|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
17-649 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1054.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 17 AAGRSRDIVCLGRLGVDLYAQQVGARLEDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCD 96
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 97 TSHVRVDHDRLTALVLLGLKDRDTFPLIFYRENCADMAVDARDFDEAFIASSKALLITGTHFSTEQVNRTSLTALDYARR 176
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 177 NNVRTVLDIDYRPVLWGLTGKADGETRFVASEGVSAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGATLL 256
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 257 VKRGPLGCQIVEGAVPASMDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAM 336
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 337 PTPAELDYFLreaaADPVRMRRPDRDATLARLHRVTPARTPRDEVLGFAFDHRNQFFDLVQQTGASEARIAYLKNLFVEA 416
Cdd:COG3892 321 PTWEELDYFL----ARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 417 VVQTERTLGLQGRIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSVPLVFDHGRSIGTTLASWPIEHTVKCLVQFHPDE 496
Cdd:COG3892 397 AAQVAAGAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 497 PIEQRLEQEAQLRALYDATQASGHELLLEVIPPRlnGKPNAPDTVYRALKRLYNIGIYPEWWKLEPTGAAQWREIDALIA 576
Cdd:COG3892 477 PAELRLEQEAQLRRLYDACRRSGHELLLEVIPPK--DGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIA 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2102983513 577 ERDPYCRGVVLLGLSAPIDQLVEGFRAAAASNTCRGFTVGRSIFYEPSVAWLAGEIGDDEVIARARRAFETLI 649
Cdd:COG3892 555 ERDPYCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLI 627
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
341-649 |
1.64e-174 |
|
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.
Pssm-ID: 430888 Cd Length: 310 Bit Score: 499.50 E-value: 1.64e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 341 ELDYFLREAAADPvrmrRPDRDATLARLHRVTPARTPRDEVLGFAFDHRNQFFDLVQQTGASEARIAYLKNLFVEAVVQT 420
Cdd:pfam09863 1 ELDYFLSRGERVP----RPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 421 ERTLGLQGRIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSVPLVFDHGRSIGTTLASWPIEHTVKCLVQFHPDEPIEQ 500
Cdd:pfam09863 77 AQEAGLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 501 RLEQEAQLRALYDATQASGHELLLEVIPPRlnGKPNAPDTVYRALKRLYNIGIYPEWWKLEPTGAAQWREIDALIAERDP 580
Cdd:pfam09863 157 RAEQEAQLRELYDACRKSGHELLLEVIPPK--DGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102983513 581 YCRGVVLLGLSAPIDQLVEGFRAAAASNTCRGFTVGRSIFYEPSVAWLAGEIGDDEVIARARRAFETLI 649
Cdd:pfam09863 235 YCRGVVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLI 303
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
21-346 |
3.47e-147 |
|
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: 429.71 E-value: 3.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 21 SRDIVCLGRLGVDLYAQQVGARLEDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHV 100
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 101 RVDHDRLTALVLLGLKDRDTFPLIFYRENCADMAVDARDFDEAFIASSKALLITGTHFSTEQVNRTSLTALDYARRNNVR 180
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 181 TVLDIDYRPVLWGltgkadgetrfvASEGVSAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGATLLVKRG 260
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 261 PLGCQIVEGAvpasmDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAMPTPA 340
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 2102983513 341 ELDYFL 346
Cdd:TIGR04382 304 ELEAFL 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
23-333 |
3.89e-85 |
|
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: 269.45 E-value: 3.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQQVGaRLEDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRV 102
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 103 DHDRLTALVLLGLKDRDTFPLIFYRENCADMAVDARDFDEAFIASSKALLITGTHFSTEQVNR-TSLTALDYARRNNVRT 181
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALSESAReALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 182 VLDIDYRPVLWGLtgkadgetrfvasEGVSAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREV--TGATLLVKR 259
Cdd:cd01166 160 SFDLNYRPKLWSA-------------EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALalGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102983513 260 GPLGCQIVEGA----VPAsmddlpmqrgVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCA 333
Cdd:cd01166 227 GAEGALVYTGGgrvfVPA----------YPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
23-342 |
2.90e-77 |
|
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: 249.03 E-value: 2.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQ----QVGARLEDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTS 98
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 99 HVRVDHDRLTALVLLGLKDRDTFPLIFYRenCADMAVDARDFDEAFIASSKALLITGTHFSTEQVNRTSLTALDYARRNN 178
