|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
6-645 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1084.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 6 GMGKTLDVITIGRSSVDLYGTQVGGRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVD 85
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 86 VRGVATDPDRLTALVLLGIRDETSFPLIFYRENCADMALSEEDIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARR 165
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 166 HGAKTALDIDYRPNLWGVAGHGDGESRFVESGKVTTKLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSEATLV 245
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 246 CKRGAKGAVAFEGPIPDSLDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAY 325
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 326 PSLAEMEFFLERGVIRPDLRNDEALEQIHWATNRQgrmgGDWSTMRVFAFDHRIQLEQMA---GYTPARGGAFKELCLKA 402
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRR----RQWDELCVFAFDHRSQFEDMAreaGADEARIPALKRLLLEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 403 ALKVARG---RPGYGILCDNRIGRAALHAASGTGLWIGRPCEWPGSRPLEIepELGPDCG-GLQEWARENVVKVLCFCHP 478
Cdd:COG3892 397 AAQVAAGaglRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRF--EHGRDIGsQLVEWPQEHVVKCLVFYHP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 479 DDDAATRRDQEATVKRLFTAARRNGLEFLLEVIPSKVAPVDDETTATLIRQFYAAGIYPDWWKLEPMvTRTAWANAIAAI 558
Cdd:COG3892 475 DDPAELRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPM-SAAAWQAIDALI 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 559 EAHDRHTRGIVVLGLDASEADLAASFEVAAEFDLVRGFAIGRTIFGEVAQGWLAGTIDDAEATDRMAERYARLCAIWDRA 638
Cdd:COG3892 554 AERDPYCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAA 633
|
....*..
gi 2183742573 639 RETARRA 645
Cdd:COG3892 634 RQAAAAA 640
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
11-335 |
1.22e-154 |
|
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: 447.82 E-value: 1.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 11 LDVITIGRSSVDLYGTQVGGRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVA 90
Cdd:TIGR04382 2 LDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 91 TDPDRLTALVLLGIRDETSFPLIFYRENCADMALSEEDIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRHGAKT 170
Cdd:TIGR04382 82 TDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 171 ALDIDYRPNLWGvaghgdgesrfvESGKVTTKLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSEATLVCKRGA 250
Cdd:TIGR04382 162 VLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 251 KGAVAFEGPipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPSLAE 330
Cdd:TIGR04382 230 EGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLEE 304
|
....*
gi 2183742573 331 MEFFL 335
Cdd:TIGR04382 305 LEAFL 309
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
330-639 |
1.87e-152 |
|
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: 442.49 E-value: 1.87e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 330 EMEFFLERGVIRPDLRNDEALEQIHWATNRQGrmggDWSTMRVFAFDHRIQLEQMA---GYTPARGGAFKELCLKAALKV 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRR----QWDELCVLAFDHRSQLEELAreaGADLARIPALKRLLLRAAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 407 AR--GRPG-YGILCDNRIGRAALHAASGTGLWIGRPCEWPGSRPLEIEpeLGPDCGG-LQEWARENVVKVLCFCHPDDDA 482
Cdd:pfam09863 77 AQeaGLQGgAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFE--HGRSIGSqLIEWPLEHVVKCLVFYHPDDDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 483 ATRRDQEATVKRLFTAARRNGLEFLLEVIPSKVAPVDDETTATLIRQFYAAGIYPDWWKLEPMvTRTAWANAIAAIEAHD 562
Cdd:pfam09863 155 ALRAEQEAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPL-SAAAWEQIDALIEERD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183742573 563 RHTRGIVVLGLDASEADLAASFEVAAEFDLVRGFAIGRTIFGEVAQGWLAGTIDDAEATDRMAERYARLCAIWDRAR 639
Cdd:pfam09863 234 PYCRGVVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
12-330 |
1.84e-78 |
|
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: 251.34 E-value: 1.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 12 DVITIGRSSVDLYGT----QVGGRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVR 87
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 88 GVATDPDRLTALVLLGIRDETSFPLIFYRenCADMALSEEDIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRHG 167
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 168 AKTALDIDYRPNLWGVAGhgdgesrfvesgkvtTKLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSEATLVCK 247
Cdd:COG0524 159 VPVSLDPNYRPALWEPAR---------------ELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 248 RGAKGAVAFEGpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPS 327
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
...
