|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
6-328 |
2.13e-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: 304.86 E-value: 2.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGlcLR 85
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLG-----ARVAMIGAVGDDAFGDELLEN--LR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 KVCIY-EKESVVSDTHTGVASITVDtTSGQNTIVVSPGANLSLRPEEVASTLTRILSStnndntqlsrgkDVVLVQLEIT 164
Cdd:cd01174 74 EEGIDvSYVEVVVGAPTGTAVITVD-ESGENRIVVVPGANGELTPADVDAALELIAAA------------DVLLLQLEIP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 165 PETAHEALKTSSRLGAITILNPAPAPKgwdISNDWLSSIDILIPNESELASLCGFDdvggDVTGEGEEAMARSLLERGVR 244
Cdd:cd01174 141 LETVLAALRAARRAGVTVILNPAPARP---LPAELLALVDILVPNETEAALLTGIE----VTDEEDAEKAARLLLAKGVK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 245 qAVIVTLGARGAMIVRRssGRTESSPStLPCKslpVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGA 324
Cdd:cd01174 214 -NVIVTLGAKGALLASG--GEVEHVPA-FKVK---AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
....
gi 223992801 325 QESY 328
Cdd:cd01174 287 QPSI 290
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
11-328 |
3.92e-88 |
|
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: 266.00 E-value: 3.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 11 GSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLCLRKVcIY 90
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLG-----AEVSMIGKVGDDAFGDELLENLKSNGI-DT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 91 EKESVVSDTHTGVASITVDTTsGQNTIVVSPGANLSLRPEEVASTLTRILSStnndntqlsrgkDVVLVQLEITPETAHE 170
Cdd:TIGR02152 75 EYVGTVKDTPTGTAFITVDDT-GENRIVVVAGANAELTPEDIDAAEALIAES------------DIVLLQLEIPLETVLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 171 ALKTSSRLGAITILNPAPAPKgwDISNDWLSSIDILIPNESELASLCGfddvggdVTGEGEEAM---ARSLLERGVrQAV 247
Cdd:TIGR02152 142 AAKIAKKHGVKVILNPAPAIK--DLDDELLSLVDIITPNETEAEILTG-------IEVTDEEDAekaAEKLLEKGV-KNV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 248 IVTLGARGAMIVrrssgrTESSPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGAQES 327
Cdd:TIGR02152 212 IITLGSKGALLV------SKDESKLIPAFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSS 285
|
.
gi 223992801 328 Y 328
Cdd:TIGR02152 286 I 286
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
7-328 |
2.26e-75 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 234.63 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 7 VVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLCLRK 86
Cdd:PTZ00292 18 VVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLG-----AKVAMVGMVGTDGFGSDTIKNFKRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 87 VCIyEKESVVSDTHTGVASITVDTTSGQNTIVVSPGANLSLRPEEVastltrilsSTNNDNTQlsRGKDVVLVQLEITPE 166
Cdd:PTZ00292 93 VNT-SFVSRTENSSTGLAMIFVDTKTGNNEIVIIPGANNALTPQMV---------DAQTDNIQ--NICKYLICQNEIPLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 167 TAHEALKTSSRLGAITILNPAPAPKGWD--ISNDWLSSIDILIPNESELASLcgfddVGGDVT-GEGEEAMARSLLERGV 243
Cdd:PTZ00292 161 TTLDALKEAKERGCYTVFNPAPAPKLAEveIIKPFLKYVSLFCVNEVEAALI-----TGMEVTdTESAFKASKELQQLGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 244 RQaVIVTLGARGAMIVrrssgRTESSPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRG 323
Cdd:PTZ00292 236 EN-VIITLGANGCLIV-----EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
....*
gi 223992801 324 AQESY 328
Cdd:PTZ00292 310 TQSSY 314
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-328 |
1.46e-70 |
|
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: 221.30 E-value: 1.46e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLR----- 80
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGA-----RVALVGAVGDDPFGDFLLAelrae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 81 GLCLRKVciyekeSVVSDTHTGVASITVDTtSGQNTIVVSPGANLSLRPEEVASTLTRilsstnndntqlsrGKDVVLVQ 160
Cdd:COG0524 76 GVDTSGV------RRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLA--------------GADILHLG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 161 L-----EITPETAHEALKTSSRLGAITILNPAPAPKGW----DISNDWLSSIDILIPNESELASLCGFDDVggdvtgege 231
Cdd:COG0524 135 GitlasEPPREALLAALEAARAAGVPVSLDPNYRPALWeparELLRELLALVDILFPNEEEAELLTGETDP--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 232 EAMARSLLERGVRqAVIVTLGARGAMIVrrssgrTESSPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMA 311
Cdd:COG0524 206 EEAAAALLARGVK-LVVVTLGAEGALLY------TGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
|
330
....*....|....*..
