|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-298 |
3.40e-103 |
|
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: 303.73 E-value: 3.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 5 EILCFGETMAMFVAEQPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVD 84
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 85 AQAPTGFQMKSREvDGADPRVEYFRRGSAASRLGLAHIREE-MLGARHLHATGIPPALSASACELSHELMRRMRGKGASL 163
Cdd:cd01166 81 PGRPTGLYFLEIG-AGGERRVLYYRAGSAASRLTPEDLDEAaLAGADHLHLSGITLALSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 164 SFDPNLRPSLWpSERRMIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYL--DMGVDAVAIKLGPSGAYYRDAHG 241
Cdd:cd01166 160 SFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKLGAEGALVYTGGG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489179783 242 EGLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDM 298
Cdd:cd01166 239 RVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-307 |
2.60e-82 |
|
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: 250.96 E-value: 2.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 6 ILCFGETMAMFVA-----EQPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRF 80
Cdd:COG0524 2 VLVIGEALVDLVArvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 81 VEVDAQAPTGFQMKSREVDGaDPRVEYFRrgSAASRLGLAHIREEML-GARHLHATGIPPAlSASACELSHELMRRMRGK 159
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDG-ERTIVFYR--GANAELTPEDLDEALLaGADILHLGGITLA-SEPPREALLAALEAARAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 160 GASLSFDPNLRPSLWPserRMIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDA 239
Cdd:COG0524 158 GVPVSLDPNYRPALWE---PARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489179783 240 HGEGLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDMEGLPKRSQL 307
Cdd:COG0524 235 GEVVHVPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-299 |
3.05e-59 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 191.79 E-value: 3.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 5 EILCFGETMAMFVA---EQPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFV 81
Cdd:pfam00294 1 KVVVIGEANIDLIGnveGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 82 EVDAQAPTGfqMKSREVDGADPRVEYFRRG--SAASRLGLAHIREEMLGARHLHATGIPPALSASACElshELMRRMRGK 159
Cdd:pfam00294 81 VIDEDTRTG--TALIEVDGDGERTIVFNRGaaADLTPEELEENEDLLENADLLYISGSLPLGLPEATL---EELIEAAKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 160 GASlsFDPNLRPSLWPserrMIAEINALAAHAHWVLPGLEEGRLLSG--WQEPADIAAFY---LDMGVDAVAIKLGPSGA 234
Cdd:pfam00294 156 GGT--FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGakLDDIEEALAALhklLAKGIKTVIVTLGADGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489179783 235 YYRDAHGEGLVPGVPVATVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDME 299
Cdd:pfam00294 230 LVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-274 |
2.59e-51 |
|
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: 171.28 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 6 ILCFGETMAMFVAEQPGeldRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDA 85
Cdd:cd01167 2 VVCFGEALIDFIPEGSG---APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 86 QAPTGFQMKSREVDGaDPRVEyFRRGSAASRLGLAHIREEML-GARHLHaTGIPPALSASACELSHELMRRMRGKGASLS 164
Cdd:cd01167 79 AAPTTLAFVTLDADG-ERSFE-FYRGPAADLLLDTELNPDLLsEADILH-FGSIALASEPSRSALLELLEAAKKAGVLIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 165 FDPNLRPSLWPSERRMIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGL 244
Cdd:cd01167 156 FDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGE 235
|
250 260 270
....*....|....*....|....*....|
gi 489179783 245 VPGVPVaTVVDTVGAGDGFAVGVVSALLEG 274
Cdd:cd01167 236 VPGIPV-EVVDTTGAGDAFVAGLLAQLLSR 264
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
4-309 |
1.95e-40 |
|
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: 143.12 E-value: 1.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 4 FEILCFGETMAMFVAEQPG-ELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVE 82
Cdd:TIGR04382 2 LDVITIGRVGVDLYPQQIGvPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 83 VDAQAPTGF---QMKSREvdgaDPRVEYFRRGSAASRLGLAHIREEML-GARHLHATGIppALSAS-ACELSHELMRRMR 157
Cdd:TIGR04382 82 TDPGRRTSLvflEIKPPD----EFPLLFYRENAADLALTPDDVDEDYIaSARALLVSGT--ALSQEpSREAVLKALEYAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 158 GKGASLSFDPNLRPSLWPSERRMIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYR 237
Cdd:TIGR04382 156 AAGVRVVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLVY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489179783 238 DAHGEGL-VPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDMEGLPKRSQLLD 309
Cdd:TIGR04382 236 TGDGEGVeVPGFPV-EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLEELEA 307
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
25-296 |
3.59e-36 |
|
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: 131.28 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 25 DRVEQFGkriaGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSreVDGADPR 104
