|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
3-308 |
0e+00 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 507.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 3 TAKLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIK 82
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 83 TECIDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYQQKIIEADAVLMQLESPLDTVQMAAEIANKNNTQV 162
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 163 ILNPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEQGsQGKIIPA 242
Cdd:PRK11142 162 ILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENG-EGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599170 243 FNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQPSVPWRKEIEQFLTQQ 308
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-297 |
1.18e-124 |
|
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: 358.02 E-value: 1.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYQQKIIEADAVLMQLESPLDTVQMAAEIANKNNTQVIL 164
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 165 NPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEqGSQGKIIPAFN 244
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS-GGEVEHVPAFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 757599170 245 VKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQPSVPW 297
Cdd:cd01174 240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
10-302 |
6.36e-123 |
|
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: 353.83 E-value: 6.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 10 GSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDAI 89
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 90 QDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYQQKIIEADAVLMQLESPLDTVQMAAEIANKNNTQVILNPAPA 169
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 170 Q-SLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQgKIIPAFNVKAV 248
Cdd:TIGR02152 161 IkDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDES-KLIPAFKVKAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 757599170 249 DTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQPSVPWRKEIE 302
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-301 |
1.40e-79 |
|
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: 243.64 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLAsyQQKIIEADAVLMQL-----ESPLDTVQMAAEIANKNN 159
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLD--EALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 160 TQVILNPA-------PAQSLPDSLLTLVDIITPNETEAEHLTGIAvndnkGAQAAAQVLHEKGISKVMITLGSRGVWYSE 232
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599170 233 QGSQGKiIPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQPSVPWRKEI 301
Cdd:COG0524 234 GGEVVH-VPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-292 |
1.36e-69 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 217.98 E-value: 1.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPqpGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYQQKIIEADAV----LMQLESPLDTVQMAAEIANKNNT 160
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 161 --QVILNPA-PAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQG 237
Cdd:pfam00294 159 fdPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 757599170 238 KIIPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQ 292
Cdd:pfam00294 239 HVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-301 |
1.09e-68 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 216.91 E-value: 1.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 2 ATAKLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNI 81
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 82 KTECIDAIQDETTGVALIYVNQQ-GENIIGISAGANAQLTTERL----ASYQQKiieADAVLMQLESPLDTVQMAAEIAN 156
Cdd:PTZ00292 94 NTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVdaqtDNIQNI---CKYLICQNEIPLETTLDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 157 KNNTQVILNPAPAQSLPDS-----LLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYS 231
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEVeiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 232 EQGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQPSVPWRKEI 301
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
5-269 |
3.02e-37 |
|
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: 133.98 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGdHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPG-HVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIdAIQDETTGVALIYVNQQGENIIGIS-AGANAQLTTERLASYQQKIIEADAVLMQLESPLDTVQMAAEIANKNNTQVI 163
Cdd:cd01941 80 GI-VFEGRSTASYTAILDKDGDLVVALAdMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 164 LNPAPAQSLPDSLLTL--VDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYS--EQGSQGKI 239
Cdd:cd01941 159 FEPTSAPKLKKLFYLLhaIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSsrEGGVETKL 238
|
250 260 270
....*....|....*....|....*....|.
gi 757599170 240 IPAFNV-KAVDTIAAGDTFNGAYVTALLEGK 269
Cdd:cd01941 239 FPAPQPeTVVNVTGAGDAFVAGLVAGLLEGM 269
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-266 |
6.36e-35 |
|
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: 125.29 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIAcvgddgigssikkqlsldnikte 84
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 cidaiqdettgvaliyvnqqgeniigisaganaqltterlasyqqkiieADAVLMQLESP-LDTVQMAAEIANKNNTQVI 163
Cdd:cd00287 58 -------------------------------------------------ADAVVISGLSPaPEAVLDALEEARRRGVPVV 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 164 LNPAPAQSLPD-----SLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQGK 238
Cdd:cd00287 89 LDPGPRAVRLDgeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEV 168
|
250 260
....*....|....*....|....*...