gi 2183742573 328 LAE 330
Cdd:COG0524 298 REE 300
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
12-322 |
4.70e-76 |
|
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: 244.79 E-value: 4.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 12 DVITIGRSSVDLYGTQvGGRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVAT 91
Cdd:cd01166 1 DVVTIGEVMVDLSPPG-GGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 92 DPDRLTALVLLGIRDETSFPLIFYRENCADMALSEEDIDEGFIAEARAVLATGTHLS-HPRTEAAVLKALTLARRHGAKT 170
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 171 ALDIDYRPNLWGvaghgdgesrfVESGKVTtkLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSE--ATLVCKR 248
Cdd:cd01166 160 SFDLNYRPKLWS-----------AEEAREA--LEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALgvKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183742573 249 GAKGAVAFEGpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCT 322
Cdd:cd01166 227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
13-320 |
1.00e-41 |
|
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: 153.18 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 13 VITIGRSSVDLYGTQVGgrleDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATD 92
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 93 PDRLTALVLLGIRD--ETSFplIFYRENCADMALsEEDIDEGFIAEARAVLaTGTH-LSHPRTEAAVLKALTLARRHGAK 169
Cdd:cd01167 78 PAAPTTLAFVTLDAdgERSF--EFYRGPAADLLL-DTELNPDLLSEADILH-FGSIaLASEPSRSALLELLEAAKKAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 170 TALDIDYRPNLWgvaghGDGESRFVESGKVttklqgtLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSEATLVCKRG 249
Cdd:cd01167 154 ISFDPNLRPPLW-----RDEEEARERIAEL-------LELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183742573 250 AKGAVAFegpipdsLDAGQTG-PGFPIEVFNVLGAGDGFFSGLLKG-------WLDGADWPTALKYANACGAFAVSRHG 320
Cdd:cd01167 222 ADGALLY-------TKGGVGEvPGIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTKAG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
12-322 |
1.07e-39 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 147.49 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 12 DVITIGRSSVDLYGTQVGGRLEDM--GSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGV 89
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVrvSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 90 ATDPDRLT--ALVLLGIRDETSFplIFYRENCADMALSEEDIDEGFIAEARAVLATGTHLSHPRtEAAVLKALTLARRHG 167
Cdd:pfam00294 81 VIDEDTRTgtALIEVDGDGERTI--VFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLP-EATLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 168 aktALDIDYRPNLWGVAghgdgesrfvesgkvtTKLQGTLHLFDLIVGTEEEF----HIAGGT-TDTLAALRAVRAVSEA 242
Cdd:pfam00294 158 ---TFDPNLLDPLGAAR----------------EALLELLPLADLLKPNEEELealtGAKLDDiEEALAALHKLLAKGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 243 TLVCKRGAKGAVAFEG----PIPdsldagqtgPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSR 318
Cdd:pfam00294 219 TVIVTLGADGALVVEGdgevHVP---------AVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
|
....
gi 2183742573 319 HGCT 322
Cdd:pfam00294 290 SGAQ 293
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
33-332 |
2.66e-28 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 115.42 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 33 EDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRD--ETSF 110
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDqgERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 111 plIFYRENCADMALSEEDIDEgF----------IAearavlatgthLSHPRTEAAVLKALTLARRHGAKTALDIDYRPNL 180
Cdd:PRK09434 98 --TFMVRPSADLFLQPQDLPP-FrqgewlhlcsIA-----------LSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 181 WGvaghGDGESRFVesgkvttkLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAV-SEATLVCKRGAKGAVA-FEG 258
Cdd:PRK09434 164 WQ----DEAELREC--------LRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRyPIALLLVTLGAEGVLVhTRG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 259 PIpdsldagQTGPGFPIEVFNVLGAGDGFFSGLLKG------WLDGADWPTALKYANACGAFAVSRHGCTPAYPSLAEME 332
