|
Name |
Accession |
Description |
Interval |
E-value |
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
8-301 |
1.40e-132 |
|
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: 378.10 E-value: 1.40e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 8 GSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEI 87
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 88 QGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVLKNKQLITNSDFIIAQFESSLDATILAFSIAKDAGKTTILNPAPA 167
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 168 RETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAVD 247
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2045671900 248 TTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQPSIPYREALE 301
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKS-LEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-296 |
1.87e-129 |
|
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: 369.96 E-value: 1.87e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSG 83
Cdd:cd01174 2 VVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 IAEIQGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVLKNKQLITNSDFIIAQFESSLDATILAFSIAKDAGKTTILN 163
Cdd:cd01174 82 VEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 164 PAPAReTIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKV 243
Cdd:cd01174 162 PAPAR-PLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2045671900 244 DAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQPSIPY 296
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLS-LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-302 |
3.97e-117 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 339.15 E-value: 3.97e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 1 MNTVTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENID 80
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 81 TSGIAEIQGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVLKNKQLITNSDFIIAQFESSLDATILAFSIAKDAGKTT 160
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 161 ILNPAPAREtIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPA 240
Cdd:PRK11142 162 ILNPAPARE-LPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045671900 241 FKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQPSIPYREALEQ 302
Cdd:PRK11142 241 FRVQAVDTIAAGDTFNGALVTALLEGKP-LPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDA 301
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-300 |
1.59e-89 |
|
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: 269.06 E-value: 1.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSG 83
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 IAEIQGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVlkNKQLITNSDFIIAQ-----FESSLDATILAFSIAKDAGK 158
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDL--DEALLAGADILHLGgitlaSEPPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 159 TTILNPA-------PARETIPtELLEKTDIIIPNETETEIITGIRvtdhnSLVAAAEKLHELGIGTVIITLGSAGAFYHT 231
Cdd:COG0524 160 PVSLDPNyrpalwePARELLR-ELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045671900 232 EKEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQPSIPYREAL 300
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-LEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
2.48e-78 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 241.18 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 1 MNTVTVIGSINMDTTLRLTNMPKPGETMHAHEiFHAG-GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENI 79
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTS-FHKGfGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 80 DTSGIAEIQGATTGQAMIMVDAA-GENSILIHAGANNAFHEQEVLKNKQLITN-SDFIIAQFESSLDATILAFSIAKDAG 157
Cdd:PTZ00292 94 NTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 158 KTTILNPAPARET----IPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAG-AFYHTE 232
Cdd:PTZ00292 174 CYTVFNPAPAPKLaeveIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGcLIVEKE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045671900 233 KEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLsNLKEAILYGNLASSVAVQSYGAQPSIPYREAL 300
Cdd:PTZ00292 254 NEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGK-DLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-291 |
4.07e-68 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 214.13 E-value: 4.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPkpGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSG 83
Cdd:pfam00294 2 VVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 IAEIQGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVLKNKQLITNSDFI----IAQFESSLDATILAFSIAKDAGKT 159
Cdd:pfam00294 80 VVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 160 T--ILNPAPARETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGA-FYHTEKEHG 236
Cdd:pfam00294 160 DpnLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGAlVVEGDGEVH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2045671900 237 IVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQ 291
Cdd:pfam00294 240 VPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKS-LEEALRFANAAAALVVQKSGAQ 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
16-290 |
4.62e-45 |
|
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: 154.66 E-value: 4.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 16 LRLTnmPKPGETMHAHEIFHAG-GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQ 94