gi 757599170 239 IIPAFNVKAVDTIAAGDTFNGAYVTALL 266
Cdd:cd00287 169 HVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-291 |
1.91e-33 |
|
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: 124.23 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHIlnvkqFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:cd01166 1 DVVTIGEVMVDLS-----PPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIDAIQDETTGVALIYVNQQGEN--IIGISAGANAQLTTERLAsyQQKIIEADAV------LMQLESPLDTVQMAAEIAN 156
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERrvLYYRAGSAASRLTPEDLD--EAALAGADHLhlsgitLALSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 157 KNNTQVILNPAPAQSLPD---------SLLTLVDIITPNETEAEHLTGiavnDNKGAQAAAQVL-HEKGISKVMITLGSR 226
Cdd:cd01166 154 ARGVTVSFDLNYRPKLWSaeearealeELLPYVDIVLPSEEEAEALLG----DEDPTDAAERALaLALGVKAVVVKLGAE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757599170 227 GVWYSEQGSQGKIiPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGA 291
Cdd:cd01166 230 GALVYTGGGRVFV-PAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-292 |
1.30e-30 |
|
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: 116.26 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 6 LVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTEC 85
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 86 IDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYqqkIIEADAVLMQLESPLdtVQMAAEIANKNNTqVILN 165
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADP---DGLADIVHLSSGPGL--IELARELAAGGIT-VSFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 166 PApaQSLP----DSLLT---LVDIITPNETEAE---HLTGIAVNDNkgaqaaaqvlhEKGISKVMITLGSRGVWYSEQGS 235
Cdd:cd01942 156 PG--QELPrlsgEELEEileRADILFVNDYEAEllkERTGLSEAEL-----------ASGVRVVVVTLGPKGAIVFEDGE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 757599170 236 QGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPGAQ 292
Cdd:cd01942 223 EVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-268 |
7.67e-29 |
|
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: 111.62 E-value: 7.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 9 LGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDA 88
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 89 IQDETTGVALIYVNQQGENIIGISAG----ANAQLTTERLASyqqkiieADAVLMQLESPlDTVQMAAEIANKNNTQVIL 164
Cdd:cd01945 85 APGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGG-------ADAVLVDGRQP-EAALHLAQEARARGIPIPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 165 NPAPAQSLPDS-LLTLVDIITPNETEAEHLTGIAVNDnkgaqaAAQVLHEKGISKVMITLGSRGVWYSEQGSQGKIIPAF 243
Cdd:cd01945 157 DLDGGGLRVLEeLLPLADHAICSENFLRPNTGSADDE------ALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPAF 230
|
250 260
....*....|....*....|....*
gi 757599170 244 NVKAVDTIAAGDTFNGAYVTALLEG 268
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEG 255
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
26-268 |
3.37e-28 |
|
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: 110.42 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 26 PGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDAIQDETTGVALIYVNQQG 105
Cdd:cd01167 14 PEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 106 E---NIIGiSAGANAQLTTERLASyqqKIIEADAV----LMQLESPL-DTVQMAAEIANKNNTQVIL----------NPA 167
Cdd:cd01167 94 ErsfEFYR-GPAADLLLDTELNPD---LLSEADILhfgsIALASEPSrSALLELLEAAKKAGVLISFdpnlrpplwrDEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 168 PAQSLPDSLLTLVDIITPNETEAEHLTGIavndnKGAQAAAQVLHEKGISKVMITLGSRGVWYSeQGSQGKIIPAFNVKA 247
Cdd:cd01167 170 EARERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLY-TKGGVGEVPGIPVEV 243
|
250 260
....*....|....*....|.