Cdd:cd01942 30 DLRREFG----GSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFIL--TDGDDNQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 105 VEYFRRGsAASRLGLAHIREEMLGARHLHATGIPPALsasacelshELMRRMRGKGASLSFDPNlrPSLWPSERRMIAEI 184
Cdd:cd01942 104 IAYFYPG-AMDELEPNDEADPDGLADIVHLSSGPGLI---------ELARELAAGGITVSFDPG--QELPRLSGEELEEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 185 nalAAHAHWVLPG---LEEGRLLSGWQEPADIAafyldmGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVGAGD 261
Cdd:cd01942 172 ---LERADILFVNdyeAELLKERTGLSEAELAS------GVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGD 242
|
250 260 270
....*....|....*....|....*....|....*
gi 489179783 262 GFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:cd01942 243 AFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
35-307 |
2.81e-35 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 129.67 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 35 AGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTgfqmkSREVDGADPRVE----YFRR 110
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRT-----STVVVDLDDQGErsftFMVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 111 GSAASRLGLahirEEMLGARH---LHATGIppALSA----SACelsHELMRRMRGKGASLSFDPNLRPSLWPSERRMIAE 183
Cdd:PRK09434 103 PSADLFLQP----QDLPPFRQgewLHLCSI--ALSAepsrSTT---FEAMRRIKAAGGFVSFDPNLREDLWQDEAELREC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 184 INALAAHAHWVLPGLEEGRLLSGWQEPAD-IAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVaTVVDTVGAGDG 262
Cdd:PRK09434 174 LRQALALADVVKLSEEELCFLSGTSQLEDaIYALADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSV-DPVDTTGAGDA 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489179783 263 FavgvVSALLEGLP----------LPDAVARGNWIGSRAVQVRGDMEGLPKRSQL 307
Cdd:PRK09434 253 F----VAGLLAGLSqaglwtdeaeLAEIIAQAQACGALATTAKGAMTALPNRQEL 303
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
20-307 |
2.35e-28 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 110.77 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQM----KS 95
Cdd:TIGR02152 16 KPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFitvdDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 96 RE-----VDGADPRV--EYFRRGSAA---SRLGLAHiREemlgarhlhatgIPPALSASACELSHELmrrmrgkGASLSF 165
Cdd:TIGR02152 96 GEnrivvVAGANAELtpEDIDAAEALiaeSDIVLLQ-LE------------IPLETVLEAAKIAKKH-------GVKVIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 166 DPNlrpslwPSERRMIAEinaLAAHAHWVLPGLEEGRLLSGwQEPADIAAF------YLDMGVDAVAIKLGPSGAYYRDA 239
Cdd:TIGR02152 156 NPA------PAIKDLDDE---LLSLVDIITPNETEAEILTG-IEVTDEEDAekaaekLLEKGVKNVIITLGSKGALLVSK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489179783 240 HGEGLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDMEGLPKRSQL 307
Cdd:TIGR02152 226 DESKLIPAFKV-KAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEV 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
20-302 |
2.26e-27 |
|
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: 108.02 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQF-----GKriaGAdsNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGfqmk 94
Cdd:cd01174 21 KPGETVLGSSFetgpgGK---GA--NQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 95 srevdgadprveyfrrgsaasrlgLAHIREEMLG----------ARHLHATGIPPALSASA--------CELSHE----L 152
Cdd:cd01174 92 ------------------------TAVITVDESGenrivvvpgaNGELTPADVDAALELIAaadvlllqLEIPLEtvlaA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 153 MRRMRGKGASLSFDPNlrpslwPserrMIAEINALAAHAHWVLPGLEEGRLLSG-----WQEPADIAAFYLDMGVDAVAI 227
Cdd:cd01174 148 LRAARRAGVTVILNPA------P----ARPLPAELLALVDILVPNETEAALLTGievtdEEDAEKAARLLLAKGVKNVIV 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489179783 228 KLGPSGAYYRDAHGEGLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDMEGLP 302
Cdd:cd01174 218 TLGAKGALLASGGEVEHVPAFKV-KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIP 291
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
6-309 |
7.78e-27 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 107.40 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 6 ILCFGETMAMFV--------AEQPGeldrveqFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLD 77
Cdd:PLN02323 13 VVCFGEMLIDFVptvsgvslAEAPA-------FKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 78 CRFVEVDAQAPTGFQMKSREVDGaDPRVEYFRRGSA-----ASRLGLAHIREemlgARHLHATGIppALSASACELSH-E 151
Cdd:PLN02323 86 NEGVRFDPGARTALAFVTLRSDG-EREFMFYRNPSAdmllrESELDLDLIRK----AKIFHYGSI--SLITEPCRSAHlA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 152 LMRRMRGKGASLSFDPNLRPSLWPSERRMIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYL-DMGVDAVAIKLG 230
Cdd:PLN02323 159 AMKIAKEAGALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLwHPNLKLLLVTEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 231 PSGAYYRDAHGEGLVPGVPVATvVDTVGAGDGFAVGVVS------ALLEGLP-LPDAVARGNWIGSRAVQVRGDMEGLPK 303
Cdd:PLN02323 239 EEGCRYYTKDFKGRVEGFKVKA-VDTTGAGDAFVGGLLSqlakdlSLLEDEErLREALRFANACGAITTTERGAIPALPT 317
|
....*.