Cdd:cd01166 10 VDLS--PPGGGRLEQADSFRKFfGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 95 AMIMVDAAGENSILI---HAGANNAFHEQEvlkNKQLITNSDFI------IAQFESSLDATILAFSIAKDAGKTTIL--- 162
Cdd:cd01166 88 YFLEIGAGGERRVLYyraGSAASRLTPEDL---DEAALAGADHLhlsgitLALSESAREALLEALEAAKARGVTVSFdln 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 163 ------NPAPARETIpTELLEKTDIIIPNETETEIITGIRVTDHnslVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHG 236
Cdd:cd01166 165 yrpklwSAEEAREAL-EELLPYVDIVLPSEEEAEALLGDEDPTD---AAERALALALGVKAVVVKLGAEGALVYTGGGRV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2045671900 237 IVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGA 290
Cdd:cd01166 241 FVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-LEEALRFANAAAALVVTRPGD 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
3-291 |
1.19e-43 |
|
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: 150.54 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 3 TVTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTS 82
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 83 GIAEIQGATTGQAMIMVDAAGENSILIHAGANNafhEQEVLKNKQLITNSDFIiaQFESSLDATILAFSIAKdAGKTTIL 162
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMD---ELEPNDEADPDGLADIV--HLSSGPGLIELARELAA-GGITVSF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 163 NPAPARETIPTE----LLEKTDIIIPNETETEIItgirVTDHNSLVAAAEKlhelGIGTVIITLGSAGA-FYHTEKEHGI 237
Cdd:cd01942 155 DPGQELPRLSGEeleeILERADILFVNDYEAELL----KERTGLSEAELAS----GVRVVVVTLGPKGAiVFEDGEEVEV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2045671900 238 VPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQ 291
Cdd:cd01942 227 PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYD-LEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
38-290 |
5.22e-40 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 141.62 E-value: 5.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 38 GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMVDAAGENSILIHAG-ANNA 116
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 117 FHEQEVlkNKQLITNSDFI----IAQFESSLDATILAF-SIAKDAGKTTIL----------NPAPARETIpTELLEKTDI 181
Cdd:cd01167 108 LLDTEL--NPDLLSEADILhfgsIALASEPSRSALLELlEAAKKAGVLISFdpnlrpplwrDEEEARERI-AELLELADI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 182 IIPNETETEIITGIRVTDhnslvAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAVDTTAAGDTFIGALSS 261
Cdd:cd01167 185 VKLSDEELELLFGEEDPE-----EIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLA 259
|
250 260 270
....*....|....*....|....*....|....*
gi 2045671900 262 TL--QPDLSN----LKEAILYGNLASSVAVQSYGA 290
Cdd:cd01167 260 QLlsRGLLALdedeLAEALRFANAVGALTCTKAGA 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
17-293 |
1.50e-35 |
|
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: 130.04 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 17 RLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSgIAEIQGATTGQAM 96
Cdd:cd01168 34 ILADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTR-YQVQPDGPTGTCA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 97 IMVDAAGENSILIHAGANNAFHEQEVlkNKQLITNSDFII---AQFESSLDATILAFSIAKDAGKTTILN------PAPA 167
Cdd:cd01168 113 VLVTPDAERTMCTYLGAANELSPDDL--DWSLLAKAKYLYlegYLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 168 RETIpTELLEKTDIIIPNETETEIITGIRVTDhnsLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVD-AV 246
Cdd:cd01168 191 KEAL-LELLPYVDILFGNEEEAEALAEAETTD---DLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIV 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2045671900 247 DTTAAGDTFIGA-LSSTLQpDLSnLKEAILYGNLASSVAVQSYGAQPS 293
Cdd:cd01168 267 DTNGAGDAFAGGfLYGLVQ-GEP-LEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
36-302 |
1.66e-35 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 130.51 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 36 AGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMVDAAGENSILI--HAGA 113
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFyrNPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 114 NNAFHEQEVlkNKQLITN-------SDFIIAqfESSLDATILAFSIAKDAGktTILN----------PAP--ARETIPTe 174
Cdd:PLN02323 121 DMLLRESEL--DLDLIRKakifhygSISLIT--EPCRSAHLAAMKIAKEAG--ALLSydpnlrlplwPSAeaAREGIMS- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 175 LLEKTDIIIPNETETEIITGIRVTDHNSLVaaaeKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAVDTTAAGDT 254
Cdd:PLN02323 194 IWDEADIIKVSDEEVEFLTGGDDPDDDTVV----KLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDA 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2045671900 255 FIGALSSTLQPDLS------NLKEAILYGNLASSVAVQSYGAQPSIPYREALEQ 302
Cdd:PLN02323 270 FVGGLLSQLAKDLSlledeeRLREALRFANACGAITTTERGAIPALPTKEAVLK 323
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
4-259 |
2.92e-34 |
|
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: 125.87 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSG 83
Cdd:cd01945 2 VLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 IAEIQGATTGQAMImVDAAGENSILIHAGANNAFHEQEVlknkqlitnSDFIIAQFESSL------DATILAFSIAKDAG 157
Cdd:cd01945 82 IVVAPGARSPISSI-TDITGDRATISITAIDTQAAPDSL---------PDAILGGADAVLvdgrqpEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 158 KTTILNPAPARETIPTELLEKTDIIIPNETETEIITGIrvtdhnSLVAAAEKLHELGIGTVIITLGSAGA-FYHTEKEHG 236
Cdd:cd01945 152 IPIPLDLDGGGLRVLEELLPLADHAICSENFLRPNTGS------ADDEALELLASLGIPFVAVTLGEAGClWLERDGELF 225
|
250 260
....*....|....*....|...
