|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-296 |
9.35e-116 |
|
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: 335.29 E-value: 9.35e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVD 83
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIEDIN--TALIAQADVLIAQFEVPFEVILAAFKIAKKNNVQTIL 161
Cdd:cd01174 81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDaaLELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 162 NPAPAVyELTSELMAVTDIVLPNETEAQLLTGInVINDEGVLNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPE 241
Cdd:cd01174 161 NPAPAR-PLPAELLALVDILVPNETEAALLTGI-EVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 738130265 242 KVDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAIPSIPT 296
Cdd:cd01174 239 KVKAVDTTGAGDTFIGALAAALARGLS-LEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
9-301 |
9.94e-111 |
|
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: 322.63 E-value: 9.94e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 9 GSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTN 88
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 89 SDVPTGSAYIMLQESGANTILIHGGANQALTIEDINTA--LIAQADVLIAQFEVPFEVILAAFKIAKKNNVQTILNPAPA 166
Cdd:TIGR02152 81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAeaLIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 167 VYELTSELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQ 246
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAE-KAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 738130265 247 DTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAIPSIPTDKEVD 301
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKS-LEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-303 |
3.15e-98 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 291.39 E-value: 3.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 1 MTKNIVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGV 80
Cdd:PRK11142 1 TMGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 81 NVDAVSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIEDINT--ALIAQADVLIAQFEVPFEVILAAFKIAKKNNVQ 158
Cdd:PRK11142 81 DTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAhrELIANADALLMQLETPLETVLAAAKIAKQHGTK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 159 TILNPAPAVyELTSELMAVTDIVLPNETEAQLLTGINVINDEGVlNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWV 238
Cdd:PRK11142 161 VILNPAPAR-ELPDELLALVDIITPNETEAEKLTGIRVEDDDDA-AKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738130265 239 QPEKVDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAIPSIPTDKEVDNY 303
Cdd:PRK11142 239 PGFRVQAVDTIAAGDTFNGALVTALLEGKP-LPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAF 302
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-300 |
3.82e-86 |
|
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: 260.20 E-value: 3.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVD 83
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIEDINTALIAQADVLIAQ-----FEVPFEVILAAFKIAKKNNVQ 158
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGgitlaSEPPREALLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 159 TILNPA--PAVY----ELTSELMAVTDIVLPNETEAQLLTGinvindEGVLNRVSDALQAKGVQRSIITLGEAGSFIADG 232
Cdd:COG0524 161 VSLDPNyrPALWeparELLRELLALVDILFPNEEEAELLTG------ETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738130265 233 QKRWWVQPEKVDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAIPSIPTDKEV 300
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLD-LEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
6.72e-77 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 237.71 E-value: 6.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 1 MTKNIVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGV 80
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 81 NVDAVSTNSDVPTGSAYIML-QESGANTILIHGGANQALTIEDI--NTALIAQ-ADVLIAQFEVPFEVILAAFKIAKKNN 156
Cdd:PTZ00292 94 NTSFVSRTENSSTGLAMIFVdTKTGNNEIVIIPGANNALTPQMVdaQTDNIQNiCKYLICQNEIPLETTLDALKEAKERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 157 VQTILNPAPAV----YELTSELMAVTDIVLPNETEAQLLTGINViNDEGVLNRVSDALQAKGVQRSIITLGEAGSFIA-D 231
Cdd:PTZ00292 174 CYTVFNPAPAPklaeVEIIKPFLKYVSLFCVNEVEAALITGMEV-TDTESAFKASKELQQLGVENVIITLGANGCLIVeK 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738130265 232 GQKRWWVQPEKVDVQDTTAAGDTFIGTLASVIAPDfSNLDDAVQRANIASAIAVTRPGAIPSIPTDKEV 300
Cdd:PTZ00292 253 ENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRG-KDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-291 |
1.55e-59 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 191.79 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMKMPRMPlvGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVD 83
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIE--DINTALIAQADVL----IAQFEVPFEVILAAFKIAKKNN- 156
