|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
2-307 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 528.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 2 TTPRLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNI 81
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 82 DTDAIRIIPKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHQYRHIIEQADALLMQLESPLDTVFEAAKQAKAHQTK 161
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 162 VILNPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPG 241
Cdd:PRK11142 161 VILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 242 FRVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPWRDEIKSFLAER 307
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
10-301 |
6.34e-135 |
|
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: 384.26 E-value: 6.34e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 10 GSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRII 89
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 90 PKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHQYRHIIEQADALLMQLESPLDTVFEAAKQAKAHQTKVILNPAPA 169
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 170 QP-LSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVD 248
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490365462 249 TIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPWRDEIK 301
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-296 |
1.60e-130 |
|
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: 373.04 E-value: 1.60e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHQYRHIIEQADALLMQLESPLDTVFEAAKQAKAHQTKVIL 164
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 165 NPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRV 244
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490365462 245 EAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPW 296
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-300 |
7.30e-91 |
|
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: 272.53 E-value: 7.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHqyRHIIEQADALLMQL-----ESPLDTVFEAAKQAKAHQ 159
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLD--EALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 160 TKVILNPA-------PAQPLSDEFLSFIDIITPNETEAEILTGISvhdevGAAKAANILHSKGIKHVLITLGSRGVWFSE 232
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490365462 233 QGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPWRDEI 300
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
4-306 |
2.80e-85 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 259.28 E-value: 2.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 4 PRLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDT 83
Cdd:PTZ00292 16 PDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 84 DAIRIIPKTPTGVAMILVN-EQGENVISIVAGANSALTPSHLHQYRHIIEQ-ADALLMQLESPLDTVFEAAKQAKAHQTK 161
Cdd:PTZ00292 96 SFVSRTENSSTGLAMIFVDtKTGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERGCY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 162 VILNPAPA-----QPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTG 236
Cdd:PTZ00292 176 TVFNPAPApklaeVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENE 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365462 237 MI-IPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPWRDEIKSFLAE 306
Cdd:PTZ00292 256 PVhVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPADVKE 326
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-292 |
3.59e-73 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 227.23 E-value: 3.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPkpGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHQYRHIIEQADAL----LMQLESPLDTVFEAAKQAKAHQT 160
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 161 K--VILNPA-PAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGM 237
Cdd:pfam00294 159 FdpNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 238 IIPGFR-VEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQS 292
Cdd:pfam00294 239 HVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-290 |
8.40e-49 |
|
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: 164.29 E-value: 8.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHImniaqFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:cd01166 1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGEN-VISIVAG-ANSALTPSHLHqyRHIIEQADAL------LMQLESPLDTVFEAAKQAK 156
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERrVLYYRAGsAASRLTPEDLD--EAALAGADHLhlsgitLALSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 157 AHQTKVIL---------NPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVgAAKAANILHskGIKHVLITLGSRG 227
Cdd:cd01166 154 ARGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDA-AERALALAL--GVKAVVVKLGAEG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365462 228 VWFSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGA 290
Cdd:cd01166 231 ALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-291 |
1.35e-41 |
|
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: 145.15 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGENVISIVAGANSALTPSHLHQYrhiieQADALLMQLESPlDTVFEAAKQAKAHQTKVIL 164
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADP-----DGLADIVHLSSG-PGLIELARELAAGGITVSF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 165 NPAPAQPLSD-----EFLSFIDIITPNETEAEIL---TGISVHDEvgaakaanilhSKGIKHVLITLGSRGVWFSEQGTG 236
Cdd:cd01942 155 DPGQELPRLSgeeleEILERADILFVNDYEAELLkerTGLSEAEL-----------ASGVRVVVVTLGPKGAIVFEDGEE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 237 MIIPGF-RVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQ 291
Cdd:cd01942 224 VEVPAVpAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
40-267 |
8.55e-38 |
|
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: 135.84 E-value: 8.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 40 GGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILVNEQGENVISIVAGANSAL 119
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 120 TPSHLHQYRhIIEQADAL----LMQLESPL-DTVFEAAKQAKAHQTKVIL----------NPAPAQPLSDEFLSFIDIIT 184
Cdd:cd01167 108 LLDTELNPD-LLSEADILhfgsIALASEPSrSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERIAELLELADIVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 185 PNETEAEILTGISVHDEvgaakAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAI 264
Cdd:cd01167 187 LSDEELELLFGEEDPEE-----IAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQL 261
|
...
