|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
98-388 |
2.01e-103 |
|
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: 307.94 E-value: 2.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQHRYIAESDVMLMQLETNIEALTEFIRLGKQGNKMIM 257
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDE-SGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 258 LNPAPYTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWS 337
Cdd:cd01174 160 LNPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446393969 338 AVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA-SSMP 388
Cdd:cd01174 240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAqPSIP 291
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
103-388 |
1.39e-77 |
|
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: 241.74 E-value: 1.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 103 GSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSYSAYRT 182
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 183 DKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQHRYIAESDVMLMQLETNIEALTEFIRLGKQGNKMIMLNPAP 262
Cdd:TIGR02152 81 KDTPTGTAFITVDD-TGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 263 YTKQVTH-LLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVK 341
Cdd:TIGR02152 160 AIKDLDDeLLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446393969 342 DAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA-SSMP 388
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAqSSIP 287
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
95-388 |
3.47e-67 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 215.50 E-value: 3.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 95 KTGKVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGI 174
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 175 TSYSAYRTDKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQHRYIAESDVMLMQLETNIEALTEFIRLGKQGNK 254
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVND-EGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 255 MIMLNPAPYTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIP 334
Cdd:PRK11142 160 KVILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446393969 335 AWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA-SSMP 388
Cdd:PRK11142 240 GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAqPSIP 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
98-386 |
1.95e-63 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 205.65 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPqsGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQHRYIAESDVM----LMQLETNIEALTEFIRLGKQGN 253
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDG-DGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 254 --KMIMLNPAPYTKQ-VTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHART 330
Cdd:pfam00294 158 tfDPNLLDPLGAAREaLLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446393969 331 LYIPA-WSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGASS 386
Cdd:pfam00294 238 VHVPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
98-388 |
3.70e-62 |
|
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: 202.42 E-value: 3.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGI-TS 176
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVdTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 177 YSAyRTDKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQhrYIAESDVMLMQL-----ETNIEALTEFIRLGKQ 251
Cdd:COG0524 81 GVR-RDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEA--LLAGADILHLGGitlasEPPREALLAALEAARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 252 GNKMIMLNPA-------PYTKQVTHLLSDIDIITPNETEASFLSGVTitdinDAKKAGNIILQSGVKKVIITLGARGSLL 324
Cdd:COG0524 157 AGVPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446393969 325 CEHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA-SSMP 388
Cdd:COG0524 232 YTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAqPALP 296
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
99-388 |
1.63e-47 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 164.91 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 99 VCVLGSFNIDVSATVPWFPQSGESILASQF--GFypGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITS 176
Cdd:PTZ00292 18 VVVVGSSNTDLIGYVDRMPQVGETLHGTSFhkGF--GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 177 YSAYRTDKAPTGSALIYVSAVDGDNIIAIYPGANMMLTTQEINEQ-HRYIAESDVMLMQLETNIEALTEFIRLGKQGNKM 255
Cdd:PTZ00292 96 SFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMVDAQtDNIQNICKYLICQNEIPLETTLDALKEAKERGCY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 256 IMLNPAPYTK-----QVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEH-AR 329
Cdd:PTZ00292 176 TVFNPAPAPKlaeveIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKeNE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 330 TLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA-SSMP 388
Cdd:PTZ00292 256 PVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTqSSYP 315
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
98-380 |
7.28e-23 |
|
