|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-290 |
3.70e-82 |
|
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: 250.19 E-value: 3.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 3 RIVCLGEAMVELSATASG-------WSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTH 75
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGrleqadsFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 76 PTRNAGLYAITTDADGERSFTYWRDASAARALFELevvDAAMAQAEAADLFYFSLISLAILPPqGRQDLLLLAARVRDRG 155
Cdd:cd01166 81 PGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPE---DLDEAALAGADHLHLSGITLALSES-AREALLEALEAAKARG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 156 GIVAFDGNYRPRLWESPEMAARMRDkAIATADIGLPTFEDEALLDGARSPQAVAAHWQR--LGCGEVIVKLGGQGCLLAD 233
Cdd:cd01166 157 VTVSFDLNYRPKLWSAEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKLGAEGALVYT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 759919285 234 -GTPVAVPKT-LQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGAI 290
Cdd:cd01166 236 gGGRVFVPAYpVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-297 |
5.63e-63 |
|
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: 201.27 E-value: 5.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 3 RIVCLGEAMVELSAT------------ASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGD 70
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlpkggetvlAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 71 LVLTHPTRNAGLYAITTDADGERSFTYWRDASAaralfELEVVDAAMAQAEAADLFYFSLISLAilPPQGRQDLLLLAAR 150
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANA-----ELTPEDLDEALLAGADILHLGGITLA--SEPPREALLAALEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 151 VRDRGGIVAFDGNYRPRLWEspEMAARMRDkAIATADIGLPTFEDEALLDGARSPQAVAAHWQRLGCGEVIVKLGGQGCL 230
Cdd:COG0524 154 ARAAGVPVSLDPNYRPALWE--PARELLRE-LLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759919285 231 LAD-GTPVAVP-KTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGAIPARDEAA 297
Cdd:COG0524 231 LYTgGEVVHVPaFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTRE 299
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-290 |
2.38e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.59 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 3 RIVCLGEAMVELSATASG----------WSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLV 72
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGlpgelvrvstVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 73 LTHPTRNAGLYAITTDADGERSFTYWRDASAARALFELEVVdaaMAQAEAADLFYFSlislAILPPQGRQDLLLLAARVR 152
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEEN---EDLLENADLLYIS----GSLPLGLPEATLEELIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 153 DRGGivAFDGNYRPRLWESPEMAARMrdkaIATADIGLPTFEDEALLDGARSPQ-----AVAAHWQRLGCGEVIVKLGGQ 227
Cdd:pfam00294 154 KNGG--TFDPNLLDPLGAAREALLEL----LPLADLLKPNEEELEALTGAKLDDieealAALHKLLAKGIKTVIVTLGAD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759919285 228 GCLLADGT----PVAVPKTlQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGAI 290
Cdd:pfam00294 228 GALVVEGDgevhVPAVPKV-KVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-290 |
2.97e-40 |
|
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: 142.00 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 3 RIVCLGEAMVELSATASGWSVGY----GGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTR 78
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 79 NAGLYAITTDADGERSFTYWRDASAARALFELEVVDaamaQAEAADLFYFSliSLAILPPQGRQDLLLLAARVRDRGGIV 158
Cdd:cd01167 81 PTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPD----LLSEADILHFG--SIALASEPSRSALLELLEAAKKAGVLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 159 AFDGNYRPRLWESPEMAARMRDKAIATADIGLPTFEDEALLDGARSPQAVAAHWQRLGCGEVIVKLGGQGCLL-ADGTPV 237
Cdd:cd01167 155 SFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLyTKGGVG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759919285 238 AVPKT-LQPIDTSGAGDAFNGGYLAA-RMRDAGIEDAAL------CGHALAGWNVMRRGAI 290