gi 490365462 265 LEG 267
Cdd:cd01167 262 LSR 264
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-267 |
3.97e-33 |
|
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: 123.17 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTD 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIPKTPTGVAMILVNEQGENVISIVAG---ANSALTPSHlhqyrhIIEQADALLMQLESPlDTVFEAAKQAKAHQTK 161
Cdd:cd01945 81 FIVVAPGARSPISSITDITGDRATISITAIdtqAAPDSLPDA------ILGGADAVLVDGRQP-EAALHLAQEARARGIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 162 VIL--NPAPAQPLsDEFLSFIDIITPNETEAEILTGISvhdEVGAAKAaniLHSKGIKHVLITLGSRGV-WFSEQGTGMI 238
Cdd:cd01945 154 IPLdlDGGGLRVL-EELLPLADHAICSENFLRPNTGSA---DDEALEL---LASLGIPFVAVTLGEAGClWLERDGELFH 226
|
250 260
....*....|....*....|....*....
gi 490365462 239 IPGFRVEAVDTIAAGDTFNGAFVTAILEG 267
Cdd:cd01945 227 VPAFPVEVVDTTGAGDVFHGAFAHALAEG 255
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-269 |
1.28e-32 |
|
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: 122.04 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 6 LAVLGSINVDHIMNIAQFPKPGETVIGHdYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDA 85
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTSNPGH-VKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 86 IRIIPK-TPTGVAMIlvNEQGENVISIV-AGANSALTPSHLHQYRHIIEQADALLMQLESPLDTVFEAAKQAKAHQTKVI 163
Cdd:cd01941 81 IVFEGRsTASYTAIL--DKDGDLVVALAdMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 164 LNPAPAQPLSDEFLSF--IDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMI--- 238
Cdd:cd01941 159 FEPTSAPKLKKLFYLLhaIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVEtkl 238
|
250 260 270
....*....|....*....|....*....|..
gi 490365462 239 -IPGFRVEAVDTIAAGDTFNGAFVTAILEGKS 269
Cdd:cd01941 239 fPAPQPETVVNVTGAGDAFVAGLVAGLLEGMS 270
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
16-269 |
2.46e-31 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 118.87 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 16 HIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTdAIRIIPKTPTG 95
Cdd:cd01168 31 GDMILADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 96 VAMILVNEQGENVISIVAGANSALTPSHLHQyrHIIEQADALLM---QLESPLDTVFEAAKQAKAHQTKVILNpapaqpL 172
Cdd:cd01168 110 TCAVLVTPDAERTMCTYLGAANELSPDDLDW--SLLAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALN------L 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 173 SDEF------------LSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGikhVLITLGSRGVWFSEQGTGMIIP 240
Cdd:cd01168 182 SAPFivqrfkeallelLPYVDILFGNEEEAEALAEAETTDDLEAALKLLALRCRI---VVITQGAKGAVVVEGGEVYPVP 258
|
250 260 270
....*....|....*....|....*....|
gi 490365462 241 GFRVE-AVDTIAAGDTFNGAFVTAILEGKS 269
Cdd:cd01168 259 AIPVEkIVDTNGAGDAFAGGFLYGLVQGEP 288
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-265 |
3.38e-30 |
|
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: 112.96 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIAcvgddaigreiiaqlktdnidtd 84
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 airiipktptgvamilvneqgenvisivagansaltpshlhqyrhiieqADALLMQLESP-LDTVFEAAKQAKAHQTKVI 163
Cdd:cd00287 58 -------------------------------------------------ADAVVISGLSPaPEAVLDALEEARRRGVPVV 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 164 LNPAPAQ-----PLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRG-VWFSEQGTGM 237
Cdd:cd00287 89 LDPGPRAvrldgEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGaIVATRGGTEV 168
|
250 260
....*....|....*....|....*...