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: 97.38 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESiLASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTS-NPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDKApTGSaliyVSAV---DGDNIIAIypgANM----MLTTQEINEQHRYIAESDVMLMQLETNIEALTEFIRLGK 250
Cdd:cd01941 80 GIVFEGRS-TAS----YTAIldkDGDLVVAL---ADMdiyeLLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 251 QGNKMIMLNP--APYTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLC--- 325
Cdd:cd01941 152 KHGVPVAFEPtsAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSsre 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446393969 326 -EHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVE 380
Cdd:cd01941 232 gGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
151-385 |
5.38e-22 |
|
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: 95.37 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 151 HFIFKVGKDQFSAFAMNHIIQSGITSySAYRTDKAPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQhrYIAESDV 230
Cdd:cd01168 73 AFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTP-DAERTMCTYLGAANELSPDDLDWS--LLAKAKY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 231 MLM---QLETNIEALTEFIRLGKQGNKMIMLN------PAPYTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKA 301
Cdd:cd01168 149 LYLegyLLTVPPEAILLAAEHAKENGVKIALNlsapfiVQRFKEALLELLPYVDILFGNEEEAEALAEAETTDDLEAALK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 302 gniILQSGVKKVIITLGARGSLLCEHARTLYIPAW-SAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVE 380
Cdd:cd01168 229 ---LLALRCRIVVITQGAKGAVVVEGGEVYPVPAIpVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQ 305
|
....*
gi 446393969 381 QVGAS 385
Cdd:cd01168 306 QLGPR 310
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
99-385 |
8.48e-22 |
|
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: 94.30 E-value: 8.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 99 VCVLGSFNIDVSATVPWFPQSGESILA------------------SQFGFYPGgkganqalaannagaaahFIFKVGKDQ 160
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVkdlrrefggsagntavalAKLGLSPG------------------LVAAVGEDF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 161 FSAFAMNHIIQSGI-TSYSAYRtDKAPTGSAliyVSAVDGDN--IIAIYPGANMmltTQEINEQHRYIAESDVMLMQLET 237
Cdd:cd01942 64 HGRLYLEELREEGVdTSHVRVV-DEDSTGVA---FILTDGDDnqIAYFYPGAMD---ELEPNDEADPDGLADIVHLSSGP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 238 NIEALTEfiRLGKQGNKMImLNPAP-----YTKQVTHLLSDIDIITPNETEASFLsgVTITDINDAkkagniILQSGVKK 312
Cdd:cd01942 137 GLIELAR--ELAAGGITVS-FDPGQelprlSGEELEEILERADILFVNDYEAELL--KERTGLSEA------ELASGVRV 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446393969 313 VIITLGARGSLLCEHARTLYIPAWSAV-VKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGAS 385
Cdd:cd01942 206 VVVTLGPKGAIVFEDGEEVEVPAVPAVkVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
98-385 |
3.44e-21 |
|
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: 92.64 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSAtvpwfPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:cd01166 1 DVVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDKAPTGSALI-YVSAVDGDNIIAIYPGANMMLTTQEINEqhRYIAESDVM------LMQLETNIEALTEFIRLGK 250
Cdd:cd01166 76 HVRVDPGRPTGLYFLeIGAGGERRVLYYRAGSAASRLTPEDLDE--AALAGADHLhlsgitLALSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 251 QGNKMI--------MLNPAPYTKQVTH-LLSDIDIITPNETEASFLSGvtITDINDAKKAGNIiLQSGVKKVIITLGARG 321
Cdd:cd01166 154 ARGVTVsfdlnyrpKLWSAEEAREALEeLLPYVDIVLPSEEEAEALLG--DEDPTDAAERALA-LALGVKAVVVKLGAEG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446393969 322 SLLCEHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGAS 385
Cdd:cd01166 231 ALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
275-384 |
1.09e-17 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 82.88 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 275 DIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNGAL 354
Cdd:COG1105 179 DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGF 258
|
90 100 110
....*....|....*....|....*....|
gi 446393969 355 AAALARQADMVAAIQYASAFASLAVEQVGA 384
Cdd:COG1105 259 LAGLARGLDLEEALRLAVAAGAAAALSPGT 288
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
152-384 |
1.81e-17 |
|
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: 82.30 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 152 FIFKVGKDQFSAFAMNHIIQSGITSYSAYRTDKAPTGSALIYVSAvDGDNIIAIY--PGANMMLTTQEINEQhryIAESD 229
Cdd:cd01167 47 FIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDA-DGERSFEFYrgPAADLLLDTELNPDL---LSEAD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 230 VM----LMQL-ETNIEALTEFIRLGKQGNKMIML----------NPAPYTKQVTHLLSDIDIITPNETEASFLSGVTITD 294
Cdd:cd01167 123 ILhfgsIALAsEPSRSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERIAELLELADIVKLSDEELELLFGEEDPE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 295 INDAKkagniILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNG-------ALAAALARQADMVAA 367
Cdd:cd01167 203 EIAAL-----LLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAgllaqllSRGLLALDEDELAEA 277
|
250
....*....|....*..