gi 223992801 312 CGVASMSVRKRGAQESY 328
Cdd:COG0524 279 NAAAALVVTRPGAQPAL 295
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
5-327 |
5.05e-59 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 192.01 E-value: 5.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 5 GKVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLCL 84
Cdd:PRK11142 3 GKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLG-----ADIAFIACVGDDSIGESMRQQLAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 85 RKVCIyEKESVVSDTHTGVASITVDtTSGQNTIVVSPGANLSLRPEEVASTLTRILSStnndntqlsrgkDVVLVQLEiT 164
Cdd:PRK11142 78 DGIDT-APVSVIKGESTGVALIFVN-DEGENSIGIHAGANAALTPALVEAHRELIANA------------DALLMQLE-T 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 165 P-ETAHEALKTSSRLGAITILNPAPAPKgwdISNDWLSSIDILIPNESELASLCGFddvggDVTGEGEEAMARSLL-ERG 242
Cdd:PRK11142 143 PlETVLAAAKIAKQHGTKVILNPAPARE---LPDELLALVDIITPNETEAEKLTGI-----RVEDDDDAAKAAQVLhQKG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 243 VrQAVIVTLGARGAMIVRRSSGRtesspsTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKR 322
Cdd:PRK11142 215 I-ETVLITLGSRGVWLSENGEGQ------RVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRK 287
|
....*
gi 223992801 323 GAQES 327
Cdd:PRK11142 288 GAQPS 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-326 |
3.61e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.97 E-value: 3.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPspGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLclR 85
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGG-----DVAFIGAVGDDNFGEFLLQEL--K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 KVCIY-EKESVVSDTHTGVASITVDTTsGQNTIVVSPGANLSLRPEEVASTLTRIlssTNNDNTQLSrgkdvVLVQLEIT 164
Cdd:pfam00294 72 KEGVDtDYVVIDEDTRTGTALIEVDGD-GERTIVFNRGAAADLTPEELEENEDLL---ENADLLYIS-----GSLPLGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 165 PETAHEALKTSSRLGAITILNPAPAPKGWDISNDWLSSIDILIPNESELASLCGFDDVggdvTGEGEEAMARSLLERGVr 244
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLD----DIEEALAALHKLLAKGI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 245 QAVIVTLGARGAMIVRRSSgrtesspsTLPCKSLP---VVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRK 321
Cdd:pfam00294 218 KTVIVTLGADGALVVEGDG--------EVHVPAVPkvkVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
|
....*
gi 223992801 322 RGAQE 326
Cdd:pfam00294 290 SGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
7-325 |
1.78e-29 |
|
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: 113.95 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 7 VVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLCLRK 86
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGL-----SPGLVAAVGEDFHGRLYLEELREEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 87 VCIYEKESVVsDTHTGVASITVDttSGQNTIVVS-PGANLSLRPEEVAST--LTRILSstnndntqLSRGKDVVLVQLEI 163
Cdd:cd01942 77 VDTSHVRVVD-EDSTGVAFILTD--GDDNQIAYFyPGAMDELEPNDEADPdgLADIVH--------LSSGPGLIELAREL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 164 TPEtahealktssrlGAITILNPAP--APKGWDISNDWLSSIDILIPNESELASLCgfddvggDVTGEGEEAMARsller 241
Cdd:cd01942 146 AAG------------GITVSFDPGQelPRLSGEELEEILERADILFVNDYEAELLK-------ERTGLSEAELAS----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 242 GVRqAVIVTLGARGAMIVrrSSGRTESSPSTLPCKslpVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRK 321
Cdd:cd01942 202 GVR-VVVVTLGPKGAIVF--EDGEEVEVPAVPAVK---VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVER 275
|
....