gi 490365462 238 IIPGFRVEAVDTIAAGDTFNGAFVTAIL 265
Cdd:cd00287 169 HVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
14-272 |
7.42e-24 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 98.67 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 14 VDHIMNIAQFpKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAiGREIIAQLKTDNIDTDAIRIIPKTP 93
Cdd:COG1105 10 LDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 94 TGVAmilVNEQGENVISIVAGANSALTPSH----LHQYRHIIEQADALLMqleS-------PLDTVFEAAKQAKAHQTKV 162
Cdd:COG1105 88 INIK---IVDPSDGTETEINEPGPEISEEElealLERLEELLKEGDWVVL---SgslppgvPPDFYAELIRLARARGAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 163 IL---NPA-----PAQPlsdeflsfiDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRG-VWFSEQ 233
Cdd:COG1105 162 VLdtsGEAlkaalEAGP---------DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGaLLVTED 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 490365462 234 GTgMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHD 272
Cdd:COG1105 233 GV-YRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
40-299 |
1.46e-21 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 92.31 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 40 GGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILVNEQGENVISIVA--GANS 117
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVrpSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 118 ALTPSHL-----HQYRHIIEQAdalLMQlESPLDTVFEAAKQAKAHQTKVIL----------NPAPAQPLSDEFLSFIDI 182
Cdd:PRK09434 108 FLQPQDLppfrqGEWLHLCSIA---LSA-EPSRSTTFEAMRRIKAAGGFVSFdpnlredlwqDEAELRECLRQALALADV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 183 ITPNETEAEILTGIsvhDEVGAAKAAnILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVDTIAAGDtfngAFVT 262
Cdd:PRK09434 184 VKLSEEELCFLSGT---SQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGD----AFVA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490365462 263 AILEGKSAHDAIRFAHAAAAI----------AVTRHGAQSSVPWRDE 299
Cdd:PRK09434 256 GLLAGLSQAGLWTDEAELAEIiaqaqacgalATTAKGAMTALPNRQE 302
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
6-267 |
2.00e-19 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 86.58 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 6 LAVLGSINVD------HIMNIAQfPKPGetvighdyKIAF--GGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLK 77
Cdd:PRK09850 7 VVIIGSANIDvagyshESLNYAD-SNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 78 TDNIDTDAIRIIPKTPTGVAMILVNEQGENVISIV-AGANSALTPSHLHQYRHIIEQADALLMQL---ESPLDTVFEaak 153
Cdd:PRK09850 78 QSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREFIQRAKVIVADCnisEEALAWILD--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 154 qaKAHQTKVILNPAPAQPLSD--EFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFS 231
Cdd:PRK09850 155 --NAANVPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYS 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 490365462 232 E-QGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEG 267
Cdd:PRK09850 233 DiSGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
14-272 |
2.21e-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: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 14 VDHIMNIAQFpKPGET-VIGHDYKIAfGGKGANQAVACGRSGADITFIACVGDDaIGREIIAQLKTDNIDTDAIRIIPKT 92
Cdd:cd01164 11 IDLTIELDQL-QPGEVnRVSSTRKDA-GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 93 PTGVAMIlvnEQGENVISIVaGANSALTPSHLHQ----YRHIIEQADALLMqleS-------PLDTVFEAAKQAKAHQTK 161
Cdd:cd01164 88 RINVKIK---EEDGTETEIN-EPGPEISEEELEAllekLKALLKKGDIVVL---SgslppgvPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 162 VILNpAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPG 241
Cdd:cd01164 161 VILD-TSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASP 239
|
250 260 270
....*....|....*....|....*....|.