gi 446393969 368 IQYASAFASLAVEQVGA 384
Cdd:cd01167 278 LRFANAVGALTCTKAGA 294
|
|
| GlpR |
COG1349 |
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ... |
1-60 |
1.85e-15 |
|
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];
Pssm-ID: 440960 [Multi-domain] Cd Length: 254 Bit Score: 75.56 E-value: 1.85e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 1 MFKEERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILNR 60
Cdd:COG1349 1 MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVS 60
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
98-352 |
5.15e-15 |
|
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: 73.28 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGanqalaannagaaahfifkvgkdqfsAFAMNHIIQSGITSy 177
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGA--------------------------ANVAVALARLGVSV- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 sayrtdkaptgsALIYVSAVdgdniiaiypganmmlttqeineqhrYIAESDVMLmqletniEALTEFIRLGKQGNKMIM 257
Cdd:cd00287 54 ------------TLVGADAV--------------------------VISGLSPAP-------EAVLDALEEARRRGVPVV 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 258 LNPAP-----YTKQVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLC-EHARTL 331
Cdd:cd00287 89 LDPGPravrlDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVAtRGGTEV 168
|
250 260
....*....|....*....|.
gi 446393969 332 YIPAWSAVVKDAAGAGDAFNG 352
Cdd:cd00287 169 HVPAFPVKVVDTTGAGDAFLA 189
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
236-386 |
6.64e-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: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 236 ETNIEALTEFIRlgkQGNKMIMLNPAP--YTKqvthlLSDIDIITPNETEASFLSGVTITDINDAKKAGNIIL-QSGVKK 312
Cdd:cd01172 150 PRVIEALIAAAR---ELGIPVLVDPKGrdYSK-----YRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLeLLNLEA 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446393969 313 VIITLGARGSLLCE-HARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGASS 386
Cdd:cd01172 222 LLVTLGEEGMTLFErDGEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAP 296
|
|
| AgaR |
NF040755 |
transcriptional repressor AgaR; |
5-59 |
2.97e-12 |
|
transcriptional repressor AgaR;
Pssm-ID: 468715 [Multi-domain] Cd Length: 256 Bit Score: 66.14 E-value: 2.97e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446393969 5 ERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILN 59
Cdd:NF040755 6 ERREQIIQRLRQQGSVQVEDLSALFGVSTVTIRNDLAFLEKQGIAVRAYGGALIN 60
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
269-380 |
7.12e-12 |
|
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: 65.17 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 269 HLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITlGAR---------GSLLCE-----HARTLYIP 334
Cdd:COG2240 134 RLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT-SVPlddtpadkiGNLAVTadgawLVETPLLP 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446393969 335 AwsavvkDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVE 380
Cdd:COG2240 213 F------SPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLE 252
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
275-383 |
1.01e-11 |
|
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: 65.25 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 275 DIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNGAL 354
Cdd:cd01164 179 FLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGF 258
|
90 100
....*....|....*....|....*....