Cdd:pfam00294 79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEelEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 157 -VQTILNPAPAVYELTSELMAVTDIVLPNETEAQLLTGINVINDEGVLNRVSdALQAKGVQRSIITLGEAGSFIADGQKR 235
Cdd:pfam00294 159 fDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH-KLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 738130265 236 WWVQPE-KVDVQDTTAAGDTFIGTLASVIApDFSNLDDAVQRANIASAIAVTRPGAI 291
Cdd:pfam00294 238 VHVPAVpKVKVVDTTGAGDSFVGGFLAGLL-AGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
25-291 |
4.84e-50 |
|
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: 167.37 E-value: 4.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 25 VGETMV---------LTEVTT---APGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVP 92
Cdd:cd01166 5 IGEVMVdlsppgggrLEQADSfrkFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 93 TGSAYIMLQESGANTIL--IHGGANQALTIEDINTALIAQADVL------IAQFEVPFEVILAAFKIAKKNNVQTI---- 160
Cdd:cd01166 85 TGLYFLEIGAGGERRVLyyRAGSAASRLTPEDLDEAALAGADHLhlsgitLALSESAREALLEALEAAKARGVTVSfdln 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 161 ----LNPAPAVYELTSELMAVTDIVLPNETEAQLLTGINVINDegvlnrVSDALQAK--GVQRSIITLGEAGSFIADGQK 234
Cdd:cd01166 165 yrpkLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTD------AAERALALalGVKAVVVKLGAEGALVYTGGG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 738130265 235 RWWVQPEKVDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAI 291
Cdd:cd01166 239 RVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWD-LEEALRFANAAAALVVTRPGDI 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
15-293 |
7.70e-38 |
|
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: 136.20 E-value: 7.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 15 NIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNsDVPTG 94
Cdd:cd01168 31 GDMILADMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 95 SAYIMLQESGANTILIHGGANQALTIEDINTALIAQADVLI---AQFEVPFEVILAAFKIAKKNNVQTILN-PAPAV--- 167
Cdd:cd01168 110 TCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYlegYLLTVPPEAILLAAEHAKENGVKIALNlSAPFIvqr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 168 -YELTSELMAVTDIVLPNETEAQLLTGINVINDegvlNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVD-V 245
Cdd:cd01168 190 fKEALLELLPYVDILFGNEEEAEALAEAETTDD----LEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 738130265 246 QDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAIPS 293
Cdd:cd01168 266 VDTNGAGDAFAGGFLYGLVQGEP-LEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-291 |
7.33e-37 |
|
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: 133.15 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNImkmPRMPLVGETmvlteVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVD 83
Cdd:cd01167 1 KVVCFGEALIDFI---PEGSGAPET-----FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVSTNSDVPTGSAYIMLQESGANTILIHGG-ANQALTIEDINTALIAQADVL----IAQFEVPF-EVILAAFKIAKKNNV 157
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDADGERSFEFYRGpAADLLLDTELNPDLLSEADILhfgsIALASEPSrSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 158 QTILNP---------APAVYELTSELMAVTDIVLPNETEAQLLTGinvindEGVLNRVSDALQAKGVQRSIITLGEAGSF 228
Cdd:cd01167 153 LISFDPnlrpplwrdEEEARERIAELLELADIVKLSDEELELLFG------EEDPEEIAALLLLFGLKLVLVTRGADGAL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738130265 229 IADGQKRWWVQPEKVDVQDTTAAGDTFIGTL------ASVIAPDFSNLDDAVQRANIASAIAVTRPGAI 291
Cdd:cd01167 227 LYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLlaqllsRGLLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-291 |
6.83e-33 |
|
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: 122.42 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 5 IVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDA 84
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 85 VSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIEDINTALIAQADVLIAQFEvpfEVILAAfKIAKKNNVQTILNPA 164
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPDGLADIVHLSSGP---GLIELA-RELAAGGITVSFDPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 165 PAVYELTSELM----AVTDIVLPNETEAQLL---TGInvindegvlnrvSDALQAKGVQRSIITLGEAGSFIADGQKRWW 237
Cdd:cd01942 158 QELPRLSGEELeeilERADILFVNDYEAELLkerTGL------------SEAELASGVRVVVVTLGPKGAIVFEDGEEVE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 738130265 238 VQPEK-VDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAI 291
Cdd:cd01942 226 VPAVPaVKVVDTTGAGDAFRAGFLYGLLRGYD-LEESLRLGNLAASLKVERRGAQ 279
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
37-300 |
1.65e-32 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 122.42 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 37 APGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVPTGSAYIMLQESGANTILI--HGGA 114