Cdd:PRK09434 232 QV-------QHFPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
13-340 |
7.31e-28 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 114.72 E-value: 7.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 13 VITIGRSSVDLYGTQVGGRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATD 92
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 93 PDRLTALVLLGIRDETSFPLIFYRENCADMALSEEDIDEGFIAEARaVLATGT-HLSHPRTEAAVLKALTLARRHGAKTA 171
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAK-IFHYGSiSLITEPCRSAHLAAMKIAKEAGALLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 172 LDIDYRPNLWGVAghgdgesrfvESGKvttklQGTLHLF---DLIVGTEEE--FHIAGGTTDTLAALRAVRAVSEATLVC 246
Cdd:PLN02323 172 YDPNLRLPLWPSA----------EAAR-----EGIMSIWdeaDIIKVSDEEveFLTGGDDPDDDTVVKLWHPNLKLLLVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 247 KrGAKG----AVAFEGPIpdsldagqtgPGFPIEVFNVLGAGDGFFSGLL------KGWL-DGADWPTALKYANACGAFA 315
Cdd:PLN02323 237 E-GEEGcryyTKDFKGRV----------EGFKVKAVDTTGAGDAFVGGLLsqlakdLSLLeDEERLREALRFANACGAIT 305
|
330 340
....*....|....*....|....*
gi 2183742573 316 VSRHGCTPAYPSLAEMEFFLERGVI 340
Cdd:PLN02323 306 TTERGAIPALPTKEAVLKLLKKAVA 330
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-327 |
6.37e-25 |
|
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: 105.32 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 37 SFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLT--ALVLLgirDETSfplif 114
Cdd:cd01174 30 SFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTgtAVITV---DESG----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 115 yrENC------ADMALSEEDID--EGFIAEARAVLatgTHLSHPrtEAAVLKALTLARRHGAKTALD----IDYRPNLWG 182
Cdd:cd01174 102 --ENRivvvpgANGELTPADVDaaLELIAAADVLL---LQLEIP--LETVLAALRAARRAGVTVILNpapaRPLPAELLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 183 VAghgdgesrfvesgkvttklqgtlhlfDLIVGTEEEFHIAGGTTDTLA--ALRAVRAVSE---ATLVCKRGAKGAVAFE 257
Cdd:cd01174 175 LV--------------------------DILVPNETEAALLTGIEVTDEedAEKAARLLLAkgvKNVIVTLGAKGALLAS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 258 GpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPS 327
Cdd:cd01174 229 G------GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
43-321 |
2.97e-23 |
|
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: 100.08 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 43 GGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRDETSFPLIFYRencADM 122
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYP---GAM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 123 ALSEEDIDEGFIAEARAVlatgthlsHPRTEAAVLkalTLARRHgAKTALDIDYRP--NLWGvaGHGDGESRFVEsgkvt 200
Cdd:cd01942 113 DELEPNDEADPDGLADIV--------HLSSGPGLI---ELAREL-AAGGITVSFDPgqELPR--LSGEELEEILE----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 201 tklqgtlhLFDLIVGTEEEF----HIAGGTTDTLAALraVRAVseatlVCKRGAKGAVAFEGpipdsldaGQT--GPGFP 274
Cdd:cd01942 174 --------RADILFVNDYEAellkERTGLSEAELASG--VRVV-----VVTLGPKGAIVFED--------GEEveVPAVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2183742573 275 -IEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGC 321
Cdd:cd01942 231 aVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
39-323 |
4.71e-21 |
|
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: 94.22 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 39 AKYI-GGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRgVATDPDRLTA--LVLLGIRDETSfpLIFY 115
Cdd:cd01168 50 VKYIaGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTR-YQVQPDGPTGtcAVLVTPDAERT--MCTY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 116 RENCADmaLSEEDIDEGFIAEARAVLATGTHLSHPrtEAAVLKALTLARRHGAKTALDI-------DYRPNLWGVAGHgd 188
Cdd:cd01168 127 LGAANE--LSPDDLDWSLLAKAKYLYLEGYLLTVP--PEAILLAAEHAKENGVKIALNLsapfivqRFKEALLELLPY-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 189 gesrfvesgkvttklqgtlhlFDLIVGTEEEFHI--AGGTTDTL-AALRAVRAVSEaTLVCKRGAKGAVAFEGpipdslD 265
