|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
1-485 |
0e+00 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 835.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 1 MYHHAFSLKFHSFSPHYALSLsnfstqspnpllPPFARVPHVTSSVCLRCRSSAADVSPVIYADGSSSICSFGETGDVAV 80
Cdd:PLN02341 1 MQAHRLIGQLGAFSPHPGLSS------------PPSPHGHLVPRRVCSRCRASARASSRARAGARSRARRRLGDTEVGSA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 81 VEKPIDVSTLGNLCVDIVLSVHELPPPSRGERKALMDELSMSPPDKKYWEAGGNCNMAIAAARLGLHCVAIGHVGDEIYG 160
Cdd:PLN02341 69 AGKEIDVATLGNLCVDIVLPVPELPPPSREERKAYMEELAASPPDKKSWEAGGNCNFAIAAARLGLRCSTIGHVGDEIYG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 161 EFLLDVLHEEGIGTVALNGGTNEKDTSS-FCETLICWVLVDPLQRHGFCSRADFKEEPAFSWITDLSDEVKMAIRQSKVL 239
Cdd:PLN02341 149 KFLLDVLAEEGISVVGLIEGTDAGDSSSaSYETLLCWVLVDPLQRHGFCSRADFGPEPAFSWISKLSAEAKMAIRQSKAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 240 FCNGYDFDDFSPSFIMSTIDYAAKVGTAIFFDPGPRGKSLSKGTPDERRALAHFLRMSDVLLLTSEEVEALTGIRNPVKA 319
Cdd:PLN02341 229 FCNGYVFDELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 320 GQEILRNGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATA 399
Cdd:PLN02341 309 GQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 400 MGCGAGRNVAKRHQVVDLMKASKLNDEEKFFEQLLaENSESSRINLLSKGMIKDGrsnKQLIETISMEKVVSELLAELEL 479
Cdd:PLN02341 389 MGCGAGRNVATLEKVLELLRASNLNEDDTFWAELL-KNSDCSEISFLSKMAINGG---SNGIVRVAATKVVSELLPSLEE 464
|
....*.
gi 15222179 480 GRCCVK 485
Cdd:PLN02341 465 ARERGI 470
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
86-414 |
1.55e-54 |
|
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: 184.70 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 86 DVSTLGNLCVDIVLSVHELPppsRGERKALMDELSMSPpdkkyweAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLD 165
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLP---KGGETVLAGSFRRSP-------GGAAANVAVALARLGARVALVGAVGDDPFGDFLLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 166 VLHEEGIGTVALnGGTNEKDTSsfcetlICWVLVDP-LQRH-GFCSRADFKEEPAfswitDLSDEvkmAIRQSKVLFCNG 243
Cdd:COG0524 71 ELRAEGVDTSGV-RRDPGAPTG------LAFILVDPdGERTiVFYRGANAELTPE-----DLDEA---LLAGADILHLGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 244 YDFD-DFSPSFIMSTIDYAAKVGTAIFFDPGPRGKSLSKGtpdeRRALAHFLRMSDVLLLTSEEVEALTGIRNPVKAGQE 322
Cdd:COG0524 136 ITLAsEPPREALLAALEAARAAGVPVSLDPNYRPALWEPA----RELLRELLALVDILFPNEEEAELLTGETDPEEAAAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 323 ILRngKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAMGC 402
Cdd:COG0524 212 LLA--RGVKLVVVTLGAEGALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRP 289
|
330
....*....|..
gi 15222179 403 GAGRNVAKRHQV 414
Cdd:COG0524 290 GAQPALPTREEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
86-404 |
1.13e-38 |
|
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: 142.33 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 86 DVSTLGNLCVDIVlsvhelppPSRGERKALMDELSMSPpdkkyweAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLD 165
Cdd:cd01166 1 DVVTIGEVMVDLS--------PPGGGRLEQADSFRKFF-------GGAEANVAVGLARLGHRVALVTAVGDDPFGRFILA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 166 VLHEEGIgtvalnggtnekDTSsfcetlicWVLVDPLQRHG--FCSRADFKEEPAFSWI-------TDLSDEVKMAIRQS 236
Cdd:cd01166 66 ELRREGV------------DTS--------HVRVDPGRPTGlyFLEIGAGGERRVLYYRagsaasrLTPEDLDEAALAGA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 237 KVLFCNGYdfddfSPSFIMSTID-------YAAKVGTAIFFDPGPRGKSLSKgtPDERRALAHFLRMSDVLLLTSEEVEA 309
Cdd:cd01166 126 DHLHLSGI-----TLALSESAREallealeAAKARGVTVSFDLNYRPKLWSA--EEAREALEELLPYVDIVLPSEEEAEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 310 LTGIRNPVKAGQEILRNGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLT 389
Cdd:cd01166 199 LLGDEDPTDAAERALALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALR 278
|
330
....*....|....*
gi 15222179 390 IANAVGAATAMGCGA 404
Cdd:cd01166 279 FANAAAALVVTRPGD 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
92-404 |
2.49e-38 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 141.33 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 92 NLCVDIVLSVHELPPPSRGERKALMDELSMSPpdkkyweAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEG 171
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKGP-------GGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 172 IGT--VALNGGTNekdtssfceTLICWVLVDPLQRHGFCsradFKEEPAFSWITDLSDEVKMAIRQSKVLFCNGYdFDDF 249
Cdd:pfam00294 75 VDTdyVVIDEDTR---------TGTALIEVDGDGERTIV----FNRGAAADLTPEELEENEDLLENADLLYISGS-LPLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 250 SPSFIMSTIDYAAKVGTaiFFDPGPRGKSLSKgtpdeRRALAHFLRMSDVLLLTSEEVEALTG-----IRNPVKAGQEIL 324
Cdd:pfam00294 141 LPEATLEELIEAAKNGG--TFDPNLLDPLGAA-----REALLELLPLADLLKPNEEELEALTGaklddIEEALAALHKLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 325 RngKGTKWVIVKMGPKGSILVTKSSVS-VAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAA--TAMG 401
Cdd:pfam00294 214 A--KGIKTVIVTLGADGALVVEGDGEVhVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALvvQKSG 291
|
...