gi 223992801 322 RGAQ 325
Cdd:cd01942 276 RGAQ 279
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
37-324 |
4.54e-26 |
|
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: 105.39 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 37 VTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRglCLRKVCIYEKESVVSDTHTGVAsitvdttsgqnT 116
Cdd:cd01168 51 KYIAGGSAANTIRGAAALG-----GSAAFIGRVGDDKLGDFLLK--DLRAAGVDTRYQVQPDGPTGTC-----------A 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 117 IVVSPGANLSLRPEEVASTLtriLSSTNNDNTQLSRGKDVVL--VQLEITPETAHEALKTSSRLGAITILNpAPAPKGWD 194
Cdd:cd01168 113 VLVTPDAERTMCTYLGAANE---LSPDDLDWSLLAKAKYLYLegYLLTVPPEAILLAAEHAKENGVKIALN-LSAPFIVQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 195 ISNDWLSSI----DILIPNESELASLCGFDdvggdvTGEGEEAmARSLLERGVRQAVIvTLGARGAMIVrrSSGRTESSP 270
Cdd:cd01168 189 RFKEALLELlpyvDILFGNEEEAEALAEAE------TTDDLEA-ALKLLALRCRIVVI-TQGAKGAVVV--EGGEVYPVP 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 223992801 271 STLPCKslpVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGA 324
Cdd:cd01168 259 AIPVEK---IVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-324 |
5.14e-26 |
|
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: 104.97 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTtytpslPSPGQTLLGTD-FVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLcl 84
Cdd:cd01166 1 DVVTIGEVMVDLS------PPGGGRLEQADsFRKFFGGAEANVAVGLARLGH-----RVALVTAVGDDPFGRFILAEL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 85 rkvciyEKESVvsDTHtgvaSITVDTTSGQNTIVVSPGAN-----LSLRPEEVASTLTRILsstnnDNTQLSRGKDVVLV 159
Cdd:cd01166 68 ------RREGV--DTS----HVRVDPGRPTGLYFLEIGAGgerrvLYYRAGSAASRLTPED-----LDEAALAGADHLHL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 160 ------QLEITPETAHEALKTSSRLGAITILNPAPAPKGWDIS------NDWLSSIDILIPNESELASLCGFDDvggdvT 227
Cdd:cd01166 131 sgitlaLSESAREALLEALEAAKARGVTVSFDLNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDED-----P 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 228 GEGEEAMARslLERGVRqAVIVTLGARGAMIVRRssGRTESSPSTlpckSLPVVDAVGAGDAFCGALAAYLSRGVDLERA 307
Cdd:cd01166 206 TDAAERALA--LALGVK-AVVVKLGAEGALVYTG--GGRVFVPAY----PVEVVDTTGAGDAFAAGFLAGLLEGWDLEEA 276
|
330
....*....|....*..