Cdd:cd01168 201 ---------------------VDILFGNEEEAEAlaEAETTDDLeAALKLLALRCR-IVVITQGAKGAVVVEG------G 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2183742573 266 AGQTGPGFPIE-VFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTP 323
Cdd:cd01168 253 EVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
13-320 |
8.77e-20 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 89.41 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 13 VITIGRSSVDLYgtqvggrlEDMGSfaKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATD 92
Cdd:PRK09813 3 LATIGDNCVDIY--------PQLGK--AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 93 PDRlTALVLLGIRDETSfplIF--YRENC-ADMALSEEDIDegfiaearavLATGTHLSHPRTEAAVLKALTLARRHGAK 169
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA----------WLAQYDIVHAAIWGHAEDAFPQLHAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 170 TALDIDYRPnlwgvaghgdgESRFVESgkvttklqgtlhlfdLIVGTEEEFHIAGGTTDTL-AALRAVRAVSEATLVCKR 248
Cdd:PRK09813 139 TAFDFSDKW-----------DSPLWQT---------------LVPHLDYAFASAPQEDEFLrLKMKAIVARGAGVVIVTL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183742573 249 GAKGAVAFEGpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHG 320
Cdd:PRK09813 193 GENGSIAWDG------AQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
43-335 |
3.95e-18 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 85.69 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 43 GGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRDETsfplifyrENC--- 119
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEG--------ENSigi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 120 ---ADMALSEEDID--EGFIAEARAVLatgTHLSHPRteAAVLKALTLARRHGAKTALDidyrPnlwgvaghgdgesrfV 194
Cdd:PRK11142 111 hagANAALTPALVEahRELIANADALL---MQLETPL--ETVLAAAKIAKQHGTKVILN----P---------------A 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 195 ESGKVTTKLqgtLHLFDLIVGTEEEFHIAGG--TTDTLAALRAVRAVSE---ATLVCKRGAKGAVAFEgpipdsldAGQT 269
Cdd:PRK11142 167 PARELPDEL---LALVDIITPNETEAEKLTGirVEDDDDAAKAAQVLHQkgiETVLITLGSRGVWLSE--------NGEG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183742573 270 G--PGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPSLAEMEFFL 335
Cdd:PRK11142 236 QrvPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
43-327 |
6.65e-17 |
|
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: 81.57 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 43 GGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPD---RLTALVLLGIRDETSfplifyRENC 119
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGarsPISSITDITGDRATI------SITA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 120 ADMALSEEDIDEGFIAEARAVLATGthlshpRTEAAVLKALTLARRHGAKTALDIDyrpnlwgvaghgdgesrfVESGKV 199
Cdd:cd01945 110 IDTQAAPDSLPDAILGGADAVLVDG------RQPEAALHLAQEARARGIPIPLDLD------------------GGGLRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 200 TTKLqgtLHLFDLIVGTEEEFHIAGGTTDTLaALRAVRAVSEATLVCKRGAKGAVAFEgpipdslDAGQTG--PGFPIEV 277
Cdd:cd01945 166 LEEL---LPLADHAICSENFLRPNTGSADDE-ALELLASLGIPFVAVTLGEAGCLWLE-------RDGELFhvPAFPVEV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2183742573 278 FNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPS 327
Cdd:cd01945 235 VDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
42-317 |
6.66e-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: 78.51 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 42 IGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVaTDPDRLTALVLLgIRDETSFPLIfyreNCAD 121
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI-VFEGRSTASYTA-ILDKDGDLVV----ALAD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 122 MALSEEdIDEGF-------IAEARAVLATGtHLShprtEAAVLKALTLARRHGAKTALDIdyrpnlwgvaghgdgesrfv 194
Cdd:cd01941 108 MDIYEL-LTPDFlrkireaLKEAKPIVVDA-NLP----EEALEYLLALAAKHGVPVAFEP-------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 195 ESGKVTTKLQGTLHLFDLIVGTEEEF-HIAGGTTDTLAALRAVRAVSEA----TLVCKRGAKGAVAFEGPIPDSLDAGQt 269
Cdd:cd01941 162 TSAPKLKKLFYLLHAIDLLTPNRAELeALAGALIENNEDENKAAKILLLpgikNVIVTLGAKGVLLSSREGGVETKLFP- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2183742573 270 gPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVS 317