gi 15222179 402 CGA 404
Cdd:pfam00294 292 AQT 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
86-404 |
4.38e-36 |
|
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: 135.37 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 86 DVSTLGNLCVDIVLSVHELPPPsrGErKALMDELSMSPpdkkyweaGGN-CNMAIAAARLGLHCVAIGHVGDEIYGEFLL 164
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKP--GE-TVLGSSFETGP--------GGKgANQAVAAARLGARVAMIGAVGDDAFGDELL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 165 DVLHEEGIGTVALNGGTNEK--------DTSSfcETLIcwvLVDPLqrhgfcsrADFKEEPAfswitdLSDEVKMAIRQS 236
Cdd:cd01174 70 ENLREEGIDVSYVEVVVGAPtgtavitvDESG--ENRI---VVVPG--------ANGELTPA------DVDAALELIAAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 237 KVLFCNGydfdDFSPSFIMSTIDYAAKVGTAIFFDPGPrgkslskGTPDerraLAHFLRMSDVLLLTSEEVEALTGI--- 313
Cdd:cd01174 131 DVLLLQL----EIPLETVLAALRAARRAGVTVILNPAP-------ARPL----PAELLALVDILVPNETEAALLTGIevt 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 314 --RNPVKAGQEILRngKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIA 391
Cdd:cd01174 196 deEDAEKAARLLLA--KGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
330
....*....|...
gi 15222179 392 NAVGAATAMGCGA 404
Cdd:cd01174 274 NAAAALSVTRPGA 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
110-404 |
9.17e-34 |
|
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: 128.91 E-value: 9.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 110 GErkALMDELSMSPPDKKYWE--AGGNC-NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTVALNGGTNEKdt 186
Cdd:cd01167 6 GE--ALIDFIPEGSGAPETFTkaPGGAPaNVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 187 ssfceTLIcwVLVdPLQRHGfcSRA-DFKEEPAFSWITDlSDEVKMAIRQSKVLFCNGYDF-DDFSPSFIMSTIDYAAKV 264
Cdd:cd01167 82 -----TTL--AFV-TLDADG--ERSfEFYRGPAADLLLD-TELNPDLLSEADILHFGSIALaSEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 265 GTAIFFDPGPRGkSLSKGTPDERRALAHFLRMSDVLLLTSEEVEALTGIRNPVKAGQEILRNGkgTKWVIVKMGPKGSIL 344
Cdd:cd01167 151 GVLISFDPNLRP-PLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFG--LKLVLVTRGADGALL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222179 345 VTKSSVSVAPAFKVEVVDTVGCGDSFVAAI--ALGYIRNM-----PLVNTLTIANAVGAATAMGCGA 404
Cdd:cd01167 228 YTKGGVGEVPGIPVEVVDTTGAGDAFVAGLlaQLLSRGLLaldedELAEALRFANAVGALTCTKAGA 294
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
87-379 |
1.84e-32 |
|
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: 122.59 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 87 VSTLGNLCVDIVLSVHELPPPsrgerkalmdELSMSPPDKKYWEAGGNCNMAIAAARLGLHCVAIGHvgdeiygeflldv 166
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLP----------GGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 167 lheegigtvalnggtnekdtssfcetlicwvlvdplqrhgfcsradfkeepafswitdlsdevkmairqsKVLFCNGYDF 246
Cdd:cd00287 59 ----------------------------------------------------------------------DAVVISGLSP 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 247 ddfSPSFIMSTIDYAAKVGTAIFFDPGPRGKSLskgtpdERRALAHFLRMSDVLLLTSEEVEALTGIRNP---VKAGQEI 323
Cdd:cd00287 69 ---APEAVLDALEEARRRGVPVVLDPGPRAVRL------DGEELEKLLPGVDILTPNEEEAEALTGRRDLevkEAAEAAA 139
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222179 324 LRNGKGTKWVIVKMGPKGSILVT-KSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYI 379
Cdd:cd00287 140 LLLSKGPKVVIVTLGEKGAIVATrGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
86-404 |
3.36e-30 |
|