gi 223992801 308 ASMACGVASMSVRKRGA 324
Cdd:cd01166 277 LRFANAAAALVVTRPGD 293
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-319 |
7.96e-25 |
|
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: 101.62 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVtSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLclR 85
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLG-----VSVALLSAVGDDSEGESILEES--E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 KVCIYEKESVVSDTHTGVASITVDTTsGQNTIVVSPGANLSLRPEEVASTLTRILSSTnndntqlsrgkDVVLVQLEITP 165
Cdd:cd01941 73 KAGLNVRGIVFEGRSTASYTAILDKD-GDLVVALADMDIYELLTPDFLRKIREALKEA-----------KPIVVDANLPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 166 ETAHEALKTSSRLGAITILNPAPAPKGWDISnDWLSSIDILIPNESELASLCGFddvgGDVTGEGEEAMARSLLERGVrQ 245
Cdd:cd01941 141 EALEYLLALAAKHGVPVAFEPTSAPKLKKLF-YLLHAIDLLTPNRAELEALAGA----LIENNEDENKAAKILLLPGI-K 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223992801 246 AVIVTLGARGAMIvrrSSGRTESSPSTLP-CKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSV 319
Cdd:cd01941 215 NVIVTLGAKGVLL---SSREGGVETKLFPaPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
16-316 |
9.90e-24 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 98.67 E-value: 9.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 16 DLTTYTPSLpSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDmGRSLLRGLclrkvciyEKESV 95
Cdd:COG1105 11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGV-----DVTALGFLGGFT-GEFIEELL--------DEEGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 96 VSDTHTgVASIT------VDTTSGQNTIVVSPGANLSlrPEEVASTLTRILSSTNNDNTqlsrgkdVVL---VQLEITPE 166
Cdd:COG1105 76 PTDFVP-IEGETrinikiVDPSDGTETEINEPGPEIS--EEELEALLERLEELLKEGDW-------VVLsgsLPPGVPPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 167 TAHEALKTSSRLGAITILnpapapkgwDISNDWL-----SSIDILIPNESELASLcgfddVGGDVTGEGE-EAMARSLLE 240
Cdd:COG1105 146 FYAELIRLARARGAKVVL---------DTSGEALkaaleAGPDLIKPNLEELEEL-----LGRPLETLEDiIAAARELLE 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223992801 241 RGVrQAVIVTLGARGAMIVRRSSGRTESSPSTlpckslPVVDAVGAGDAFCGALAAYLSRGVDLERAA--SMACGVAS 316
Cdd:COG1105 212 RGA-ENVVVSLGADGALLVTEDGVYRAKPPKV------EVVSTVGAGDSMVAGFLAGLARGLDLEEALrlAVAAGAAA 282
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
10-328 |
1.31e-20 |
|
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: 89.66 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 10 VGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGIVSRtssvhMIGRVGDDDMGRSLLRGLclrkvci 89
Cdd:cd01945 5 VGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQAR-----LIGVVGDDAIGRLILAEL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 90 yEKESVvsDTHTgvasitvdttsgqntIVVSPGANlSLRPEEVASTLTRILSSTNNDNTQLSRGK---------DVVLVQ 160
Cdd:cd01945 73 -AAEGV--DTSF---------------IVVAPGAR-SPISSITDITGDRATISITAIDTQAAPDSlpdailggaDAVLVD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 161 LEiTPETAHEALKTSSRLG--AITILNPAPAPKGWDIsndwLSSIDILIPNESELASLCGfddvggdvtgEGEEAMARSL 238
Cdd:cd01945 134 GR-QPEAALHLAQEARARGipIPLDLDGGGLRVLEEL----LPLADHAICSENFLRPNTG----------SADDEALELL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 239 LERGVRqAVIVTLGARGaMIVRRSSGRTESSPSTlpckSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMS 318
