57.53 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 16 MVEISGSPLTKKF---GGDTlNTALYLSRLTQHQNLSVHyatgLGSDELSQNMIDGWQLEGIQThfVERIPNKLPG---- 88
Cdd:PLN02341 104 MEELAASPPDKKSweaGGNC-NFAIAAARLGLRCSTIGH----VGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGdsss 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 89 ------LYMVETDETGeRHFHYWRSDaavkfyFQIDNLNKQADDL-NKLEIALieKQVDAVYISGIsiaILDDASRERLF 161
Cdd:PLN02341 177 asyetlLCWVLVDPLQ-RHGFCSRAD------FGPEPAFSWISKLsAEAKMAI--RQSKALFCNGY---VFDELSPSAIA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 162 KAISVFSNQGGKVIFDNNYRPQ--LWSTEQAQHWYAKLLPLVDIALITEDD--DLLVWGNSESVQQRCLRLGC--QEIVI 235
Cdd:PLN02341 245 SAVDYAIDVGTAVFFDPGPRGKslLVGTPDERRALEHLLRMSDVLLLTSEEaeALTGIRNPILAGQELLRPGIrtKWVVV 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1327222203 236 KRGCEPCkiVQVEQDDVveSYVSATRVsNVVDTCAAGDSFAA----GYL 280
Cdd:PLN02341 325 KMGSKGS--ILVTRSSV--SCAPAFKV-NVVDTVGCGDSFAAaialGYI 368
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
139-284 |
1.84e-07 |
|
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: 50.56 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 139 VDAVYISGISIAilddasRERLFKAISVFSNQGGKVIFDNNYRPQLWSTEQaqhwYAKLLPLVDI--------ALITEDD 210
Cdd:cd00287 58 ADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE----LEKLLPGVDIltpneeeaEALTGRR 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327222203 211 DLLVWGNSESVQQRcLRLGCQEIVIKRGCEPCkIVQVEQDDVVESyvsATRVSNVVDTCAAGDSFAAGYLAARL 284
Cdd:cd00287 128 DLEVKEAAEAAALL-LSKGPKVVIVTLGEKGA-IVATRGGTEVHV---PAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
233-312 |
2.40e-07 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 51.64 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 233 IVIKRGCEPckiVQVEQDDVVESY-VSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAII 311
Cdd:PLN02548 249 VVITQGADP---TVVAEDGKVKEFpVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTY 325
|
.
gi 1327222203 312 P 312
Cdd:PLN02548 326 P 326
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
56-309 |
2.72e-07 |
|
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: 51.06 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 56 LGSDELSQNMIDGWQLEGIQTHFVERIPNKLPGLYMVETDETGERhfhywrsdaavkfyfQI-----DNLNKQADDLNKL 130
Cdd:TIGR02152 54 VGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGEN---------------RIvvvagANAELTPEDIDAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 131 EIALIEKQVdavYISGISIAIldDASRErlfkAISVFSNQGGKVIFdnNYRPQLWSTEQAqhwyakLLPLVDI------- 203
Cdd:TIGR02152 119 EALIAESDI---VLLQLEIPL--ETVLE----AAKIAKKHGVKVIL--NPAPAIKDLDDE------LLSLVDIitpnete 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 204 -ALITEDDdllvWGNSESVQ---QRCLRLGCQEIVIKRGCEPCKIVqvEQDDVVesYVSATRVsNVVDTCAAGDSFAAGY 279
Cdd:TIGR02152 182 aEILTGIE----VTDEEDAEkaaEKLLEKGVKNVIITLGSKGALLV--SKDESK--LIPAFKV-KAVDTTAAGDTFNGAF 252
|
250 260 270
....*....|....*....|....*....|
gi 1327222203 280 LAARLTGESAIEAAKLGHQLASTVIQYSGA 309
Cdd:TIGR02152 253 AVALAEGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
264-309 |
3.91e-07 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 50.51 E-value: 3.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1327222203 264 NVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGA 309
Cdd:PRK09813 214 TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
3-280 |
2.27e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.38 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 3 ASSNFNIVFFGE---------CMVEISGSPLTKKF-GGDTLNTALYLSRLTQhqnlSVHYATGLGSDELSQNMIDGWQLE 72
Cdd:PLN02323 7 TAESSLVVCFGEmlidfvptvSGVSLAEAPAFKKApGGAPANVAVGISRLGG----SSAFIGKVGDDEFGHMLADILKKN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 73 GIQTHFVERIPNKLPGLYMVETDETGERHFHYWRSDAAvkfyfqiDNLNKQADdlnkLEIALIEKQvdAVYISGiSIAIL 152
Cdd:PLN02323 83 GVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSA-------DMLLRESE----LDLDLIRKA--KIFHYG-SISLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 153 DDASRERLFKAISVFSNQGGKVIFDNNYRPQLW-STEQAQHWYAKLLPLVDIALITEDDDLLVWGNSESVQQRCLRL--- 228
Cdd:PLN02323 149 TEPCRSAHLAAMKIAKEAGALLSYDPNLRLPLWpSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLwhp 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1327222203 229 GCQEIVIKRGCEPCKIVQVEQDDVVESYvsatRVsNVVDTCAAGDSFAAGYL 280
Cdd:PLN02323 229 NLKLLLVTEGEEGCRYYTKDFKGRVEGF----KV-KAVDTTGAGDAFVGGLL 275
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
220-308 |
4.56e-05 |
|
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: 44.34 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 220 SVQQRCLRLGCQE---IVIKRGCEPCKIVQVE-QDDVVESYvsatRVSnVVDTCAAGDSFAAGYLAARLTGESAIEAAKL 295
Cdd:cd01944 202 AAEASALRIYAKTaapVVVRLGSNGAWIRLPDgNTHIIPGF----KVK-AVDTIGAGDTHAGGMLAGLAKGMSLADAVLL 276
|
90
....*....|...
gi 1327222203 296 GHQLASTVIQYSG 308
Cdd:cd01944 277 ANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
223-312 |
4.76e-05 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 44.36 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 223 QRCLRLGCQEIVIKRGCEPCkiVQVEQDDVVesYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLAST 302
Cdd:COG1105 207 RELLERGAENVVVSLGADGA--LLVTEDGVY--RAKPPKV-EVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAA 281
|
90
....*....|
gi 1327222203 303 VIQYSGAIIP 312
Cdd:COG1105 282 AALSPGTGLP 291
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
158-308 |
1.84e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 42.86 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 158 ERLFKAISVFSNQGGKVIFDnnyrpqLWSTEQAQHWYAKLLPL-----VDIALITEDDDL-LVWGNSESVQQRCLR-LG- 229
Cdd:PLN02379 191 EVIEAAIRLAKQEGLSVSLD------LASFEMVRNFRSPLLQLlesgkIDLCFANEDEAReLLRGEQESDPEAALEfLAk 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 230 -CQEIVIKRGCEPCkiVQVEQDDVVEsyVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSG 308
Cdd:PLN02379 265 yCNWAVVTLGSKGC--IARHGKEVVR--VPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
251-310 |
2.18e-04 |
|
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: 42.02 E-value: 2.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327222203 251 DVVESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESAIEAAKLGHQLASTVIQYSGAI 310
Cdd:cd01947 206 PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
266-319 |
2.53e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.49 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1327222203 266 VDTCAAGDSFAAGYLAARLTGESAIEAA-KLGHQLASTVIQYSGAIIPVSAMNHL 319
Cdd:PLN02813 347 VDTCGAGDAYAAGILYGLLRGVSDLRGMgELAARVAATVVGQQGTRLRVEDAVEL 401
|
|
| |