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFyrNPSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 115 NQALTIEDINTALIAQADVL----IAQFEVPFEVI-LAAFKIAKKN--------NVQTILNPAPAvyELTSELMAV---T 178
Cdd:PLN02323 121 DMLLRESELDLDLIRKAKIFhygsISLITEPCRSAhLAAMKIAKEAgallsydpNLRLPLWPSAE--AAREGIMSIwdeA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 179 DIVLPNETEAQLLTGINVINDEGVLNRVSDALQAkgvqrSIITLGEAGSFIADGQKRWWVQPEKVDVQDTTAAGDTFIGT 258
Cdd:PLN02323 199 DIIKVSDEEVEFLTGGDDPDDDTVVKLWHPNLKL-----LLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGG 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 738130265 259 LASVIAPDFSNLDD------AVQRANIASAIAVTRPGAIPSIPTDKEV 300
Cdd:PLN02323 274 LLSQLAKDLSLLEDeerlreALRFANACGAITTTERGAIPALPTKEAV 321
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
4-285 |
2.90e-26 |
|
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: 104.70 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDnIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVD 83
Cdd:cd01941 1 EIVVIGAANID-LRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVsTNSDVPTGSaYIMLQESGANTILIHG--GANQALTIEDIN--TALIAQADVLIAQFEVPFEVILAAFKIAKKNNVQT 159
Cdd:cd01941 80 GI-VFEGRSTAS-YTAILDKDGDLVVALAdmDIYELLTPDFLRkiREALKEAKPIVVDANLPEEALEYLLALAAKHGVPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 160 ILNPAPAV-YELTSELMAVTDIVLPNETEAQLLTGINvINDEGVLNRVSDALQAKGVQRSIITLGEAGSFIAD---GQKR 235
Cdd:cd01941 158 AFEPTSAPkLKKLFYLLHAIDLLTPNRAELEALAGAL-IENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSregGVET 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 738130265 236 WWVQPEKVD-VQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAV 285
Cdd:cd01941 237 KLFPAPQPEtVVNVTGAGDAFVAGLVAGLLEGMS-LDDSLRFAQAAAALTL 286
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
22-296 |
1.09e-24 |
|
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: 100.45 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 22 MPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVPTGSAYIMLQ 101
Cdd:cd01945 19 FPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 102 ESGANTILIHGGANQALtIEDINTALIAQADVLIAQFEVPfEVILAAFKIAKKNNVQTILNPAPAVYELTSELMAVTDIV 181
Cdd:cd01945 99 TGDRATISITAIDTQAA-PDSLPDAILGGADAVLVDGRQP-EAALHLAQEARARGIPIPLDLDGGGLRVLEELLPLADHA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 182 LPNETEAQLLTGINvindegvLNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWW-VQPEKVDVQDTTAAGDTFIGTLA 260
Cdd:cd01945 177 ICSENFLRPNTGSA-------DDEALELLASLGIPFVAVTLGEAGCLWLERDGELFhVPAFPVEVVDTTGAGDVFHGAFA 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 738130265 261 SVIApDFSNLDDAVQRANIASAIAVTRPGAIPSIPT 296
Cdd:cd01945 250 HALA-EGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
5-289 |
5.29e-24 |
|
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: 98.65 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 5 IVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGkGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVdA 84
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 85 VSTNSDVPTGSAYIMLQESGANTILIHGGANQALTIEDINTALIAQAD-VLIAQFEVPFE----VILAAFKIAKKNNVQT 159
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDyVYLSGYTLASEnaskVILLEWLEALPAGTTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 160 ILNPAPAVYELT----SELMAVTDIVLPNETEAQLLTGINVINDEgvlnRVSDALQAKGVQRSIITLGEAGSFI--ADGQ 233
Cdd:cd01944 160 VFDPGPRISDIPdtilQALMAKRPIWSCNREEAAIFAERGDPAAE----ASALRIYAKTAAPVVVRLGSNGAWIrlPDGN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 738130265 234 KRwWVQPEKVDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPG 289
Cdd:cd01944 236 TH-IIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMS-LADAVLLANAAAAIVVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
25-290 |
1.36e-23 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 97.90 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 25 VGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGnDANGQFMRATLLTNGVNVDAVSTNSDVPTgSAYIMLQESG 104
Cdd:COG1105 21 PGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGETRI-NIKIVDPSDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 105 ANTILIHGGAnqALTIEDINtALIAQADVLIAQFE-----------VPFEVILAAFKIAKKNNVQTIL---NPApavyel 170
Cdd:COG1105 99 TETEINEPGP--EISEEELE-ALLERLEELLKEGDwvvlsgslppgVPPDFYAELIRLARARGAKVVLdtsGEA------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 171 tseLMAVT----DIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQ 246
Cdd:COG1105 170 ---LKAALeagpDLIKPNLEELEELLGRPLETLEDII-AAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 738130265 247 DTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGA 290
Cdd:COG1105 246 STVGAGDSMVAGFLAGLARGLD-LEEALRLAVAAGAAAALSPGT 288
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
4-295 |
1.36e-22 |
|