Cdd:cd01945 199 ASLGIP-FVAVTLGEAG-CLWLERDGELFHVPAF----PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALK 272
|
330
....*....|
gi 223992801 319 VRKRGAQESY 328
Cdd:cd01945 273 CRGLGGRAGL 282
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
27-324 |
3.88e-19 |
|
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: 85.77 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 27 PGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLCLRKVciyEKESVVSDTH--TGVA 104
Cdd:cd01167 14 PEGSGAPETFTKAPGGAPANVAVALARLGG-----KAAFIGKVGDDEFGDFLLETLKEAGV---DTRGIQFDPAapTTLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 105 SITVDTTSG-QNTIVVSPGANLSLRPEEVAStltrilsstnndntqLSRGKDVV----LVQL-EITPETAHEALKTSSRL 178
Cdd:cd01167 86 FVTLDADGErSFEFYRGPAADLLLDTELNPD---------------LLSEADILhfgsIALAsEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 179 GAITILNPAPAPKGWDISNDWLSSI-------DILIPNESELASLCGfddvggdvtGEGEEAMARSLLERGvRQAVIVTL 251
Cdd:cd01167 151 GVLISFDPNLRPPLWRDEEEARERIaellelaDIVKLSDEELELLFG---------EEDPEEIAALLLLFG-LKLVLVTR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 252 GARGAmIVRRSSGRTEsspstLPCKSLPVVDAVGAGDAFCGA-LAAYLSRGVD------LERAASMACGVASMSVRKRGA 324
Cdd:cd01167 221 GADGA-LLYTKGGVGE-----VPGIPVEVVDTTGAGDAFVAGlLAQLLSRGLLaldedeLAEALRFANAVGALTCTKAGA 294
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
16-316 |
5.38e-18 |
|
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: 82.58 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 16 DLTTYTPSLpSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDdMGRSLLRGLclrkvciyEKESV 95
Cdd:cd01164 12 DLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGV-----EVTALGFLGGF-TGDFFEALL--------KEEGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 96 VSDTHTGVA----SITVDTTSGQNTIVVSPGANLSlrPEEVASTLTRILsstnndntQLSRGKDVVLVQLEITPETAHEA 171
Cdd:cd01164 77 PDDFVEVAGetriNVKIKEEDGTETEINEPGPEIS--EEELEALLEKLK--------ALLKKGDIVVLSGSLPPGVPADF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 172 LKTSSRL----GAITILnpapapkgwDISNDWLSSI-----DILIPNESELASLCG-----FDDVggdvtgegeEAMARS 237
Cdd:cd01164 147 YAELVRLarekGARVIL---------DTSGEALLAAlaakpFLIKPNREELEELFGrplgdEEDV---------IAAARK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 238 LLERGVrQAVIVTLGARGAMIVRRSSGRTESSPSTlpckslPVVDAVGAGDAFCGALAAYLSRGVDLERAA--SMACGVA 315
Cdd:cd01164 209 LIERGA-ENVLVSLGADGALLVTKDGVYRASPPKV------KVVSTVGAGDSMVAGFVAGLAQGLSLEEALrlAVAAGSA 281
|
.
gi 223992801 316 S 316
Cdd:cd01164 282 T 282
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
40-325 |
6.08e-16 |
|
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: 76.83 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 40 AGGkGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLclrkvciyEKESVvsDTHtGVASITVDTTsgQNTIVV 119
Cdd:cd01172 39 LGG-AANVANNLASLG-----AKVTLLGVVGDDEAGDLLRKLL--------EKEGI--DTD-GIVDEGRPTT--TKTRVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 120 SPGANLsLRpeevASTLTRILSSTNNDNTQL----SRGKDVVLVQLE------ITPETAHEALKTSSRLGAITILNPapa 189
Cdd:cd01172 100 ARNQQL-LR----VDREDDSPLSAEEEQRLIeriaERLPEADVVILSdygkgvLTPRVIEALIAAARELGIPVLVDP--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 190 pKGWDISNdwLSSIDILIPNESELASLCGFDDVggdvTGEGEEAMARSLLERGVRQAVIVTLGARGAMIVRRSSGRTEss 269