gi 489179783 304 RSQLLD 309
Cdd:PLN02323 318 KEAVLK 323
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
20-296 |
1.51e-24 |
|
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: 100.73 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSlGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSR--- 96
Cdd:TIGR03168 20 TPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGETRINVKIKESsge 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 97 --EVDGADPRVeyfrRGSAASRLgLAHIREEMLGARHLHATG-IPPALSASACElshELMRRMRGKGASLSFD---PNLR 170
Cdd:TIGR03168 99 etELNEPGPEI----SEEELEQL-LEKLRELLASGDIVVISGsLPPGVPPDFYA---QLIAIARKKGAKVILDtsgEALR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 171 pslwpserrmiaeiNALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGeGLV 245
Cdd:TIGR03168 171 --------------EALAAKPFLIKPNHEEleelfGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEG-ALK 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489179783 246 PGVPVATVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:TIGR03168 236 ATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG 286
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
20-307 |
1.28e-22 |
|
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: 95.35 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSlGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSR--- 96
Cdd:TIGR03828 20 TLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVRVPGETRINVKIKEPsgt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 97 --EVDGADPRVeyfrRGSAASRLgLAHIREEMLGARHLHATG-IPPALSASACElshELMRRMRGKGASLSFD---PNLR 170
Cdd:TIGR03828 99 etKLNGPGPEI----SEEELEAL-LEKLRAQLAEGDWLVLSGsLPPGVPPDFYA---ELIALAREKGAKVILDtsgEALR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 171 pslwpserrmiaeiNALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEgLV 245
Cdd:TIGR03828 171 --------------DGLKAKPFLIKPNDEEleelfGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGA-LF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489179783 246 PGVPVATVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGdmEGLPKRSQL 307
Cdd:TIGR03828 236 AQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDI 295
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
36-296 |
1.03e-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: 93.06 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 36 GADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQaPTGfQMKSREVDGADPRveYFRRGSAAS 115
Cdd:cd01168 56 GSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDG-PTG-TCAVLVTPDAERT--MCTYLGAAN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 116 RLGLAHIREEMLgaRHLHATGIPPALSASACELSHELMRRMRGKGASLSF---DPNLrpslwpsERRMIAEINALAAHAH 192
Cdd:cd01168 132 ELSPDDLDWSLL--AKAKYLYLEGYLLTVPPEAILLAAEHAKENGVKIALnlsAPFI-------VQRFKEALLELLPYVD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 193 WVLPGLEEGRLLSGWQ--EPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVGAGDGFAVGVVSA 270
Cdd:cd01168 203 ILFGNEEEAEALAEAEttDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYG 282
|
250 260
....*....|....*....|....*.