gi 446393969 355 AAALARQADMVAAIQYASAFASLAVEQVG 383
Cdd:cd01164 259 VAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
99-379 |
3.70e-11 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 63.85 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 99 VCVLGSFNIDVSAtvpwFPQSGESILASQFG---FYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGIt 175
Cdd:PRK09850 7 VVIIGSANIDVAG----YSHESLNYADSNPGkikFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 176 sysayRTDK---APTGSALIYVSAVD--GDNIIAIypgaNMMLTTQEIN----EQHR-YIAESDVMLMQLETNIEALTEF 245
Cdd:PRK09850 82 -----YVDKcliVPGENTSSYLSLLDntGEMLVAI----NDMNISNAITaeylAQHReFIQRAKVIVADCNISEEALAWI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 246 irLGKQGNKMIMLNPAPYTK--QVTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSL 323
Cdd:PRK09850 153 --LDNAANVPVFVDPVSAWKcvKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVY 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 324 LCEHARTlyiPAWSAVVK----DAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAV 379
Cdd:PRK09850 231 YSDISGE---SGWSAPIKtnviNVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMAL 287
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
152-388 |
1.48e-10 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 61.85 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 152 FIFKVGKDQFSAFAMNH-----IIQSGITSYSAYRTD------KAPTGSALIYVSavdgDNIiaiypgANMMLTTQEINE 220
Cdd:TIGR04382 53 FITRVGDDQFGRFVRDYlrregVDTSHVVTDPGRRTSlvfleiKPPDEFPLLFYR----ENA------ADLALTPDDVDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 221 QhrYIAESDVML-----MQLETNIEALTEFIRLGKQGNKMIML----------NPAPYTKQVTHLLSDIDIITPNETEas 285
Cdd:TIGR04382 123 D--YIASARALLvsgtaLSQEPSREAVLKALEYARAAGVRVVLdidyrpylwkSPEEAGIYLRLVLPLVDVIIGTREE-- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 286 FLSGVTITDINDAKKAgniILQSGVKKVIITLGARGSLLceHART---LYIPAWSAVVKDAAGAGDAFNGALAAALARQA 362
Cdd:TIGR04382 199 FDIAGGEGDDEAAARA---LLDAGVEILVVKRGPEGSLV--YTGDgegVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGW 273
|
250 260
....*....|....*....|....*..
gi 446393969 363 DMVAAIQYASAFASLAVEQVG-ASSMP 388
Cdd:TIGR04382 274 DLEKALRYGNACGAIVVSRHScSPAMP 300
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
98-384 |
2.98e-10 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 60.51 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDkaPTGSALIYVSAvDGDNIIAIYPGANMMLTTQEIneqhryIAESDVMLMQLETNIEALTEFIRLgkqgNKMIM 257
Cdd:cd01947 81 VAWRDK--PTRKTLSFIDP-NGERTITVPGERLEDDLKWPI------LDEGDGVFITAAAVDKEAIRKCRE----TKLVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 258 LNPAPYTK--QVTHLLSDIDIITPNETEASFLSgvtitdinDAKKagniILQSGVKKVIITLGARGSLLCEHARTLYIPA 335
Cdd:cd01947 148 LQVTPRVRvdELNQALIPLDILIGSRLDPGELV--------VAEK----IAGPFPRYLIVTEGELGAILYPGGRYNHVPA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446393969 336 WSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA 384
Cdd:cd01947 216 KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
98-383 |
3.18e-10 |
|
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: 60.51 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 98 KVCVLGSFNIDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIfKVGKDQFSAFAMNHIIQSGITSY 177
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAG-PLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 178 SAYRTDKApTGSALIYVSAvDGDNIIAIYPGANMMLTTQEINEQHryIAESDVM------LMQLETNIEALTEFIrLGKQ 251
Cdd:cd01944 80 LPPRGGDD-GGCLVALVEP-DGERSFISISGAEQDWSTEWFATLT--VAPYDYVylsgytLASENASKVILLEWL-EALP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 252 GNKMIMLNPAPYTKQVT-HLLSDI----DIITPNETEASFLSGVTITDINDAKKAGNIILQSGVkkvIITLGARGSLLCE 326
Cdd:cd01944 155 AGTTLVFDPGPRISDIPdTILQALmakrPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAPV---VVRLGSNGAWIRL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446393969 327 HAR-TLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVG 383
Cdd:cd01944 232 PDGnTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
271-383 |
6.81e-10 |
|
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: 59.40 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 271 LSDIDIITPNETEASFLSGVTitdinDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWS-AVVKDAAGAGDA 349
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPlESVFDPTGAGDT 235
|
90 100 110
....*....|....*....|....*....|....*....