Cdd:cd01172 172 -KGRDYSK--YRGATLLTPNEKEAREALGDEIN----DDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQH-- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 223992801 270 pstLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGAQ 325
Cdd:cd01172 243 ---IPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTA 295
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
16-326 |
2.01e-14 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 72.61 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 16 DLTTYTPSLpSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDmGRSLLRGLclrkvciyEKESV 95
Cdd:TIGR03168 11 DLTIEVDGL-TPGEVNRVAAVRKDAGGKGINVARVLARLGA-----EVVATGFLGGFT-GEFIEALL--------AEEGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 96 VSDTHTGVAS----ITVDTTSGQNTIVVSPGANLSlrPEEVASTLTRILSstnndntQLSRGKDVVL---VQLEITPETA 168
Cdd:TIGR03168 76 KNDFVEVKGEtrinVKIKESSGEETELNEPGPEIS--EEELEQLLEKLRE-------LLASGDIVVIsgsLPPGVPPDFY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 169 HEALKTSSRLGAITILnpapapkgwDISNDWLSS-----IDILIPNESELASLcgfddVGGDVTGEGE-EAMARSLLERG 242
Cdd:TIGR03168 147 AQLIAIARKKGAKVIL---------DTSGEALREalaakPFLIKPNHEELEEL-----FGRELKTLEEiIEAARELLDRG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 243 VrQAVIVTLGARGAMIVRrSSGRTESSPstLPCKslpVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKR 322
Cdd:TIGR03168 213 A-ENVLVSLGADGALLVT-KEGALKATP--PKVE---VVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSP 285
|
....
gi 223992801 323 GAQE 326
Cdd:TIGR03168 286 GTGL 289
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-324 |
1.10e-13 |
|
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: 69.75 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLCLR 85
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLG-----NDVRFFSNLGRDEIGIQSLEELESG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 KVCIYekeSVVSDTHTGVASITVDTtSGQNTIVVSPGAnlsLRPEEVASTLTRIlsstnndntqlsrgkDVVLvqleITP 165
Cdd:cd01947 76 GDKHT---VAWRDKPTRKTLSFIDP-NGERTITVPGER---LEDDLKWPILDEG---------------DGVF----ITA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 166 ETAHEALKTSSRLGAITILNPAPaPKGWDISNDWLSSIDILIPNESELaslcgfddvggdvtgeGEEAMARSLLERGVRq 245
Cdd:cd01947 130 AAVDKEAIRKCRETKLVILQVTP-RVRVDELNQALIPLDILIGSRLDP----------------GELVVAEKIAGPFPR- 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223992801 246 AVIVTLGARGAMIVrrSSGRTESSPStlpcKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGA 324
Cdd:cd01947 192 YLIVTEGELGAILY--PGGRYNHVPA----KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-323 |
2.78e-12 |
|
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: 66.29 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGkGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLclR 85
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGI-----PTVNAGPLGNGNWADQIRQAM--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 KVCIYEKESVVSDTHTGVASITVDTtSGQNTIVVSPGA----------NLSLRPEEVASTLTRILSSTNndntqlsRGKD 155
Cdd:cd01944 73 DEGIEILLPPRGGDDGGCLVALVEP-DGERSFISISGAeqdwstewfaTLTVAPYDYVYLSGYTLASEN-------ASKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 156 VVLVQLEITPETAHEALKTSSRLGAI--TILNPAPApkgwdiSNDWLSSidilipNESELASLCGFDDVGGDVTGEGEEA 233