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: 94.93 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVD--NIMKMPRMPLVGETMVLT--EVTTAPGGkGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNG 79
Cdd:cd01172 1 KVLVVGDVILDeyLYGDVERISPEAPVPVVKveREEIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 80 VNVDAVsTNSDVPT-------GSAYIML---QESgantILIHGGANQALTIEDINtALIAQADVLI----AQFEVPFEVI 145
Cdd:cd01172 80 IDTDGI-VDEGRPTttktrviARNQQLLrvdRED----DSPLSAEEEQRLIERIA-ERLPEADVVIlsdyGKGVLTPRVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 146 LAAFKIAKKNNVQTILNPAPAVYELtselMAVTDIVLPNETEAQLLTGINVINDEGVLNRVSDALQAKGVQRSIITLGEA 225
Cdd:cd01172 154 EALIAAARELGIPVLVDPKGRDYSK----YRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLELLNLEALLVTLGEE 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738130265 226 GSFIADGQKRWWVQPEK-VDVQDTTAAGDTFIGTLASVIAPDfSNLDDAVQRANIASAIAVTRPGAIPSIP 295
Cdd:cd01172 230 GMTLFERDGEVQHIPALaKEVYDVTGAGDTVIATLALALAAG-ADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
38-301 |
9.11e-22 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 92.69 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 38 PGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVPTGSAYIMLQESGAN--TILIHGGAN 115
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 116 QALTIEDI----------------------NTALIAQADVLIAQFEVPFEVilaafkiakknNVQTILNPAPAvyELTSE 173
Cdd:PRK09434 107 LFLQPQDLppfrqgewlhlcsialsaepsrSTTFEAMRRIKAAGGFVSFDP-----------NLREDLWQDEA--ELREC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 174 LM---AVTDIVLPNETEAQLLTGINVInDEGvLNRVSDALQAKGVqrsIITLGEAGSFIAD-GQKRWWVQPeKVDVQDTT 249
Cdd:PRK09434 174 LRqalALADVVKLSEEELCFLSGTSQL-EDA-IYALADRYPIALL---LVTLGAEGVLVHTrGQVQHFPAP-SVDPVDTT 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 738130265 250 AAGDTFIG----TLASV-IAPDFSNLDDAVQRANIASAIAVTRPGAIPSIPTDKEVD 301
Cdd:PRK09434 248 GAGDAFVAgllaGLSQAgLWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
5-264 |
2.25e-21 |
|
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: 89.46 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 5 IVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAvgndangqfmratlltngvnvDA 84
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA---------------------DA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 85 VSTNSDVPTGsayimlqesgantilihgganqaltiedintaliaqadvliaqfevpfEVILAAFKIAKKNNVQTILNPA 164
Cdd:cd00287 61 VVISGLSPAP------------------------------------------------EAVLDALEEARRRGVPVVLDPG 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 165 P----AVYELTSELMAVTDIVLPNETEAQLLTGINVInDEGVLNRVSDALQAKGVQRSIITLGEAGSFIADGQK-RWWVQ 239
Cdd:cd00287 93 PravrLDGEELEKLLPGVDILTPNEEEAEALTGRRDL-EVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGtEVHVP 171
|
250 260
....*....|....*....|....*
gi 738130265 240 PEKVDVQDTTAAGDTFIGTLASVIA 264
Cdd:cd00287 172 AFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
31-264 |
2.08e-20 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 88.18 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 31 LTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTnsdVPTGSAYIMLQESGANTILI 110
Cdd:cd01940 14 LHLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV---KEGENAVADVELVDGDRIFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 111 H----GGANQALTIEDINtaliaqadvLIAQFEVPFEVILAAFKIAKKNNVQTILNPAPAVYEL-TSELMAVTDIVLPNe 185
Cdd:cd01940 91 LsnkgGVAREHPFEADLE---------YLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFsDRWDDDYLQLVCPY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 186 TEAQLLTGINVINDEGvlNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQDTTAAGDTFI-GTLASVIA 264
Cdd:cd01940 161 VDFAFFSASDLSDEEV--KAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIaGFLLSLLA 238
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-291 |
1.11e-15 |
|
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: 75.15 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVd 83
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 aVSTNSDVPTGSAYIMLQESGANTILIHGGAnqalTIEDINTALIAQADVLiaqFEVPFEVILAAFKIAKkNNVQTILNP 163
Cdd:cd01947 80 -TVAWRDKPTRKTLSFIDPNGERTITVPGER----LEDDLKWPILDEGDGV---FITAAAVDKEAIRKCR-ETKLVILQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 164 APAV-YELTSELMAVTDIVLPNETEAQLLTginvindegvlnrVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEK 242
Cdd:cd01947 151 TPRVrVDELNQALIPLDILIGSRLDPGELV-------------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 738130265 243 VDVQDTTAAGDTFIGTLASVIAPDFSnLDDAVQRANIASAIAVTRPGAI 291
Cdd:cd01947 218 AKVPDSTGAGDSFAAGFIYGLLKGWS-IEEALELGAQCGAICVSHFGPY 265
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
22-298 |
7.50e-13 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 68.13 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 22 MPLVGETMVLTEVTTAPGGKGANQA-VAASRQGA---NVSFIGAVGNDANGQFMRATLLTNGVNVdAVSTNSDVPTGSAY 97