Cdd:cd01167 235 EVPGIpVEVVDTTGAGDAFVAGLLAQlLSRGLLALDEDElaealrFANAVGALTCTKAGAI 295
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
15-292 |
4.77e-29 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 112.26 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 15 SATASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDADGERS 94
Cdd:cd01174 25 TVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 95 FTYwrDASAARALfELEVVDAAMAQAEAADLFyfsLISLAIlPPQGRQDLLLLAarvRDRGGIVAFDGnyrprlweSPem 174
Cdd:cd01174 105 IVV--VPGANGEL-TPADVDAALELIAAADVL---LLQLEI-PLETVLAALRAA---RRAGVTVILNP--------AP-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 175 AARMRDKAIATADIGLPTfEDEALL------DGARSPQAVAAHWQRLGCGEVIVKLGGQGCLLADGT-PVAVP-KTLQPI 246
Cdd:cd01174 165 ARPLPAELLALVDILVPN-ETEAALltgievTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGeVEHVPaFKVKAV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 759919285 247 DTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGAIPA 292
Cdd:cd01174 244 DTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPS 289
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
4-299 |
1.14e-27 |
|
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: 109.22 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 4 IVCLGEAMVELSAT--------ASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTH 75
Cdd:TIGR04382 4 VITIGRVGVDLYPQqigvpledVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 76 PTRNAGLYAITTDADGERSFTYWRDASAAralFELEVVDAAMAQAEAADLFYFSLISLAilPPQGRQDLLLLAARVRDRG 155
Cdd:TIGR04382 84 PGRRTSLVFLEIKPPDEFPLLFYRENAAD---LALTPDDVDEDYIASARALLVSGTALS--QEPSREAVLKALEYARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 156 GIVAFDGNYRPRLWESPEMAARMRDKAIATADIGLPTFEDEALLDGARSPQAVAAHWQRLGCGEVIVKLGGQGCL--LAD 233
Cdd:TIGR04382 159 VRVVLDIDYRPYLWKSPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRGPEGSLvyTGD 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759919285 234 GTPVAVP----KTLQPIdtsGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRG---AIPARDEAAPY 299
Cdd:TIGR04382 239 GEGVEVPgfpvEVLNVL---GAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHScspAMPTLEELEAF 308
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-290 |
7.17e-24 |
|
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: 98.15 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 24 GYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDADGERSFTYWRDASA 103
Cdd:cd01942 34 EFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 104 aralfELEVVDAAMAQAEaadlfyfslisLAILPPQGRQDLLLLAARVRDRGGIVAFDGNYRPRLWESPEMAarmrdKAI 183
Cdd:cd01942 114 -----ELEPNDEADPDGL-----------ADIVHLSSGPGLIELARELAAGGITVSFDPGQELPRLSGEELE-----EIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 184 ATADIGLPTfEDEALLDGARSpqAVAAHWQRLGCGEVIVKLGGQGCLL-ADGTPVAVP--KTLQPIDTSGAGDAFNGGYL 260
Cdd:cd01942 173 ERADILFVN-DYEAELLKERT--GLSEAELASGVRVVVVTLGPKGAIVfEDGEEVEVPavPAVKVVDTTGAGDAFRAGFL 249
|
250 260 270
....*....|....*....|....*....|
gi 759919285 261 AARMRDAGIEDAALCGHALAGWNVMRRGAI 290
Cdd:cd01942 250 YGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-262 |
3.51e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 96.93 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 1 MARIVCLGEAMVELSATASGwsvGY----GGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHP 76
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPEGEN---RYlkcpGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 77 TRNAGLYAITTDADGERSFTYWRDASAAraLFeLEVVDAAMAQAEaaDLFYFSLISLAILPpqGRQDLLLLAARVRDRGG 156
Cdd:PRK09434 79 AHRTSTVVVDLDDQGERSFTFMVRPSAD--LF-LQPQDLPPFRQG--EWLHLCSIALSAEP--SRSTTFEAMRRIKAAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 157 IVAFDGNYRPRLWESPEMAARMRDKAIATADIGLPTFEDEALLDGARS-PQAVAAHWQRLGCGEVIVKLGGQGCLLAD-G 234
Cdd:PRK09434 152 FVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQlEDAIYALADRYPIALLLVTLGAEGVLVHTrG 231
|
250 260
....*....|....*....|....*....
