|
Name |
Accession |
Description |
Interval |
E-value |
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-288 |
2.78e-150 |
|
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: 422.22 E-value: 2.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 3 KTLVIGAAFVDVIVDVPKLPKTGDDIPGNLKSYVVGGsAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRELKIPIK 82
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 83 LPVRGNDNGWDI-SFIEPGGERSFLTIQGIEQDWKTEWFKTININEYKYFYLSGYEMENENAGKVILKELQKRIPE-SLL 160
Cdd:cd01944 80 LPPRGGDDGGCLvALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAgTTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 161 LFDASPRISSISKTIIQKIMKKNVIINCNKEEANYFMPKGHSLEEK-ARRIYAKTESPVIVTLGSNGSYYY--DGNDHII 237
Cdd:cd01944 160 VFDPGPRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAEAsALRIYAKTAAPVVVRLGSNGAWIRlpDGNTHII 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 692895231 238 PSEKKdKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKES 288
Cdd:cd01944 240 PGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-287 |
1.20e-41 |
|
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: 145.41 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 3 KTLVIGAAFVDVIVDVPKLPKTGDDIPGNLKSYVVGGSAFNV------FGtlkhekINTDLFVPVGEGNYANQIKEKMRE 76
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVavalarLG------ARVALVGAVGDDPFGDFLLAELRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 77 LKIPIKLPVRGND--NGWDISFIEPGGERSFLTIQGIEQDWKTEWFKTININEYKYFYLSGYEMENENAGKVILKELQK- 153
Cdd:COG0524 75 EGVDTSGVRRDPGapTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 154 RIPESLLLFDASPRISSISKT--IIQKIMKK-NVIInCNKEEANYFMPKgHSLEEKARRIYAKTESPVIVTLGSNGSYYY 230
Cdd:COG0524 155 RAAGVPVSLDPNYRPALWEPAreLLRELLALvDILF-PNEEEAELLTGE-TDPEEAAAALLARGVKLVVVTLGAEGALLY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 692895231 231 DGNDHI-IPSEKKDkIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKE 287
Cdd:COG0524 233 TGGEVVhVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRP 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-291 |
8.78e-32 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 119.37 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 6 VIGAAFVDVIVDVPKLPKTGDDIPGNLKSYvvGGSAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRELKIPIKLPV 85
Cdd:pfam00294 4 VIGEANIDLIGNVEGLPGELVRVSTVEKGP--GGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 86 R--GNDNGWDISFIEPGGERSFLTIQGIEQDWKTEWFKTI--NINEYKYFYLSGY---EM--ENENAGKVILKELQKRIP 156
Cdd:pfam00294 82 IdeDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGSlplGLpeATLEELIEAAKNGGTFDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 157 eslLLFDASPRISSISKTIIQKImkkNVIInCNKEEANYFM-PKGHSLEEKARR---IYAKTESPVIVTLGSNGSYYYDG 232
Cdd:pfam00294 162 ---NLLDPLGAAREALLELLPLA---DLLK-PNEEELEALTgAKLDDIEEALAAlhkLLAKGIKTVIVTLGADGALVVEG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 233 ND-HIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKESGSL 291
Cdd:pfam00294 235 DGeVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-284 |
2.83e-27 |
|
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: 107.70 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 1 MNKTLVIGAAFVDVIVDVPK--LPKTG--------------DDIPGNLKS-YVVGGSAFNVFGTLKHEKINTDLFVPVGE 63
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDafLEKLGlkkgdmiladmeeqEELLAKLPVkYIAGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 64 GNYANQIKEKMRELKIPIKLPVR-GNDNGWDISFIEPGGERSFLTIQGIEQDWKTEWFKTININEYKYFYLSGY------ 136