gi 2045671900 237 IVPAFKVDAVDTTAAGDTFIGAL 259
Cdd:cd01945 226 HVPAFPVEVVDTTGAGDVFHGAF 248
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
3-302 |
2.19e-30 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 116.39 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 3 TVTvigsIN--MDTTLRLTNMpKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTS---FIGGvgadSEGQQLLDLLTKE 77
Cdd:COG1105 3 TVT----LNpaLDRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTalgFLGG----FTGEFIEELLDEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 78 NIDTSGIaEIQGATtGQAMIMVDAA-GENSILIHAGANNAFHEQEVLKNK--QLITNSDFIIAqfeS-----SLDATILA 149
Cdd:COG1105 74 GIPTDFV-PIEGET-RINIKIVDPSdGTETEINEPGPEISEEELEALLERleELLKEGDWVVL---SgslppGVPPDFYA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 150 --FSIAKDAGKTTIL--NPAPARETIPtellEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSA 225
Cdd:COG1105 149 elIRLARARGAKVVLdtSGEALKAALE----AGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGAD 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045671900 226 GAFYHTEKEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGAQpsIPYREALEQ 302
Cdd:COG1105 225 GALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLD-LEEALRLAVAAGAAAALSPGTG--LPDREDVEE 298
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
34-295 |
3.25e-30 |
|
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: 115.73 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 34 FHAGGGkgANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATT--------GQAMIMVDAAGEN 105
Cdd:cd01172 37 IRLGGA--ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTTtktrviarNQQLLRVDREDDS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 106 SILIHAGANNAFHEQEVLKNKQLITNSDF---IIAqfESSLDATIlafSIAKDAGKTTILNPAPARETIptelLEKTDII 182
Cdd:cd01172 115 PLSAEEEQRLIERIAERLPEADVVILSDYgkgVLT--PRVIEALI---AAARELGIPVLVDPKGRDYSK----YRGATLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 183 IPNETETEIITGIRVTDHNSLVAAAEKL-HELGIGTVIITLGSAG-AFYHTEKEHGIVPAFKVDAVDTTAAGDTFIGALS 260
Cdd:cd01172 186 TPNEKEAREALGDEINDDDELEAAGEKLlELLNLEALLVTLGEEGmTLFERDGEVQHIPALAKEVYDVTGAGDTVIATLA 265
|
250 260 270
....*....|....*....|....*....|....*
gi 2045671900 261 STLQPDLsNLKEAILYGNLASSVAVQSYGAQPSIP 295
Cdd:cd01172 266 LALAAGA-DLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-287 |
4.94e-28 |
|
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: 109.71 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGeTMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSG 83
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPG-TSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 IaEIQGATTGQAMIMVDAAGEnsiLIHAGAN----NAFHEQEVLKNKQLITNSDFIIAQFESSLDATILAFSIAKDAGKT 159
Cdd:cd01941 81 I-VFEGRSTASYTAILDKDGD---LVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 160 TILNPAPARETIP-TELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFY---HTEKEH 235
Cdd:cd01941 157 VAFEPTSAPKLKKlFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLssrEGGVET 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2045671900 236 GIVPAFKVDAV-DTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQS 287
Cdd:cd01941 237 KLFPAPQPETVvNVTGAGDAFVAGLVAGLLEGMS-LDDSLRFAQAAAALTLES 288
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
4-289 |
9.31e-27 |
|
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: 106.35 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGETMHAHEI-FHAGGGkgANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTS 82
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKsYVIGGG--FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 83 gIAEIQGATTGQAMIMVDAAGENSILIHAGANN-----AFHEQEVLKNKQLITnSDFIIAQfESSLDATILAFSIAKDAG 157
Cdd:cd01944 80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQdwsteWFATLTVAPYDYVYL-SGYTLAS-ENASKVILLEWLEALPAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 158 KTTILNPAPARETIPTELLEKTDIIIP----NETETEIITGirvTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYH-TE 232
Cdd:cd01944 157 TTLVFDPGPRISDIPDTILQALMAKRPiwscNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRlPD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045671900 233 KEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYG 289
Cdd:cd01944 234 GNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMS-LADAVLLANAAAAIVVTRSG 289
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
38-301 |
4.67e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 96.54 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 38 GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMVDAAGENSI--LIHAGANn 115
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFtfMVRPSAD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 116 AFHEQEVL----KNKQLITNSDFIIAqfESSLDATILAFSIAKDAGKTTILNPApARETI---PTELLE-------KTDI 181
Cdd:PRK09434 107 LFLQPQDLppfrQGEWLHLCSIALSA--EPSRSTTFEAMRRIKAAGGFVSFDPN-LREDLwqdEAELREclrqalaLADV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 182 IIPNETETEIITGirvTDHnsLVAAAEKL-HELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAVDTTAAGDTFIGAL- 259
Cdd:PRK09434 184 VKLSEEELCFLSG---TSQ--LEDAIYALaDRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLl 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2045671900 260 ----SSTLQPDLSNLKEAILYGNLASSVAVQSYGAQPSIPYREALE 301
Cdd:PRK09434 259 aglsQAGLWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
4-259 |
1.21e-22 |
|
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: 92.93 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGgvgadsegqqlldlltkenidtsg 83
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 84 iaeiqgattgqamimVDAagensILIHAGAnnafheqevlknkqlitnsdfiiaqfeSSLDATILAFSIAKDAGKTTILN 163
Cdd:cd00287 58 ---------------ADA-----VVISGLS---------------------------PAPEAVLDALEEARRRGVPVVLD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 164 PAP----ARETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGA-FYHTEKEHGIV 238
Cdd:cd00287 91 PGPravrLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAiVATRGGTEVHV 170
|
250 260
....*....|....*....|.