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: 118.57 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 86 DVSTLGNLCVDIVLSVHELPPPsrgERKALMDELSMSPPdkkyweaGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLD 165
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGP---FESVLVKDLRREFG-------GSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 166 VLHEEGIGTvalnGGTNEKDTSSfceTLICWVLVDplqrhGFCSRADFKEEPAFSWITDlsDEVKMAIRQSKVL-FCNGY 244
Cdd:cd01942 71 ELREEGVDT----SHVRVVDEDS---TGVAFILTD-----GDDNQIAYFYPGAMDELEP--NDEADPDGLADIVhLSSGP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 245 DFDDFSPSFimstidyaAKVGTAIFFDPGPRgksLSKGTPDErraLAHFLRMSDVLLLTSEE---VEALTGIRNPVKAgq 321
Cdd:cd01942 137 GLIELAREL--------AAGGITVSFDPGQE---LPRLSGEE---LEEILERADILFVNDYEaelLKERTGLSEAELA-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 322 eilrngKGTKWVIVKMGPKGSILVTKS-SVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAM 400
Cdd:cd01942 201 ------SGVRVVVVTLGPKGAIVFEDGeEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVE 274
|
....
gi 15222179 401 GCGA 404
Cdd:cd01942 275 RRGA 278
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
89-420 |
1.39e-26 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 109.07 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 89 TLgNLCVDIVLSVHELPPpsrgERKALMDELSMSPpdkkyweAGGNCNMAIAAARLGLHCVAIGHVGDEIyGEFLLDVLH 168
Cdd:COG1105 5 TL-NPALDRTYEVDELEP----GEVNRASEVRLDP-------GGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 169 EEGIGT--VALNGgtnekdtssfcETLICWVLVDPlqrhgfcsrADFKE----EPAFSW----ITDLSDEVKMAIRQSKV 238
Cdd:COG1105 72 EEGIPTdfVPIEG-----------ETRINIKIVDP---------SDGTEteinEPGPEIseeeLEALLERLEELLKEGDW 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 239 LFCNGydfddfS------PSFIMSTIDYAAKVGTAIFFDpgprgkslskgTPDErrALAHFLRMS-DVLLLTSEEVEALT 311
Cdd:COG1105 132 VVLSG------SlppgvpPDFYAELIRLARARGAKVVLD-----------TSGE--ALKAALEAGpDLIKPNLEELEELL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 312 GIRNP-----VKAGQEILRngKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVN 386
Cdd:COG1105 193 GRPLEtlediIAAARELLE--RGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
330 340 350
....*....|....*....|....*....|....
gi 15222179 387 TLTIANAVGAATAMGCGAGrnVAKRHQVVDLMKA 420
Cdd:COG1105 271 ALRLAVAAGAAAALSPGTG--LPDREDVEELLAQ 302
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
84-402 |
4.24e-22 |
|
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: 96.53 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 84 PIDVSTLGNLCVDIVLSVHELPPPSRGERK--------ALMDELSMSPPDKKywEAGGNC-NMAIAAARLGLHCVAIGHV 154
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKgdmiladmEEQEELLAKLPVKY--IAGGSAaNTIRGAAALGGSAAFIGRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 155 GDEIYGEFLLDVLHEEGIGTVALNGGTNEKDTssfcetliCWVLVDPLQRHGFC----SRADFKEEpafswitdlsDEVK 230
Cdd:cd01168 79 GDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGT--------CAVLVTPDAERTMCtylgAANELSPD----------DLDW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 231 MAIRQSKVLFCNGYdFDDFSPSFIMSTIDYAAKVGTAIFFDpgprgksLSkgTPDE----RRALAHFLRMSDVLLLTSEE 306
Cdd:cd01168 141 SLLAKAKYLYLEGY-LLTVPPEAILLAAEHAKENGVKIALN-------LS--APFIvqrfKEALLELLPYVDILFGNEEE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 307 VEALTGI--RNPVKAGQEILRngKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVE-VVDTVGCGDSFVAAIALGYIRNMP 383
Cdd:cd01168 211 AEALAEAetTDDLEAALKLLA--LRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEP 288
|
330 340
....*....|....*....|.