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVQpDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYlltvpp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 137 -------EMENENAGKVILkelqkripeSLllfdASPRISSISKTIIQKIMKKNVIINCNKEEA-NYFMPKGHSLEEKAR 208
Cdd:cd01168 161 eaillaaEHAKENGVKIAL---------NL----SAPFIVQRFKEALLELLPYVDILFGNEEEAeALAEAETTDDLEAAL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692895231 209 RIYAKTESPVIVTLGSNGSYYYDGNDHI-IPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVV 284
Cdd:cd01168 228 KLLALRCRIVVITQGAKGAVVVEGGEVYpVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVI 304
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-288 |
4.05e-22 |
|
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: 92.87 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 3 KTLVIGAAFVDVIVDVPKLPKTGDDIPGNLKSYVVGGSAFNV---FGTLKHEkinTDLFVPVGEGNYANQIKEKMRELKI 79
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVavqLAKLGND---VRFFSNLGRDEIGIQSLEELESGGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 80 PIKLPVRGNDNGWDISFIEPGGERSFLtiqgIEQDWKTEWFKTININEYKYFYLSGYemenenagkVILKELQKRIPESL 159
Cdd:cd01947 78 KHTVAWRDKPTRKTLSFIDPNGERTIT----VPGERLEDDLKWPILDEGDGVFITAA---------AVDKEAIRKCRETK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 160 L-LFDASPRISSIsktIIQKIMKKNVIINCNKEEanyfmPKGHSLEEKARRIYAKTespVIVTLGSNGSYYYDGNDHIIP 238
Cdd:cd01947 145 LvILQVTPRVRVD---ELNQALIPLDILIGSRLD-----PGELVVAEKIAGPFPRY---LIVTEGELGAILYPGGRYNHV 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 692895231 239 SEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKES 288
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-290 |
3.42e-20 |
|
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: 87.75 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 5 LVIGAAFVDVIVDVPKLPK--TGDDIPGNLKSYvvGGSAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRELKIPI- 81
Cdd:cd01942 3 AVVGHLNYDIILKVESFPGpfESVLVKDLRREF--GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 82 -KLPVRGNDNGWDISFIEPGGERSFLTIQGIEQDWKTEWFKTiNINEYKYFYLSGYEmenenagKVILKELQKRIPESLL 160
Cdd:cd01942 81 hVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEAD-PDGLADIVHLSSGP-------GLIELARELAAGGITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 161 LFDASPRISSISKTIIQKIMKKNVIINCNKEEANYFMPKgHSLEEKARRIYAKTespVIVTLGSNGSY-YYDGNDHIIPS 239
Cdd:cd01942 153 SFDPGQELPRLSGEELEEILERADILFVNDYEAELLKER-TGLSEAELASGVRV---VVVTLGPKGAIvFEDGEEVEVPA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 692895231 240 EKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKESGS 290
Cdd:cd01942 229 VPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-263 |
3.66e-15 |
|
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: 73.82 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 3 KTLVIGAAFVDVIVDVPKLPKTGDDIPGnlksyvvgGSAFNV------FGtlkhekINTDLFVPVGEGNYANQIKEKMRE 76
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFTKAPG--------GAPANVavalarLG------GKAAFIGKVGDDEFGDFLLETLKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 77 LKIPIKLPVRgnDNGW--DISF--IEPGGERSFLTIqgIEQDWKTEWFKTIN---INEYKYFYLSGYEMENENAGKVILk 149
Cdd:cd01167 67 AGVDTRGIQF--DPAAptTLAFvtLDADGERSFEFY--RGPAADLLLDTELNpdlLSEADILHFGSIALASEPSRSALL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 150 ELQKRIPES--LLLFDASPRISSISKT-----IIQKIMKKNVIINCNKEEAnYFMPKGHSLEEKARRIYAKTESPVIVTL 222
Cdd:cd01167 142 ELLEAAKKAgvLISFDPNLRPPLWRDEeeareRIAELLELADIVKLSDEEL-ELLFGEEDPEEIAALLLLFGLKLVLVTR 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 692895231 223 GSNGSYYY-DGNDHIIPSEKkDKIINTIGAGDTHCGGILAGL 263