gi 759919285 235 TPVAVP-KTLQPIDTSGAGDAFNGGYLAA 262
Cdd:PRK09434 232 QVQHFPaPSVDPVDTTGAGDAFVAGLLAG 260
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
4-292 |
1.31e-20 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 90.07 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 4 IVCLGEAMVELSATASGWSVGY--------GGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTH 75
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEapafkkapGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 76 PTRNAGLYAITTDADGERSFTYWRDASAARALFELEVvdaamaqaeAADL------FYFSLISLAILPPQGRQdllLLAA 149
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESEL---------DLDLirkakiFHYGSISLITEPCRSAH---LAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 150 RV-RDRGGIVAFDGNYRPRLWESPEmAARMRDKAI-ATADIgLPTFEDE-ALLDGARSP--QAVAAHWqRLGCGEVIVKL 224
Cdd:PLN02323 161 KIaKEAGALLSYDPNLRLPLWPSAE-AAREGIMSIwDEADI-IKVSDEEvEFLTGGDDPddDTVVKLW-HPNLKLLLVTE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 225 GGQGCLL--------ADGTPVavpktlQPIDTSGAGDAFNGGYLAARMRDAGI-EDAALCGHALAGWN------VMRRGA 289
Cdd:PLN02323 238 GEEGCRYytkdfkgrVEGFKV------KAVDTTGAGDAFVGGLLSQLAKDLSLlEDEERLREALRFANacgaitTTERGA 311
|
...
gi 759919285 290 IPA 292
Cdd:PLN02323 312 IPA 314
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
18-295 |
2.46e-20 |
|
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: 88.81 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 18 ASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDADGERSFTY 97
Cdd:TIGR02152 23 GHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 98 wrdASAARALFELEVVDAAMAQAEAADLFyfsLISLAIlPPQGRQDLLLLAARvrdRGGIVAFDgnyrprlwesPEMAAR 177
Cdd:TIGR02152 103 ---VAGANAELTPEDIDAAEALIAESDIV---LLQLEI-PLETVLEAAKIAKK---HGVKVILN----------PAPAIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 178 -MRDKAIATADIGLPTfEDEALL------DGARSPQAVAAHWQRLGCGEVIVKLGGQGCLLAD-GTPVAVP-KTLQPIDT 248
Cdd:TIGR02152 163 dLDDELLSLVDIITPN-ETEAEIltgievTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSkDESKLIPaFKVKAVDT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 759919285 249 SGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGA---IPARDE 295
Cdd:TIGR02152 242 TAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAqssIPYLEE 291
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
26-277 |
7.89e-20 |
|
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: 87.02 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 26 GGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAglYAITTDADGERSFT-YWRDASAA 104
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENA--VADVELVDGDRIFGlSNKGGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 105 RALFElevvdaamaqaeaADLFYFSLISLAILPPQGRQDLLLLAARVRDRGGI-VAFDGNYRprlWESPEMAARMR--DK 181
Cdd:cd01940 100 EHPFE-------------ADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGAlISFDFSDR---WDDDYLQLVCPyvDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 182 AIATADiGLPTFEDEALLDGARSPqavaahwqrlGCGEVIVKLGGQGCLLADG---TPVAvPKTLQPIDTSGAGDAFNGG 258
Cdd:cd01940 164 AFFSAS-DLSDEEVKAKLKEAVSR----------GAKLVIVTRGEDGAIAYDGavfYSVA-PRPVEVVDTLGAGDSFIAG 231
|
250 260
....*....|....*....|....*....