Cdd:cd01944 145 ILLEWLEALPAGTTLVFDPGPRISDIpdTILQALMA------KRPIWSC------NREEAAIFAERGDPAAEASALRIYA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 234 MARSLlergvrqaVIVTLGARGAMIvrRSSGRTessPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACG 313
Cdd:cd01944 213 KTAAP--------VVVRLGSNGAWI--RLPDGN---THIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANA 279
|
330
....*....|
gi 223992801 314 VASMSVRKRG 323
Cdd:cd01944 280 AAAIVVTRSG 289
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
34-323 |
3.59e-12 |
|
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: 66.08 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 34 TDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDMGRSLLRGLCLRKVciyEKESVVSDTH--TGVA--SITVD 109
Cdd:TIGR04382 27 TSFAKYLGGSPANIAVGAARLGL-----KTAFITRVGDDQFGRFVRDYLRREGV---DTSHVVTDPGrrTSLVflEIKPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 110 TTSGQnTIVVSPGANLSLRPEEVASTL---TRILSSTNndnTQLSRgkdvvlvqlEITPETAHEALKTSSRLGAITILNP 186
Cdd:TIGR04382 99 DEFPL-LFYRENAADLALTPDDVDEDYiasARALLVSG---TALSQ---------EPSREAVLKALEYARAAGVRVVLDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 187 APAPKGWDISND---WLSSI----DILIPNESElaslcgFDDVGGdvTGEGEEAmARSLLERGVrQAVIVTLGARGAmIV 259
Cdd:TIGR04382 166 DYRPYLWKSPEEagiYLRLVlplvDVIIGTREE------FDIAGG--EGDDEAA-ARALLDAGV-EILVVKRGPEGS-LV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223992801 260 RrssGRTESSPSTLPCKsLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRG 323
Cdd:TIGR04382 235 Y---TGDGEGVEVPGFP-VEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHS 294
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
40-325 |
1.66e-11 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 64.15 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 40 AGGKGANQAVAAASIGIvsrtsSVHMIGRVGDDDmGRSLLRGLclrkvciyEKESVVSDTHT--GVASITVDT--TSGQN 115
Cdd:TIGR03828 34 AGGKGINVSRVLKNLGV-----DVVALGFLGGFT-GDFIEALL--------REEGIKTDFVRvpGETRINVKIkePSGTE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 116 TIVVSPGANLSlrPEEVASTLTRILSstnndntQLSRGKDVVL---VQLEITPETAHEALKTSSRLGAITILnpapapkg 192
Cdd:TIGR03828 100 TKLNGPGPEIS--EEELEALLEKLRA-------QLAEGDWLVLsgsLPPGVPPDFYAELIALAREKGAKVIL-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 193 wDISNDWLSSI-----DILIPNESELASLcgfddVGGDVTGEGE-EAMARSLLERGVrQAVIVTLGARGAMIVRRSSGRT 266
Cdd:TIGR03828 163 -DTSGEALRDGlkakpFLIKPNDEELEEL-----FGRELKTLEEiIEAARELLDLGA-ENVLISLGADGALLVTKEGALF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 223992801 267 ESSPSTlpckslPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGAQ 325
Cdd:TIGR03828 236 AQPPKG------EVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTG 288
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
162-324 |
1.96e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 64.47 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 162 EITPETAHEALKTSSRLGAITILNPAPAPK----GWDISNDWLSSI----DILIPNESELASLCGFddvgGDVTGEGEEa 233
Cdd:PLN02341 237 ELSPSAIASAVDYAIDVGTAVFFDPGPRGKsllvGTPDERRALEHLlrmsDVLLLTSEEAEALTGI----RNPILAGQE- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 234 marsLLERGVR-QAVIVTLGARGAMIVrrssgrTESSPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASMAC 312
Cdd:PLN02341 312 ----LLRPGIRtKWVVVKMGSKGSILV------TRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLAN 381
|
170
....*....|..