gi 2045671900 239 PAFKVDAVDTTAAGDTFIGAL 259
Cdd:cd00287 171 PAFPVKVVDTTGAGDAFLAAL 191
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
3-289 |
2.01e-21 |
|
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: 91.82 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 3 TVTVIGSInmDTTLRLTNmPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSeGQQLLDLLTKENIDTS 82
Cdd:cd01164 4 TVTLNPAI--DLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 83 GIaEIQGATTgQAMIMVDAAGENSILIHAGANNAFHEQEVLKN--KQLITNSDFIIA--QFESSLDATILA--FSIAKDA 156
Cdd:cd01164 80 FV-EVAGETR-INVKIKEEDGTETEINEPGPEISEEELEALLEklKALLKKGDIVVLsgSLPPGVPADFYAelVRLAREK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 157 GKTTIL--NPAPARETIPtellEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKE 234
Cdd:cd01164 158 GARVILdtSGEALLAALA----AKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2045671900 235 HGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYG 289
Cdd:cd01164 234 VYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLS-LEEALRLAVAAGSATAFSPG 287
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
36-259 |
1.38e-20 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 91.43 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 36 AGGGkgANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAE--IQGATTGQA------MIMVDAAGENSI 107
Cdd:PLN02341 119 AGGN--CNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEgtDAGDSSSASyetllcWVLVDPLQRHGF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 108 LIHA--GANNAF-------HE-QEVLKNKQLITNSDFIIAQFesSLDATILAFSIAKDAGKTTILNPAPARETIPTE--- 174
Cdd:PLN02341 197 CSRAdfGPEPAFswisklsAEaKMAIRQSKALFCNGYVFDEL--SPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGtpd 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 175 -------LLEKTDIIIPNETETEIITGIRvtdhNSLVAAAEKLHElGIGT--VIITLGSAGAFYHTEKEHGIVPAFKVDA 245
Cdd:PLN02341 275 erralehLLRMSDVLLLTSEEAEALTGIR----NPILAGQELLRP-GIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNV 349
|
250
....*....|....
gi 2045671900 246 VDTTAAGDTFIGAL 259
Cdd:PLN02341 350 VDTVGCGDSFAAAI 363
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-290 |
1.76e-20 |
|
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: 88.63 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 3 TVTVIGSINMDTTLRLTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENI-DT 81
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDkHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 82 SGIAEIQgatTGQAMIMVDAAGENSILIHAGANNAFHEQEVLKNKQLItnsdFIIAqfeSSLDATILAFSIAKDAGkttI 161
Cdd:cd01947 81 VAWRDKP---TRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGDGV----FITA---AAVDKEAIRKCRETKLV---I 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 162 LNPAP-ARETIPTELLEKTDIIIPNETETEIITgirvtdhnslvaAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPA 240
Cdd:cd01947 148 LQVTPrVRVDELNQALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPA 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2045671900 241 FKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYGA 290
Cdd:cd01947 216 KKAKVPDSTGAGDSFAAGFIYGLLKGWS-IEEALELGAQCGAICVSHFGP 264
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
169-289 |
1.56e-15 |
|
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: 75.19 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 169 ETIPTEL---LEKTDIIIPNETETEIITGirvtdHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDA 245
Cdd:cd01946 151 SIKPEKLkkvLAKVDVVIINDGEARQLTG-----AANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLES 225
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2045671900 246 V-DTTAAGDTF----IGALSSTLQPDLSNLKEAILYGNLASSVAVQSYG 289
Cdd:cd01946 226 VfDPTGAGDTFaggfIGYLASQKDTSEANMRRAIIYGSAMASFCVEDFG 274
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-294 |
1.62e-14 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 72.71 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 4 VTVIGSINMDT------TLRLTNmPKPGEtmhaheIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKE 77
Cdd:PRK09850 7 VVIIGSANIDVagysheSLNYAD-SNPGK------IKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 78 NIDTSGIAEIQGATTGQAMIMVDAAGENSILIHAGANNAFHEQEVL-KNKQLITNSDFIIAQFESSLDATILafsIAKDA 156
Cdd:PRK09850 80 GVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLaQHREFIQRAKVIVADCNISEEALAW---ILDNA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 157 GKTTI-LNPAPARETIPT-ELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFY-HTEK 233
Cdd:PRK09850 157 ANVPVfVDPVSAWKCVKVrDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYsDISG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045671900 234 EHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQS-YGAQPSI 294