gi 489179783 271 LLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:cd01168 283 LVQGEPLEECIRLGSYAAAEVIQQLG 308
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
20-307 |
8.77e-20 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 87.50 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSlGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSR--- 96
Cdd:COG1105 20 EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPsdg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 97 ---EVDGADPRVEyfrrGSAASRLgLAHIREEMLGARHLHATG-IPPALSASACElshELMRRMRGKGASLSFD---PNL 169
Cdd:COG1105 99 tetEINEPGPEIS----EEELEAL-LERLEELLKEGDWVVLSGsLPPGVPPDFYA---ELIRLARARGAKVVLDtsgEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 170 RpslwpserrmiaeiNALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGL 244
Cdd:COG1105 171 K--------------AALEAGPDLIKPNLEEleellGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489179783 245 VPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGdmEGLPKRSQL 307
Cdd:COG1105 237 AKPPKV-EVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDV 296
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
20-293 |
2.45e-19 |
|
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: 86.05 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSlGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSR--- 96
Cdd:cd01164 21 QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVEVAGETRINVKIKEEdgt 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 97 --EVDGADPRVEyfrrgSAASRLGLAHIREEMLGARHLHATG-IPPALSASACElshELMRRMRGKGASLSFD---PNLR 170
Cdd:cd01164 100 etEINEPGPEIS-----EEELEALLEKLKALLKKGDIVVLSGsLPPGVPADFYA---ELVRLAREKGARVILDtsgEALL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 171 pslwpserrmiaeiNALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLV 245
Cdd:cd01164 172 --------------AALAAKPFLIKPNREEleelfGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489179783 246 PGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQ 293
Cdd:cd01164 238 SPPKV-KVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAF 284
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
17-282 |
5.17e-18 |
|
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: 82.34 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 17 VAEQPGE------LDRVEQFGkriaGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTG 90
Cdd:cd01945 16 VASFPGGdgkivaTDYAVIGG----GNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 91 FQMKSReVDGADPRVEYFRRGSAASRLGLAHirEEMLGARHLHATGIPPALSASACELSHElmrrmRGKGASLSFDP-NL 169
Cdd:cd01945 92 ISSITD-ITGDRATISITAIDTQAAPDSLPD--AILGGADAVLVDGRQPEAALHLAQEARA-----RGIPIPLDLDGgGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 170 RPslwpserrmIAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFyldmGVDAVAIKLGPSGAYYRDAHGE-GLVPGV 248
Cdd:cd01945 164 RV---------LEELLPLADHAICSENFLRPNTGSADDEALELLASL----GIPFVAVTLGEAGCLWLERDGElFHVPAF 230
|
250 260 270
....*....|....*....|....*....|....
gi 489179783 249 PVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVA 282
Cdd:cd01945 231 PV-EVVDTTGAGDVFHGAFAHALAEGMPLREALR 263
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
40-293 |
8.94e-17 |
|
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: 78.89 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 40 NVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEV-DAQAPTGFQMKSREVD----GADPRVEyfrrgSAA 114
Cdd:cd01941 40 NIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFeGRSTASYTAILDKDGDlvvaLADMDIY-----ELL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 115 SRLGLAHIREemlgarhlhatgippALSASACE-----LSHELMRRM----RGKGASLSFDPnlrpslwPSERRMiAEIN 185
Cdd:cd01941 115 TPDFLRKIRE---------------ALKEAKPIvvdanLPEEALEYLlalaAKHGVPVAFEP-------TSAPKL-KKLF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 186 ALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEG---LVPGVPVATVVDTV 257
Cdd:cd01941 172 YLLHAIDLLTPNRAElealaGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVetkLFPAPQPETVVNVT 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 489179783 258 GAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQ 293
Cdd:cd01941 252 GAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
20-307 |
1.90e-15 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 75.54 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSreVD 99
Cdd:PTZ00292 37 QVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIF--VD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 100 GADPRVEYFRRGSAASrlglaHIREEMLGARhlhATGIPPALSASAC------ELSHELMRRMRGKGASLSFdpNLRPSL 173
Cdd:PTZ00292 115 TKTGNNEIVIIPGANN-----ALTPQMVDAQ---TDNIQNICKYLICqneiplETTLDALKEAKERGCYTVF--NPAPAP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 174 WPSERRMIAEINALAAhahWVLPGLEEGRLLSGWQ----EPADIAA-FYLDMGVDAVAIKLGPSG-AYYRDAHGEGLVPG 247