gi 490365462 242 FRVEAVDTIAAGDTFNGAFVTAILEGKSAHD 272
Cdd:cd01164 240 PKVKVVSTVGAGDSMVAGFVAGLAQGLSLEE 270
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-290 |
3.46e-19 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 85.16 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 6 LAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNI-DTD 84
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 AIRIIpktPTGVAMILVNEQGENVISIVAGANSALTPShlhqyrHIIEQADALLMQLESPLDTVFEAAKQAKAhqtkVIL 164
Cdd:cd01947 82 AWRDK---PTRKTLSFIDPNGERTITVPGERLEDDLKW------PILDEGDGVFITAAAVDKEAIRKCRETKL----VIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 165 NPAPAQPLS--DEFLSFIDIITPNETEAEILTGISVhdevgaakaaniLHSKGIKHVLITLGSRGVWFSEQGTGMIIPGF 242
Cdd:cd01947 149 QVTPRVRVDelNQALIPLDILIGSRLDPGELVVAEK------------IAGPFPRYLIVTEGELGAILYPGGRYNHVPAK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490365462 243 RVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGA 290
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
5-289 |
9.90e-19 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 84.40 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 5 RLAVLGSINVDHIMNIAQFPKPGETVIGHDYKIAFGGkGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTd 84
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 85 airIIPKTP---TGVAMILVNEQGENVISIVAGANSALTPSHLHQyrhIIEQADALLM----QLESP--LDTVFEAAKQA 155
Cdd:cd01944 79 ---LLPPRGgddGGCLVALVEPDGERSFISISGAEQDWSTEWFAT---LTVAPYDYVYlsgyTLASEnaSKVILLEWLEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 156 KAHQTKVILNPAPAQP-LSDEFLSFI----DIITPNETEAEILTGisvHDEVGAAKAANILHSKGIKHVLITLGSRGVW- 229
Cdd:cd01944 153 LPAGTTLVFDPGPRISdIPDTILQALmakrPIWSCNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWi 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 230 FSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHG 289
Cdd:cd01944 230 RLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
8-272 |
1.33e-14 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 73.43 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 8 VLGSINVDhIMNIAQFPKPGETVIGHDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNID-TDAI 86
Cdd:PRK09954 62 VVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNvSGCI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 87 RIIPKTpTGVAMILVNEQGENVISIvagaNSA-----LTPSHLHQYRHIIEQADALLMQLE---SPLDTVFEAA------ 152
Cdd:PRK09954 141 RLHGQS-TSTYLAIANRQDETVLAI----NDThilqqLTPQLLNGSRDLIRHAGVVLADCNltaEALEWVFTLAdeipvf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 153 ----KQAKAHQTKvilnpapaqplsdEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRGV 228
Cdd:PRK09954 216 vdtvSEFKAGKIK-------------HWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESV 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490365462 229 WFSEQ-GTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHD 272
Cdd:PRK09954 283 FCSEKdGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRD 327
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
54-256 |
1.62e-14 |
|
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: 72.59 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 54 GADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIiPKTPTgVAMILVNEQGENVISIVAGANSALTPSHLHQ----YRH 129
Cdd:cd01172 53 GAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVD-EGRPT-TTKTRVIARNQQLLRVDREDDSPLSAEEEQRlierIAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 130 IIEQADALLMQ-----LESPlDTVFEAAKQAKAHQTKVILNPapaQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGA 204
Cdd:cd01172 131 RLPEADVVILSdygkgVLTP-RVIEALIAAARELGIPVLVDP---KGRDYSKYRGATLLTPNEKEAREALGDEINDDDEL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490365462 205 AKAA-NILHSKGIKHVLITLGSRGV-WFSEQGTGMIIPGFRVEAVDTIAAGDTF 256
Cdd:cd01172 207 EAAGeKLLELLNLEALLVTLGEEGMtLFERDGEVQHIPALAKEVYDVTGAGDTV 260
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
35-265 |
2.17e-13 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 69.65 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 35 YKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILVNEQGE-------N 107
Cdd:PLN02323 38 FKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGErefmfyrN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 108 visivAGANSALTPSHLHQyrHIIEQADAL----LMQLESPLDTV-FEAAKQAKahQTKVILNPAP---------AQPLS 173
Cdd:PLN02323 118 -----PSADMLLRESELDL--DLIRKAKIFhygsISLITEPCRSAhLAAMKIAK--EAGALLSYDPnlrlplwpsAEAAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 174 DEFLSF---IDIITPNETEAEILTGISVHDEvgaAKAANILHSKgIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVDTI 250
Cdd:PLN02323 189 EGIMSIwdeADIIKVSDEEVEFLTGGDDPDD---DTVVKLWHPN-LKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTT 264
|
250
....*....|....*
gi 490365462 251 AAGDtfngAFVTAIL 265
Cdd:PLN02323 265 GAGD----AFVGGLL 275
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
118-269 |
2.33e-12 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 65.68 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 118 ALTPSHLHQY------RHIIEQADALL---MQLESPLDTVFEAAKQAKAH--QTKVILNP-----------AP--AQPLS 173
Cdd:cd01173 51 VLSAEELEDLlegleaLGLLLEYDAVLtgyLGSAEQVEAVAEIVKRLKEKnpNLLYVCDPvmgdngklyvvAEeiVPVYR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 174 DEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITlgsrGVWFSEQGTGMIIpGFRVEAVDTIA-- 251
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT----SVELADDDRIEML-GSTATEAWLVQrp 205
|
170 180
....*....|....*....|....*...