gi 446393969 350 FNGALAAALARQ-----ADMVAAIQYASAFASLAVEQVG 383
Cdd:cd01946 236 FAGGFIGYLASQkdtseANMRRAIIYGSAMASFCVEDFG 274
|
|
| PRK09802 |
PRK09802 |
DeoR family transcriptional regulator; |
5-58 |
1.09e-09 |
|
DeoR family transcriptional regulator;
Pssm-ID: 182086 [Multi-domain] Cd Length: 269 Bit Score: 58.71 E-value: 1.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446393969 5 ERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGIL 58
Cdd:PRK09802 17 ERREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGIAVRAYGGALI 70
|
|
| HTH_DEOR |
smart00420 |
helix_turn_helix, Deoxyribose operon repressor; |
6-58 |
1.20e-09 |
|
helix_turn_helix, Deoxyribose operon repressor;
Pssm-ID: 197714 [Multi-domain] Cd Length: 53 Bit Score: 53.77 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446393969 6 RRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGIL 58
Cdd:smart00420 1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLTRVHGGAVS 53
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
269-316 |
1.78e-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: 57.98 E-value: 1.78e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446393969 269 HLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT 316
Cdd:cd01173 132 LLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT 179
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
268-398 |
6.32e-09 |
|
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: 56.97 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 268 THLLSDIDIITPNETEASFLSGVTI--TDINDAKKAGNI------ILQSGVKKVIITLGARGSLL--CEHARTLYIPAW- 336
Cdd:cd01943 175 LQALPRVDVFSPNLEEAARLLGLPTsePSSDEEKEAVLQallfsgILQDPGGGVVLRCGKLGCYVgsADSGPELWLPAYh 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446393969 337 --SAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGassMPQHLQVLHRMR 398
Cdd:cd01943 255 tkSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG---LPRLTKVEGEEL 315
|
|
| HTH_DeoR |
pfam08220 |
DeoR-like helix-turn-helix domain; |
6-59 |
1.35e-08 |
|
DeoR-like helix-turn-helix domain;
Pssm-ID: 285436 [Multi-domain] Cd Length: 57 Bit Score: 50.72 E-value: 1.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446393969 6 RRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILN 59
Cdd:pfam08220 1 RIQQILELLKQQGTLSVEELAELLGVSEMTIRRDLNELEEQGLLTRTHGGAVSN 54
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
275-384 |
2.29e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 54.94 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 275 DIITPNETEASFLSGvtITDINDAKKAgnIILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNG-- 352
Cdd:PRK09434 182 DVVKLSEEELCFLSG--TSQLEDAIYA--LADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAgl 257
|
90 100 110
....*....|....*....|....*....|....*.
gi 446393969 353 ----ALAAALARQADMVAAIQYASAFASLAVEQVGA 384
Cdd:PRK09434 258 laglSQAGLWTDEAELAEIIAQAQACGALATTAKGA 293
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
270-316 |
2.52e-08 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 55.09 E-value: 2.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446393969 270 LLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT 316
Cdd:PTZ00344 136 LIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
|
|
| srlR |
PRK10434 |
DNA-binding transcriptional repressor; |
1-83 |
3.37e-08 |
|
DNA-binding transcriptional repressor;
Pssm-ID: 182457 [Multi-domain] Cd Length: 256 Bit Score: 54.31 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 1 MFKEERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILNRDALSKLI-------TENKID 73
Cdd:PRK10434 1 MKPRQRQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLVILEHAGTVIRTYGGVVLNKEESDPPIdhktlinTHKKEL 80
|
90
....*....|
gi 446393969 74 ISSTIATPIH 83
Cdd:PRK10434 81 IAEAAVSLIH 90
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
269-350 |
2.63e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 52.53 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 269 HLL--SDIDIITPNETEAsflsgvtITDINDAKKAGNIILQSGV--KKVIITLGARGSLLCEHARTLYIPAWSAVVKDAA 344
Cdd:PLN02341 281 HLLrmSDVLLLTSEEAEA-------LTGIRNPILAGQELLRPGIrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTV 353
|
....*.