gi 757599170 248 VDTIAAGDTFNGAYVTALLEG 268
Cdd:cd01167 244 VDTTGAGDAFVAGLLAQLLSR 264
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
5-290 |
3.59e-23 |
|
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: 96.72 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGkGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTE 84
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 cIDAIQDETTGVALIYVNQQGENIIGISAGANAQLTTERLASYQqkIIEADAVLM---QLESP--LDTVQMAAEIANKNN 159
Cdd:cd01944 80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLT--VAPYDYVYLsgyTLASEnaSKVILLEWLEALPAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 160 TQVILNPAPA-QSLPDSLLTLV----DIITPNETEAEHLTGiavndnKG---AQAAAQVLHEKGISKVMITLGSRGVWYS 231
Cdd:cd01944 157 TTLVFDPGPRiSDIPDTILQALmakrPIWSCNREEAAIFAE------RGdpaAEASALRIYAKTAAPVVVRLGSNGAWIR 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 757599170 232 EQGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEGKADEDAIIFAHAAAAIAVTRPG 290
Cdd:cd01944 231 LPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
15-273 |
1.93e-21 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 92.12 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 15 DHILNVKQFpQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDgIGSSIKKQLSLDNIKTECIDaIQDET- 93
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGF-TGEFIEELLDEEGIPTDFVP-IEGETr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 94 TGVALIY--------VNQQGENIigiSAGANAQLtterLASYQQKIIEADAVLMqleS-------PLDTVQMAAEIANKN 158
Cdd:COG1105 88 INIKIVDpsdgteteINEPGPEI---SEEELEAL----LERLEELLKEGDWVVL---SgslppgvPPDFYAELIRLARAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 159 NTQVIL---NPApaqsLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRG-VWYSEQG 234
Cdd:COG1105 158 GAKVVLdtsGEA----LKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGaLLVTEDG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 757599170 235 S-QGKIIPafnVKAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:COG1105 234 VyRAKPPK---VEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
40-269 |
3.23e-21 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 91.52 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 40 GGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTEcIDAIQDETTGVALIYVNQQGENIIGISAGANAQL 119
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTR-YQVQPDGPTGTCAVLVTPDAERTMCTYLGAANEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 120 TTERLAsyqQKIIEADAVL----MQLESPLDTVQMAAEIANKNNTQVILNpAPAQSLPD-------SLLTLVDIITPNET 188
Cdd:cd01168 134 SPDDLD---WSLLAKAKYLylegYLLTVPPEAILLAAEHAKENGVKIALN-LSAPFIVQrfkeallELLPYVDILFGNEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 189 EAEHLTGIAVNDnkgAQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEG 268
Cdd:cd01168 210 EAEALAEAETTD---DLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQG 286
|
.
gi 757599170 269 K 269
Cdd:cd01168 287 E 287
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
5-273 |
9.40e-21 |
|
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: 89.40 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTe 84
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 cIDAIQDETTGVALIYVNQQGENIIGISAGA-NAQLTTERLASYqqkiieaDAVLMQLESPLDTVQMAAEiankNNTQVI 163
Cdd:cd01947 80 -TVAWRDKPTRKTLSFIDPNGERTITVPGERlEDDLKWPILDEG-------DGVFITAAAVDKEAIRKCR----ETKLVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 164 LNPAPAQSL--PDSLLTLVDIITPNETEAEHLTgiavndnkgaqaAAQVLHEKGISKVMITLGSRG-VWYSeqGSQGKII 240
Cdd:cd01947 148 LQVTPRVRVdeLNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGaILYP--GGRYNHV 213
|
250 260 270
....*....|....*....|....*....|...
gi 757599170 241 PAFNVKAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEE 246
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
54-257 |
2.76e-15 |
|
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: 74.90 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 54 GADITFIACVGDDGIGSSIKKQLSLDNIKTECIdAIQDETTGVALIYV--NQQ-----GENIIGISAGANAQLtterLAS 126
Cdd:cd01172 53 GAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTTKTRVIarNQQllrvdREDDSPLSAEEEQRL----IER 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 127 YQQKIIEADAVLMQ-----LESPlDTVQMAAEIANKNNTQVILNPapaQSLPDSLLTLVDIITPNETEAEHLTGIAVNDN 201
Cdd:cd01172 128 IAERLPEADVVILSdygkgVLTP-RVIEALIAAARELGIPVLVDP---KGRDYSKYRGATLLTPNEKEAREALGDEINDD 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 757599170 202 KGAQAAAQVLHEK-GISKVMITLGSRGVWYSEQGSQGKIIPAFNVKAVDTIAAGDTF 257