Cdd:PRK09850 237 ESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMP-FAESVRFAQGCSSMALSCeYTNNPDL 297
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
29-290 |
2.16e-14 |
|
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: 71.62 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 29 HAHEIFhAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIaEIQGATTGQAMIMVDA------- 101
Cdd:cd01940 14 LHLGKM-YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVDgdrifgl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 102 ------AGENSI-----------LIHAGANNafHEQEVLKNKQLITNSDFIIAqFESSLDATilafsiAKDAGKttilnp 164
Cdd:cd01940 92 snkggvAREHPFeadleylsqfdLVHTGIYS--HEGHLEKALQALVGAGALIS-FDFSDRWD------DDYLQL------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 165 aparetipteLLEKTDIII---PNETETEIItgirvtdhnslvAAAEKLHELGIGTVIITLGSAGAF-YHTEK--EHGIV 238
Cdd:cd01940 157 ----------VCPYVDFAFfsaSDLSDEEVK------------AKLKEAVSRGAKLVIVTRGEDGAIaYDGAVfySVAPR 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2045671900 239 PafkVDAVDTTAAGDTFI-GALSSTLQPDLSnLKEAILYGNLASSVAVQSYGA 290
Cdd:cd01940 215 P---VEVVDTLGAGDSFIaGFLLSLLAGGTA-IAEAMRQGAQFAAKTCGHEGA 263
|
|
| PLN02967 |
PLN02967 |
kinase |
36-272 |
5.88e-10 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 60.06 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 36 AGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMVDAAGE-NSILIHAGAN 114
Cdd:PLN02967 241 APGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRlKTTCVKPCAE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 115 NAFHEQE----VLKN-KQLITNSDFIIAQfeSSLDATILAFSIAKDAGKTTI--LN-PAP----ARET--IPTELLEKTD 180
Cdd:PLN02967 321 DSLSKSEinidVLKEaKMFYFNTHSLLDP--TMRSTTLRAIKISKKLGGVIFydLNlPLPlwssSEETksFIQEAWNLAD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 181 IIIPNETETEIITGIRVTD-------------HNSLVAAAEKLHElGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAV- 246
Cdd:PLN02967 399 IIEVTKQELEFLCGIEPTEefdtkdndkskfvHYSPEVVAPLWHE-NLKVLFVTNGTSKIHYYTKEHNGAVHGMEDAPIt 477
|
250 260 270
....*....|....*....|....*....|..
gi 2045671900 247 ----DTTAAGDTFIGALSS--TLQPDLSNLKE 272
Cdd:PLN02967 478 pftsDMSASGDGIVAGLMRmlTVQPHLITDKG 509
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
38-290 |
2.52e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.67 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 38 GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATtgqAMIMVDAAGENSILihaG----- 112
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT---AQTQVELHDNDRVF---Gdyteg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 113 --ANNAFHEQEVlknkQLITNSDFIIAQFESSLDAtilAFSIAKDAGKTTILNPA-----PARETipteLLEKTDIII-- 183
Cdd:PRK09813 97 vmADFALSEEDY----AWLAQYDIVHAAIWGHAED---AFPQLHAAGKLTAFDFSdkwdsPLWQT----LVPHLDYAFas 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 184 -PNETETeiitgIRVTdhnslvaaAEKLHELGIGTVIITLGSAGA-------FYhtekEHGIVPafkVDAVDTTAAGDTF 255
Cdd:PRK09813 166 aPQEDEF-----LRLK--------MKAIVARGAGVVIVTLGENGSiawdgaqFW----RQAPEP---VTVVDTMGAGDSF 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 2045671900 256 I-GALSSTLQPDlsNLKEAILYGNLASSVAVQSYGA 290
Cdd:PRK09813 226 IaGFLCGWLAGM--TLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
49-289 |
5.24e-09 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 56.26 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 49 KRSGArTSFIGGVGADSEGQQLldlltKENIDTSGI----AEIQGATTGQ-AMIMVDaaGENSILIHAGANNAFHEQEVL 123
Cdd:PLN02548 67 QIPGA-TSYMGCIGKDKFGEEM-----KKCATAAGVnvhyYEDESTPTGTcAVLVVG--GERSLVANLSAANCYKVEHLK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 124 K--NKQLITNSDFI-IAQF--ESSLDATILAFSIAKDAGKTTILN-PAP----ARETIPTELLEKTDIIIPNETETEIIT 193
Cdd:PLN02548 139 KpeNWALVEKAKFYyIAGFflTVSPESIMLVAEHAAANNKTFMMNlSAPficeFFKDQLMEALPYVDFLFGNETEARTFA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 194 GIRVTDHNSLVAAAEKLHELGIG------TVIITLGSAGAFYHTE---KEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQ 264
Cdd:PLN02548 219 KVQGWETEDVEEIALKISALPKAsgthkrTVVITQGADPTVVAEDgkvKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLV 298
|
250 260
....*....|....*....|....*
gi 2045671900 265 PDlSNLKEAILYGNLASSVAVQSYG 289
Cdd:PLN02548 299 QG-KDIEECVRAGNYAANVIIQRSG 322
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
167-274 |
5.49e-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: 55.57 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 167 ARETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGA--------FYHTEKEHgIV 238
Cdd:pfam08543 108 AIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHLEGeeavvtdvLYDGGGFY-TL 186
|
90 100 110
....*....|....*....|....*....|....*.