gi 15222179 384 LVNTLTIANAVGAA--TAMGC 402
Cdd:cd01168 289 LEECIRLGSYAAAEviQQLGP 309
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
131-400 |
1.33e-20 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 92.25 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 131 AGGNCNMAIAAARLGLHCVAIGHVGDEiYGEFLLDVLHEEGIGT--VALNGgtnekdtssfcETLICWVLVDPlqrhgfc 208
Cdd:TIGR03168 35 GGKGINVARVLARLGAEVVATGFLGGF-TGEFIEALLAEEGIKNdfVEVKG-----------ETRINVKIKES------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 209 SRADFKE-EPAFSwITD-----LSDEVKMAIRQSKVLFCNGYDFDDFSPSFIMSTIDYAAKVGTAIFFDPGprGKSLskg 282
Cdd:TIGR03168 96 SGEETELnEPGPE-ISEeeleqLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKVILDTS--GEAL--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 283 tpdeRRALA---HFLRMSDvllltsEEVEALTG-----IRNPVKAGQEILrnGKGTKWVIVKMGPKGSILVTKSSVSVAP 354
Cdd:TIGR03168 170 ----REALAakpFLIKPNH------EELEELFGrelktLEEIIEAARELL--DRGAENVLVSLGADGALLVTKEGALKAT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15222179 355 AFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAM 400
Cdd:TIGR03168 238 PPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAF 283
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
305-400 |
1.55e-20 |
|
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: 91.44 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 305 EEVEALTGIRNP-----VKAGQEILrnGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYI 379
Cdd:cd01164 186 EELEELFGRPLGdeedvIAAARKLI--ERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLA 263
|
90 100
....*....|....*....|.
gi 15222179 380 RNMPLVNTLTIANAVGAATAM 400
Cdd:cd01164 264 QGLSLEEALRLAVAAGSATAF 284
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
90-396 |
6.68e-18 |
|
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: 84.01 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 90 LGNLCVDIVLSVHELPPPSrGERKAlmdelsmsppDKKYWEAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHE 169
Cdd:cd01944 5 IGAAVVDIVLDVDKLPASG-GDIEA----------KSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 170 EGIGTValngGTNEKDTSSFCetliCWVLVDPLQRHGFCS----RADFKEEpafsWITDLSdevkmaIRQSKVLFCNGYD 245
Cdd:cd01944 74 EGIEIL----LPPRGGDDGGC----LVALVEPDGERSFISisgaEQDWSTE----WFATLT------VAPYDYVYLSGYT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 246 FDD--FSPSFIMSTIDyAAKVGTAIFFDPGPRGKSLSKgtpderralaHFLR--MSDVLLLTS--EEVEALTGiRNPVKA 319
Cdd:cd01944 136 LASenASKVILLEWLE-ALPAGTTLVFDPGPRISDIPD----------TILQalMAKRPIWSCnrEEAAIFAE-RGDPAA 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222179 320 GQEILRNGKGTKW-VIVKMGPKGS-ILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGA 396
Cdd:cd01944 204 EASALRIYAKTAApVVVRLGSNGAwIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
136-410 |
2.62e-16 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 79.59 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 136 NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTVALNggTNEKDTSSFcetlicwVLVDpLQRHGfcsradfke 215
Cdd:PRK09434 33 NVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLR--LDPAHRTST-------VVVD-LDDQG--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 216 EPAFSWItdlsdevkmaIRQSKVLFCNGYDFDDFSPS--FIMSTIDYAA---------------KVGTAIFFDPGPRgKS 278
Cdd:PRK09434 94 ERSFTFM----------VRPSADLFLQPQDLPPFRQGewLHLCSIALSAepsrsttfeamrrikAAGGFVSFDPNLR-ED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 279 LSKGTPDERRALAHFLRMSDVLLLTSEEVEALTGIRNpVKAGQEILRNGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKV 358
Cdd:PRK09434 163 LWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQ-LEDAIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15222179 359 EVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAmgCGAGRNVAK 410
Cdd:PRK09434 242 DPVDTTGAGDAFVAGLLAGLSQAGLWTDEAELAEIIAQAQA--CGALATTAK 291
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
131-405 |
7.22e-16 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 78.01 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 131 AGGN-CNMAIAAARLGLHCVAIGHVGDEiYGEFLLDVLHEEGIGT--VALNGgtnekdtssfcETLICWVLVDPLQRH-- 205
Cdd:TIGR03828 34 AGGKgINVSRVLKNLGVDVVALGFLGGF-TGDFIEALLREEGIKTdfVRVPG-----------ETRINVKIKEPSGTEtk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 206 ----GFCSRADFKEEpafswitdLSDEVKMAIRQSKVLFCNGYDFDDFSPSFIMSTIDYAAKVGTAIFFDPGprGKSLSK 281
Cdd:TIGR03828 102 lngpGPEISEEELEA--------LLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKVILDTS--GEALRD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 282 GtpderralahfLRMSDVLLL-TSEEVEALTGiRNP------VKAGQEILrnGKGTKWVIVKMGPKGSILVTKSSVSVAP 354
Cdd:TIGR03828 172 G-----------LKAKPFLIKpNDEELEELFG-RELktleeiIEAARELL--DLGAENVLISLGADGALLVTKEGALFAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15222179 355 AFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAMGCGAG 405
Cdd:TIGR03828 238 PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTG 288
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
131-396 |
5.75e-15 |
|
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: 75.02 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 131 AGGNC-NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTVALNggTNEKDTSSFceTLICWVLVDPLQRHGFCS 209
Cdd:cd01945 35 GGGNAaNAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIV--VAPGARSPI--SSITDITGDRATISITAI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 210 RADFKEEPAFSWITDLSDEVKMAIRQSKVlfcngydfddfspSFIMSTIDYAAKVGTAIFFDPGprgkslskGTPDERRA 289
Cdd:cd01945 111 DTQAAPDSLPDAILGGADAVLVDGRQPEA-------------ALHLAQEARARGIPIPLDLDGG--------GLRVLEEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 290 LAHflrmSDVLLLTSEEVEALTGIRNPVKAgqEILRNgKGTKWVIVKMGPKGSILV--TKSSVSVaPAFKVEVVDTVGCG 367
Cdd:cd01945 170 LPL----ADHAICSENFLRPNTGSADDEAL--ELLAS-LGIPFVAVTLGEAGCLWLerDGELFHV-PAFPVEVVDTTGAG 241
|
250 260
....*....|....*....|....*....