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 179 VRTVLDIDYRPVLWgltgkadgetrfvasEGVSAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGATLLVK 258
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 259 RGPLGCQIVEGavpasmDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAMPT 338
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 2102983513 339 PAEL 342
Cdd:COG0524 298 REEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
23-333 |
2.67e-48 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 171.37 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQQVGARLED--VSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHV 100
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 101 RVDHDRLTALVL-LGLKDRDTFpLIFYRENCADMAVDARDFDEAFIASSKALLITGthFSTEQVNRTSLTALDYARRNNv 179
Cdd:pfam00294 81 VIDEDTRTGTALiEVDGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISG--SLPLGLPEATLEELIEAAKNG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 180 rTVLDIDYRPVLWGLTGKadgetrfvasegvsahLQRILPLFDLVIGTEEEFRIAGGK-----EALVDALKRVREVTGAT 254
Cdd:pfam00294 157 -GTFDPNLLDPLGAAREA----------------LLELLPLADLLKPNEEELEALTGAklddiEEALAALHKLLAKGIKT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102983513 255 LLVKRGPLGCQIVEGAvpasmDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCA 333
Cdd:pfam00294 220 VIVTLGADGALVVEGD-----GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
24-331 |
5.69e-44 |
|
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: 159.72 E-value: 5.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 24 IVCLGRLGVDLYAQQVGarleDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVD 103
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 104 HDRLTALVLLGLKDRD--TFplIFYRENCADMAVDARDFDEAFiasSKALLItgtHFSTE-QVNRTS----LTALDYARR 176
Cdd:cd01167 78 PAAPTTLAFVTLDADGerSF--EFYRGPAADLLLDTELNPDLL---SEADIL---HFGSIaLASEPSrsalLELLEAAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 177 NNVRTVLDIDYRPVLWgltgkADGETRFvasegvsAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGATLL 256
Cdd:cd01167 150 AGVLISFDPNLRPPLW-----RDEEEAR-------ERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 257 VKRGPLGCQI----VEGAVPasmddlpmqrGVEVDVLNVLGAGDAFASGFLSGWLRD-------ATLEDCARSANACGAL 325
Cdd:cd01167 218 VTRGADGALLytkgGVGEVP----------GIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGAL 287
|
....*.
gi 2102983513 326 VVSRHG 331
Cdd:cd01167 288 TCTKAG 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
24-351 |
1.96e-32 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 128.20 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 24 IVCLGRLGVDLYAQQVGARLEDVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVD 103
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 104 HDRLTALVLLGLKDRDTFPLIFYRENCADMAVDARDFDEAFIASSKALlitgtHFS-----TEQVNRTSLTALDYARRNN 178
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIF-----HYGsisliTEPCRSAHLAAMKIAKEAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 179 VRTVLDIDYRPVLWgltgkadgETRFVASEGVSAhlqrILPLFDLVIGTEEE--FRIAGGKEALVDALKRVREvTGATLL 256
Cdd:PLN02323 168 ALLSYDPNLRLPLW--------PSAEAAREGIMS----IWDEADIIKVSDEEveFLTGGDDPDDDTVVKLWHP-NLKLLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 257 VKRGPLGC----QIVEGAVPasmddlpmqrGVEVDVLNVLGAGDAFASGFLSGWLRDAT-LEDCAR------SANACGAL 325
Cdd:PLN02323 235 VTEGEEGCryytKDFKGRVE----------GFKVKAVDTTGAGDAFVGGLLSQLAKDLSlLEDEERlrealrFANACGAI 304
|
330 340
....*....|....*....|....*.
gi 2102983513 326 VVSRHGCAPAMPTPAELDYFLREAAA 351
Cdd:PLN02323 305 TTTERGAIPALPTKEAVLKLLKKAVA 330
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
23-332 |
7.71e-31 |
|
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: 123.11 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQ-----------QVG-------ARLEDVSTFAKYL---GGSSANIAFGCARLGLKSAMLTRVGDDH 81
Cdd:cd01168 3 DVLGLGNALVDILAQvddafleklglKKGdmiladmEEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGDDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 82 MGRFLVETLAKEGCDTsHVRVDHDRLTA--LVLLGLKDRDTfpLIFYRENCADMAVDarDFDEAFIASSKALLITGTHFS 159
Cdd:cd01168 83 LGDFLLKDLRAAGVDT-RYQVQPDGPTGtcAVLVTPDAERT--MCTYLGAANELSPD--DLDWSLLAKAKYLYLEGYLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 160 TEqvNRTSLTALDYARRNNVRTVLDidyrpvlwgltgkadgetrFVASEGVSAH---LQRILPLFDLVIGTEEEFRI--- 233
Cdd:cd01168 158 VP--PEAILLAAEHAKENGVKIALN-------------------LSAPFIVQRFkeaLLELLPYVDILFGNEEEAEAlae 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 234 AGGKEALVDALKRVREVTGaTLLVKRGPLGCQIVEGA----VPAsmddLPmqrgvEVDVLNVLGAGDAFASGFLSGWLRD 309
Cdd:cd01168 217 AETTDDLEAALKLLALRCR-IVVITQGAKGAVVVEGGevypVPA----IP-----VEKIVDTNGAGDAFAGGFLYGLVQG 286
|
330 340
....*....|....*....|...