gi 490365462 252 ----------AGDTFNGAFVTAILEGKS 269
Cdd:cd01173 206 kipfpayfngTGDLFAALLLARLLKGKS 233
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
33-267 |
9.60e-12 |
|
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: 63.91 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 33 HDYKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPkTPTGVAMILVnEQGENVI--- 109
Cdd:cd01940 15 HLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKE-GENAVADVEL-VDGDRIFgls 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 110 --SIVAGANSaltpshLHQYRHIIEQADALLMQLESPLDTVFEAAKQAKAHQTKVilnpapAQPLSDEFLS-FIDIITPN 186
Cdd:cd01940 93 nkGGVAREHP------FEADLEYLSQFDLVHTGIYSHEGHLEKALQALVGAGALI------SFDFSDRWDDdYLQLVCPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 187 ETEAEILTGISVHDEVGaaKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILE 266
Cdd:cd01940 161 VDFAFFSASDLSDEEVK--AKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLA 238
|
.
gi 490365462 267 G 267
Cdd:cd01940 239 G 239
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
142-261 |
5.32e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 62.93 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 142 ESPLDTVFEAAKQAKAHQTKVILNPAP-AQPLSDE----------FLSFIDIITPNETEAEILTGISvhDEVGAAKAanI 210
Cdd:PLN02341 237 ELSPSAIASAVDYAIDVGTAVFFDPGPrGKSLLVGtpderralehLLRMSDVLLLTSEEAEALTGIR--NPILAGQE--L 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490365462 211 LH-SKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFV 261
Cdd:PLN02341 313 LRpGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIA 364
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
175-222 |
7.44e-11 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 61.64 E-value: 7.44e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490365462 175 EFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLIT 222
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
140-272 |
4.16e-10 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 58.92 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 140 QLESPLDTVFEA-----------AKQA----KAHQ-TKVILNPA---------PAQPLSDEFLSF---IDIITPNETEAE 191
Cdd:PRK12413 62 QLDSLKDVPFSAikigllpnveiAEQAldfiKGHPgIPVVLDPVlvckethdvEVSELRQELIQFfpyVTVITPNLVEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 192 ILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRgvwFSEQ--------GTGMIIPGFRVEAVDTIAAGDTFNGAFVTA 263
Cdd:PRK12413 142 LLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR---LSQKkaidlfydGKEFVILESPVLEKNNIGAGCTFASSIASQ 218
|
....*....
gi 490365462 264 ILEGKSAHD 272
Cdd:PRK12413 219 LVKGKSPLE 227
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
181-272 |
6.51e-10 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 58.62 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 181 DIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITlGSRGVWFSEQGTGMIIPG----FRVEA----VDTIAA 252
Cdd:COG2240 140 DIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT-SVPLDDTPADKIGNLAVTadgaWLVETpllpFSPNGT 218
|
90 100
....*....|....*....|
gi 490365462 253 GDTFNGAFVTAILEGKSAHD 272
Cdd:COG2240 219 GDLFAALLLAHLLRGKSLEE 238
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
22-269 |
1.97e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 57.90 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 22 QFPKPGETVIGHD-------------YKIAFGGKGANQAVACGRSGA--------DITFIACVGDDAIGREIIAQLKTDN 80
Cdd:PLN02813 95 GLEKGTRKVINHEergkvlraldgcsYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRAN 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 81 IDTDAIRIIPKTpTGVAMILVNEQGENVISIVAGANSALtpSHLHQYRHIIEQADALLMQ-----LESPLDTVFEAAKQA 155
Cdd:PLN02813 175 VHFLSQPVKDGT-TGTVIVLTTPDAQRTMLSYQGTSSTV--NYDSCLASAISKSRVLVVEgylweLPQTIEAIAQACEEA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 156 KAHQTKVILNPAPAQPLS---DEFLSFI----DIITPNETEAEILTGISVhDEVGAAKAANILHSkgIKHVLITLGSRGV 228
Cdd:PLN02813 252 HRAGALVAVTASDVSCIErhrDDFWDVMgnyaDILFANSDEARALCGLGS-EESPESATRYLSHF--CPLVSVTDGARGS 328
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490365462 229 WFSEQGTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKS 269
Cdd:PLN02813 329 YIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYGLLRGVS 369
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
164-256 |
3.41e-09 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 56.34 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 164 LNPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLG--------SRGVWFSEQGT 235
Cdd:pfam08543 104 LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeavVTDVLYDGGGF 183
|
90 100
....*....|....*....|.