gi 15222179 368 DSFVAAIALGYIRNMPLVNTLTIANAVGA 396
Cdd:cd01945 242 DVFHGAFAHALAEGMPLREALRFASAAAA 270
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
131-396 |
6.55e-15 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 75.29 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 131 AGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIgtvalnggtnekDTSSFCE-----TLICWVLVDplQRH 205
Cdd:cd01172 39 LGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI------------DTDGIVDegrptTTKTRVIAR--NQQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 206 GFcsRADFKEEPAFSwiTDLSDEVKMAIRQS----KVLFCNGYDFDDFSPSFIMSTIDYAAKVGTAIFFDPGPRGKSLSK 281
Cdd:cd01172 105 LL--RVDREDDSPLS--AEEEQRLIERIAERlpeaDVVILSDYGKGVLTPRVIEALIAAARELGIPVLVDPKGRDYSKYR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 282 G----TPDERralahflrmsdvllltseEVEALTGIRNP-----VKAGQEILRNgKGTKWVIVKMGPKGSILVTKSSVSV 352
Cdd:cd01172 181 GatllTPNEK------------------EAREALGDEINdddelEAAGEKLLEL-LNLEALLVTLGEEGMTLFERDGEVQ 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15222179 353 A-PAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGA 396
Cdd:cd01172 242 HiPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAG 286
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
119-422 |
5.57e-14 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 72.73 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 119 LSMSPPDKKYwEAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTVALNGGTNEKDTSSFCeTLicwvl 198
Cdd:PLN02323 32 LAEAPAFKKA-PGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFV-TL----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 199 vdplqrhgfcsRADFKEEpaFSWITDLS-------DEVKMA-IRQSKVlfcngydFDDFSPSFI--------MSTIDYAA 262
Cdd:PLN02323 105 -----------RSDGERE--FMFYRNPSadmllreSELDLDlIRKAKI-------FHYGSISLItepcrsahLAAMKIAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 263 KVGTAIFFDPGPRgKSLSKGTPDERRALAHFLRMSDVLLLTSEEVEALTGIRNP-----VKAGQEILrngkgtKWVIVKM 337
Cdd:PLN02323 165 EAGALLSYDPNLR-LPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPdddtvVKLWHPNL------KLLLVTE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 338 GPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLV-------NTLTIANAVGAATAMGCGAGRNVAK 410
Cdd:PLN02323 238 GEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLedeerlrEALRFANACGAITTTERGAIPALPT 317
|
330
....*....|..