gi 2102983513 310 ATLEDCARSANACGALVVSRHGC 332
Cdd:cd01168 287 EPLEECIRLGSYAAAEVIQQLGP 309
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
23-338 |
9.81e-29 |
|
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: 116.50 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQ-----QVGARLEdVSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDT 97
Cdd:cd01174 1 KVVVVGSINVDLVTRvdrlpKPGETVL-GSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 98 SHVRVDHDRLT--ALVLLglkDRDtfplifyRENC------ADMAVDARDFDEA--FIASSKALLITGthfstEQVNRTS 167
Cdd:cd01174 80 SYVEVVVGAPTgtAVITV---DES-------GENRivvvpgANGELTPADVDAAleLIAAADVLLLQL-----EIPLETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 168 LTALDYARRNNVRTVLDidyrPVlwgltgkadgetrfvaseGVSAHLQRILPLFDLVIGTEEEF-RIAGGKEALVDALKR 246
Cdd:cd01174 145 LAALRAARRAGVTVILN----PA------------------PARPLPAELLALVDILVPNETEAaLLTGIEVTDEEDAEK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 247 VrevtgATLLVKRGPlGCQIV----EGAVPASMDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANAC 322
Cdd:cd01174 203 A-----ARLLLAKGV-KNVIVtlgaKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAA 276
|
330
....*....|....*.
gi 2102983513 323 GALVVSRHGCAPAMPT 338
Cdd:cd01174 277 AALSVTRPGAQPSIPT 292
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
54-343 |
2.06e-28 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 115.80 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 54 GGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRDTFPLIFYRENCADM 133
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 134 AVDARDF-----DEAFIASSKALlitgthfSTEQVNRTSLTALDYARRNNVRTVLDIDYRPVLWgltgKADGETRFVase 208
Cdd:PRK09434 108 FLQPQDLppfrqGEWLHLCSIAL-------SAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLW----QDEAELREC--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 209 gvsahLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTG-ATLLVKRGPlgcqivEGAVPASMDDLPMQRGVEVD 287
Cdd:PRK09434 174 -----LRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRYPiALLLVTLGA------EGVLVHTRGQVQHFPAPSVD 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102983513 288 VLNVLGAGDAFASGFLSG------WLRDATLEDCARSANACGALVVSRHGCAPAMPTPAELD 343
Cdd:PRK09434 243 PVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
23-332 |
2.42e-28 |
|
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: 115.10 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYAQQVGARLEDVSTFAK----YLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTS 98
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 99 HVRVdhdrltalvllglKDRDTFPLIFYRENCADMAV------DARDFDEAFIASSKALLItGTHFSTEQVnrtsLTALD 172
Cdd:cd01942 81 HVRV-------------VDEDSTGVAFILTDGDDNQIayfypgAMDELEPNDEADPDGLAD-IVHLSSGPG----LIELA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 173 YARRNNVRTVLdIDYRPVLWGLTGKAdgetrfvasegvsahLQRILPLFDLVIGTEEEFRI----AGGKEALVDALKRVr 248
Cdd:cd01942 143 RELAAGGITVS-FDPGQELPRLSGEE---------------LEEILERADILFVNDYEAELlkerTGLSEAELASGVRV- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 249 evtgatLLVKRGPLGCQIVEGAVPASMDDLPmqrgvEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVS 328
Cdd:cd01942 206 ------VVVTLGPKGAIVFEDGEEVEVPAVP-----AVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVE 274
|
....