Cdd:cd01172 204 DELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGEVQHIPALAKEVYDVTGAGDTV 260
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
6-268 |
1.64e-14 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 72.71 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 6 LVVLGSINAD------HILNVKQfPQPGetvrgdhyQVAF--GGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLS 77
Cdd:PRK09850 7 VVIIGSANIDvagyshESLNYAD-SNPG--------KIKFtpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 78 LDNIKTECIDAIQDETTGVALIYVNQQGENIIGIS-AGANAQLTTERLASYQQ-----KIIEADAVLMqlESPLDTVqma 151
Cdd:PRK09850 78 QSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNAITAEYLAQHREfiqraKVIVADCNIS--EEALAWI--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 152 aeIANKNNTQVILNPAPAQSLPD--SLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVW 229
Cdd:PRK09850 153 --LDNAANVPVFVDPVSAWKCVKvrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVY 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 757599170 230 YSEQGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEG 268
Cdd:PRK09850 231 YSDISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDG 269
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
7-273 |
2.71e-13 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 69.57 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 7 VVLGSINADhILNVKQFPQPGETVRGDHYQVAFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIK-TEC 85
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNvSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 86 IdAIQDETTGVALIYVNQQGENIIGIS-AGANAQLTTERLASYQQKIIEADAVLMQLESPLDTVQMAAEIANKNNTQVIL 164
Cdd:PRK09954 140 I-RLHGQSTSTYLAIANRQDETVLAINdTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLADEIPVFVDT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 165 NPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQGKIIPAFN 244
Cdd:PRK09954 219 VSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTAPA 298
|
250 260
....*....|....*....|....*....
gi 757599170 245 VKAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:PRK09954 299 HTTVDSFGADDGFMAGLVYSFLEGYSFRD 327
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
174-273 |
5.91e-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: 64.53 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 174 DSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT---LGSRGVWYSeQGSQGKIIPAFNVKAVDT 250
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveLADDDRIEM-LGSTATEAWLVQRPKIPF 209
|
90 100
....*....|....*....|....*..
gi 757599170 251 IA----AGDTFNGAYVTALLEGKADED 273
Cdd:cd01173 210 PAyfngTGDLFAALLLARLLKGKSLAE 236
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
6-262 |
2.43e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 64.08 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 6 LVVLGSINADHILNVKQFPQPGETVR-------------GDHYQVafgGKGANQAVAAGRSGADITFIACVGDDgigssI 72
Cdd:PLN02341 75 VATLGNLCVDIVLPVPELPPPSREERkaymeelaasppdKKSWEA---GGNCNFAIAAARLGLRCSTIGHVGDE-----I 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 73 KKQLSLDNIKTECIDAIQDETTGVALIYVNQQGENII------GISAGA---NAQLTTERLASYQQKII-EADAVLMQL- 141
Cdd:PLN02341 147 YGKFLLDVLAEEGISVVGLIEGTDAGDSSSASYETLLcwvlvdPLQRHGfcsRADFGPEPAFSWISKLSaEAKMAIRQSk 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 142 ----------ESPLDTVQMAAEIANKNNTQVILNPAP-AQSL----PDS------LLTLVDIITPNETEAEHLTGIAvnd 200
Cdd:PLN02341 227 alfcngyvfdELSPSAIASAVDYAIDVGTAVFFDPGPrGKSLlvgtPDErralehLLRMSDVLLLTSEEAEALTGIR--- 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757599170 201 nKGAQAAAQVLHEKGISK-VMITLGSRGVWYSEQGSQGkIIPAFNVKAVDTIAAGDTFNGAYV 262
Cdd:PLN02341 304 -NPILAGQELLRPGIRTKwVVVKMGSKGSILVTRSSVS-CAPAFKVNVVDTVGCGDSFAAAIA 364
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
40-270 |
3.50e-11 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 62.65 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 40 GGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDAIQDETTGVALIYVNQQGEN--IIGISAGANA 117
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 118 QLTTERLASYQQK-------IieadaVLMQLESPLDTVQMAAEIA--------NKN-NTQVILNPAPAQSLPDSLLTLVD 181
Cdd:PRK09434 108 FLQPQDLPPFRQGewlhlcsI-----ALSAEPSRSTTFEAMRRIKaaggfvsfDPNlREDLWQDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 182 IITPNETEAEHLTGIAVNDnkgaQAAAQVLHEKGISKVMITLGSRGVWYSEQGSQgKIIPAFNVKAVDTIAAGDtfngAY 261
Cdd:PRK09434 183 VVKLSEEELCFLSGTSQLE----DAIYALADRYPIALLLVTLGAEGVLVHTRGQV-QHFPAPSVDPVDTTGAGD----AF 253
|
....*....