Cdd:PTZ00247 45 LPIFEELESIPNVSYVPGGSALNTArVAQWMLQApkgFVCYVGCVGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTCA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 98 IMLqeSGANTILIH--GGANQaLTIEDINTALIaQADVLIAQF--------EVPFEVILAAFKIAKKNNVQTILN-PAP- 165
Cdd:PTZ00247 124 VLV--CGKERSLVAnlGAANH-LSAEHMQSHAV-QEAIKTAQLyylegfflTVSPNNVLQVAKHARESGKLFCLNlSAPf 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 166 AVYELTSELMAV---TDIVLPNETEAQLLTGINVINDEGV---LNRVSdALQAKGVQRS---IITLGEAGSFIADGQKRW 236
Cdd:PTZ00247 200 ISQFFFERLLQVlpyVDILFGNEEEAKTFAKAMKWDTEDLkeiAARIA-MLPKYSGTRPrlvVFTQGPEPTLIATKDGVT 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738130265 237 WVQPEKVDVQ---DTTAAGDTFIGTLASVIAPDfSNLDDAVQRANIASAIAVTRPGA-IPSIPTDK 298
Cdd:PTZ00247 279 SVPVPPLDQEkivDTNGAGDAFVGGFLAQYANG-KDIDRCVEAGHYSAQVIIQHNGCtYPEKPPFL 343
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
5-261 |
3.10e-12 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 65.78 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 5 IVVLGSLNVDnIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDA 84
Cdd:PRK09850 7 VVIIGSANID-VAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 85 VSTNSDVPTGSAYIMLQESGANTILIhggaNQALTIEDINTALIAQ-------ADVLIAQFEVPFEVIlaAFKIAKKNNV 157
Cdd:PRK09850 86 CLIVPGENTSSYLSLLDNTGEMLVAI----NDMNISNAITAEYLAQhrefiqrAKVIVADCNISEEAL--AWILDNAANV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 158 QTILNPAPA-----VYELTSELMAVTdivlPNETEAQLLTGINVINDEGVlNRVSDALQAKGVQRSIITLGEAGSFIADG 232
Cdd:PRK09850 160 PVFVDPVSAwkcvkVRDRLNQIHTLK----PNRLEAETLSGIALSGREDV-AKVAAWFHQHGLNRLVLSMGGDGVYYSDI 234
|
250 260 270
....*....|....*....|....*....|
gi 738130265 233 Q-KRWWVQPEKVDVQDTTAAGDTFIGTLAS 261
Cdd:PRK09850 235 SgESGWSAPIKTNVINVTGAGDAMMAGLAS 264
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
38-290 |
3.52e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 65.14 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 38 PGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTnSDVPTGSAYIMLQESGAntilIHGG---- 113
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHT-KHGVTAQTQVELHDNDR----VFGDyteg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 114 --ANQALTIED---------INTALIAQADVLIAQFEVpfEVILAAFKIAKKNNVQTILNPAPAV-YELTSElmavtdiv 181
Cdd:PRK09813 97 vmADFALSEEDyawlaqydiVHAAIWGHAEDAFPQLHA--AGKLTAFDFSDKWDSPLWQTLVPHLdYAFASA-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 182 lPNETEAqlltginvindegvLNRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQDTTAAGDTFI-GTLA 260
Cdd:PRK09813 167 -PQEDEF--------------LRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIaGFLC 231
|
250 260 270
....*....|....*....|....*....|
gi 738130265 261 SVIAPDfsNLDDAVQRANIASAIAVTRPGA 290
Cdd:PRK09813 232 GWLAGM--TLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
4-283 |
5.91e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 65.62 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMKMPRMP----LVGETMVLTEVTTAPGGK------GANQAVAASRQGANVSFIGAVGNDANGQFMRA 73
Cdd:PLN02341 74 DVATLGNLCVDIVLPVPELPppsrEERKAYMEELAASPPDKKsweaggNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 74 TLLTNGVNVDAVSTNSD-VPTGSAYimlqesgANTILI---------HGGANQALT--------IEDINTAL---IAQAD 132
Cdd:PLN02341 154 VLAEEGISVVGLIEGTDaGDSSSAS-------YETLLCwvlvdplqrHGFCSRADFgpepafswISKLSAEAkmaIRQSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 133 VLIAQ---F-EVPFEVILAAFKIAKKNNVQTILNPAPAVYELT----------SELMAVTDIVLPNETEAQLLTGIN--V 196
Cdd:PLN02341 227 ALFCNgyvFdELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLvgtpderralEHLLRMSDVLLLTSEEAEALTGIRnpI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 197 INDEGVLNRvsdALQAKGVqrsIITLGEAGS--FIADGQKRwwVQPEKVDVQDTTAAGDTFigtlASVIAPDFSNLDDAV 274
Cdd:PLN02341 307 LAGQELLRP---GIRTKWV---VVKMGSKGSilVTRSSVSC--APAFKVNVVDTVGCGDSF----AAAIALGYIHNLPLV 374
|
....*....
gi 738130265 275 QRANIASAI 283
Cdd:PLN02341 375 NTLTLANAV 383
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
37-264 |
1.03e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 59.05 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 37 APGGKGANQAVAASRQGA--------NVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTnSDVPTGSAYIMLQESGANTI 108
Cdd:PLN02813 124 SAGGSLSNTLVALARLGSqsaagpalNVAMAGSVGSDPLGDFYRTKLRRANVHFLSQPV-KDGTTGTVIVLTTPDAQRTM 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 109 LIHGGANQALTIEDINTALIAQADVLIAQ---FEVP--FEVILAAFKIAKKNNVQTILNPA-PAV----YELTSELMA-V 177
Cdd:PLN02813 203 LSYQGTSSTVNYDSCLASAISKSRVLVVEgylWELPqtIEAIAQACEEAHRAGALVAVTASdVSCierhRDDFWDVMGnY 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 178 TDIVLPNETEAQLLTGINVindEGVLNRVSDALqAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQDTTAAGDTF-- 255
Cdd:PLN02813 283 ADILFANSDEARALCGLGS---EESPESATRYL-SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYaa 358
|
250 260
....*....|....*....|....