gi 2102983513 329 RHGC 332
Cdd:cd01942 275 RRGA 278
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
24-331 |
8.06e-21 |
|
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: 92.80 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 24 IVCLGRLGVDLYAQQVGArledvstfakYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVD 103
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 104 HdRLTALVLLGLKDRDTfplIFYRENCADMAvDARDFDEAFIASSKALLItgtHFSTEQVNRTSLTALDYARRNNVRTVL 183
Cdd:cd01940 72 E-GENAVADVELVDGDR---IFGLSNKGGVA-REHPFEADLEYLSQFDLV---HTGIYSHEGHLEKALQALVGAGALISF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 184 DIDYRpvlwgltgkadgetrfvaseGVSAHLQRILPLFDLVIGTEEEFriagGKEALVDALKRVREVTGATLLVKRGPLG 263
Cdd:cd01940 144 DFSDR--------------------WDDDYLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGEDG 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102983513 264 CQIVEGAVPASmddlpmQRGVEVDVLNVLGAGDAFASGFLSGWLR-DATLEDCARSANACGALVVSRHG 331
Cdd:cd01940 200 AIAYDGAVFYS------VAPRPVEVVDTLGAGDSFIAGFLLSLLAgGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
54-338 |
9.93e-20 |
|
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: 90.05 E-value: 9.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 54 GGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRDTfplIFYRENCADM 133
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDR---ATISITAIDT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 134 AVDARDFDEAFIASSKALLITGtHFSTeqvnrTSLTALDYARRNNVRTVLDIDyrpvlwgltgkadgetrfvasEGVSAH 213
Cdd:cd01945 113 QAAPDSLPDAILGGADAVLVDG-RQPE-----AALHLAQEARARGIPIPLDLD---------------------GGGLRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 214 LQRILPLFDLVIGTEEEFRIAGGkEALVDALKRVREVTGATLLVKRGPLGCQIVEGA-----VPAsmddlpmqrgVEVDV 288
Cdd:cd01945 166 LEELLPLADHAICSENFLRPNTG-SADDEALELLASLGIPFVAVTLGEAGCLWLERDgelfhVPA----------FPVEV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2102983513 289 LNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAMPT 338
Cdd:cd01945 235 VDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
51-331 |
2.16e-19 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 88.26 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 51 KYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRlTALVLLGLKDRDTfplIF--YRE 128
Cdd:PRK09813 20 AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGV-TAQTQVELHDNDR---VFgdYTE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 129 NC-ADMAVDarDFDEAFIASSKaLLITGTHFSTEQV-----NRTSLTALDYARRNN----VRTVLDIDYrpvlwgLTGKA 198
Cdd:PRK09813 96 GVmADFALS--EEDYAWLAQYD-IVHAAIWGHAEDAfpqlhAAGKLTAFDFSDKWDsplwQTLVPHLDY------AFASA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 199 DGETRFVasegvsahlqrilplfdlvigteeefriaggKEALVDALKRVREVTGATlLVKRGPL---GCQIVEGAVpasm 275
Cdd:PRK09813 167 PQEDEFL-------------------------------RLKMKAIVARGAGVVIVT-LGENGSIawdGAQFWRQAP---- 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2102983513 276 ddlpmqrgVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHG 331
Cdd:PRK09813 211 --------EPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
46-331 |
9.39e-19 |
|
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: 86.70 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 46 VSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEG-CDTSHVRVDHDRLTALVLLGLKDRDTFpli 124
Cdd:cd01947 28 SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGdKHTVAWRDKPTRKTLSFIDPNGERTIT--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 125 fyRENCADMAvdarDFDEAFIASSKALLITGTHFSTEQVNRTSLTALdyarrnnvrtvldidyrpVLWGLTGKADgetrf 204
Cdd:cd01947 105 --VPGERLED----DLKWPILDEGDGVFITAAAVDKEAIRKCRETKL------------------VILQVTPRVR----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 205 vasegvSAHLQRILPLFDLVIGTEEEFriAGGKEALVDALKRVRevtgaTLLVKRGPLGCQIVEG----AVPAsmddlpm 280
Cdd:cd01947 156 ------VDELNQALIPLDILIGSRLDP--GELVVAEKIAGPFPR-----YLIVTEGELGAILYPGgrynHVPA------- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2102983513 281 qrgVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHG 331
Cdd:cd01947 216 ---KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
23-348 |
2.91e-18 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 86.33 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 23 DIVCLGRLGVDLYA-----QQVGARLEDVStFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDT 97
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVGETLHGTS-FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 98 SHVRVDHDRLT--ALVLLGLKDRDTFPLIFYRENCA---DMAVDARDFdeafIASSKALLITGTHFSTEqvnrTSLTALD 172
Cdd:PTZ00292 96 SFVSRTENSSTglAMIFVDTKTGNNEIVIIPGANNAltpQMVDAQTDN----IQNICKYLICQNEIPLE----TTLDALK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 173 YARRNNVRTVLDIDYRPvlwgltgkADGETRFVASegvsahlqrILPLFDLVIGTEEEFRIAGGKEA--LVDALKRVRE- 249
Cdd:PTZ00292 168 EAKERGCYTVFNPAPAP--------KLAEVEIIKP---------FLKYVSLFCVNEVEAALITGMEVtdTESAFKASKEl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 250 -VTGA-TLLVKRGPLGCQIVEgavpasMDDLPMQ-RGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALV 326
Cdd:PTZ00292 231 qQLGVeNVIITLGANGCLIVE------KENEPVHvPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAIS 304
|
330 340
....*....|....*....|..