gi 757599170 262 VTALLEGKA 270
Cdd:PRK09434 254 VAGLLAGLS 262
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
28-271 |
4.18e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 63.29 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 28 ETVRGDHYQVAFGGKGANQAVAAGRSGA--------DITFIACVGDDGIGSSIKKQLSLDNIKTECIdAIQDETTGVALI 99
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQ-PVKDGTTGTVIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 100 YVNQQGENIIGISAGANAQLT-TERLASYQQK--IIEADAVLMQLESPLDTVQMAAEIANKNNTQVILNPAPA------- 169
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNyDSCLASAISKsrVLVVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDVscierhr 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 170 QSLPDSLLTLVDIITPNETEAEHLTGIAVNDNkGAQAAAQVLHEkgISKVMITLGSRGvwySEQGSQGKI--IPAFNVKA 247
Cdd:PLN02813 273 DDFWDVMGNYADILFANSDEARALCGLGSEES-PESATRYLSHF--CPLVSVTDGARG---SYIGVKGEAvyIPPSPCVP 346
|
250 260
....*....|....*....|....
gi 757599170 248 VDTIAAGDTFNGAYVTALLEGKAD 271
Cdd:PLN02813 347 VDTCGAGDAYAAGILYGLLRGVSD 370
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
174-273 |
7.07e-11 |
|
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: 61.70 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 174 DSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT----------------LGSRGVWYSEQgsqg 237
Cdd:COG2240 133 RRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpadkignlaVTADGAWLVET---- 208
|
90 100 110
....*....|....*....|....*....|....*.
gi 757599170 238 kiiPAFNVKAVDTiaaGDTFNGAYVTALLEGKADED 273
Cdd:COG2240 209 ---PLLPFSPNGT---GDLFAALLLAHLLRGKSLEE 238
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
176-222 |
5.19e-09 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 56.24 E-value: 5.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 757599170 176 LLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT 222
Cdd:PTZ00344 136 LIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
174-268 |
7.95e-09 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 55.90 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 174 DSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITL----GSRGVWYSEQGSQGKIIPAFNVkAVD 249
Cdd:PLN02978 144 EKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSididGKLLLVGSHRKEKGARPEQFKI-VIP 222
|
90
....*....|....*....
gi 757599170 250 TIAAGDTFNGAYVTALLEG 268
Cdd:PLN02978 223 KIPAYFTGTGDLMAALLLG 241
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
164-266 |
8.54e-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: 55.18 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 164 LNPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLG--------SRGVWYSEQGS 235
Cdd:pfam08543 104 LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeavVTDVLYDGGGF 183
|
90 100 110
....*....|....*....|....*....|.
gi 757599170 236 QgkIIPAFNVKAVDTIAAGDTFnGAYVTALL 266
Cdd:pfam08543 184 Y--TLEAPRIPTKNTHGTGCTL-SAAIAANL 211
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
38-308 |
1.02e-08 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 55.40 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 38 AFGGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDAIQDETTGVALIYVNQQGE-------Niig 110
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGErefmfyrN--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 111 isAGANAQLTTERLasyQQKIIEADAVLMQ-----LESPLDTVQMAA-EIANKN--------NTQVILNPAP--AQSLPD 174
Cdd:PLN02323 118 --PSADMLLRESEL---DLDLIRKAKIFHYgsislITEPCRSAHLAAmKIAKEAgallsydpNLRLPLWPSAeaAREGIM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 175 SLLTLVDIITPNETEAEHLTGiavNDNKGAQAAAQVLHEKgiSKVMI-TLGSRGVWYSEQGSQGKIiPAFNVKAVDTIAA 253
Cdd:PLN02323 193 SIWDEADIIKVSDEEVEFLTG---GDDPDDDTVVKLWHPN--LKLLLvTEGEEGCRYYTKDFKGRV-EGFKVKAVDTTGA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599170 254 GDTFNGAYVTALLEGKA---DEDAIIFAHAAAAI----AVTRPGAQPSVPWRKEIEQFLTQQ 308
Cdd:PLN02323 267 GDAFVGGLLSQLAKDLSlleDEERLREALRFANAcgaiTTTERGAIPALPTKEAVLKLLKKA 328
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
162-222 |
5.86e-08 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 52.95 E-value: 5.86e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757599170 162 VILNPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT 222
Cdd:PRK05756 121 CIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
181-272 |
1.77e-07 |
|
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: 51.75 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 181 DIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT----LGS-------------RGVWYSEqgsqgKIIPAF 243
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThlirAGSqrdrsfeglvatqEGRWHIS-----RPLAVF 214
|
90 100
....*....|....*....|....*....