gi 15222179 411 RHQVVDLMKASK 422
Cdd:PLN02323 318 KEAVLKLLKKAV 329
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
87-397 |
9.17e-13 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 68.21 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 87 VSTLGNLCVDIVLSVHElpPPSRGERKALMDELSmSPpdkkyweAGGNCNMAIAAARLGLHCVAIGHVGDEIYGEFLLDV 166
Cdd:cd01947 2 IAVVGHVEWDIFLSLDA--PPQPGGISHSSDSRE-SP-------GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 167 LHEEGI-GTVALNGGTNEKdtssfceTLIcwvLVDPlqrHGfcsradfkeEPAFSWITD-LSDEVKMAIrqskvlfCNGY 244
Cdd:cd01947 72 LESGGDkHTVAWRDKPTRK-------TLS---FIDP---NG---------ERTITVPGErLEDDLKWPI-------LDEG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 245 DFDDFSPSFIMSTIDYAAKVGTAIFFDPGPRGKSLSkgtpderraLAHFLRMSDVLLLTSEEVEALTgirnpvkAGQEIL 324
Cdd:cd01947 123 DGVFITAAAVDKEAIRKCRETKLVILQVTPRVRVDE---------LNQALIPLDILIGSRLDPGELV-------VAEKIA 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222179 325 rnGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAA 397
Cdd:cd01947 187 --GPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
72-396 |
1.83e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 72 FGE-TGDVAVVEKPIDVstLGNLCVDIVLSVHELPPPsrGErkalmdelSMSPPDKKYWEAGGNCNMAIAAARLGLHCVA 150
Cdd:PTZ00292 4 AGEvASHGGEAEPDVVV--VGSSNTDLIGYVDRMPQV--GE--------TLHGTSFHKGFGGKGANQAVMASKLGAKVAM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 151 IGHVGDEIYGEFLLDVLHEEGIGTVALnggTNEKDTSSFCETlicwVLVDPLQRHG---FCSRADFKEEPAFswITDLSD 227
Cdd:PTZ00292 72 VGMVGTDGFGSDTIKNFKRNGVNTSFV---SRTENSSTGLAM----IFVDTKTGNNeivIIPGANNALTPQM--VDAQTD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 228 EVKmaiRQSKVLFCNgydfDDFSPSFIMSTIDYAAKVGTAIFFDPGPRGKslskgtPDERRALAHFLRMSDVLLLTSEEV 307
Cdd:PTZ00292 143 NIQ---NICKYLICQ----NEIPLETTLDALKEAKERGCYTVFNPAPAPK------LAEVEIIKPFLKYVSLFCVNEVEA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 308 EALTGIR-----NPVKAGQEILRngKGTKWVIVKMGPKGSILVTKSSVSV-APAFKVEVVDTVGCGDSFVAAIALGYIRN 381
Cdd:PTZ00292 210 ALITGMEvtdteSAFKASKELQQ--LGVENVIITLGANGCLIVEKENEPVhVPGKRVKAVDTTGAGDCFVGSMAYFMSRG 287
|
330
....*....|....*
gi 15222179 382 MPLVNTLTIANAVGA 396
Cdd:PTZ00292 288 KDLKESCKRANRIAA 302
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
90-420 |
8.69e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 66.05 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 90 LGNLCVDIVLSVHELPPPsrGErkALMDelsmsppdKKYWEA-GGN-CNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVL 167
Cdd:PRK11142 8 LGSINADHVLNLESFPRP--GE--TLTG--------RHYQVAfGGKgANQAVAAARLGADIAFIACVGDDSIGESMRQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 168 HEEGIGTVALNGGTNEKdtssfceTLICWVLVDPLQRHGFCSRAdfkEEPAfswitDLSDEVkmaIRQSKVLFCNGydfd 247
Cdd:PRK11142 76 AKDGIDTAPVSVIKGES-------TGVALIFVNDEGENSIGIHA---GANA-----ALTPAL---VEAHRELIANA---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 248 DF------SPsfiMSTIDYAAKV----GTAIFFDPGPrGKSLskgtPDErralahFLRMSDVLLLTSEEVEALTGIR--- 314
Cdd:PRK11142 134 DAllmqleTP---LETVLAAAKIakqhGTKVILNPAP-AREL----PDE------LLALVDIITPNETEAEKLTGIRved 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 315 --NPVKAGQeILrNGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIAN 392
Cdd:PRK11142 200 ddDAAKAAQ-VL-HQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAH 277
|
330 340
....*....|....*....|....*...
gi 15222179 393 AVGAATAMGCGAGRNVAKRHQVVDLMKA 420
Cdd:PRK11142 278 AAAAIAVTRKGAQPSIPWREEIDAFLQE 305
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
282-400 |
6.11e-11 |
|
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: 62.87 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 282 GTPDErraLAHFLRMSDVLLLTSEEVEALTGIRNPVKAGQEILrnGKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVE-V 360
Cdd:cd01946 152 IKPEK---LKKVLAKVDVVIINDGEARQLTGAANLVKAARLIL--AMGPKALIIKRGEYGALLFTDDGYFAAPAYPLEsV 226
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15222179 361 VDTVGCGDSFVAAIaLGYIRNMPLVNTLTIANAVGAATAM 400
Cdd:cd01946 227 FDPTGAGDTFAGGF-IGYLASQKDTSEANMRRAIIYGSAM 265
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
132-399 |
6.19e-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: 62.76 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 132 GGNC-NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTvalnggtnekdtsSFCET------LICWVLVDPLQR 204
Cdd:cd01940 22 GGNAlNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDI-------------SHCRVkegenaVADVELVDGDRI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 205 HGFCSRADFKEEPAFSwiTDLSdevkmAIRQSKVLFCNGYDFDDFSPSfIMSTIDYAakvGTAIFFDPGPRGKSlskgtP 284