Cdd:cd01167 221 GADGALLYtKGGVGEVPGIP-VEVVDTTGAGDAFVAGLLAQL 261
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-287 |
6.38e-15 |
|
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: 73.35 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 5 LVIGAAFVDVIVDVPKLPKTGDDIPGNLKSYVVGGSAFN---VFGTLKHekiNTDLFVPVGEGNYANQIKEKMRELKIPI 81
Cdd:cd01174 3 VVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANqavAAARLGA---RVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 82 KL--PVRGNDNGWDISFIEPGGERSFLTIQG---------IEQDWktEWFKtinineykyfylsgyemenenAGKVILke 150
Cdd:cd01174 80 SYveVVVGAPTGTAVITVDESGENRIVVVPGangeltpadVDAAL--ELIA---------------------AADVLL-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 151 LQKRIPES--------------LLLFDASPrissiSKTIIQKIMKKNVIINCNKEEA----NYFMPKGHSLEEKARRIYA 212
Cdd:cd01174 135 LQLEIPLEtvlaalraarragvTVILNPAP-----ARPLPAELLALVDILVPNETEAalltGIEVTDEEDAEKAARLLLA 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692895231 213 KTESPVIVTLGSNGSYYYDGNDHI-IPSEKkDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKE 287
Cdd:cd01174 210 KGVKNVIVTLGAKGALLASGGEVEhVPAFK-VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRP 284
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-284 |
2.37e-14 |
|
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: 71.84 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 3 KTLVIGAAFVDVivdVPKLPKTGDDIPGNLKSYvvGGSAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRELKIPIK 82
Cdd:cd01166 1 DVVTIGEVMVDL---SPPGGGRLEQADSFRKFF--GGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 83 LPVRGNDNGWDISFIE--PGGERSFLT---------IQGIEQDWKtewfktiNINEYKYFYLSGYEM-ENENAGKVILKE 150
Cdd:cd01166 76 HVRVDPGRPTGLYFLEigAGGERRVLYyragsaasrLTPEDLDEA-------ALAGADHLHLSGITLaLSESAREALLEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 151 LQK-RIPESLLLFDASPRISSIS----KTIIQKIMKKNVIINCNKEEANYF--MPKGHSLEEKARRIYAKTESpVIVTLG 223
Cdd:cd01166 149 LEAaKARGVTVSFDLNYRPKLWSaeeaREALEELLPYVDIVLPSEEEAEALlgDEDPTDAAERALALALGVKA-VVVKLG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692895231 224 SNGSYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVV 284
Cdd:cd01166 228 AEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVV 288
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
218-276 |
1.23e-09 |
|
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: 57.71 E-value: 1.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692895231 218 VIVTLGSNGSYYYDGND----HIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILA 276
Cdd:cd01941 216 VIVTLGAKGVLLSSREGgvetKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
162-263 |
3.12e-09 |
|
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: 55.56 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 162 FDASPRISSISKTIIQKIMKKNVIINCNKEEANYFM----PKGHSLEEKARRIYAKTESPVIVTLGSNGSYYYDGNDHII 237
Cdd:cd00287 89 LDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTgrrdLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEV 168
|
90 100
....*....|....*....|....*..
gi 692895231 238 PSEKKD-KIINTIGAGDTHCGGILAGL 263
Cdd:cd00287 169 HVPAFPvKVVDTTGAGDAFLAALAAGL 195
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
202-287 |
2.69e-08 |
|
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: 53.69 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 202 SLEEKARRIYAKTESPVIVTLGSNGSYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSG 281
Cdd:cd01164 201 DVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGS 280
|
....*.