gi 490365462 236 gMIIPGFRVEAVDTIAAGDTF 256
Cdd:pfam08543 184 -YTLEAPRIPTKNTHGTGCTL 203
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
181-270 |
9.51e-09 |
|
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273221 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 181 DIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLIT-LGSRGVWFSEQGTGMIIPG------------FRVEAV 247
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQRDRSFEGLVATQegrwhisrplavFDPPPV 219
|
90 100
....*....|....*....|...
gi 490365462 248 DTiaaGDTFNGAFVTAILEGKSA 270
Cdd:TIGR00687 220 GT---GDLIAALLLATLLHGNSL 239
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
172-256 |
2.42e-08 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 53.89 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 172 LSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLITLGSRG------VWFSEQGTgMIIPGFRVE 245
Cdd:COG0351 119 LRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPgdeavdVLYDGDGV-REFSAPRID 197
|
90
....*....|.
gi 490365462 246 AVDTIAAGDTF 256
Cdd:COG0351 198 TGNTHGTGCTL 208
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
58-269 |
4.08e-08 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 53.57 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 58 TFIACVGDDAIGREIIAQLKTDNIDTdAIRIIPKTPTGVAMILVNEqGENviSIVAGANSA--LTPSHLHQYRH--IIEQ 133
Cdd:PLN02548 73 SYMGCIGKDKFGEEMKKCATAAGVNV-HYYEDESTPTGTCAVLVVG-GER--SLVANLSAAncYKVEHLKKPENwaLVEK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 134 AD----ALLMQLESPlDTVFEAAKQAKAHQTKVILN-PAP--AQPLSD---EFLSFIDIITPNETEAEILT---GISVHD 200
Cdd:PLN02548 149 AKfyyiAGFFLTVSP-ESIMLVAEHAAANNKTFMMNlSAPfiCEFFKDqlmEALPYVDFLFGNETEARTFAkvqGWETED 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 201 -EVGAAKAANILHSKGiKH---VLITLGSRGVWFSEQG---TGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKS 269
Cdd:PLN02548 228 vEEIALKISALPKASG-THkrtVVITQGADPTVVAEDGkvkEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKD 302
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
142-272 |
6.32e-08 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 53.21 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 142 ESPLDTVFEAAKQAKAHQTKVI--------------LNPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKA 207
Cdd:PLN02978 98 VSFLRTVLRVVKKLRSVNPNLTyvcdpvlgdegklyVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREA 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490365462 208 ANILHSKGIKHVLIT----------LGSRGVWFSEQGTGMIIpgfrveAVDTIAAGDTFNGAFVTAILEGKSAHD 272
Cdd:PLN02978 178 CAILHAAGPSKVVITsididgklllVGSHRKEKGARPEQFKI------VIPKIPAYFTGTGDLMAALLLGWSHKY 246
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
181-272 |
7.86e-08 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 52.44 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 181 DIITPNETEAEILTGISVHDEVGAAK-AANILHSKGIKHVLITLG-------SRGVWFSeqGTGMIIpgFRVEAVDTIA- 251
Cdd:PRK06427 135 TLITPNLPEAEALTGLPIADTEDEMKaAARALHALGCKAVLIKGGhlldgeeSVDWLFD--GEGEER--FSAPRIPTKNt 210
|
90 100
....*....|....*....|....
gi 490365462 252 --AGDTFNGAfVTAIL-EGKSAHD 272
Cdd:PRK06427 211 hgTGCTLSAA-IAAELaKGASLLD 233
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
177-261 |
5.22e-07 |
|
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: 50.16 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 177 LSFIDIITPNETEAEILTGisvhdEVGAAKAANILHSKGIKHVLITLGSRGVWFSEQGTGMIIPGFRVEAV-DTIAAGDT 255
Cdd:cd01946 161 LAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGDT 235
|
....*.