gi 2045671900 239 PAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAI 274
Cdd:pfam08543 187 EAPRIPTKNTHGTGCTLSAAIAANLAKGLS-LPEAV 221
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
35-290 |
6.86e-09 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 56.19 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 35 HAGGGKGANQA-VA---AKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSgIAEIQGATTGQAMIMVdAAGENSILIH 110
Cdd:PTZ00247 59 YVPGGSALNTArVAqwmLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEML-FEYTTKAPTGTCAVLV-CGKERSLVAN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 111 AGANNAF--------HEQEVLKNKQLITNSDFIIAqfeSSLDATILAFSIAKDAGKTTILN-PAP----ARETIPTELLE 177
Cdd:PTZ00247 137 LGAANHLsaehmqshAVQEAIKTAQLYYLEGFFLT---VSPNNVLQVAKHARESGKLFCLNlSAPfisqFFFERLLQVLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 178 KTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHEL--GIGT----VIITLGSAGAFYHTEKEHGIVPAFKVDA---VDT 248
Cdd:PTZ00247 214 YVDILFGNEEEAKTFAKAMKWDTEDLKEIAARIAMLpkYSGTrprlVVFTQGPEPTLIATKDGVTSVPVPPLDQekiVDT 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2045671900 249 TAAGDTFIGALSSTL--QPDLSNLKEAilyGNLASSVAVQSYGA 290
Cdd:PTZ00247 294 NGAGDAFVGGFLAQYanGKDIDRCVEA---GHYSAQVIIQHNGC 334
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
174-221 |
8.51e-09 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 55.47 E-value: 8.51e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2045671900 174 ELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT 221
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
175-264 |
8.99e-09 |
|
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: 55.28 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 175 LLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT---LGSAG-----AFYHTEKEHGIVPAFKVDAV 246
Cdd:cd01173 133 LVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveLADDDriemlGSTATEAWLVQRPKIPFPAY 212
|
90 100 110
....*....|....*....|....*....|.
gi 2045671900 247 -----DTTAA--------GDTFIGALSSTLQ 264
Cdd:cd01173 213 fngtgDLFAAlllarllkGKSLAEALEKALN 243
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
6-259 |
7.01e-08 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 53.01 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 6 VIGSINMDttLR-LTNMPKPGETMHAHEIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGI 84
Cdd:PRK09954 62 VVGAINMD--IRgMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 85 AEIQGATTGQAMIMVDAAGENSILIhaganNAFHEQEVLK------NKQLITNSDFIIAQFESSLDATILAFSIAkDAGK 158
Cdd:PRK09954 140 IRLHGQSTSTYLAIANRQDETVLAI-----NDTHILQQLTpqllngSRDLIRHAGVVLADCNLTAEALEWVFTLA-DEIP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 159 TTILNPAPARETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAF-YHTEKEHGI 237
Cdd:PRK09954 214 VFVDTVSEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFcSEKDGEQFL 293
|
250 260
....*....|....*....|..
gi 2045671900 238 VPAFKVDAVDTTAAGDTFIGAL 259
Cdd:PRK09954 294 LTAPAHTTVDSFGADDGFMAGL 315
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
174-221 |
1.13e-07 |
|
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: 52.07 E-value: 1.13e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2045671900 174 ELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT 221
Cdd:COG2240 134 RLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT 181
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
180-260 |
2.81e-07 |
|
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: 50.86 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 180 DIIIPNETETEIItgirvtdhNSLVAAAEKLHELGIGTVIITLGSAGA--FYHTEKEHgiVPAFKVDAVDTTAAGDTFIG 257
Cdd:cd01937 157 DVLKLSRVEAEVI--------STPTELARLIKETGVKEIIVTDGEEGGyiFDGNGKYT--IPASKKDVVDPTGAGDVFLA 226
|
...