gi 738130265 256 ---------------IGTLASVIA 264
Cdd:PLN02813 359 gilygllrgvsdlrgMGELAARVA 382
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
143-287 |
1.08e-08 |
|
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: 55.15 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 143 EVILAAFKIAKKNNVQTI-------------LNPAPAVYE-LTSELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSD 208
Cdd:COG2240 90 DIIADFVARVKAANPDALylcdpvmgdngkgYYVFPGIAEfIMRRLVPLADIITPNLTELALLTGRPYETLEEAL-AAAR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 209 ALQAKGVQRSIIT--------LGEAGSFIADGQKRWWVQPEKVDVQdTTAAGDTFIGTLASVIAPDFSnLDDAVQRAN-- 278
Cdd:COG2240 169 ALLALGPKIVVVTsvplddtpADKIGNLAVTADGAWLVETPLLPFS-PNGTGDLFAALLLAHLLRGKS-LEEALERAAaf 246
|
....*....
gi 738130265 279 IASAIAVTR 287
Cdd:COG2240 247 VYEVLERTA 255
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
174-287 |
2.09e-08 |
|
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: 54.13 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 174 LMAVTDIVLPNETEAQLLTGINvINDEGVLNRVSDALQAKGVQRSIIT---LGEAGSF---IADGQKRWWVQPEKVD-VQ 246
Cdd:cd01173 133 LVPLADIITPNQFELELLTGKK-INDLEDAKAAARALHAKGPKTVVVTsveLADDDRIemlGSTATEAWLVQRPKIPfPA 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 738130265 247 DTTAAGDTFIGTLASVIAPDFSnLDDAVQRAN--IASAIAVTR 287
Cdd:cd01173 212 YFNGTGDLFAALLLARLLKGKS-LAEALEKALnfVHEVLEATY 253
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
6-259 |
1.40e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 52.24 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 6 VVLGSLNVDnIMKMPRMPLVGETMVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAV 85
Cdd:PRK09954 61 VVVGAINMD-IRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGC 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 86 STNSDVPTgSAYIMLQESGANTILIHGGAN--QALTIEDINTA--LIAQADVLIAQFEVPFEVILAAFKIAkknnvqtil 161
Cdd:PRK09954 140 IRLHGQST-STYLAIANRQDETVLAINDTHilQQLTPQLLNGSrdLIRHAGVVLADCNLTAEALEWVFTLA--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 162 NPAPAVYELTSELMAVT--------DIVLPNETEAQLLTGiNVINDEGVLNRVSDALQAKGVQRSIITLGEAGSFIA--D 231
Cdd:PRK09954 210 DEIPVFVDTVSEFKAGKikhwlahiHTLKPTQPELEILWG-QAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSekD 288
|
250 260
....*....|....*....|....*...
gi 738130265 232 GQKRWWVQPEKVDVqDTTAAGDTFIGTL 259
Cdd:PRK09954 289 GEQFLLTAPAHTTV-DSFGADDGFMAGL 315
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
31-257 |
8.69e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 49.79 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 31 LTEVTTAPGGKGANQAVAASRQ-GANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDvPTGSAYIMLQESGANTI- 108
Cdd:PLN02379 78 LSPIKTMAGGSVANTIRGLSAGfGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKG-PTAQCVCLVDALGNRTMr 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 109 --LIHGGANQA--LTIEDINTA--LIaqadVLIAQFEVpfEVILAAFKIAKKNNVQTILNPAP--AVYELTSELMAV--- 177
Cdd:PLN02379 157 pcLSSAVKLQAdeLTKEDFKGSkwLV----LRYGFYNL--EVIEAAIRLAKQEGLSVSLDLASfeMVRNFRSPLLQLles 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 178 --TDIVLPNETEA-QLLTGINVINDEGVLNrvsdaLQAKGVQRSIITLGEAGSFIADGQKRWWVQP-EKVDVQDTTAAGD 253
Cdd:PLN02379 231 gkIDLCFANEDEArELLRGEQESDPEAALE-----FLAKYCNWAVVTLGSKGCIARHGKEVVRVPAiGETNAVDATGAGD 305
|
....
gi 738130265 254 TFIG 257
Cdd:PLN02379 306 LFAS 309
|
|
| PLN02967 |
PLN02967 |
kinase |
37-134 |
2.02e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 48.89 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 37 APGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVPTGSAYIML-QESGANTILIHGGAN 115
Cdd:PLN02967 241 APGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIaKRGRLKTTCVKPCAE 320
|
90
....*....|....*....
gi 738130265 116 QALTIEDINTALIAQADVL 134
Cdd:PLN02967 321 DSLSKSEINIDVLKEAKMF 339
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
4-259 |
2.68e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 47.78 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 4 NIVVLGSLNVDNIMkmprmplvgetmVLTEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDangqFMRATLLTNGVNVD 83
Cdd:cd01937 1 KIVIIGHVTIDEIV------------TNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGRD----YPDKWSDLFDNGIE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 84 AVStNSDVPTGSAYIMLQESGANTILihgganQALTIEDINTALIAQAD----VLIAqfEVPFEVILAAFKIakknnvqt 159
Cdd:cd01937 65 VIS-LLSTETTTFELNYTNEGRTRTL------LAKCAAIPDTESPLSTItaeiVILG--PVPEEISPSLFRK-------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 160 ilnPAPAVYELTSELMAVTDIVLPNETEAQLLTGINVINDEGV----LNRVSDALQAKGVQRSIITLGEAGSFIADGQKR 235
Cdd:cd01937 128 ---FAFISLDAQGFLRRANQEKLIKCVILKLHDVLKLSRVEAEvistPTELARLIKETGVKEIIVTDGEEGGYIFDGNGK 204
|
250 260
....*....|....*....|....