Cdd:PTZ00292 185 KLAEVEIIKPFLKYVS---LFCVNEVEAALITGMEvtdtESAFKASkELQQLGVENVIITLGANGcLIVEKENEPVHVPG 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 248 VPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRGDMEGLPKRSQL 307
Cdd:PTZ00292 262 KRV-KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
35-289 |
5.93e-15 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 74.87 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 35 AGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGL------------DCR---------FVEVDAQAPTGFQm 93
Cdd:PLN02341 119 AGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGIsvvgliegtdagDSSsasyetllcWVLVDPLQRHGFC- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 94 kSREVDGADPRVEYFRRGSAASRLGLAHireemlgARHLHATG-----IPPALSASACELShelmrrmRGKGASLSFDPN 168
Cdd:PLN02341 198 -SRADFGPEPAFSWISKLSAEAKMAIRQ-------SKALFCNGyvfdeLSPSAIASAVDYA-------IDVGTAVFFDPG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 169 LR-PSLW---PSERRMIAEinaLAAHAHWVLPGLEEGRLLSGWQEPADIAAFYLDMGVDA--VAIKLGPSGAYYRDAHGE 242
Cdd:PLN02341 263 PRgKSLLvgtPDERRALEH---LLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSV 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489179783 243 GLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGS 289
Cdd:PLN02341 340 SCAPAFKV-NVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
24-296 |
2.13e-14 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 71.69 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 24 LDRVEQFGKRIAGADS-NVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQMksrEVDGAD 102
Cdd:PRK09813 11 VDIYPQLGKAFSGGNAvNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQV---ELHDND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 103 pRV--EYFRRGSAASRLGLAHIReeMLGARHLHATGIPPAlsasacelSHELMRRMRGKGASLSFDPNLRPS--LWpseR 178
Cdd:PRK09813 88 -RVfgDYTEGVMADFALSEEDYA--WLAQYDIVHAAIWGH--------AEDAFPQLHAAGKLTAFDFSDKWDspLW---Q 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 179 RMIAEINALAAHAHWvlpglEEGRLLSGWQEpadiaafYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVaTVVDTVG 258
Cdd:PRK09813 154 TLVPHLDYAFASAPQ-----EDEFLRLKMKA-------IVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPV-TVVDTMG 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 489179783 259 AGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:PRK09813 221 AGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
26-281 |
4.67e-14 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 71.44 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 26 RVEQFGKriaGAdsNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQM----KSRE---- 97
Cdd:PRK11142 35 QVAFGGK---GA--NQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALifvnDEGEnsig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 98 -VDGADPRV--EYFRRGSAasrlglaHIREE--------------MLGARHLHATGIPPALS-ASACELSHELMRRMrgk 159
Cdd:PRK11142 110 iHAGANAALtpALVEAHRE-------LIANAdallmqletpletvLAAAKIAKQHGTKVILNpAPARELPDELLALV--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 160 gaslsfDpnlrpslwpserrMIAeinalaahahwvlPGLEEGRLLSGWQ----EPADIAAFYL-DMGVDAVAIKLGPSGA 234
Cdd:PRK11142 180 ------D-------------IIT-------------PNETEAEKLTGIRveddDDAAKAAQVLhQKGIETVLITLGSRGV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489179783 235 YYRDAHGEGLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAV 281
Cdd:PRK11142 228 WLSENGEGQRVPGFRV-QAVDTIAAGDTFNGALVTALLEGKPLPEAI 273
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
160-296 |
2.28e-11 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 63.21 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 160 GASLSFDPNLRPSLWPSerrmiAEINALAAHAHWVLPGLEEGRLLSGWQEPADIAAFYLDMGVDA--VAIKLGPSGAYYR 237
Cdd:cd01944 156 GTTLVFDPGPRISDIPD-----TILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAapVVVRLGSNGAWIR 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 238 DAHGE-GLVPGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:cd01944 231 LPDGNtHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-274 |
9.11e-11 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 61.22 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 40 NVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVdAQAPTGFQMKsrEVDGADPRVEYFRRGSAASRLGL 119
Cdd:cd01940 27 NVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV-KEGENAVADV--ELVDGDRIFGLSNKGGVAREHPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 120 AHIREEMLGARHLHAtgippaLSASACELSHELMRRMRGKGASLSFDPNLRpslwpserrmiaeinALAAHAHWVLPGLE 199
Cdd:cd01940 104 EADLEYLSQFDLVHT------GIYSHEGHLEKALQALVGAGALISFDFSDR---------------WDDDYLQLVCPYVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 200 EGrLLSGWQEPADIAAFYLDM----GVDAVAIKLGPSGAYYrdAHGEGLVPGVPVA-TVVDTVGAGDGFAVGVVSALLEG 274