Cdd:cd01940 89 FGLSNKGGVAREHPFE--ADLE-----YLSQFDLVHTGIYSHEGHLEK-ALQALVGA---GALISFDFSDRWDD-----D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 285 DERRALAH----FLRMSDvllLTSEEVEALTGirnpvkagqEILRNGkgTKWVIVKMGPKGSILVTKSSVSVAPAFKVEV 360
Cdd:cd01940 153 YLQLVCPYvdfaFFSASD---LSDEEVKAKLK---------EAVSRG--AKLVIVTRGEDGAIAYDGAVFYSVAPRPVEV 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 15222179 361 VDTVGCGDSFVAAIALGYIRNMplvNTLTIANAVGAATA 399
Cdd:cd01940 219 VDTLGAGDSFIAGFLLSLLAGG---TAIAEAMRQGAQFA 254
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
130-398 |
1.63e-10 |
|
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: 61.95 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 130 EAGGNC-NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGI---GTVALNGGT------NEKDTssfcETLIcwVLV 199
Cdd:cd01941 33 SPGGVGrNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLnvrGIVFEGRSTasytaiLDKDG----DLVV--ALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 200 DplqrhgfcsrADFKEEPAFSWItdlsDEVKMAIRQSKVLFCNGydfdDFSPSFIMSTIDYAAKVGTAIFFDPGPRGKSl 279
Cdd:cd01941 107 D----------MDIYELLTPDFL----RKIREALKEAKPIVVDA----NLPEEALEYLLALAAKHGVPVAFEPTSAPKL- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 280 skgtPDERRALAHFlrmsDVLLLTSEEVEALTGI----RNPVKAGQEILRnGKGTKWVIVKMGPKGSILVTKSSVS---- 351
Cdd:cd01941 168 ----KKLFYLLHAI----DLLTPNRAELEALAGAlienNEDENKAAKILL-LPGIKNVIVTLGAKGVLLSSREGGVetkl 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15222179 352 VAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAAT 398
Cdd:cd01941 239 FPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
317-396 |
6.62e-08 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 54.32 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 317 VKAGQEiLRNgKGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGA 396
Cdd:PRK09513 206 IEAAHA-LRE-QGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSA 283
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
125-398 |
9.38e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.20 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 125 DKKYweAGGN-CNMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIgtvalnggtnekDTSSF----CETLICWVLV 199
Cdd:PRK09813 18 GKAF--SGGNaVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGV------------DISHVhtkhGVTAQTQVEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 200 DPLQR-HGFCSR---ADFKeepafswitdLSDEvkmairqsKVLFCNGYDFddfspsfIMSTI------DYAA--KVGTA 267
Cdd:PRK09813 84 HDNDRvFGDYTEgvmADFA----------LSEE--------DYAWLAQYDI-------VHAAIwghaedAFPQlhAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 268 IFFDPGPRGKSlskgtPDERRALAHflrmsdVLLLTSEEVEALTGIRNPVKAGQEilrngKGTKWVIVKMGPKGSILVTK 347
Cdd:PRK09813 139 TAFDFSDKWDS-----PLWQTLVPH------LDYAFASAPQEDEFLRLKMKAIVA-----RGAGVVIVTLGENGSIAWDG 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15222179 348 SSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAAT 398
Cdd:PRK09813 203 AQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKT 253
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
289-403 |
1.56e-07 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 52.86 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 289 ALAHFLRMSDVLLL--TSEEVEALTG--IRNP---VKAGQEILRNGKgTKWVIVKMGPKGSILV-TKSSVSVAPAfKVEV 360
Cdd:PRK10294 171 ALSAALAIGNIELVkpNQKELSALVNrdLTQPddvRKAAQELVNSGK-AKRVVVSLGPQGALGVdSENCIQVVPP-PVKS 248
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15222179 361 VDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAMGCG 403
Cdd:PRK10294 249 QSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQG 291
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
151-385 |
1.40e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 50.41 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 151 IGHVGDEIYGEFLLDVLHEEGIgtVALNGGTNEKDTSSfcetliCWVLVDPLQRhgfCSRADFKEEPAFSWITDLSDEVK 230
Cdd:PTZ00247 86 VGCVGDDRFAEILKEAAEKDGV--EMLFEYTTKAPTGT------CAVLVCGKER---SLVANLGAANHLSAEHMQSHAVQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 231 MAIRQSKVLFCNGYdFDDFSPSFIMSTIDYAAKVGtAIFfdpgprgkSLSKGTP-------DERRALAHFLrmsDVLLLT 303
Cdd:PTZ00247 155 EAIKTAQLYYLEGF-FLTVSPNNVLQVAKHARESG-KLF--------CLNLSAPfisqfffERLLQVLPYV---DILFGN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 304 SEEVEAL-TGIRNPVKAGQEILR--------NGKGTKWVIVKMGPKGSILVTKS---SVSVAPAFKVEVVDTVGCGDSFV 371
Cdd:PTZ00247 222 EEEAKTFaKAMKWDTEDLKEIAAriamlpkySGTRPRLVVFTQGPEPTLIATKDgvtSVPVPPLDQEKIVDTNGAGDAFV 301
|
250
....*....|....