gi 490365462 256 FNGAFV 261
Cdd:cd01946 236 FAGGFI 241
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
182-294 |
7.09e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 49.69 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 182 IITPNETEAEILTG---ISVHDEVGAAKAaniLHSKGIKHVLITLGSRG-VWFSEQGTGMIIPGfRVEAVDTIAAGDTFN 257
Cdd:PRK09513 183 LVKPNRRELEIWAGrklPELKDVIEAAHA---LREQGIAHVVISLGAEGaLWVNASGEWIAKPP-ACDVVSTVGAGDSMV 258
|
90 100 110
....*....|....*....|....*....|....*..
gi 490365462 258 GAFVTAILEGKSAHDAIRFAHAAAAIAVTrhgaQSSV 294
Cdd:PRK09513 259 GGLIYGLLMRESSEHTLRLATAVSALAVS----QSNV 291
|
|
| PLN02967 |
PLN02967 |
kinase |
35-203 |
2.59e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 48.89 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 35 YKIAFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILVNEQGENVISIVAG 114
Cdd:PLN02967 238 FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 115 -ANSALTPSHLHQyrHIIEQADALLMQLESPLD-----TVFEAAKQAKAHQTKVI--LN-PAPAQPLSDEFLSFI----- 180
Cdd:PLN02967 318 cAEDSLSKSEINI--DVLKEAKMFYFNTHSLLDptmrsTTLRAIKISKKLGGVIFydLNlPLPLWSSSEETKSFIqeawn 395
|
170 180
....*....|....*....|....*
gi 490365462 181 --DIITPNETEAEILTGISVHDEVG 203
Cdd:PLN02967 396 laDIIEVTKQELEFLCGIEPTEEFD 420
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
93-208 |
5.86e-06 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 47.31 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 93 PTGVAMILVNEQGENVISIVAGANSALTPSHLHQyrHIIEQADAL-----LMQLeSPLDTVFEAAKQA----KAHQTKVI 163
Cdd:PRK15074 148 PIGRCFTLISEDGERTFAISPGHMNQLRPESIPE--DVIAGASALvltayLVRC-KPGEPMPEATMKAieyaKKHNVPVV 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 164 L----------NPAPAQplsdEFLS-FIDIITPNETEAEILTGISvhDEVGAAKAA 208
Cdd:PRK15074 225 LtlgtkfviedNPQWWQ----EFLKeHVSILAMNEDEAEALTGES--DPLLASDKA 274
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
175-270 |
1.35e-05 |
|
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: 45.47 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 175 EFLSFIDIITPNETEAEILtgisvhdeVGAAKAANILHSKGIKHVLITLGSRGVW-FSeqGTGMI-IPGFRVEAVDTIAA 252
Cdd:cd01937 151 VILKLHDVLKLSRVEAEVI--------STPTELARLIKETGVKEIIVTDGEEGGYiFD--GNGKYtIPASKKDVVDPTGA 220
|
90
....*....|....*...
gi 490365462 253 GDTFNGAFVTAILEGKSA 270
Cdd:cd01937 221 GDVFLAAFLYSRLSGKDI 238
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
57-269 |
2.50e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.40 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 57 ITFIACVGDDAIGREIIAQLKTDNIDTdAIRIIPKTPTGVAMILVNEQGEnviSIVA--GANSALTPSHLHQYRHIIEQA 134
Cdd:PTZ00247 83 VCYVGCVGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTCAVLVCGKER---SLVAnlGAANHLSAEHMQSHAVQEAIK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 135 DALLMQLE------SPlDTVFEAAKQAKAHQTKVILN---PAPAQPLSDEF---LSFIDIITPNETEAEILTGISVHDEV 202
Cdd:PTZ00247 159 TAQLYYLEgffltvSP-NNVLQVAKHARESGKLFCLNlsaPFISQFFFERLlqvLPYVDILFGNEEEAKTFAKAMKWDTE 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365462 203 G----AAKAANILHSKGIKH--VLITLGSRGVWFSEQGTGMIIPGFRVEA---VDTIAAGDTFNGAFVTAILEGKS 269
Cdd:PTZ00247 238 DlkeiAARIAMLPKYSGTRPrlVVFTQGPEPTLIATKDGVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKD 313
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
162-222 |
2.84e-05 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 44.86 E-value: 2.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365462 162 VILNPAPAQPLSDEFLSFIDIITPNETEAEILTGISVHDEVGAAKAANILHSKGIKHVLIT 222
Cdd:PRK05756 121 CIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
38-193 |
9.81e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 43.74 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 38 AFGGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILV--NEQGENVISIVAGA 115
Cdd:PLN02543 170 APGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIkfRDGGKMVAETVKEA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 116 ------NSALTPSHLHQYRHIIEQADALL---MQlesplDTVFEAAKQAKAHQTKVILNPAPAQPL---SDEFLSFI--- 180
Cdd:PLN02543 250 aedsllASELNLAVLKEARMFHFNSEVLTspsMQ-----STLFRAIELSKKFGGLIFFDLNLPLPLwrsRDETRELIkka 324
|
170
....*....|....*..