Cdd:cd01940 163 FA-FFSASDLSDEEVKAKLKEavsrGAKLVIVTRGEDGAIA--YDGAVFYSVAPRPvEVVDTLGAGDSFIAGFLLSLLAG 239
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
20-296 |
2.91e-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: 59.74 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 20 QPGELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLtREGLDCRFVEVDAQaPTGFQMKSreVD 99
Cdd:cd01947 21 QPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGGDKHTVAWRDK-PTRKTLSF--ID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 100 GADPRveyfrrgsAASRLGLAhiREEMLGarhlhatgiPPALS------ASACELSHELMRRMRGKGASLSfDPNLRPSL 173
Cdd:cd01947 97 PNGER--------TITVPGER--LEDDLK---------WPILDegdgvfITAAAVDKEAIRKCRETKLVIL-QVTPRVRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 174 wpserrmiAEINALAAHAHWVLPGLEEGRLLSgwqePADIAAFyldMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVaTV 253
Cdd:cd01947 157 --------DELNQALIPLDILIGSRLDPGELV----VAEKIAG---PFPRYLIVTEGELGAILYPGGRYNHVPAKKA-KV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489179783 254 VDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:cd01947 221 PDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
22-296 |
5.41e-10 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 60.29 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 22 GELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFQMKSREVDGA 101
Cdd:COG3892 25 GRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDDET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 102 DPRVeYFRRGSAASRLGLAHIREEMLG-ARHLHATGI----PPALSASACELshelmRRMRGKGASLSFDPNLRPSLW-- 174
Cdd:COG3892 105 FPLI-FYRENCADMALTEDDIDEAFIAsARALLITGThlshPRTRAAVLKAL-----RYARAHGGKVVLDIDYRPVLWgl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 175 ----PSERRMIAeINALAAHAHWVLPGL-------EEGRLLSGwqEPADIAAFyldMGVDAVA-----IKLGPSG----- 233
Cdd:COG3892 179 tghgDGETRFVA-SDAVTAHLQEVLPLFdlivgteEEFHIAGG--STDTLAAL---RAVRRVStatlvCKRGALGcvvfe 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489179783 234 -AYYRDAHGEGLVPGVPVAtVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:COG3892 253 gAIPDDLDDGITGPGFPVE-VFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHG 315
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
29-176 |
8.35e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 59.54 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 29 QFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTG-FQMKSREVDGADPRVEY 107
Cdd:PLN02543 166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTAcSRMKIKFRDGGKMVAET 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489179783 108 FRRGSA----ASRLGLAHIREemlgARHLHATG---IPPALSAS---ACELSHELmrrmrgkGASLSFDPNLRPSLWPS 176
Cdd:PLN02543 246 VKEAAEdsllASELNLAVLKE----ARMFHFNSevlTSPSMQSTlfrAIELSKKF-------GGLIFFDLNLPLPLWRS 313
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
36-281 |
9.42e-10 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 58.85 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 36 GADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGldcrfVEVDaqaptgfqmKSREVDGAdprveyfrrgSAAS 115
Cdd:PRK09850 41 GVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSG-----VYVD---------KCLIVPGE----------NTSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 116 RLGLAHIREEMLGArhLHATGIPPALSA-----------------SACELSHE-LMRRMRGKGASLSF-DPnlrPSLWPS 176
Cdd:PRK09850 97 YLSLLDNTGEMLVA--INDMNISNAITAeylaqhrefiqrakvivADCNISEEaLAWILDNAANVPVFvDP---VSAWKC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 177 E--RRMIAEINALAAHAhwvlpgLE----EGRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGE-GLVPgvP 249
Cdd:PRK09850 172 VkvRDRLNQIHTLKPNR------LEaetlSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGEsGWSA--P 243
|
250 260 270
....*....|....*....|....*....|...
gi 489179783 250 VAT-VVDTVGAGDGFAVGVVSALLEGLPLPDAV 281
Cdd:PRK09850 244 IKTnVINVTGAGDAMMAGLASCWVDGMPFAESV 276
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
35-285 |
5.94e-09 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 56.36 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 35 AGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGFqmKSREVDGA------DpRVEYF 108
Cdd:COG2870 55 PGGAANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTT--KTRVIAGGqqllrlD-FEDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 109 RRGSAASRLGLAHIREEMLGARHL----HATGippALSASACElshELMRRMRGKGASLSFDPNLRPSlwpserrmiaei 184
Cdd:COG2870 132 PLSAELEARLLAALEAALPEVDAVilsdYGKG---VLTPELIQ---ALIALARAAGKPVLVDPKGRDF------------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 185 nALAAHAHWVLPGLEEGRLLSG--WQEPADI--AAFYL--DMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVG 258
Cdd:COG2870 194 -SRYRGATLLTPNLKEAEAAVGipIADEEELvaAAAELleRLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTG 272
|
250 260
....*....|....*....|....*..