gi 15222179 372 AAIALGYIRNMPLV 385
Cdd:PTZ00247 302 GGFLAQYANGKDID 315
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
14-401 |
3.29e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 49.42 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 14 SPHYALSLSNFSTQSPNPLLPPFARVPHVTSSVCLRCRSSAADVspVIYADGSSSIcSFGETGDVAVVEKpIDVSTLGNL 93
Cdd:PLN02813 3 SSSTASTSPSLYVPKPNRRLRRVTSQRGAPGLFRIHSRANNAAL--AIQQDEEQPE-GFGPIPEKAVPER-WDVLGLGQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 94 CVDI-------VLSVHELPPPSRG-----ERKALMDELSMSPPDKKyweAGGN-CNMAIAAARLGLHCVA--------IG 152
Cdd:PLN02813 79 MVDFsgmvddeFLERLGLEKGTRKvinheERGKVLRALDGCSYKAS---AGGSlSNTLVALARLGSQSAAgpalnvamAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 153 HVGDEIYGEFLLDVLHEEGIGTVAL---NGGTNekdtssfceTLIcwVLVDPLQRHGFCSRAdfkeepAFSWITDLSDEV 229
Cdd:PLN02813 156 SVGSDPLGDFYRTKLRRANVHFLSQpvkDGTTG---------TVI--VLTTPDAQRTMLSYQ------GTSSTVNYDSCL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 230 KMAIRQSKVLFCNGYDFDdfspsfIMSTIDYAAKV-------GTAIFF---DPGprgkSLSKGTPDERRALAHFlrmSDV 299
Cdd:PLN02813 219 ASAISKSRVLVVEGYLWE------LPQTIEAIAQAceeahraGALVAVtasDVS----CIERHRDDFWDVMGNY---ADI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 300 LLLTSEEVEALTGI---RNPVKAGQEILRNgkgTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIAL 376
Cdd:PLN02813 286 LFANSDEARALCGLgseESPESATRYLSHF---CPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILY 362
|
410 420
....*....|....*....|....*.
gi 15222179 377 GYIRNMPLVNTL-TIANAVgAATAMG 401
Cdd:PLN02813 363 GLLRGVSDLRGMgELAARV-AATVVG 387
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
285-397 |
3.93e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 48.17 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 285 DERRALAHFLRMSDVLLLTSEEVEALtgirnpvKAGQEILRNGK--GTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVD 362
Cdd:cd01937 144 QEKLIKCVILKLHDVLKLSRVEAEVI-------STPTELARLIKetGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVD 216
|
90 100 110
....*....|....*....|....*....|....*
gi 15222179 363 TVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAA 397
Cdd:cd01937 217 PTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
328-400 |
2.70e-05 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 45.87 E-value: 2.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222179 328 KGTKWVIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAM 400
Cdd:PRK13508 213 EGIEWIIVSLGADGAFAKHNDTFYKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQ 285
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
128-394 |
9.25e-05 |
|
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: 44.32 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 128 YWEAGGNC-NMAIAAARLGLHCVAIGHVGDEIYGEFLLDVLHEEGIGTVALNGGTNEKDTSSF--------CETLICWvl 198
Cdd:cd01939 32 RWQRGGNAsNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCYRKDIDEPASSYiirsraggRTTIVND-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 199 vDPLQRhgfCSRADFK--EEPAFSWItdlSDEVKMAIRQSKVLFCngydFDDFSPSFIMSTIdyaakvgtaiffdpgprg 276
Cdd:cd01939 110 -NNLPE---VTYDDFSkiDLTQYGWI---HFEGRNPDETLRMMQH----IEEHNNRRPEIRI------------------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 277 kSLSKGTPDERRALAHFLRMSDVLLLTSEEVEALtGIRNPVKAGQEILRNGKGTKWVIVKMGPKG-SILVTKSSVSVAPA 355
Cdd:cd01939 161 -TISVEVEKPREELLELAAYCDVVFVSKDWAQSR-GYKSPEECLRGEGPRAKKAALLVCTWGDQGaGALGPDGEYVHSPA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15222179 356 FKVE-VVDTVGCGDSFVAAIALG-YIRNMPLVNTLTIANAV 394
Cdd:cd01939 239 HKPIrVVDTLGAGDTFNAAVIYAlNKGPDDLSEALDFGNRV 279
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
285-403 |
7.62e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 41.70 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222179 285 DERRALAHFLRMSDVLLLTSEEVEALTGIRNPVKAGQEILRN--GKGTKWVIVKMGPKGSILVTKSSVSVAPAFK-VEVV 361
Cdd:PLN02379 219 NFRSPLLQLLESGKIDLCFANEDEARELLRGEQESDPEAALEflAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAV 298
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15222179 362 DTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAATAMGCG 403
Cdd:PLN02379 299 DATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
333-398 |
7.71e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.63 E-value: 7.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222179 333 VIVKMGPKGSILVTKSSVSVAPAFKVEVVDTVGCGDSFVAAIALGYIRNMPLVNTLTIANAVGAAT 398
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLA 271
|
|
| |