gi 757599170 244 NVKAVDTiaaGDTFNGAYVTALLEGKADE 272
Cdd:TIGR00687 215 DPPPVGT---GDLIAALLLATLLHGNSLK 240
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
164-222 |
2.81e-07 |
|
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: 50.81 E-value: 2.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 757599170 164 LNPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMIT 222
Cdd:COG0351 111 LDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVK 169
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
170-266 |
6.60e-07 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 49.74 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 170 QSLPDSLLTLVDIITPNETEAEHLTGIAVNDNK-GAQAAAQVLHEKGISKVMITLG-------SRGVWYSEQGSQgkiip 241
Cdd:PRK06427 124 AALRERLLPLATLITPNLPEAEALTGLPIADTEdEMKAAARALHALGCKAVLIKGGhlldgeeSVDWLFDGEGEE----- 198
|
90 100
....*....|....*....|....*...
gi 757599170 242 AFNVKAVDTIA---AGDTFNGAyVTALL 266
Cdd:PRK06427 199 RFSAPRIPTKNthgTGCTLSAA-IAAEL 225
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
109-224 |
1.67e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 48.96 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 109 IGISAGANAQLTTerlasyqQKIIEADA-VLMQLESPL--DTVQMAAEIANknntqvILNPAPAQSLPDSLLTLVDIITP 185
Cdd:PRK08573 70 MGIDAAKTGMLSN-------REIIEAVAkTVSKYGFPLvvDPVMIAKSGAP------LLREDAVDALIKRLLPLATVVTP 136
|
90 100 110
....*....|....*....|....*....|....*....
gi 757599170 186 NETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLG 224
Cdd:PRK08573 137 NRPEAEKLTGMKIRSVEDARKAAKYIVEELGAEAVVVKG 175
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
175-273 |
1.72e-06 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 48.52 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 175 SLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSR-------GVWYSeqgsqGK--IIPAFNV 245
Cdd:PRK12413 125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNRlsqkkaiDLFYD-----GKefVILESPV 199
|
90 100
....*....|....*....|....*...
gi 757599170 246 KAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:PRK12413 200 LEKNNIGAGCTFASSIASQLVKGKSPLE 227
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
5-269 |
4.83e-06 |
|
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: 47.01 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 5 KLVVLGSINADHIlnvkqfPQPGETVrgdhyqVAFGGKGANQAVAAGRSGADITFIACVGDDgigsSIKKQLSLDNIKTE 84
Cdd:cd01937 1 KIVIIGHVTIDEI------VTNGSGV------VKPGGPATYASLTLSRLGLTVKLVTKVGRD----YPDKWSDLFDNGIE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 85 CIDAIQDETTGVALIYVNQqGENIIGISAGANAQLTTERLAsyqqkIIEADAVLMqleSPL------DTVQMAAEIA--- 155
Cdd:cd01937 65 VISLLSTETTTFELNYTNE-GRTRTLLAKCAAIPDTESPLS-----TITAEIVIL---GPVpeeispSLFRKFAFISlda 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 156 -----NKNNTQVILNPApaqslpdslLTLVDIITPNETEAEHLTGIAvndnkgaqAAAQVLHEKGISKVMITLGSRGVwY 230
Cdd:cd01937 136 qgflrRANQEKLIKCVI---------LKLHDVLKLSRVEAEVISTPT--------ELARLIKETGVKEIIVTDGEEGG-Y 197
|
250 260 270
....*....|....*....|....*....|....*....