gi 446393969 345 GAGDAF 350
Cdd:PLN02341 354 GCGDSF 359
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
267-316 |
1.16e-06 |
|
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: 49.40 E-value: 1.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446393969 267 VTHLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT 316
Cdd:pfam08543 113 KEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK 162
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
269-373 |
1.26e-06 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 49.48 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 269 HLLSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT----------------LGARGSLLCEHARtly 332
Cdd:PRK05756 134 RALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypadrfemllVTADGAWHISRPL--- 210
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446393969 333 IPAWSAVVkdaaGAGDAFNGALAAALARQADMVAAIQYASA 373
Cdd:PRK05756 211 VDFMRQPV----GVGDLTSALFLARLLQGGSLEEALEHTTA 247
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
271-380 |
1.31e-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: 49.32 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 271 LSDIDIITPNETEASflsgvtitDINDAKKAGNIILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAF 350
Cdd:cd01937 153 LKLHDVLKLSRVEAE--------VISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVF 224
|
90 100 110
....*....|....*....|....*....|
gi 446393969 351 NGALAAALARQADMVAAIQYASAFASLAVE 380
Cdd:cd01937 225 LAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
107-384 |
3.15e-06 |
|
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: 48.44 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 107 IDVSATVPWFPQSGESILASQFGFYPGGKGANQALAANNAGAAAHFIFKVGKDqfsafAMNHIIQSGITSY---SAYRTD 183
Cdd:cd01945 10 LDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDD-----AIGRLILAELAAEgvdTSFIVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 184 KAPTGSALIYVSAVDGDN----IIAIYPGANMMLTTQEIneqhryIAESDVMLM---QLETNIEALTEFIRLGKQgnKMI 256
Cdd:cd01945 85 APGARSPISSITDITGDRatisITAIDTQAAPDSLPDAI------LGGADAVLVdgrQPEAALHLAQEARARGIP--IPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 257 MLNPAPyTKQVTHLLSDIDIITPNEteaSFLSGVTITDINDAKKAgniiLQS-GVKKVIITLGARGSLLCEHA-RTLYIP 334
Cdd:cd01945 157 DLDGGG-LRVLEELLPLADHAICSE---NFLRPNTGSADDEALEL----LASlGIPFVAVTLGEAGCLWLERDgELFHVP 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446393969 335 AWSAVVKDAAGAGDAFNGALAAALARQADMVAAIQYASAFASLAVEQVGA 384
Cdd:cd01945 229 AFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG 278
|
|
| PRK10411 |
PRK10411 |
L-fucose operon activator; |
3-54 |
6.49e-06 |
|
L-fucose operon activator;
Pssm-ID: 236684 [Multi-domain] Cd Length: 240 Bit Score: 47.11 E-value: 6.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446393969 3 KEERRHAIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYG 54
Cdd:PRK10411 2 KAARQQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNHG 53
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
269-403 |
9.72e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 47.11 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 269 HLLSDIDIITPNETEASFLsgvtitDINDAKKAgniilqsgvKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGD 348
Cdd:PLN02630 177 DMLPRIGFLKASSEEALFI------DVEEVRQK---------CCVIVTNGKKGCRIYWKDGEMRVPPFPAIQVDPTGAGD 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446393969 349 AFNGALAAALARQADMVAAIQYASAFASLAVEQVGASSMPQHLqvLHRMRTQSNK 403
Cdd:PLN02630 242 SFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVGIPKFDLRQ--LQRVKDEVQR 294
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
275-316 |
1.93e-05 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 46.27 E-value: 1.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446393969 275 DIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT 316
Cdd:PLN02978 151 TMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVIT 192
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
232-384 |
5.65e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 45.18 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 232 LMQLETNIEALTEFIRLGKQGNKMIML---NPAPYTKQVTHLLSDI----DIITPNETEASFLSGVTITDIND-AKKAgn 303
Cdd:PLN02813 234 LWELPQTIEAIAQACEEAHRAGALVAVtasDVSCIERHRDDFWDVMgnyaDILFANSDEARALCGLGSEESPEsATRY-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 304 iiLQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQA-DMVAAIQYASAFASLAVEQV 382
Cdd:PLN02813 312 --LSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQ 389
|
..