gi 738130265 236 WWVQPEKVDVQDTTAAGDTFIGTL 259
Cdd:cd01937 205 YTIPASKKDVVDPTGAGDVFLAAF 228
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
164-259 |
5.51e-06 |
|
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: 47.13 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 164 APAVYELTSE-LMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIIT-LGEAGS--------FIADGQ 233
Cdd:TIGR00687 124 APDLLEVYREkAIPVADIITPNQFELELLTGRRINTEEEAL-AAADALIAMGPDIVLVThLIRAGSqrdrsfegLVATQE 202
|
90 100 110
....*....|....*....|....*....|...
gi 738130265 234 KRWWV-------QPEKVDVQDTTAAgdTFIGTL 259
Cdd:TIGR00687 203 GRWHIsrplavfDPPPVGTGDLIAA--LLLATL 233
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
57-289 |
1.38e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 45.86 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 57 SFIGAVGNDANGQFMRATLLTNGVNVdAVSTNSDVPTGSAYIMLQeSGANTILIHGGANQALTIEDI----NTALIAQAD 132
Cdd:PLN02548 73 SYMGCIGKDKFGEEMKKCATAAGVNV-HYYEDESTPTGTCAVLVV-GGERSLVANLSAANCYKVEHLkkpeNWALVEKAK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 133 VL-IAQF--EVPFEVILAAFKIAKKNNVQTILN-PAPAVYE-LTSELMAV---TDIVLPNETEAQLLT---GINVINDEG 201
Cdd:PLN02548 151 FYyIAGFflTVSPESIMLVAEHAAANNKTFMMNlSAPFICEfFKDQLMEAlpyVDFLFGNETEARTFAkvqGWETEDVEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 202 VLNRVSDALQAKGVQR--SIITLGEAGSFIA-DGQ-KRWWVQP-EKVDVQDTTAAGDTFIGTLASVIAPDfSNLDDAVQR 276
Cdd:PLN02548 231 IALKISALPKASGTHKrtVVITQGADPTVVAeDGKvKEFPVIPlPKEKLVDTNGAGDAFVGGFLSQLVQG-KDIEECVRA 309
|
250
....*....|...
gi 738130265 277 ANIASAIAVTRPG 289
Cdd:PLN02548 310 GNYAANVIIQRSG 322
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
38-290 |
1.41e-05 |
|
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: 46.36 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 38 PGGkGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNsDVPTgsayIM-LQESGANTILIH----- 111
Cdd:PRK11316 50 PGG-AANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCDFVSVP-THPT----ITkLRVLSRNQQLIRldfee 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 112 --GGANQALTIEDINTALiAQADVLI-------AQFEVPfEVIlaafKIAKKNNVQTILNPAPAVYE-------LT---S 172
Cdd:PRK11316 124 gfEGVDPQPLLERIEQAL-PSIGALVlsdyakgALASVQ-AMI----QLARKAGVPVLIDPKGTDFEryrgatlLTpnlS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 173 ELMAVtdiVLPNETEAQLLT-GINVINDEGVlnrvsDALqakgvqrsIITLGEAG-SFIADGQKRWWVQPEKVDVQDTTA 250
Cdd:PRK11316 198 EFEAV---VGKCKDEAELVEkGMKLIADYDL-----SAL--------LVTRSEQGmTLLQPGKAPLHLPTQAREVYDVTG 261
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 738130265 251 AGDTFIGTLASVIApDFSNLDDAVQRANIASAIAVTRPGA 290
Cdd:PRK11316 262 AGDTVISVLAAALA-AGNSLEEACALANAAAGVVVGKLGT 300
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
32-279 |
2.12e-05 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 45.48 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 32 TEVTTAPGGKGANQAVAASRQGANVSFIGAVGNDaNGQFMRATLltngvnvdavstnsDVPTGSAYIMLQESGANTILIH 111
Cdd:PRK13508 29 VDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGE-LGQFIAEHL--------------DDQIKHAFYKIKGETRNCIAIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 112 GGANQALTIEDINTALIAQADVLIAQFEVPFEVILAA------------------FKIAKKNNVQTILNPAPAVYELTSE 173
Cdd:PRK13508 94 HEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVaisgslpaglpvdyyaqlIELANQAGKPVVLDCSGAALQAVLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 174 LMAVTDIVLPNETEAQLLTGINVINDegvLNRVSDALQA---KGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQDTTA 250
Cdd:PRK13508 174 SPYKPTVIKPNIEELSQLLGKEVSED---LDELKEVLQQplfEGIEWIIVSLGADGAFAKHNDTFYKVDIPKIEVVNPVG 250
|
250 260
....*....|....*....|....*....