gi 2102983513 327 VSRHGCAPAMPTPAELDYFLRE 348
Cdd:PTZ00292 305 VTRHGTQSSYPHPSELPADVKE 326
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
24-328 |
1.27e-16 |
|
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: 80.82 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 24 IVCLGRLGVDLYAQ-----QVGARLEDVSTFAkyLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTs 98
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 99 HVRVDHDRLTALVLLGL-KDRDTfpLIfyreNCADMAV------DARDFDEAFIASSKALLITGThfSTEQVNRTSLTal 171
Cdd:cd01941 79 RGIVFEGRSTASYTAILdKDGDL--VV----ALADMDIyelltpDFLRKIREALKEAKPIVVDAN--LPEEALEYLLA-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 172 dYARRNNVRTVLDIdyrpvlwgltgkadgetrfvASEGVSAHLQRILPLFDLVIGTEEEFRI-----AGGKEALVDALKR 246
Cdd:cd01941 149 -LAAKHGVPVAFEP--------------------TSAPKLKKLFYLLHAIDLLTPNRAELEAlagalIENNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 247 VREVTGATLLVKRGPLGCQIVEGAVPASMDDLPMqrGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALV 326
Cdd:cd01941 208 LLLPGIKNVIVTLGAKGVLLSSREGGVETKLFPA--PQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
..
gi 2102983513 327 VS 328
Cdd:cd01941 286 LE 287
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
42-348 |
2.72e-14 |
|
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: 74.15 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 42 RLEDVSTFAkylGGSSANIAFGCARLGLKSAMLTRVGDDHmGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRDTf 121
Cdd:TIGR03168 26 RVAAVRKDA---GGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESSGEET- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 122 plifyRENCADMAVDARDFDE------AFIASSKALLITG-------THFSTEQVNRtsltaldyARRNNVRTVLDIDyR 188
Cdd:TIGR03168 101 -----ELNEPGPEISEEELEQlleklrELLASGDIVVISGslppgvpPDFYAQLIAI--------ARKKGAKVILDTS-G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 189 PVLWgltgkadgetrfvasEGVSAHLQRILP-------LFDLVIGTEEEFrIAGGKEALVDALKRVrevtgatlLVKRGP 261
Cdd:TIGR03168 167 EALR---------------EALAAKPFLIKPnheeleeLFGRELKTLEEI-IEAARELLDRGAENV--------LVSLGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 262 lgcqivEGAVPASMDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGcaPAMPTPAE 341
Cdd:TIGR03168 223 ------DGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPED 294
|
....*..
gi 2102983513 342 LDYFLRE 348
Cdd:TIGR03168 295 VEELLDQ 301
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
42-348 |
1.77e-13 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 71.70 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 42 RLEDVSTFAkylGGSSANIAFGCARLGLKSAMLTRVGDdHMGRFLVETLAKEGCDTSHVRVDHD-RlTALVLLGLKDRDT 120
Cdd:COG1105 26 RASEVRLDP---GGKGINVARVLKALGVDVTALGFLGG-FTGEFIEELLDEEGIPTDFVPIEGEtR-INIKIVDPSDGTE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 121 fplifYRENCADMAVDARDFDEAF------IASSKALLITGT---HFSTEQVNRtsLTALdyARRNNVRTVLDidyrpvl 191
Cdd:COG1105 101 -----TEINEPGPEISEEELEALLerleelLKEGDWVVLSGSlppGVPPDFYAE--LIRL--ARARGAKVVLD------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 192 wgltgkADGET-RFVASEGVsahlqrilplfDLVIGTEEEFR-IAGGK----EALVDALKRVREvTGATL-LVKRGPlgc 264
Cdd:COG1105 165 ------TSGEAlKAALEAGP-----------DLIKPNLEELEeLLGRPletlEDIIAAARELLE-RGAENvVVSLGA--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 265 qivEGAVPASMDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGcaPAMPTPAELDY 344
Cdd:COG1105 224 ---DGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEE 298
|
....