gi 446393969 383 GA 384
Cdd:PLN02813 390 GT 391
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
276-318 |
1.08e-04 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 44.33 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446393969 276 IITPNETEASFLSGVTITDINDAKKAGNIILQS-GVKKVIITLG 318
Cdd:PRK08573 133 VVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKGG 176
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
268-322 |
1.19e-04 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 43.58 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446393969 268 THLLSDIDIITPNETEASFLSGVTITDINDA-KKAGNIILQSGVKKVIITLGARGS 322
Cdd:PRK06427 128 ERLLPLATLITPNLPEAEALTGLPIADTEDEmKAAARALHALGCKAVLIKGGHLLD 183
|
|
| PRK10906 |
PRK10906 |
DeoR/GlpR family transcriptional regulator; |
3-88 |
1.92e-04 |
|
DeoR/GlpR family transcriptional regulator;
Pssm-ID: 182827 [Multi-domain] Cd Length: 252 Bit Score: 42.92 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 3 KEERRH-AIINLLIKDNSVSVSKLSDLYKVSQETIRSDLRYFQKSGMLQRCYGGGILNRDALSK-------LITENKIDI 74
Cdd:PRK10906 2 KQTQRHdAIIELVKQQGYVSTEELVEHFSVSPQTIRRDLNDLAEQNKILRHHGGAALPSSSVNTpwhdrkaTQTEEKERI 81
|
90
....*....|....
gi 446393969 75 SSTIATPIHQDAKL 88
Cdd:PRK10906 82 ARKVASQIPNGATL 95
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
275-322 |
3.49e-04 |
|
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: 42.12 E-value: 3.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446393969 275 DIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIIT-LGARGS 322
Cdd:TIGR00687 140 DIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVThLIRAGS 188
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
271-378 |
4.35e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 42.08 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 271 LSDIDIITPNETEASFLSGVTITDINDAKKAGNIILQSG-VKKVIITLGARGSLLCEHArtlyipAWSAVV------KDA 343
Cdd:PRK10294 178 IGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSE------NCIQVVpppvksQST 251
|
90 100 110
....*....|....*....|....*....|....*
gi 446393969 344 AGAGDAFNGALAAALARQADMVAAIQYASAFASLA 378
Cdd:PRK10294 252 VGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAA 286
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
276-389 |
5.57e-04 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 41.60 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 276 IITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSL-LCEHARTLYIPAWSAVVKdAAGAGDAfngal 354
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALwVNASGEWIAKPPACDVVS-TVGAGDS----- 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446393969 355 aaalarqadMVAAIQY--------------ASAFASLAVEQ--VGASSMPQ 389
Cdd:PRK09513 257 ---------MVGGLIYgllmressehtlrlATAVSALAVSQsnVGITDRPQ 298
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
276-381 |
1.17e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 40.41 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 276 IITPNETEASFLSGV-TITDINDAKKAGNIILQSGVKKVIITLGarGSLLCEHARTLYIPAWSAVVKDAA--------GA 346
Cdd:PRK12616 137 VITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITGG--GKLKHEKAVDVLYDGETAEVLESEmidtpythGA 214
|
90 100 110
....*....|....*....|....*....|....*
gi 446393969 347 GDAFNGALAAALARQADMVAAIQYASAFASLAVEQ 381
Cdd:PRK12616 215 GCTFSAAVTAELAKGSEVKEAIYAAKEFITAAIKE 249
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
131-384 |
1.40e-03 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 40.11 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 131 YPGGKGANQALAANNAGAAAHFIFKVGKDQFSAFAMNHIIQSGITSySAYRTDKAPTgsALIYVSAVDGDNIIAIYPG-- 208
Cdd:PRK09813 21 FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI-SHVHTKHGVT--AQTQVELHDNDRVFGDYTEgv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 209 -ANMMLTTQEIneqhRYIAESDVMLMQLETNIEAltEFIRLgKQGNKMIMLNpapYTKQVTHLLSDIdiiTPNETEASFL 287
Cdd:PRK09813 98 mADFALSEEDY----AWLAQYDIVHAAIWGHAED--AFPQL-HAAGKLTAFD---FSDKWDSPLWQT---LVPHLDYAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 288 SGVTITD-INDAKKAgniILQSGVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAFNGALAAALARQADMVA 366
Cdd:PRK09813 165 SAPQEDEfLRLKMKA---IVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQ 241
|
250
....*....|....*...