gi 759919285 259 YLAAR----------MRDAGIEDAALCGH 277
Cdd:cd01940 232 FLLSLlaggtaiaeaMRQGAQFAAKTCGH 260
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
25-291 |
1.70e-16 |
|
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: 78.42 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 25 YGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDaDGERSF-TYwrdaSA 103
Cdd:cd01168 54 AGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTP-DAERTMcTY----LG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 104 ARALFELEVVDAAMAQAEaaDLFYFSlislAILPPQGRQDLLLLAARVRDRGGIVAFDGNyrprlweSPEMAARMRD--- 180
Cdd:cd01168 129 AANELSPDDLDWSLLAKA--KYLYLE----GYLLTVPPEAILLAAEHAKENGVKIALNLS-------APFIVQRFKEall 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 181 KAIATADIgLPTFEDEALL---DGARSPQAVAAHWQRLGCGEVIVKLGGQGCLLADG---TPVAVPKTLQPIDTSGAGDA 254
Cdd:cd01168 196 ELLPYVDI-LFGNEEEAEAlaeAETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGgevYPVPAIPVEKIVDTNGAGDA 274
|
250 260 270
....*....|....*....|....*....|....*..
gi 759919285 255 FNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGAIP 291
Cdd:cd01168 275 FAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
27-288 |
5.22e-15 |
|
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: 73.61 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 27 GDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDgDLVLTHPTRNAGLYAITTDADGERSFTYWRDASAara 106
Cdd:cd01944 36 GGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE-ILLPPRGGDDGGCLVALVEPDGERSFISISGAEQ--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 107 lfELEVVDAAMAQAEAADLFYFSLISLAilPPQGRQDLLLLAARVRDRGGIVAFDGNYRPRLWESPEMAARMRDKAIATA 186
Cdd:cd01944 112 --DWSTEWFATLTVAPYDYVYLSGYTLA--SENASKVILLEWLEALPAGTTLVFDPGPRISDIPDTILQALMAKRPIWSC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 187 DiglptfEDEALLDGARSPQAVAAHWQRLGCGE---VIVKLGGQGC--LLADGTPVAVP--KTlQPIDTSGAGDAFNGGY 259
Cdd:cd01944 188 N------REEAAIFAERGDPAAEASALRIYAKTaapVVVRLGSNGAwiRLPDGNTHIIPgfKV-KAVDTIGAGDTHAGGM 260
|
250 260
....*....|....*....|....*....
gi 759919285 260 LAARMRDAGIEDAALCGHALAGWNVMRRG 288
Cdd:cd01944 261 LAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-295 |
4.46e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 62.83 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 1 MARIVCLGEAMvelsaTASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNA 80
Cdd:PTZ00292 32 VDRMPQVGETL-----HGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSST 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 81 GLYAITTD-ADGERSFTYWRDASAAralFELEVVDAAMAQaeaadlfYFSLISLAIL----PPQGRQDLLLLAarvRDRG 155
Cdd:PTZ00292 107 GLAMIFVDtKTGNNEIVIIPGANNA---LTPQMVDAQTDN-------IQNICKYLICqneiPLETTLDALKEA---KERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 156 GIVAFDGNYRPRLWESPEMAarmrdKAIATADIGLPTFEDEALLDGAR-SPQAVAA----HWQRLGCGEVIVKLGGQGCL 230
Cdd:PTZ00292 174 CYTVFNPAPAPKLAEVEIIK-----PFLKYVSLFCVNEVEAALITGMEvTDTESAFkaskELQQLGVENVIITLGANGCL 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759919285 231 LA--DGTPVAVP-KTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGA---IPARDE 295
Cdd:PTZ00292 249 IVekENEPVHVPgKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTqssYPHPSE 319
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
17-295 |
4.52e-11 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 62.58 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 17 TASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDADGERSFT 96
Cdd:PRK11142 30 TGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 97 YwrdASAARALFELEVVDAAMAQAEAADLFYFSLISlailPPQGrqdlLLLAARV-RDRGGIVAFDgnyrprlwesPEMA 175
Cdd:PRK11142 110 I---HAGANAALTPALVEAHRELIANADALLMQLET----PLET----VLAAAKIaKQHGTKVILN----------PAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 176 ARMRDKAIATADIGLPTfEDEA-LLDGAR-----SPQAVAAHWQRLGCGEVIVKLGGQGCLLA-DGTPVAVPK-TLQPID 247
Cdd:PRK11142 169 RELPDELLALVDIITPN-ETEAeKLTGIRvedddDAAKAAQVLHQKGIETVLITLGSRGVWLSeNGEGQRVPGfRVQAVD 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 759919285 248 TSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGA---IPARDE 295
Cdd:PRK11142 248 TIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAqpsIPWREE 298
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
207-295 |
5.41e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 59.38 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 207 AVAAHWQRLGCGEVIVKLGGQGCLLADGTPV--AVPKTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNV 284
Cdd:COG1105 204 AAARELLERGAENVVVSLGADGALLVTEDGVyrAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAA 283
|
90
....*....|..