Cdd:cd01941 241 -APQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
12-331 |
7.66e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 12 DVITIGRSSVDLYG-----TQVGgrlEDM--GSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGV 84
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVG---ETLhgTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 85 DVRGVATDPDRLTALVLLGIRDETSFPLIFYRENcADMALSEEDIDEGF--IAEARAVLATGTHLSHPRTeaavLKALTL 162
Cdd:PTZ00292 94 NTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPG-ANNALTPQMVDAQTdnIQNICKYLICQNEIPLETT----LDALKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 163 ARRHGAKTALDIDYRPNLWGVAghgdgesrfvesgkvttKLQGTLHLFDL-IVGTEEEFHIAGGT-TDTLAALRAVRA-- 238
Cdd:PTZ00292 169 AKERGCYTVFNPAPAPKLAEVE-----------------IIKPFLKYVSLfCVNEVEAALITGMEvTDTESAFKASKElq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 239 -VSEATLVCKRGAKGAVAFE-GPIPDSLdagqtgPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAV 316
Cdd:PTZ00292 232 qLGVENVIITLGANGCLIVEkENEPVHV------PGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISV 305
|
330
....*....|....*
gi 2183742573 317 SRHGCTPAYPSLAEM 331
Cdd:PTZ00292 306 TRHGTQSSYPHPSEL 320
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
13-320 |
9.99e-13 |
|
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: 68.53 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 13 VITIGRSSVDLYGTQVGGrledmgsfakYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATD 92
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 93 PdRLTALVLLGIRDETSfplIFYREN---CADMALSEEDIDegFIAEARAVlatgtHLSHPRTEAAVLKALTLARRHGAK 169
Cdd:cd01940 72 E-GENAVADVELVDGDR---IFGLSNkggVAREHPFEADLE--YLSQFDLV-----HTGIYSHEGHLEKALQALVGAGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 170 TALDIDYRpnlwgvaghgdgesrfvesgkvttklqGTLHLFDLIV-GTEEEFHIAGGTTDTL--AALRAVRAVSEATLVC 246
Cdd:cd01940 141 ISFDFSDR---------------------------WDDDYLQLVCpYVDFAFFSASDLSDEEvkAKLKEAVSRGAKLVIV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183742573 247 KRGAKGAVAFEGpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADW-PTALKYANACGAFAVSRHG 320
Cdd:cd01940 194 TRGEDGAIAYDG------AVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEG 262
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
30-320 |
1.06e-12 |
|
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: 69.10 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 30 GRLEDMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEhMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRDETs 109
Cdd:cd01164 23 GEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGTE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 110 fplifYRENCADMALSEEDIDEgFIAEARAVLATGTHL----SHPR--TEAAVLKALTLARRHGAKTALDIDYRPNLWGV 183
Cdd:cd01164 101 -----TEINEPGPEISEEELEA-LLEKLKALLKKGDIVvlsgSLPPgvPADFYAELVRLAREKGARVILDTSGEALLAAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 184 AGHGDgesrfvesgkvttklqgtlhlfdLIVGTEEEF-----HIAGGTTDTLAALRAVRAVSEATLVCKRGAKGAVAFEG 258
Cdd:cd01164 175 AAKPF-----------------------LIKPNREELeelfgRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183742573 259 pipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHG 320
Cdd:cd01164 232 ------DGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
40-324 |
3.26e-12 |
|
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: 67.60 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 40 KYIGGSPTNIACGTARLGLKTAVITRVGdEHMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRDETsfplifYRENC 119
Cdd:TIGR03168 32 KDAGGKGINVARVLARLGAEVVATGFLG-GFTGEFIEALLAEEGIKNDFVEVKGETRINVKIKESSGEE------TELNE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 120 ADMALSEEDIDEgFIAEARAVLATGTHL----SHPR-TEAAVLKALT-LARRHGAKTALDIDYRPNLWGVAGHGD----- 188
Cdd:TIGR03168 105 PGPEISEEELEQ-LLEKLRELLASGDIVvisgSLPPgVPPDFYAQLIaIARKKGAKVILDTSGEALREALAAKPFlikpn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 189 ----GEsrfvesgkvttklqgtlhLFDLIVGTEEEFhiaggttdtLAALRAVRAVSEATLVCKRGAKGAVAFEGpipdsl 264