gi 446393969 367 AIQYASAFASLAVEQVGA 384
Cdd:PRK09813 242 AMAQGTACAAKTIQYHGA 259
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
274-381 |
1.64e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 40.05 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 274 IDIITPNETEASFLSGVTITDINDAKKAGNIILQSGVKKVIITLGARGSL-----LCEHARTLYIPAWSAVVKDAAGAGD 348
Cdd:PRK12413 130 VTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNRLSQkkaidLFYDGKEFVILESPVLEKNNIGAGC 209
|
90 100 110
....*....|....*....|....*....|...
gi 446393969 349 AFNGALAAALARQADMVAAIQYASAFASLAVEQ 381
Cdd:PRK12413 210 TFASSIASQLVKGKSPLEAVKNSKDFVYQAIQQ 242
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
156-372 |
1.73e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 40.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 156 VGKDQFSAfAMNHIIQSGITSYSAYRTDKAPTGSALIYVsaVDGD-NIIAIYPGANMM----LTTQE---INEQHRYIAE 227
Cdd:PLN02548 78 IGKDKFGE-EMKKCATAAGVNVHYYEDESTPTGTCAVLV--VGGErSLVANLSAANCYkvehLKKPEnwaLVEKAKFYYI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 228 SDVMLMqleTNIEALTEFIRLGKQGNKMIMLN-PAPY-----TKQVTHLLSDIDIITPNETEASFLSGVTITDIND---- 297
Cdd:PLN02548 155 AGFFLT---VSPESIMLVAEHAAANNKTFMMNlSAPFiceffKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDveei 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 298 AKKAGNIILQSGVKK--VIITLGARGSLLCEHARTLYIPAwSAVVK----DAAGAGDAFNGALAAALARQADM---VAAI 368
Cdd:PLN02548 232 ALKISALPKASGTHKrtVVITQGADPTVVAEDGKVKEFPV-IPLPKeklvDTNGAGDAFVGGFLSQLVQGKDIeecVRAG 310
|
....
gi 446393969 369 QYAS 372
Cdd:PLN02548 311 NYAA 314
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
309-375 |
2.97e-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: 39.26 E-value: 2.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446393969 309 GVKKVIITLGARGSLLCEHARTLYIPAWSAVVKDAAGAGDAF-NGALAAALARQADMVAAIQYASAFA 375
Cdd:cd01940 187 GAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFiAGFLLSLLAGGTAIAEAMRQGAQFA 254
|
|
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
3-71 |
8.70e-03 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 38.30 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 3 KEERRHAIIN-LLIKDNSVSVSKLSDLYKVSQETIRSDL----RYFQKSGM-LQRCYGGGIL-------NRDALSKLITE 69
Cdd:COG3711 79 PKERVAYILLrLLLAGDPISLDDLAEELFVSRSTILNDLkkieKILKKYGLtLERKPNYGIKlegseldIRKALAELLSE 158
|
..
gi 446393969 70 NK 71
Cdd:COG3711 159 LL 160
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
239-316 |
9.16e-03 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 37.59 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446393969 239 IEALTEFIRLGKQGNKMIMLNP------APYT-------KQVTHLLSDIDIITPNETEASFLSG-------VTITDIND- 297
Cdd:PRK07105 90 IQIVSDFIKYFKKKDLLVVVDPvmgdngKLYQgfdqemvEEMRKLIQKADVITPNLTEACLLLDkpyleksYSEEEIKQl 169
|
90
....*....|....*....
gi 446393969 298 AKKAGNIilqsGVKKVIIT 316
Cdd:PRK07105 170 LRKLADL----GPKIVIIT 184
|
|
| |