gi 2045671900 258 ALS 260
Cdd:cd01937 227 AFL 229
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
162-293 |
2.90e-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: 50.98 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 162 LNPAPARETIPTellekTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT-LGSAGAFYHTEKEHGIVPA 240
Cdd:TIGR00687 127 LLEVYREKAIPV-----ADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGSQRDRSFEGLVATQ 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045671900 241 ------FKVDAV---DTTAAGDTFIGALSST-LQPdlSNLKEAI------LYGNLASSVAVQSYGAQPS 293
Cdd:TIGR00687 202 egrwhiSRPLAVfdpPPVGTGDLIAALLLATlLHG--NSLKEALektvsaVYHVLRTTIQLGKYELQPV 268
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
218-289 |
8.99e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 49.81 E-value: 8.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045671900 218 VIITLGSAGA-FYHTEKEHGIvPAFKVDAVDTTAAGDTFIGALSSTLQPDLSnLKEAILYGNLASSVAVQSYG 289
Cdd:PLN02630 206 VIVTNGKKGCrIYWKDGEMRV-PPFPAIQVDPTGAGDSFLGGFVAGLVQGLA-VPDAALLGNYFGSLAVEQVG 276
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
52-291 |
9.48e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 49.79 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 52 GARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGaTTGQAMIMVDAAGE--------NSILIHAganNAFHEQEVL 123
Cdd:PLN02379 101 GVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKG-PTAQCVCLVDALGNrtmrpclsSAVKLQA---DELTKEDFK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 124 KNKQLITNSDFIiaqfesSLDATILAFSIAKDAGKTTILNPAP---ARETIPT--ELLE--KTDIIIPNETET-EIITGI 195
Cdd:PLN02379 177 GSKWLVLRYGFY------NLEVIEAAIRLAKQEGLSVSLDLASfemVRNFRSPllQLLEsgKIDLCFANEDEArELLRGE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 196 RVTDHNSLVAAAEKLHELGIgtviITLGSAGAFYHTEKEHGIVPAFK-VDAVDTTAAGDTFIGALSSTLQPDLSnLKEAI 274
Cdd:PLN02379 251 QESDPEAALEFLAKYCNWAV----VTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLFASGFLYGLIKGLS-LEECC 325
|
250
....*....|....*..
gi 2045671900 275 LYGNLASSVAVQSYGAQ 291
Cdd:PLN02379 326 KVGACSGGSVVRALGGE 342
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
184-259 |
9.89e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 49.31 E-value: 9.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045671900 184 PNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGSAGAFYHTEKEHGIVPAFKVDAVDTTAAGDTFIGAL 259
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGL 261
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
38-289 |
1.15e-06 |
|
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: 48.94 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 38 GGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMVDAAGENSILIHagaNNAF 117
Cdd:cd01939 36 GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCYRKDIDEPASSYIIRSRAGGRTTIVN---DNNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 118 HEQEVLKNKQLITNSD----FIIAQFESSLDaTILAFsIAKDAGKttilnpAPARETIPTELLEKTDIIIPNETETEII- 192
Cdd:cd01939 113 PEVTYDDFSKIDLTQYgwihFEGRNPDETLR-MMQHI-EEHNNRR------PEIRITISVEVEKPREELLELAAYCDVVf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 193 TGIRVTDHNSLVAAAEKLHELGI-----GTVIITLGSAGAFYHT-EKEHGIVPAFKVD-AVDTTAAGDTFIGALSSTLQP 265
Cdd:cd01939 185 VSKDWAQSRGYKSPEECLRGEGPrakkaALLVCTWGDQGAGALGpDGEYVHSPAHKPIrVVDTLGAGDTFNAAVIYALNK 264
|
250 260
....*....|....*....|....