Cdd:TIGR03168 184 heelEE------------------LFGRELKTLEEI---------IEAARELLDRGAENVLVSLGADGALLVTK------ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183742573 265 DAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHG---CTPA 324
Cdd:TIGR03168 231 EGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGtglPDPE 293
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-337 |
1.13e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 66.31 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 40 KYIGGSPTNIACGTARLGLKTAVITRVGdEHMGRFIREQLVREGVDVRGVATDPD-RL-TALVLLGIRDETSFplifyre 117
Cdd:COG1105 32 LDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtRInIKIVDPSDGTETEI------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 118 NCADMALSEEDIDEgFIAEARAVLATGTHL----SHPR--TEAAVLKALTLARRHGAKTALD---------IDYRPnlwg 182
Cdd:COG1105 104 NEPGPEISEEELEA-LLERLEELLKEGDWVvlsgSLPPgvPPDFYAELIRLARARGAKVVLDtsgealkaaLEAGP---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 183 vaghgdgesrfvesgkvttklqgtlhlfDLIVGTEEEF-HIAGGTTDTLAALR-AVRAVSEA---TLVCKRGAKGAV--- 254
Cdd:COG1105 179 ----------------------------DLIKPNLEELeELLGRPLETLEDIIaAARELLERgaeNVVVSLGADGALlvt 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 255 ---AFEGPIPdsldagqtgpgfPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGctPAYPSLAEM 331
Cdd:COG1105 231 edgVYRAKPP------------KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDV 296
|
....*.
gi 2183742573 332 EFFLER 337
Cdd:COG1105 297 EELLAQ 302
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
37-320 |
2.50e-11 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 64.75 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 37 SFAKYIGGSpTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRG-VATDPDRLTALVLLGIRDETSFPLIFY 115
Cdd:cd01944 30 SKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLpPRGGDDGGCLVALVEPDGERSFISISG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 116 RENcadmALSEEDIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRhgAKTALDIDYRPNLWGVAGHgdgesrfve 195
Cdd:cd01944 109 AEQ----DWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALP--AGTTLVFDPGPRISDIPDT--------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 196 sgkvttKLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVR--AVSEATLVCKRGAKGAVAFEgpiPDslDAGQTGPGF 273
Cdd:cd01944 174 ------ILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRiyAKTAAPVVVRLGSNGAWIRL---PD--GNTHIIPGF 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2183742573 274 PIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHG 320
Cdd:cd01944 243 KVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
13-322 |
4.55e-10 |
|
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: 60.89 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 13 VITIGRSSVDLYGT-----QVGGRLEdMGSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVR 87
Cdd:cd01947 2 IAVVGHVEWDIFLSldappQPGGISH-SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 88 GVATDPDRLTALVLLGIRDETSFpLIFYRENCADMALSEEDIDEGFIAEARAVLATgthlshprteaavlkaltlARRHG 167
Cdd:cd01947 81 VAWRDKPTRKTLSFIDPNGERTI-TVPGERLEDDLKWPILDEGDGVFITAAAVDKE-------------------AIRKC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 168 AKTALDIdyrpnlWGVAGHgdgeSRFVEsgkvttkLQGTLHLFDLIVGTEEEFhiAGGTTDTLAALRAVRavseaTLVCK 247
Cdd:cd01947 141 RETKLVI------LQVTPR----VRVDE-------LNQALIPLDILIGSRLDP--GELVVAEKIAGPFPR-----YLIVT 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183742573 248 RGAKGAVAFEGpipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCT 322
Cdd:cd01947 197 EGELGAILYPG------GRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PLN02967 |
PLN02967 |
kinase |
14-219 |
8.19e-10 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 61.60 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 14 ITIGRSSVDLYGTQVGGRLEDM----GSFAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGV 89
Cdd:PLN02967 210 VPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 90 ATDPDRLTALVLLGIRDETSFPLIFYREnCADMALSEEDIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRHGAK 169