gi 2102983513 345 FLRE 348
Cdd:COG1105 299 LLAQ 302
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
42-331 |
2.92e-13 |
|
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: 70.64 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 42 RLEDVSTFAkylGGSSANIAFGCARLGLKSAMLTRVGDDhMGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRDTf 121
Cdd:cd01164 27 RVSSTRKDA---GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGTET- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 122 plifyRENCADMAVDARDFdEAFIASSKALLITGTHF----STEQ-VNRTSLTAL-DYARRNNVRTVLDIDYRPVLWGLT 195
Cdd:cd01164 102 -----EINEPGPEISEEEL-EALLEKLKALLKKGDIVvlsgSLPPgVPADFYAELvRLAREKGARVILDTSGEALLAALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 196 GKADgetrfvasegvsahlqrilplfdLVIGTEEEF-----RIAGGKEALVDALKRVREvtgatllvkrgpLGCQIV--- 267
Cdd:cd01164 176 AKPF-----------------------LIKPNREELeelfgRPLGDEEDVIAAARKLIE------------RGAENVlvs 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2102983513 268 ---EGAVPASMDDLPMQRGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHG 331
Cdd:cd01164 221 lgaDGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
6-324 |
3.78e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 69.09 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 6 STASRSTPGRFAAGRSRDIVCLGRLGVDL-----------------YAQQVGARLEDvstfAKYL-GGSSANIAFGCARL 67
Cdd:PLN02341 57 RRRLGDTEVGSAAGKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPD----KKSWeAGGNCNFAIAAARL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 68 GLKSAMLTRVGDDHMGRFLVETLAKEGCDT--------SHVRVDHDRLTAL--VLLGLKDRDTF---------PLIfyrE 128
Cdd:PLN02341 133 GLRCSTIGHVGDEIYGKFLLDVLAEEGISVvgliegtdAGDSSSASYETLLcwVLVDPLQRHGFcsradfgpePAF---S 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 129 NCADMAVDARdfdeAFIASSKALLITGTHF---STEQVnrtsLTALDYARRNNVRTVLDIDYRpvlwgltgkadGETRFV 205
Cdd:PLN02341 210 WISKLSAEAK----MAIRQSKALFCNGYVFdelSPSAI----ASAVDYAIDVGTAVFFDPGPR-----------GKSLLV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 206 ASEGVSAHLQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGAT--LLVKRGPlgcqivEGAVPASMDDLPMQRG 283
Cdd:PLN02341 271 GTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGS------KGSILVTRSSVSCAPA 344
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2102983513 284 VEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGA 324
Cdd:PLN02341 345 FKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
51-342 |
2.67e-11 |
|
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: 64.89 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 51 KYLGGSsANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDhDRLTALvllglKDR---DTFPLI-FY 126
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDE-GRPTTT-----KTRviaRNQQLLrVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 127 RENCADMAVDARD----FDEAFIASSKALLIT--GTHFSTEqvnRTSLTALDYARRNNVRTVLDidyrPvlwgltgKADG 200
Cdd:cd01172 110 REDDSPLSAEEEQrlieRIAERLPEADVVILSdyGKGVLTP---RVIEALIAAARELGIPVLVD----P-------KGRD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 201 ETRFVAsegvsahlqrilplFDLVIGTEEEFRIAGGKEA-----LVDALKRVREVTGA-TLLVKRGPLGCQIVEG----- 269
Cdd:cd01172 176 YSKYRG--------------ATLLTPNEKEAREALGDEIndddeLEAAGEKLLELLNLeALLVTLGEEGMTLFERdgevq 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2102983513 270 AVPAsmddlpmqrgVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAmpTPAEL 342
Cdd:cd01172 242 HIPA----------LAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPV--TPKEL 302
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
42-348 |
3.99e-11 |
|
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: 64.53 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 42 RLEDVSTFAkylGGSSANIAFGCARLGLKSAMLTRVGDDHmGRFLVETLAKEGCDTSHVRVDHD------------RLTA 109
Cdd:TIGR03828 26 RVESTRIDA---GGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPGEtrinvkikepsgTETK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 110 LVLLGlkdrdtfPLIfyRENCADMAVD-----ARDFDEAFIASSKALLITGTHFSTeqvnrtsLTALdyARRNNVRTVLD 184
Cdd:TIGR03828 102 LNGPG-------PEI--SEEELEALLEklraqLAEGDWLVLSGSLPPGVPPDFYAE-------LIAL--AREKGAKVILD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 185 IDYRPVLwgltgkadgetrfvasEGVSAHLQRILP-------LFDLVIGTEEEFrIAGGKEALVDALKRVrevtgatlLV 257
Cdd:TIGR03828 164 TSGEALR----------------DGLKAKPFLIKPndeeleeLFGRELKTLEEI-IEAARELLDLGAENV--------LI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 258 KRGPLGCQIV--EGAVPASmddlpmqrGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGcaPA 335
Cdd:TIGR03828 219 SLGADGALLVtkEGALFAQ--------PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TG 288
|
330
....*....|...