gi 489179783 259 AGDGFAVGVVSALLEGLPLPDAVARGN 285
Cdd:COG2870 273 AGDTVIATLALALAAGASLEEAAELAN 299
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
235-303 |
2.76e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 54.43 E-value: 2.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 235 YYRDahGEGLVPGVPvATVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAV-QVrgdmeGLPK 303
Cdd:PLN02630 218 YWKD--GEMRVPPFP-AIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVeQV-----GIPK 279
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
113-272 |
3.00e-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: 52.87 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 113 AASRLGLahiREEMLGARHLHATGIPPALSASAcelshELMRRMRGKGASLSFDPNLRPSLWPSErrmiaEINALAAHAH 192
Cdd:cd00287 45 ALARLGV---SVTLVGADAVVISGLSPAPEAVL-----DALEEARRRGVPVVLDPGPRAVRLDGE-----ELEKLLPGVD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 193 WVLPGLEEGRLLSG-----WQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVGAGDGFAVGV 267
Cdd:cd00287 112 ILTPNEEEAEALTGrrdleVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAAL 191
|
....*
gi 489179783 268 VSALL 272
Cdd:cd00287 192 AAGLA 196
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
36-274 |
3.61e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 51.09 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 36 GADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLD---CrfVEVDAQaptgfqmksrevdgadprveyfrrgS 112
Cdd:PRK09954 94 GVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNvsgC--IRLHGQ-------------------------S 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 113 AASRLGLAHIREEMLGArhLHATGIPPALSASACELSHELMRRmrgKGASLSfDPNLRPSL--W--------PSERRMIA 182
Cdd:PRK09954 147 TSTYLAIANRQDETVLA--INDTHILQQLTPQLLNGSRDLIRH---AGVVLA-DCNLTAEAleWvftladeiPVFVDTVS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 183 EINALA-----AHAHWVLPGLEEGRLLsgWQEP----ADIAAFYLDM---GVDAVAIKLGPSGAYYRDAHGEGLVPGVPV 250
Cdd:PRK09954 221 EFKAGKikhwlAHIHTLKPTQPELEIL--WGQAitsdADRNAAVNALhqqGVQQIFVYLPDESVFCSEKDGEQFLLTAPA 298
|
250 260
....*....|....*....|....
gi 489179783 251 ATVVDTVGAGDGFAVGVVSALLEG 274
Cdd:PRK09954 299 HTTVDSFGADDGFMAGLVYSFLEG 322
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
32-296 |
1.72e-06 |
|
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: 48.71 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 32 KRIAGAdSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVeVDAQAPTGFqmKSREVDGA--DPRVEYFR 109
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTT--KTRVIARNqqLLRVDRED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 110 RgsaasRLGLAHIREEMLGARHLHATG-------------IPPALSASACELSHELMRRM----------RGKGASLsFD 166
Cdd:cd01172 113 D-----SPLSAEEEQRLIERIAERLPEadvvilsdygkgvLTPRVIEALIAAARELGIPVlvdpkgrdysKYRGATL-LT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 167 PNLRpslwpsERRMIAEInaLAAHAHWVLPGLEegRLLSgwqepadiaafylDMGVDAVAIKLGPSGAYYRDAHGEGL-V 245
Cdd:cd01172 187 PNEK------EAREALGD--EINDDDELEAAGE--KLLE-------------LLNLEALLVTLGEEGMTLFERDGEVQhI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489179783 246 PGVPVaTVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:cd01172 244 PALAK-EVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
22-276 |
3.46e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 47.77 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 22 GELDRVEQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLdSLTREGLDCRFVEVDAQapTGFQMKSREVDGA 101
Cdd:PRK09513 26 GEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQ-LFSELGIANRFQVVQGR--TRINVKLTEKDGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 102 dprVEYFrrgsaaSRLGLaHIREE-----------MLGARHLHAT--GIPPALSAsacELSHELMRRMRGKGASLSFDpn 168
Cdd:PRK09513 103 ---VTDF------NFSGF-EVTPAdwerfvtdslsWLGQFDMVAVsgSLPRGVSP---EAFTDWMTRLRSQCPCIIFD-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 169 lrpslwpSERRmiAEINALAAHAHWVLPGLEE-----GRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEG 243
Cdd:PRK09513 168 -------SSRE--ALVAGLKAAPWLVKPNRREleiwaGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEW 238
|
250 260 270
....*....|....*....|....*....|....