Cdd:PLN02967 290 CIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGV 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2183742573 170 TALDIDYRPNLWgvaghgdgesrfvESGKVTTKL-QGTLHLFDLIVGTEEE 219
Cdd:PLN02967 369 IFYDLNLPLPLW-------------SSSEETKSFiQEAWNLADIIEVTKQE 406
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
40-330 |
1.40e-09 |
|
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: 59.91 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 40 KYIGGSPTNIACGTARLGLKTAVITRVGdEHMGRFIREQLVREGVDVRGVATDPDRLTALVLLGIRDETsfplifYRENC 119
Cdd:TIGR03828 32 IDAGGKGINVSRVLKNLGVDVVALGFLG-GFTGDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGTE------TKLNG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 120 ADMALSEEDIDEgFIAEARAVLATGTHL----SHPR-TEAAVLKALT-LARRHGAKTALD---------IDYRPNLWGVA 184
Cdd:TIGR03828 105 PGPEISEEELEA-LLEKLRAQLAEGDWLvlsgSLPPgVPPDFYAELIaLAREKGAKVILDtsgealrdgLKAKPFLIKPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 185 GHGDGEsrfvesgkvttklqgtlhLFDLIVGTEEEFHIAGgttDTLAALRAvravsEATLVcKRGAKGAVAFEGPipDSL 264
Cdd:TIGR03828 184 DEELEE------------------LFGRELKTLEEIIEAA---RELLDLGA-----ENVLI-SLGADGALLVTKE--GAL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183742573 265 DAgqTGPgfPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPSLAE 330
Cdd:TIGR03828 235 FA--QPP--KGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIE 296
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
40-331 |
3.48e-09 |
|
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: 58.73 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 40 KYIGGSpTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVaTDPDRLTaLVLLGIRDETSFPLIFYRENc 119
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPT-TTKTRVIARNQQLLRVDRED- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 120 aDMALSEE------DIDEGFIAEARAVL----ATGThLShPRteaaVLKALTLARRHGAKTALdidyrpnlwgVAGHGDG 189
Cdd:cd01172 113 -DSPLSAEeeqrliERIAERLPEADVVIlsdyGKGV-LT-PR----VIEALIAAARELGIPVL----------VDPKGRD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 190 ESRFVEsgkvttklqgtlhlFDLIVGTEEEFHIAGGTTDT-----LAALRAVRAVSEATLVC-KRGAKGAVAFEGPipds 263
Cdd:cd01172 176 YSKYRG--------------ATLLTPNEKEAREALGDEINdddelEAAGEKLLELLNLEALLvTLGEEGMTLFERD---- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183742573 264 lDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAYPSLAEM 331
Cdd:cd01172 238 -GEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
8-313 |
3.51e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 59.46 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 8 GKTLDVITIGRSSVD-------LYGTQVGGRLEDMGSFA------KY--IGGSpTNIACGTARLGLKTAVITRVGDEHMG 72
Cdd:PLN02341 70 GKEIDVATLGNLCVDivlpvpeLPPPSREERKAYMEELAasppdkKSweAGGN-CNFAIAAARLGLRCSTIGHVGDEIYG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 73 RFIREQLVREGVDVRGVATDPDR----------LTALVLL------------GIRDETSFPLIFYRENCADMALSeedid 130
Cdd:PLN02341 149 KFLLDVLAEEGISVVGLIEGTDAgdsssasyetLLCWVLVdplqrhgfcsraDFGPEPAFSWISKLSAEAKMAIR----- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 131 egfiaEARAVLATGTHLSHPRTEaAVLKALTLARRHGAKTALDIDYRpnlwgvaghgdGESRFVESGKVTTKLQGTLHLF 210
Cdd:PLN02341 224 -----QSKALFCNGYVFDELSPS-AIASAVDYAIDVGTAVFFDPGPR-----------GKSLLVGTPDERRALEHLLRMS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 211 DLIVGTEEEFHIAGGTTDTLAALRAVRAVSEAT--LVCKRGAKGAVAFegpipdSLDAGQTGPGFPIEVFNVLGAGDGFF 288
Cdd:PLN02341 287 DVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILV------TRSSVSCAPAFKVNVVDTVGCGDSFA 360
|
330 340
....*....|....*....|....*
gi 2183742573 289 SGLLKGWLDGADWPTALKYANACGA 313
Cdd:PLN02341 361 AAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
38-181 |
7.14e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 58.77 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 38 FAKYIGGSPTNIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLTA--LVLLGIRDETSFPLIFY 115