gi 490365462 181 ----DIITPNETEAEIL 193
Cdd:PLN02543 325 wneaDIIEVSRQELEFL 341
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
40-290 |
1.31e-03 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 39.72 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 40 GGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKtPTGVA-MILVNEQ---GENVISIVAGA 115
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG-VTAQTqVELHDNDrvfGDYTEGVMADF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 116 nsALTPSHL-----HQYRH--IIEQADALLMQL-ESPLDTVFEAAKQakahqtkvilnpaPAQPLSDEFLSFIDI---IT 184
Cdd:PRK09813 102 --ALSEEDYawlaqYDIVHaaIWGHAEDAFPQLhAAGKLTAFDFSDK-------------WDSPLWQTLVPHLDYafaSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 185 PNETEaeiltgiSVHDEVGAAKAanilhsKGIKHVLITLGSRG--VWFSEQGTGMiiPGFRVEAVDTIAAGDTFNGAFVT 262
Cdd:PRK09813 167 PQEDE-------FLRLKMKAIVA------RGAGVVIVTLGENGsiAWDGAQFWRQ--APEPVTVVDTMGAGDSFIAGFLC 231
|
250 260
....*....|....*....|....*...
gi 490365462 263 AILEGKSAHDAIRFAHAAAAIAVTRHGA 290
Cdd:PRK09813 232 GWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
40-305 |
8.00e-03 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 37.95 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 40 GGKGANQAVACGRSGADITFIACVGDDAIGREIIAQLKTDNIDTDAIRIIPKTPTGVAMILVNEQgENVISIVAGANSA- 118
Cdd:COG3892 38 GGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSGVVTDPERLTALVLLGIRDD-ETFPLIFYRENCAd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 119 --LTPSHLHQyrHIIEQADALLM---QLESP--LDTVFEAAKQAKAHQTKVIL----NP---------------APAQPL 172
Cdd:COG3892 117 maLTEDDIDE--AFIASARALLItgtHLSHPrtRAAVLKALRYARAHGGKVVLdidyRPvlwgltghgdgetrfVASDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 173 SD---EFLSFIDIITpnETEAEILTGISVHDEVGAAKAANILHSKGIkhVLITLGSRGVWFSEQG-----TGMIIPGFRV 244
Cdd:COG3892 195 TAhlqEVLPLFDLIV--GTEEEFHIAGGSTDTLAALRAVRRVSTATL--VCKRGALGCVVFEGAIpddldDGITGPGFPV 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365462 245 EAVDTIAAGDTFNGAFVTAILEGKSAHDAIRFAHAAAAIAVTRHGAQSSVPWRDEIKSFLA 305
Cdd:COG3892 271 EVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMPTWEELDYFLA 331
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
135-272 |
8.25e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 37.26 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365462 135 DALLMQLESPLDTVFEAAKQAKAHQTK-VILNPA--------PAQP-----LSDEFLSFIDIITPNETEAEILTGISVHD 200
Cdd:PRK12412 74 DALKTGMLGSVEIIEMVAETIEKHNFKnVVVDPVmvckgadeALHPetndcLRDVLVPKALVVTPNLFEAYQLSGVKINS 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490365462 201 EVGAAKAANILHSKGIKHVLITLGSR-------GVWFSEQgTGMIIPGFRVEAVDTIAAGDTFNGAFVTAILEGKSAHD 272
Cdd:PRK12412 154 LEDMKEAAKKIHALGAKYVLIKGGSKlgtetaiDVLYDGE-TFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231
|
|
| |