gi 738130265 251 AGDTFIGTLASVIAPDFSNlDDAVQRANI 279
Cdd:PRK13508 251 SGDSTVAGIASGLLHQEDD-ADLLKKANV 278
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
166-284 |
6.17e-05 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 43.58 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 166 AVYELTSELMAVTDIVLPNETEAQLLTGINVINDEGVLNRVSDALQAKGVQRSIITLG------EAGSFIADGQKRWWVQ 239
Cdd:PRK06427 122 AVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMKAAARALHALGCKAVLIKGGhlldgeESVDWLFDGEGEERFS 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 738130265 240 PEKVDVQDTTAAGDtfigTLASVIA---PDFSNLDDAVQRAN--IASAIA 284
Cdd:PRK06427 202 APRIPTKNTHGTGC----TLSAAIAaelAKGASLLDAVQTAKdyVTRAIR 247
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
170-259 |
8.83e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 43.53 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 170 LTSELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIITLGEAGSFIADGQKRWWVQPEKVDVQDTT 249
Cdd:PRK09513 173 LVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVI-EAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTV 251
|
90
....*....|
gi 738130265 250 AAGDTFIGTL 259
Cdd:PRK09513 252 GAGDSMVGGL 261
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
173-293 |
5.82e-04 |
|
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: 40.79 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 173 ELMAVTDIVLPNETEAQLLTGINV---------INDEGVLNRVSDALQAKGVqrSIITLGEAGSFIA---DGQKRW---- 236
Cdd:cd01943 176 QALPRVDVFSPNLEEAARLLGLPTsepssdeekEAVLQALLFSGILQDPGGG--VVLRCGKLGCYVGsadSGPELWlpay 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 738130265 237 WVQPEKVdvQDTTAAGDTFIGTLASVIAPDfSNLDDAVQRANIASAIAVTRPGaIPS 293
Cdd:cd01943 254 HTKSTKV--VDPTGGGNSFLGGFAAGLALT-KSIDEACIYGSVAASFAIEQVG-LPR 306
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
173-221 |
7.47e-04 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 40.45 E-value: 7.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 738130265 173 ELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIIT 221
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDAL-EAIDWFHEQGIPVVVIT 182
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
163-287 |
9.35e-04 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 40.11 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 163 PAPAVYELTSELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIIT---LGEAGSFIADGQKRWWVQ 239
Cdd:PLN02978 135 PPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAR-EACAILHAAGPSKVVITsidIDGKLLLVGSHRKEKGAR 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 738130265 240 PE--KVDVQDT----TAAGDTFIGTLASVIAPDFSNLDDAVQRAnIASAIAVTR 287
Cdd:PLN02978 214 PEqfKIVIPKIpayfTGTGDLMAALLLGWSHKYPDNLDKAAELA-VSSLQAVLR 266
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
33-154 |
1.04e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 40.28 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 33 EVTTAPGGKGANQAVAASRQGANVSFIGAVGNDANGQFMRATLLTNGVNVDAVSTNSDVPTGSAYIMLQ-ESGANTIL-- 109
Cdd:PLN02543 166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAet 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 738130265 110 IHGGANQALTIEDINTALIAQADVliaqFEVPFEVILA---------AFKIAKK 154
Cdd:PLN02543 246 VKEAAEDSLLASELNLAVLKEARM----FHFNSEVLTSpsmqstlfrAIELSKK 295
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
175-274 |
1.10e-03 |
|
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: 39.76 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 175 MAVTDIVLPNETEAQLLTGinvindEGVLNRVSDALQAKGVQRSIITLGEAGS--FIADGQKRWWVQPEKvDVQDTTAAG 252
Cdd:cd01946 161 LAKVDVVIINDGEARQLTG------AANLVKAARLILAMGPKALIIKRGEYGAllFTDDGYFAAPAYPLE-SVFDPTGAG 233
|
90 100
....*....|....*....|....*.
gi 738130265 253 DT----FIGTLASVIAPDFSNLDDAV 274
Cdd:cd01946 234 DTfaggFIGYLASQKDTSEANMRRAI 259
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
125-277 |
7.41e-03 |
|
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: 37.08 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 125 TALIAQ------------ADVLIAQFEVPFEVI-LAAFKI---------------AKKNNVQTILNP------------A 164
Cdd:pfam08543 27 TALTAQntlgvqgvhplpPEFVAAQLDAVLEDIpVDAVKTgmlgsaeiieavaekLDKYGVPVVLDPvmvaksgdslldD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738130265 165 PAVYELTSELMAVTDIVLPNETEAQLLTGINVINDEGVLnRVSDALQAKGVQRSIITLGEAGS--------FIADGQKRW 236
Cdd:pfam08543 107 EAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMK-EAAKKLLALGAKAVLIKGGHLEGeeavvtdvLYDGGGFYT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 738130265 237 WVQPeKVDVQDTTAAGDTFigtlASVIA---PDFSNLDDAVQRA 277
Cdd:pfam08543 186 LEAP-RIPTKNTHGTGCTL----SAAIAanlAKGLSLPEAVREA 224
|
|
| |