gi 759919285 285 MRRGA-IPARDE 295
Cdd:COG1105 284 LSPGTgLPDRED 295
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-280 |
9.53e-09 |
|
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: 55.40 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 4 IVCLGEAMVELSATASG-----------WSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDgDLV 72
Cdd:cd01941 2 IVVIGAANIDLRGKVSGslvpgtsnpghVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLN-VRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 73 LTHPTRNAGLYAITTDADGE-----------RSFTYWRDASAARALFE--LEVVDaamaqaeaadlfyfslislAILPPQ 139
Cdd:cd01941 81 IVFEGRSTASYTAILDKDGDlvvaladmdiyELLTPDFLRKIREALKEakPIVVD-------------------ANLPEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 140 GRQDLLLLAarvRDRGGIVAFdgnyrprlweSPEMAARMRDKAIATADIGLPT---FEDEALLDGARSP----QAVAAHW 212
Cdd:cd01941 142 ALEYLLALA---AKHGVPVAF----------EPTSAPKLKKLFYLLHAIDLLTpnrAELEALAGALIENnedeNKAAKIL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759919285 213 QRLGCGEVIVKLGGQGCLLADGTPVAVPKTLQP------IDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALA 280
Cdd:cd01941 209 LLPGIKNVIVTLGAKGVLLSSREGGVETKLFPApqpetvVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAA 282
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
18-272 |
2.99e-08 |
|
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: 53.84 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 18 ASGWSVGYGGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDGDLVLTHPTRNAGLYAITTDA-DGERSFT 96
Cdd:cd01945 28 ATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITgDRATISI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 97 YWRDASAARALFELEVVDaamaqaeaadlfyfsliSLAILPPQGRQD--LLLLAARVRDRGGIVAFDGNyrPRLWESPEM 174
Cdd:cd01945 108 TAIDTQAAPDSLPDAILG-----------------GADAVLVDGRQPeaALHLAQEARARGIPIPLDLD--GGGLRVLEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 175 AARMRDKAIATADIGLPtfedealLDGARSPQAVAAHWqRLGCGEVIVKLGGQGCLL--ADGTPVAVPKT-LQPIDTSGA 251
Cdd:cd01945 169 LLPLADHAICSENFLRP-------NTGSADDEALELLA-SLGIPFVAVTLGEAGCLWleRDGELFHVPAFpVEVVDTTGA 240
|
250 260
....*....|....*....|.
gi 759919285 252 GDAFNGGYLAARMRDAGIEDA 272
Cdd:cd01945 241 GDVFHGAFAHALAEGMPLREA 261
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
26-280 |
4.15e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.20 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 26 GGDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDgdlvLTHPTRNAGLYAITTD--ADGERSFTYWRDASA 103
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVD----ISHVHTKHGVTAQTQVelHDNDRVFGDYTEGVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 104 ARALFELEVVDAamaqaeaadLFYFSLISLAILppqGRQDLLLlaARVRDRGGIVAFDGNYRprlWESPemaarMRDKAI 183
Cdd:PRK09813 99 ADFALSEEDYAW---------LAQYDIVHAAIW---GHAEDAF--PQLHAAGKLTAFDFSDK---WDSP-----LWQTLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 184 ATADIGLPTF--EDEALLDGARSPQAvaahwqrLGCGEVIVKLGGQGCLLADGT--------PVAVpktlqpIDTSGAGD 253
Cdd:PRK09813 157 PHLDYAFASApqEDEFLRLKMKAIVA-------RGAGVVIVTLGENGSIAWDGAqfwrqapePVTV------VDTMGAGD 223
|
250 260
....*....|....*....|....*..