gi 692895231 282 LVVEKE 287
Cdd:cd01164 281 ATAFSP 286
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
25-263 |
6.30e-08 |
|
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: 52.74 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 25 GD---DIPGNLKSYVVGGSAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRELKIPIK-LPVRGNDNGWDIsFIEPG 100
Cdd:cd01940 6 GDnvvDKYLHLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIShCRVKEGENAVAD-VELVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 101 GERSFL-----TIQG---IEQDWktEWfktinINEYKYFYLSGYEMENEnagkvILKELQKRIPESLLL-FDASPRISS- 170
Cdd:cd01940 85 GDRIFGlsnkgGVARehpFEADL--EY-----LSQFDLVHTGIYSHEGH-----LEKALQALVGAGALIsFDFSDRWDDd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 171 ISKTIIQKImkKNVIINCNKEEANyfmpkghSLEEKARRIYAKTESPVIVTLGSNGSYYYDGNDHIIPSEKKDKIINTIG 250
Cdd:cd01940 153 YLQLVCPYV--DFAFFSASDLSDE-------EVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLG 223
|
250
....*....|...
gi 692895231 251 AGDTHCGGILAGL 263
Cdd:cd01940 224 AGDSFIAGFLLSL 236
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
202-286 |
7.32e-08 |
|
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: 52.56 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 202 SLEEKARRIYAKTESP-VIVTLGSNGSYYYDGND--HIIP---SEKKDkiinTIGAGDTHCGGILAGLNKDMSFKDSVIL 275
Cdd:cd01172 205 ELEAAGEKLLELLNLEaLLVTLGEEGMTLFERDGevQHIPalaKEVYD----VTGAGDTVIATLALALAAGADLEEAAFL 280
|
90
....*....|.
gi 692895231 276 ANRLSGLVVEK 286
Cdd:cd01172 281 ANAAAGVVVGK 291
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
218-276 |
1.90e-07 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 51.29 E-value: 1.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692895231 218 VIVTLGSNGSYYYDGND--HIIPseKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILA 276
Cdd:COG1105 217 VVVSLGADGALLVTEDGvyRAKP--PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
197-285 |
1.03e-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: 48.94 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 197 MPKGHSLEEKARRIYAKTESPVIVTLGSNGSYYYDGND-HIIPSEKKDkIINTIGAGDTHCGGILAGLNKDMSFKDSVIL 275
Cdd:cd01937 166 AEVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGkYTIPASKKD-VVDPTGAGDVFLAAFLYSRLSGKDIKEAAEF 244
|
90
....*....|
gi 692895231 276 ANRLSGLVVE 285
Cdd:cd01937 245 AAAAAAKFIE 254
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
218-286 |
3.12e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 47.88 E-value: 3.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692895231 218 VIVTLGSNGS--YYYDGNDHIIPSEKKDkiINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEK 286
Cdd:PLN02630 206 VIVTNGKKGCriYWKDGEMRVPPFPAIQ--VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQ 274
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
113-281 |
9.44e-06 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 46.25 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 113 QDWKTEWFKTININEYKYFYLSG------------YEMENENAGKVILK---ELQKRIPESLLLFDASPRISsISKTIIQ 177
Cdd:cd01939 113 PEVTYDDFSKIDLTQYGWIHFEGrnpdetlrmmqhIEEHNNRRPEIRITisvEVEKPREELLELAAYCDVVF-VSKDWAQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 178 KIMKKNviincnkeeanyfmpkghsLEEKARRIY--AKTESPVIVTLGSNGSYYY--DGNDHIIPSEKKDKIINTIGAGD 253
Cdd:cd01939 192 SRGYKS-------------------PEECLRGEGprAKKAALLVCTWGDQGAGALgpDGEYVHSPAHKPIRVVDTLGAGD 252
|
170 180
....*....|....*....|....*....