gi 2045671900 266 DLSNLKEAILYGNLASSVAVQSYG 289
Cdd:cd01939 265 GPDDLSEALDFGNRVASQKCTGVG 288
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
173-289 |
2.73e-06 |
|
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: 48.11 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 173 TELLEKTDIIIPNETETEIITGIRVTDHNSL---VAAAEKLHELGIGT-----VIITLGSAGAFYHTEKEHGI--VPAFK 242
Cdd:cd01943 175 LQALPRVDVFSPNLEEAARLLGLPTSEPSSDeekEAVLQALLFSGILQdpgggVVLRCGKLGCYVGSADSGPElwLPAYH 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2045671900 243 VDA---VDTTAAGDTFIGALSSTLQpdLS-NLKEAILYGNLASSVAVQSYG 289
Cdd:cd01943 255 TKStkvVDPTGGGNSFLGGFAAGLA--LTkSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
36-285 |
3.73e-06 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 47.90 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 36 AGGGkgANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQAMIMvdaaGENSILIHAGANN 115
Cdd:PRK11316 50 PGGA--ANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVPTHPTITKLRVL----SRNQQLIRLDFEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 116 AFHEQEvlknkqlitnSDFIIAQFESSL---DATILAfsiakDAGKTTILNPAP----ARET-IPT---------ELLEK 178
Cdd:PRK11316 124 GFEGVD----------PQPLLERIEQALpsiGALVLS-----DYAKGALASVQAmiqlARKAgVPVlidpkgtdfERYRG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 179 TDIIIPNETETEIITGiRVTDHNSLVAAAEKL-HELGIGTVIITLGsagafyhtekEHGI-----------VPAFKVDAV 246
Cdd:PRK11316 189 ATLLTPNLSEFEAVVG-KCKDEAELVEKGMKLiADYDLSALLVTRS----------EQGMtllqpgkaplhLPTQAREVY 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 2045671900 247 DTTAAGDTFIGALSSTLQpDLSNLKEAILYGNLASSVAV 285
Cdd:PRK11316 258 DVTGAGDTVISVLAAALA-AGNSLEEACALANAAAGVVV 295
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
32-108 |
5.56e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 47.59 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 32 EIFHAGGGKGANQAVAAKRSGARTSFIGGVGADSEGQQLLDLLTKENIDTSGIAEIQGATTGQA-------------MIM 98
Cdd:PLN02543 166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSrmkikfrdggkmvAET 245
|
90
....*....|
gi 2045671900 99 VDAAGENSIL 108
Cdd:PLN02543 246 VKEAAEDSLL 255
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
167-263 |
3.10e-05 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 44.73 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 167 ARETIPTELLEKTDIIIPNETETEIITGIRVTDHNS-LVAAAEKLHELGIGTVIIT----LGSAGA--FYHTEKEHGIVP 239
Cdd:PRK06427 122 AVAALRERLLPLATLITPNLPEAEALTGLPIADTEDeMKAAARALHALGCKAVLIKgghlLDGEESvdWLFDGEGEERFS 201
|
90 100
....*....|....*....|....
gi 2045671900 240 AFKVDAVDTTAAGDTFIGALSSTL 263
Cdd:PRK06427 202 APRIPTKNTHGTGCTLSAAIAAEL 225
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
179-263 |
2.56e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 41.59 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 179 TDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGS------AGAFYHTEKEHGIVpAFKVDAVDTTAAG 252
Cdd:PRK12413 130 VTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNrlsqkkAIDLFYDGKEFVIL-ESPVLEKNNIGAG 208
|
90
....*....|.
gi 2045671900 253 DTFIGALSSTL 263
Cdd:PRK12413 209 CTFASSIASQL 219
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
155-221 |
6.15e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 40.62 E-value: 6.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045671900 155 DAGKTTILNPAPArETIPTELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT 221
Cdd:PRK05756 116 DPEKGCIVAPGVA-EFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
174-221 |
8.81e-04 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 40.49 E-value: 8.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2045671900 174 ELLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIIT 221
Cdd:PLN02978 145 KVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVIT 192
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
175-274 |
1.60e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 39.57 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 175 LLEKTDIIIPNETETEIITGIRVTDHNSLVAAAEKLHELGIGTVIITLGS------AGAFYHTEKEHGIVPAFKVDAVDT 248
Cdd:PRK12412 129 LVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSklgtetAIDVLYDGETFDLLESEKIDTTNT 208
|
90 100
....*....|....*....|....*.
gi 2045671900 249 TAAGDTFIGALSSTLQPDlSNLKEAI 274
Cdd:PRK12412 209 HGAGCTYSAAITAELAKG-KPVKEAV 233
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
118-279 |
5.17e-03 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 37.78 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 118 HEQEVLKNKQLITNSDFIIAQFESSLDATILafSIAKDAGKTTILNPAPARETIPTELLEKTDIIIPNETETEIITGIRV 197
Cdd:PRK13508 119 HFKQLLESVEVVAISGSLPAGLPVDYYAQLI--ELANQAGKPVVLDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 198 T-DHNSLVAA-AEKLHElGIGTVIITLGSAGAFY-HTEKEHGI-VPAFKVdaVDTTAAGDTFIGALSSTL---QPDLSNL 270
Cdd:PRK13508 197 SeDLDELKEVlQQPLFE-GIEWIIVSLGADGAFAkHNDTFYKVdIPKIEV--VNPVGSGDSTVAGIASGLlhqEDDADLL 273
|
....*....
gi 2045671900 271 KEAILYGNL 279
Cdd:PRK13508 274 KKANVLGML 282
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
157-274 |
9.37e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 36.95 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045671900 157 GKTTILNPAPArETIPTELLEKTDIIIPNETETEIITGI-RVTDHNSLVAAAEKLHELGIGTVIITLGsaGAFYHTE--- 232
Cdd:PRK12616 114 GANEVLYPEHA-EALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITGG--GKLKHEKavd 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2045671900 233 -----KEHGIVPAFKVDAVDTTAAGDTFIGALSSTLQPDlSNLKEAI 274
Cdd:PRK12616 191 vlydgETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKG-SEVKEAI 236
|
|
| |