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTAcsRMKIKFRDGGKMVAETV 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183742573 116 RENCADMALSEEdIDEGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRHGAKTALDIDYRPNLW 181
Cdd:PLN02543 247 KEAAEDSLLASE-LNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLW 311
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
48-332 |
7.92e-09 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 57.51 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 48 NIACGTARLGLKTAVITRVGDEHMGRFIREQLVREGVDVRGVATDPDRLTAL---VLLG----IR--DETSFPLifyren 118
Cdd:COG2870 60 NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrVIAGgqqlLRldFEDRFPL------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 119 caDMALSEEDID--EGFIAEARAVL----ATGThLSHPRTEAAVlkalTLARRHGAKTALD------IDYR------PNL 180
Cdd:COG2870 134 --SAELEARLLAalEAALPEVDAVIlsdyGKGV-LTPELIQALI----ALARAAGKPVLVDpkgrdfSRYRgatlltPNL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 181 wgvaghgdgeSRFVEsgkvttklqgtlhLFDLIVGTEEEFHIAGgttdtlAALRAVRAVsEATLVCkRGAKGAVAFE-GP 259
Cdd:COG2870 207 ----------KEAEA-------------AVGIPIADEEELVAAA------AELLERLGL-EALLVT-RGEEGMTLFDaDG 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183742573 260 IPDSLdagqtgPGFPIEVFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVSRHGCTPAypSLAEME 332
Cdd:COG2870 256 PPHHL------PAQAREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATV--SPEELL 320
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
43-320 |
4.98e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 52.50 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 43 GGSPTNIACGTARLG--------LKTAVITRVGDEHMGRFIREQLVREGVD------VRG------VATDPD-RLTALVL 101
Cdd:PLN02813 126 GGSLSNTLVALARLGsqsaagpaLNVAMAGSVGSDPLGDFYRTKLRRANVHflsqpvKDGttgtviVLTTPDaQRTMLSY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 102 LGIRDETSFplifyrencaDMALSeedideGFIAEARAVLATGTHLSHPRTEAAVLKALTLARRHG---AKTALDID--- 175
Cdd:PLN02813 206 QGTSSTVNY----------DSCLA------SAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGalvAVTASDVScie 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 176 -YRPNLWGVAGHG-------DGESR-FVESGKVTTKLQGTLHLFDLIvgteeefhiaggttdtlaALRAVRAVSEATLVc 246
Cdd:PLN02813 270 rHRDDFWDVMGNYadilfanSDEARaLCGLGSEESPESATRYLSHFC------------------PLVSVTDGARGSYI- 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183742573 247 krGAKGAVAFegpIPDSldagqtgPGFPIEVfnvLGAGDGFFSGLLKGWLDGA-DWPTALKYANACGAFAVSRHG 320
Cdd:PLN02813 331 --GVKGEAVY---IPPS-------PCVPVDT---CGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQG 390
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
152-296 |
1.54e-05 |
|
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: 46.32 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 152 TEAAVLKALTLARRHGAKTALDIDYRPNLWgvaghgdgesrfvesgkVTTKLQGTLHLFDLIVGTEEEFHIAGGTTDTLA 231
Cdd:cd00287 69 APEAVLDALEEARRRGVPVVLDPGPRAVRL-----------------DGEELEKLLPGVDILTPNEEEAEALTGRRDLEV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 232 ALRAVRAVSEA-----TLVCKRGAKGAVAFEGPipdslDAGQTGPGFPIEVFNVLGAGDGFFSGLLKGWL 296
Cdd:cd00287 132 KEAAEAAALLLskgpkVVIVTLGEKGAIVATRG-----GTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
202-320 |
1.94e-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: 46.69 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183742573 202 KLQGTLHLFDLIVGTEEEFHIAGGTTDTLAALRAVRAVSEATLVCKRGAKGAVAFegpipdSLDAGQTGPGFPIE-VFNV 280
Cdd:cd01946 156 KLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLF------TDDGYFAAPAYPLEsVFDP 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2183742573 281 LGAGDGF---FSGLL--KGWLDGADWPTALKYANACGAFAVSRHG 320
Cdd:cd01946 230 TGAGDTFaggFIGYLasQKDTSEANMRRAIIYGSAMASFCVEDFG 274
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
267-317 |
1.77e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 44.21 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2183742573 267 GQTGPGFPIE--VFNVLGAGDGFFSGLLKGWLDGADWPTALKYANACGAFAVS 317
Cdd:PRK09850 236 GESGWSAPIKtnVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| |