gi 2102983513 336 MPTPAELDYFLRE 348
Cdd:TIGR03828 289 LPDPEDIEELLPQ 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
54-348 |
1.38e-10 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 62.96 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 54 GGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRDtfplifyrENC--- 130
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEG--------ENSigi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 131 -----ADMAVDARDFDEAFIASSKALLItgthfSTEQVNRTSLTALDYARRNNVRTVLDidyrPvlwgltgkadGETRFV 205
Cdd:PRK11142 111 haganAALTPALVEAHRELIANADALLM-----QLETPLETVLAAAKIAKQHGTKVILN----P----------APAREL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 206 ASEgvsahlqrILPLFDLVIGTEEEFRIAGGKEA--LVDALKrvrevtGATLLVKRGP------LGCQIV-------EGA 270
Cdd:PRK11142 172 PDE--------LLALVDIITPNETEAEKLTGIRVedDDDAAK------AAQVLHQKGIetvlitLGSRGVwlsengeGQR 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102983513 271 VPasmddlpmqrGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCAPAMPTPAELDYFLRE 348
Cdd:PRK11142 238 VP----------GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQE 305
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
46-331 |
1.03e-09 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 60.13 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 46 VSTFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTS-HVRVDHDRLTALVLLGLKDRDTFPLI 124
Cdd:cd01944 27 EAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILlPPRGGDDGGCLVALVEPDGERSFISI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 125 FYRENcadmAVDARDFDEAFIASSKALLITGTHFSTEQVNRTSLtaLDYARRNNVRTVLDIDYRPVLWGLTGkadgetrf 204
Cdd:cd01944 107 SGAEQ----DWSTEWFATLTVAPYDYVYLSGYTLASENASKVIL--LEWLEALPAGTTLVFDPGPRISDIPD-------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 205 vasegvsAHLQRILPLFDLVIGTEEEFRIAGGKEALV--DALKRVREVTGATLLVKRGPLGCQIVEGA-----VPasmdd 277
Cdd:cd01944 173 -------TILQALMAKRPIWSCNREEAAIFAERGDPAaeASALRIYAKTAAPVVVRLGSNGAWIRLPDgnthiIP----- 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2102983513 278 lpmqrGVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHG 331
Cdd:cd01944 241 -----GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
137-307 |
1.21e-08 |
|
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: 55.56 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 137 ARDFDEAFIASSKALLITGTHFSTEQVnrtsLTALDYARRNNVRTVLDIDYRPVLWGLTGkadgetrfvasegvsahLQR 216
Cdd:cd00287 47 ARLGVSVTLVGADAVVISGLSPAPEAV----LDALEEARRRGVPVVLDPGPRAVRLDGEE-----------------LEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 217 ILPLFDLVIGTEEEFRIAGGKEALVD-----ALKRVREVTGATLLVKRGPLGCQIV-----EGAVPAsmddlpmqrgVEV 286
Cdd:cd00287 106 LLPGVDILTPNEEEAEALTGRRDLEVkeaaeAAALLLSKGPKVVIVTLGEKGAIVAtrggtEVHVPA----------FPV 175
|
170 180
....*....|....*....|.