gi 759919285 254 AFNGGYLAARMRDAGIEDAALCGHALA 280
Cdd:PRK09813 224 SFIAGFLCGWLAGMTLPQAMAQGTACA 250
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
124-262 |
1.25e-07 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 50.94 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 124 DLFYFSLISLAILPPqGRQDLLLLAARVRDRGGIVAFDGNYRPRLWESPEMAARMRdkaiaTADIGLPTFEDEALLDGAR 203
Cdd:cd00287 54 TLVGADAVVISGLSP-APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKLLP-----GVDILTPNEEEAEALTGRR 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759919285 204 SP-----QAVAAHWQRLGCGEVIVKLGGQGCLLA--DGTPVAVP-KTLQPIDTSGAGDAFNGGYLAA 262
Cdd:cd00287 128 DLevkeaAEAAALLLSKGPKVVIVTLGEKGAIVAtrGGTEVHVPaFPVKVVDTTGAGDAFLAALAAG 194
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
188-288 |
5.10e-07 |
|
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: 50.22 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 188 IGLPTFEDEALLDGARSPQAvaahwqrLGCGEVIVKLGGQGCLLA--DGTPVAVPKTLQPIDTSGAGDAFNGGYLAARMR 265
Cdd:cd01164 192 FGRPLGDEEDVIAAARKLIE-------RGAENVLVSLGADGALLVtkDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQ 264
|
90 100
....*....|....*....|...
gi 759919285 266 DAGIEDAALCGHALAGWNVMRRG 288
Cdd:cd01164 265 GLSLEEALRLAVAAGSATAFSPG 287
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
11-289 |
3.07e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 45.21 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 11 MVELSATA---SGWSVGyggDTLNTAIHLARAGHEVAYMTALGEDTFSAHLRTAWAAEGIDgdlvltHPTRNAGlyaitT 87
Cdd:PLN02341 104 MEELAASPpdkKSWEAG---GNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGIS------VVGLIEG-----T 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 88 DADGERSFTY-----W-------RDASAARALFELEVVdaamaqaeaadlfyFSLIS-------LAI------------- 135
Cdd:PLN02341 170 DAGDSSSASYetllcWvlvdplqRHGFCSRADFGPEPA--------------FSWISklsaeakMAIrqskalfcngyvf 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 136 --LPPQGRQDLLLLAArvrDRGGIVAFDGNYRPR-LWESPEMAARMRDKAIATADIGLPTFEDEALLDGARSPQAVAAHW 212
Cdd:PLN02341 236 deLSPSAIASAVDYAI---DVGTAVFFDPGPRGKsLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 213 QRLGCGE--VIVKLGGQGCLLA--DGTPVAVPKTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRG 288
Cdd:PLN02341 313 LRPGIRTkwVVVKMGSKGSILVtrSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCG 392
|
.