gi 489179783 244 LV-PgvPVATVVDTVGAGDGFAVGVVSALLEGLP 276
Cdd:PRK09513 239 IAkP--PACDVVSTVGAGDSMVGGLIYGLLMRES 270
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
199-271 |
4.10e-06 |
|
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: 4.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489179783 199 EEGRLLSGWQEPADIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVGAGDGFAVGVVSAL 271
Cdd:cd01946 172 GEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFIGYL 244
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
206-296 |
1.54e-04 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 42.78 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 206 GWQEPADIAAFYLDMGVDAVAI--KLGPSGAYYRDAHGEGL-VPGVPVATVVDTVGAGDGFAVGVVSALLEG-LPLPDAV 281
Cdd:cd01939 194 GYKSPEECLRGEGPRAKKAALLvcTWGDQGAGALGPDGEYVhSPAHKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEAL 273
|
90
....*....|....*
gi 489179783 282 ARGNWIGSRAVQVRG 296
Cdd:cd01939 274 DFGNRVASQKCTGVG 288
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
36-276 |
2.89e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.10 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 36 GADSNVAIGLARLGFA--------VAWLSRVGDDSLGRFVLDSLTREGLDCRFVEV--------------DAQAPT-GFQ 92
Cdd:PLN02813 127 GSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVkdgttgtvivlttpDAQRTMlSYQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 93 MKSREVDgADPRVeyfRRGSAASRL--------GLAHIREEMLGA-RHLHATGIPPALSAS--ACELSH-ELMRRMRGKG 160
Cdd:PLN02813 207 GTSSTVN-YDSCL---ASAISKSRVlvvegylwELPQTIEAIAQAcEEAHRAGALVAVTASdvSCIERHrDDFWDVMGNY 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 161 ASLSFdpnlrpslwpserrmiaeINALAAHAhwvLPGLEEgrllsgwQEPADIAAFYLDMGVDAVAIKLGPSGAYYrDAH 240
Cdd:PLN02813 283 ADILF------------------ANSDEARA---LCGLGS-------EESPESATRYLSHFCPLVSVTDGARGSYI-GVK 333
|
250 260 270
....*....|....*....|....*....|....*..
gi 489179783 241 GEGL-VPGVPVATVvDTVGAGDGFAVGVVSALLEGLP 276
Cdd:PLN02813 334 GEAVyIPPSPCVPV-DTCGAGDAYAAGILYGLLRGVS 369
|
|
| PLN02967 |
PLN02967 |
kinase |
28-94 |
5.37e-04 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 41.57 E-value: 5.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489179783 28 EQFGKRIAGADSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQAPTGF-QMK 94
Cdd:PLN02967 236 EKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVsTMK 303
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
26-89 |
5.81e-04 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 41.35 E-value: 5.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489179783 26 RVEQFGKRIAGAdSNVAIGLARLGFAVAWLSRVGDDSLGRFVLDSLTREGLDCRFVEVDAQaPT 89
Cdd:PRK11316 42 KVNQIEERPGGA-ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVPTH-PT 103
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
254-296 |
8.49e-04 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 40.47 E-value: 8.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489179783 254 VDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:PLN02548 280 VDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSG 322
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
245-296 |
1.99e-03 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 39.24 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489179783 245 VPGVPVATVVDTVGAGDGFAVGVVSALLEGLPLPDAVARGNWIGSRAVQVRG 296
Cdd:PTZ00247 282 VPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNG 333
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
199-296 |
2.61e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.00 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179783 199 EEGRLLSGWQEPA-DIAAFYLDMGVDAVAIKLGPSGAYYRDAHGEGLVPGVPVATVVDTVGAGDGFAVGVVSALLEGLPL 277
Cdd:PLN02379 242 EARELLRGEQESDpEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSL 321
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90
....*....|....*....
gi 489179783 278 PDAVARGNWIGSRAVQVRG 296
Cdd:PLN02379 322 EECCKVGACSGGSVVRALG 340
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