gi 692895231 254 THCGGILAGLNK-DMSFKDSVILANRLSG 281
Cdd:cd01939 253 TFNAAVIYALNKgPDDLSEALDFGNRVAS 281
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
34-287 |
1.54e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.79 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 34 SYVVGGSAFN---VFGTLKHEKINTDLFVP-VGEGNYANQIKEKMrelkipiklpvrgNDNGWDISFIE----PGG---- 101
Cdd:PTZ00247 58 SYVPGGSALNtarVAQWMLQAPKGFVCYVGcVGDDRFAEILKEAA-------------EKDGVEMLFEYttkaPTGtcav 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 102 -----ERSFLTIQGIEQDWKTEWFKT----ININEYKYFYLSGYEM--ENENAGKVILKELQKRIPESLLLfdASPRISS 170
Cdd:PTZ00247 125 lvcgkERSLVANLGAANHLSAEHMQShavqEAIKTAQLYYLEGFFLtvSPNNVLQVAKHARESGKLFCLNL--SAPFISQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 171 ISKTIIQKIMKKNVIINCNKEEANYF---MPKGH-SLEEKARRIYA------KTESPVIVTLGSNGSYYYDgNDHI---- 236
Cdd:PTZ00247 203 FFFERLLQVLPYVDILFGNEEEAKTFakaMKWDTeDLKEIAARIAMlpkysgTRPRLVVFTQGPEPTLIAT-KDGVtsvp 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 692895231 237 IPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEKE 287
Cdd:PTZ00247 282 VPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHN 332
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
203-285 |
4.05e-05 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 43.96 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 203 LEEKARRIYAKTESPVIVTLGSNGSYYYDGNDH----IIPSEkkdkIINTIGAGDTHCGGILAGLNKDMSFKDSVILANR 278
Cdd:PRK09813 173 LRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFwrqaPEPVT----VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTA 248
|
....*..
gi 692895231 279 LSGLVVE 285
Cdd:PRK09813 249 CAAKTIQ 255
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-286 |
4.78e-05 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 44.34 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 1 MNKTLVIGAAFVDVIVDVPKLPKTGDDIPGNLKSYVVGGSAFNVFGTLKHEKINTDLFVPVGEGNYANQIKEKMRelkip 80
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFK----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 81 iklpvrgnDNGWDISFIEpggeRSFLTIQG---IEQDWKTEWFKTI---NINEY-KYFYLSGYEMENENAGKVILkeLQK 153
Cdd:PTZ00292 90 --------RNGVNTSFVS----RTENSSTGlamIFVDTKTGNNEIViipGANNAlTPQMVDAQTDNIQNICKYLI--CQN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 154 RIP-ESLL-------------LFDASPRISSISKTIIQKIMKKNVIINCNKEEANYFMPKGHSLEEKARRIY----AKTE 215
Cdd:PTZ00292 156 EIPlETTLdalkeakergcytVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASkelqQLGV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692895231 216 SPVIVTLGSNG-SYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVVEK 286
Cdd:PTZ00292 236 ENVIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTR 307
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
218-284 |
6.40e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 43.92 E-value: 6.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692895231 218 VIVTLGSNGSYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLVV 284
Cdd:PRK09513 220 VVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAV 286
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
218-263 |
1.36e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 42.62 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 692895231 218 VIVTLGSNGSYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGL 263
Cdd:PRK09434 216 LLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGL 261
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
219-271 |
3.05e-04 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 41.53 E-value: 3.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 692895231 219 IVTLGSNGSYYYDGNDHIIPSEKKDKIINTIGAGDTHCGGILAGLNKDMS-FKD 271
Cdd:PLN02323 234 LVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSlLED 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
209-286 |
6.94e-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: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692895231 209 RIYAKTESPVIVTLGSNGSYYYDGNDHII---PS--EKKDKIINTIGAGDTHCGGILAGLNKDMSFKDSVILANRLSGLV 283
Cdd:cd01943 219 GILQDPGGGVVLRCGKLGCYVGSADSGPElwlPAyhTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFA 298
|
...
gi 692895231 284 VEK 286
Cdd:cd01943 299 IEQ 301
|
|
| |