gi 2102983513 287 DVLNVLGAGDAFASGFLSGWL 307
Cdd:cd00287 176 KVVDTTGAGDAFLAALAAGLA 196
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
77-337 |
1.95e-08 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 56.57 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 77 VGDDHMGRFLVETLAKEGCDTsHVRVDHDRLTAL--VLLGLKDRDTFPLIFYRENCADMAVDARDFDEAfIASSKALLIT 154
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTcaVLVCGKERSLVANLGAANHLSAEHMQSHAVQEA-IKTAQLYYLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 155 GtHFSTEQVNRTSLTAlDYARRNNVRTVLDIDyRPVLwgltgkadgetrfvaSEGVSAHLQRILPLFDLVIGTEEEFRIA 234
Cdd:PTZ00247 167 G-FFLTVSPNNVLQVA-KHARESGKLFCLNLS-APFI---------------SQFFFERLLQVLPYVDILFGNEEEAKTF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 235 G-----GKEALVDALKRV-----------REVTG-----ATLLVKRGplgcQIVEGAVPAsmddlpmqrgVEVD-VLNVL 292
Cdd:PTZ00247 229 AkamkwDTEDLKEIAARIamlpkysgtrpRLVVFtqgpePTLIATKD----GVTSVPVPP----------LDQEkIVDTN 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2102983513 293 GAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCA-PAMP 337
Cdd:PTZ00247 295 GAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
44-327 |
6.99e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 55.18 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 44 EDVSTFAKYLGGSSANIAFG-CARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRLTALVLL--GLKDRDT 120
Cdd:PLN02379 76 DDLSPIKTMAGGSVANTIRGlSAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLvdALGNRTM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 121 FPlifyrenCADMAV--DARDFDEAFIASSKALLITGTHFSTEQVNRtsltALDYARRNNVRTVLDI-------DYRPVL 191
Cdd:PLN02379 156 RP-------CLSSAVklQADELTKEDFKGSKWLVLRYGFYNLEVIEA----AIRLAKQEGLSVSLDLasfemvrNFRSPL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 192 WGLTGKADGETRFvASEGVSAHLqrilplfdlvIGTEEEFriagGKEALVDALKRVREVTGATLlvkrGPLGC------Q 265
Cdd:PLN02379 225 LQLLESGKIDLCF-ANEDEAREL----------LRGEQES----DPEAALEFLAKYCNWAVVTL----GSKGCiarhgkE 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102983513 266 IVEgaVPASmddlpmqrgVEVDVLNVLGAGDAFASGFLSGWLRDATLEDCARSANACGALVV 327
Cdd:PLN02379 286 VVR--VPAI---------GETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVV 336
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
49-119 |
1.17e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 51.45 E-value: 1.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102983513 49 FAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHVRVDHDRLTALVLLGLKDRD 119
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKFRD 237
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
214-307 |
1.15e-05 |
|
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: 47.46 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 214 LQRILPLFDLVIGTEEEFRIAGGKEALVDALKRVREVTGATLLVKRGPLGCQIVEG----AVPAsmddLPMQrgvevDVL 289
Cdd:cd01946 157 LKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPA----YPLE-----SVF 227
|
90
....*....|....*...
gi 2102983513 290 NVLGAGDAFASGFLsGWL 307
Cdd:cd01946 228 DPTGAGDTFAGGFI-GYL 244
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
293-338 |
8.86e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 45.09 E-value: 8.86e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2102983513 293 GAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHGCA-PAMPT 338
Cdd:PLN02548 284 GAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTyPEKPD 330
|
|
| PLN02967 |
PLN02967 |
kinase |
25-192 |
8.66e-04 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 42.34 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 25 VCLGRLGVDLYAQQVGARLEDV----STFAKYLGGSSANIAFGCARLGLKSAMLTRVGDDHMGRFLVETLAKEGCDTSHV 100
Cdd:PLN02967 210 VPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 101 RVDHDRLTALVLLGLKDRDTFPLIFYREnCADMAVDARDFDEAFIASSKaLLITGTHFSTEQVNRTSLT-ALDYARRNNV 179
Cdd:PLN02967 290 CIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAK-MFYFNTHSLLDPTMRSTTLrAIKISKKLGG 367
|
170
....*....|...
gi 2102983513 180 RTVLDIDYRPVLW 192
Cdd:PLN02967 368 VIFYDLNLPLPLW 380
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
210-331 |
3.29e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 40.18 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983513 210 VSAHLQRILPLFDLVIGT-------EEEF-----RI----AGGKEALVDALKRVREVTgaTLLVKRGPLGCQIV----EG 269
Cdd:PLN02630 147 VVVDIQALIRVFDPVDGTvklvkleETGFydmlpRIgflkASSEEALFIDVEEVRQKC--CVIVTNGKKGCRIYwkdgEM 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2102983513 270 AVPAsmddLPmqrGVEVDVLnvlGAGDAFASGFLSGWLRDATLEDCARSANACGALVVSRHG 331
Cdd:PLN02630 225 RVPP----FP---AIQVDPT---GAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| |