gi 759919285 289 A 289
Cdd:PLN02341 393 A 393
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
235-287 |
1.57e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 42.71 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 759919285 235 TPVAVPKTLQP--IDTSGAGDAFNGGYLAARMRDAGIEDAALCGHAlAGWNVMRR 287
Cdd:PTZ00247 278 TSVPVPPLDQEkiVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHY-SAQVIIQH 331
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
26-290 |
2.34e-04 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 42.02 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 26 GGDTLNTAIHLARAGHEVAYMTALGEDtFSAHLRTAWAAEGIDGDLVL--THPTRNAGlyaITTDADGERSFTywRDASA 103
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRD-EIGIQSLEELESGGDKHTVAwrDKPTRKTL---SFIDPNGERTIT--VPGER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 104 ARALFELEVVDAAmaqaeaaDLFYfsLISLAILPPqgrqdlLLLAARVRdRGGIVAFDGNYRprlWESPEMAARMRDKAI 183
Cdd:cd01947 110 LEDDLKWPILDEG-------DGVF--ITAAAVDKE------AIRKCRET-KLVILQVTPRVR---VDELNQALIPLDILI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 184 ATA-DIGLPTFEDEALLDGARSpqavaahwqrlgcgeVIVKLGGQGCLLADGTPV-AVPKTLQP-IDTSGAGDAFNGGYL 260
Cdd:cd01947 171 GSRlDPGELVVAEKIAGPFPRY---------------LIVTEGELGAILYPGGRYnHVPAKKAKvPDSTGAGDSFAAGFI 235
|
250 260 270
....*....|....*....|....*....|
gi 759919285 261 AARMRDAGIEDAALCGHALAGWNVMRRGAI 290
Cdd:cd01947 236 YGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
213-292 |
5.51e-04 |
|
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: 41.01 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 213 QRLGCGEVIVKLGGQGCLL--ADGTPVAVP-KTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGA 289
Cdd:cd01172 215 ELLNLEALLVTLGEEGMTLfeRDGEVQHIPaLAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGT 294
|
...
gi 759919285 290 IPA 292
Cdd:cd01172 295 APV 297
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
202-288 |
1.01e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 40.08 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 202 ARSPQAVAAHwQRL-----GCGEVIVKLGGQGCLLadgtPVAVPKTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCG 276
Cdd:PLN02548 236 SALPKASGTH-KRTvvitqGADPTVVAEDGKVKEF----PVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAG 310
|
90
....*....|..
gi 759919285 277 HALAGWNVMRRG 288
Cdd:PLN02548 311 NYAANVIIQRSG 322
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
220-291 |
2.32e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 39.02 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759919285 220 VIVKLGGQGCLL--ADGTPVAVPKTLQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAGWNVMRRGaIP 291
Cdd:PLN02630 206 VIVTNGKKGCRIywKDGEMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG-IP 278
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
194-286 |
3.82e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 38.62 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 194 EDEA--LLDGAR--SPQAVAAHWQRLgCGEVIVKLGGQGCLLADGTP-VAVPKTLQ--PIDTSGAGDAFNGGYLAARMRD 266
Cdd:PLN02379 240 EDEAreLLRGEQesDPEAALEFLAKY-CNWAVVTLGSKGCIARHGKEvVRVPAIGEtnAVDATGAGDLFASGFLYGLIKG 318
|
90 100
....*....|....*....|
gi 759919285 267 AGIEDAALCGhALAGWNVMR 286
Cdd:PLN02379 319 LSLEECCKVG-ACSGGSVVR 337
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
214-281 |
3.86e-03 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 38.15 E-value: 3.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 214 RLGCGEVIVKLGGQGCLLADGT-PVAVPKT-LQPIDTSGAGDAFNGGYLAARMRDAGIEDAALCGHALAG 281
Cdd:cd01937 181 ETGVKEIIVTDGEEGGYIFDGNgKYTIPASkKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAA 250
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
186-265 |
9.88e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 37.48 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759919285 186 ADIgLPTFEDEAL----LDGARSPQAVAAHWQRLgCGEVIVKLGGQGCLL-ADGTPVAVPKTLQ-PIDTSGAGDAFNGGY 259
Cdd:PLN02813 283 ADI-LFANSDEARalcgLGSEESPESATRYLSHF-CPLVSVTDGARGSYIgVKGEAVYIPPSPCvPVDTCGAGDAYAAGI 360
|
....*.
gi 759919285 260 LAARMR 265
Cdd:PLN02813 361 LYGLLR 366
|
|
| |