gi 757599170 231 SEQGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEGK 269
Cdd:cd01937 198 IFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGK 236
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
33-273 |
9.17e-06 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 46.63 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 33 DHYQVAFGGKGANQ---AVAA---GRSGAdITFIACVGDDGIGSSIKKQLSLDNIKtecIDAIQDET--TGVALIYVNQQ 104
Cdd:PLN02548 43 SKYNVEYIAGGATQnsiRVAQwmlQIPGA-TSYMGCIGKDKFGEEMKKCATAAGVN---VHYYEDEStpTGTCAVLVVGG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 105 GENIIGISAGANAQLTTERLASYQQKIIEAD-----AVLMQLESPlDTVQMAAEIANKNNTQVILN-PAP--AQSLPDSL 176
Cdd:PLN02548 119 ERSLVANLSAANCYKVEHLKKPENWALVEKAkfyyiAGFFLTVSP-ESIMLVAEHAAANNKTFMMNlSAPfiCEFFKDQL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 177 LTL---VDIITPNETEAEHLT---GIAVNDNKG-AQAAAQVLHEKGISK--VMITLGSRGVWYSEQGSQGK--IIPAFNV 245
Cdd:PLN02548 198 MEAlpyVDFLFGNETEARTFAkvqGWETEDVEEiALKISALPKASGTHKrtVVITQGADPTVVAEDGKVKEfpVIPLPKE 277
|
250 260
....*....|....*....|....*...
gi 757599170 246 KAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:PLN02548 278 KLVDTNGAGDAFVGGFLSQLVQGKDIEE 305
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
141-269 |
1.14e-05 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 46.18 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 141 LESPLDTVQMAAEIAN--------KNNTQVIL-NPAPAQSLPDSLLTL------VDIITPNETEAEHLTGIAVNDN---K 202
Cdd:cd01943 127 ICSPERCASIVDDIINlfkllkgnSPTRPKIVwEPLPDSCDPENLEDLlqalprVDVFSPNLEEAARLLGLPTSEPssdE 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599170 203 GAQAAAQVLHEKGISK-----VMITLGSRGVWYSEQGSQGKI-IPAF---NVKAVDTIAAGDTFNGAYVTALLEGK 269
Cdd:cd01943 207 EKEAVLQALLFSGILQdpgggVVLRCGKLGCYVGSADSGPELwLPAYhtkSTKVVDPTGGGNSFLGGFAAGLALTK 282
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
21-269 |
1.44e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 46.17 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 21 KQFPQPGETVrgDHYQVAF--GGKGANQA-VA---AGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTEcIDAIQDETT 94
Cdd:PTZ00247 43 KQLPIFEELE--SIPNVSYvpGGSALNTArVAqwmLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEML-FEYTTKAPT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 95 GVALIYVNQQGENIIGiSAGANAQLTTERLASYQQKIIEADAVLMQLE------SPlDTVQMAAEIANKNNTQVILN--- 165
Cdd:PTZ00247 120 GTCAVLVCGKERSLVA-NLGAANHLSAEHMQSHAVQEAIKTAQLYYLEgffltvSP-NNVLQVAKHARESGKLFCLNlsa 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 166 PAPAQSLPDSLLTL---VDIITPNETEAEHLtGIAVNDNKG-----AQAAAQVLHEKGiSK---VMITLGSRGVWYSEQG 234
Cdd:PTZ00247 198 PFISQFFFERLLQVlpyVDILFGNEEEAKTF-AKAMKWDTEdlkeiAARIAMLPKYSG-TRprlVVFTQGPEPTLIATKD 275
|
250 260 270
....*....|....*....|....*....|....*..
gi 757599170 235 SQGKI-IPAFNV-KAVDTIAAGDTFNGAYVTALLEGK 269
Cdd:PTZ00247 276 GVTSVpVPPLDQeKIVDTNGAGDAFVGGFLAQYANGK 312
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
137-262 |
9.99e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 43.22 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 137 VLMQLESP----LDTVQMAAEIAnknntqvilnpapaqslPDSL---LTLVDIITPNETEAEHLTGIAvndnkGAQAAAQ 209
Cdd:cd01946 131 VLEQVKDPklvvMDTMNFWISIK-----------------PEKLkkvLAKVDVVIINDGEARQLTGAA-----NLVKAAR 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 757599170 210 VLHEKGISKVMITLGSRGVWYSEQgSQGKIIPAFNVKAV-DTIAAGDTFNGAYV 262
Cdd:cd01946 189 LILAMGPKALIIKRGEYGALLFTD-DGYFAAPAYPLESVfDPTGAGDTFAGGFI 241
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
93-269 |
1.46e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 42.65 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 93 TTGVALIYVNQQGENIIGISAGA-NAQLTTerlasyqqkIIEA---DAVLMQLESPLDTVQMAAEIANKNNTQVI----- 163
Cdd:PRK12412 37 TTIVTMDPHNGWAHNVFPIPASTlKPQLET---------TIEGvgvDALKTGMLGSVEIIEMVAETIEKHNFKNVvvdpv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 164 ---------LNPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITLGSR-------G 227
Cdd:PRK12412 108 mvckgadeaLHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetaiD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 757599170 228 VWYSeqGSQGKIIPAFNVKAVDTIAAGDTFNGAYVTALLEGK 269
Cdd:PRK12412 188 VLYD--GETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGK 227
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
145-273 |
8.16e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 40.54 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 145 LDTVQMAAEIANKNNTQVILNPAPAQSLPDSLLTL--------VDIITPNETEAEHLtgIAVNDNKGAQAAAQVLhEKGI 216
Cdd:PLN02379 190 LEVIEAAIRLAKQEGLSVSLDLASFEMVRNFRSPLlqllesgkIDLCFANEDEAREL--LRGEQESDPEAALEFL-AKYC 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 757599170 217 SKVMITLGSRGVwYSEQGSQGKIIPAF-NVKAVDTIAAGDTFNGAYVTALLEGKADED 273
Cdd:PLN02379 267 NWAVVTLGSKGC-IARHGKEVVRVPAIgETNAVDATGAGDLFASGFLYGLIKGLSLEE 323
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
165-273 |
3.33e-03 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 38.48 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 165 NPAPAQSLPDSLLTLVDIITPNETEAEHLTGIAVNDNKGAQAAAQVLHEKGISKVMITlgSRGVWYSEQGSQGKIIPA-- 242
Cdd:PRK08176 138 KPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVIT--SAAGNEENQEMQVVVVTAds 215
|
90 100 110
....*....|....*....|....*....|....*.
gi 757599170 243 FNVKA---VDTIA--AGDTFNGAYVTALLEGKADED 273
Cdd:PRK08176 216 VNVIShprVDTDLkgTGDLFCAELVSGLLKGKALTD 251
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
228-271 |
4.49e-03 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 38.16 E-value: 4.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 757599170 228 VWYSEQGS-----QGKII--PAFN-VKAVDTIAAGDTFNGAYVTALLEGKAD 271
Cdd:cd01939 217 CTWGDQGAgalgpDGEYVhsPAHKpIRVVDTLGAGDTFNAAVIYALNKGPDD 268
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-271 |
7.07e-03 |
|
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: 37.33 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 40 GGKGANQAVAAGRSGADITFIACVGDDGIGSSIKKQLSLDNIKTECIDAIQDETtGVALIYVnQQGENIIGIS---AGAN 116
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGEN-AVADVEL-VDGDRIFGLSnkgGVAR 99
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 117 AQLTTERLAsyqqKIIEADAVLMQLESPLDTvqmaaeiANKNNTQVILNPAPA------QSLPDSLLTLVDIITPNETEA 190
Cdd:cd01940 100 EHPFEADLE----YLSQFDLVHTGIYSHEGH-------LEKALQALVGAGALIsfdfsdRWDDDYLQLVCPYVDFAFFSA 168
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599170 191 EHLTgiavnDNKGAQAAAQVlHEKGISKVMITLGSRG--VWYSEQGSQGKIIPafnVKAVDTIAAGDTFNGAYVTALLEG 268
Cdd:cd01940 169 SDLS-----DEEVKAKLKEA-VSRGAKLVIVTRGEDGaiAYDGAVFYSVAPRP---VEVVDTLGAGDSFIAGFLLSLLAG 239
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gi 757599170 269 KAD 271
Cdd:cd01940 240 GTA 242
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