gi 223992801 313 GVASMSVRKRGA 324
Cdd:PLN02341 382 AVGAATAMGCGA 393
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
29-325 |
3.65e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 63.67 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 29 QTLLGTDFVTSAGGKGANQAVAAASIGIVSRTSS---VHMIGRVGDDDMGrSLLRGLcLRKVCIYEKESVVSDTHTGVAs 105
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQSAAGPalnVAMAGSVGSDPLG-DFYRTK-LRRANVHFLSQPVKDGTTGTV- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 106 ITVDTTSGQNTIVVSPGANLSLRPEEVastLTRILSSTNndntqlsrgkdVVLV-----QLEITPETAHEALKTSSRLGA 180
Cdd:PLN02813 191 IVLTTPDAQRTMLSYQGTSSTVNYDSC---LASAISKSR-----------VLVVegylwELPQTIEAIAQACEEAHRAGA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 181 ITILNPAPA-------PKGWDISNdwlSSIDILIPNESELASLCGFDDVggdvtgEGEEAMARSLLErgVRQAVIVTLGA 253
Cdd:PLN02813 257 LVAVTASDVscierhrDDFWDVMG---NYADILFANSDEARALCGLGSE------ESPESATRYLSH--FCPLVSVTDGA 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223992801 254 RGAMIVRRssGRTESSPSTlPCKSlpvVDAVGAGDAFCGALAAYLSRGV-DLERAASMACGVASMSVRKRGAQ 325
Cdd:PLN02813 326 RGSYIGVK--GEAVYIPPS-PCVP---VDTCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQGTR 392
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
40-324 |
9.73e-11 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 61.49 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 40 AGGKGANQAVAAASIGIVSRtssvhMIGRVGDDDMGRSLLRGLCLRKVCIyekESVVSDTHTGVASITVD-TTSGQN--T 116
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESG-----FIGRVGDDPFGRFMQQTLQDEGVDT---TYLRLDPAHRTSTVVVDlDDQGERsfT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 117 IVVSPGANLSLRPEEVAstltrilsstnndntQLSRGK-----DVVLVQlEITPETAHEALKTSSRLGAITILNPAPAPK 191
Cdd:PRK09434 99 FMVRPSADLFLQPQDLP---------------PFRQGEwlhlcSIALSA-EPSRSTTFEAMRRIKAAGGFVSFDPNLRED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 192 GW-------DISNDWLSSIDILIPNESELASLCGFDDVGgdvtgEGEEAMARSLLERgvrqAVIVTLGARGAMIvrrssg 264
Cdd:PRK09434 163 LWqdeaelrECLRQALALADVVKLSEEELCFLSGTSQLE-----DAIYALADRYPIA----LLLVTLGAEGVLV------ 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223992801 265 RTESSPSTLPCKSLPVVDAVGAGDAFCGALAAYLSRGVDLERAASM--------ACGvaSMSVRKRGA 324
Cdd:PRK09434 228 HTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTDEAELaeiiaqaqACG--ALATTAKGA 293
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-298 |
1.63e-10 |
|
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: 59.42 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 6 KVVVVGSINQDLTTYTPSLPSPGQTLLGTDFVTSAGGKGANQAVAAASIGIvsrtsSVHMIGrvgdddmgrslLRGLCLr 85
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGV-----SVTLVG-----------ADAVVI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 86 kvciyekesvvsdthtgvasitvdttsgqntivvspgANLSLRPEEVAstltrilsstnndntqlsrgkdvvlvqleitp 165
Cdd:cd00287 64 -------------------------------------SGLSPAPEAVL-------------------------------- 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 166 etahEALKTSSRLGAITILNPAPAPKGWDISNDW--LSSIDILIPNESELASLCGFDDVggdvTGEGEEAMARSLLERGV 243
Cdd:cd00287 75 ----DALEEARRRGVPVVLDPGPRAVRLDGEELEklLPGVDILTPNEEEAEALTGRRDL----EVKEAAEAAALLLSKGP 146
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 223992801 244 rQAVIVTLGARGAMIVrrSSGRTEsspstLPCKSLP--VVDAVGAGDAFCGALAAYL 298
Cdd:cd00287 147 -KVVIVTLGEKGAIVA--TRGGTE-----VHVPAFPvkVVDTTGAGDAFLAALAAGL 195
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
170-323 |
2.33e-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: 57.74 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 170 EALKTSSRLGAITILNPAP---APKGWDISNDWLSSIDILIPNESELASLCGFDDvggdvtgEGEEAMARSLLERGVRQA 246
Cdd:cd01943 145 KLLKGNSPTRPKIVWEPLPdscDPENLEDLLQALPRVDVFSPNLEEAARLLGLPT-------SEPSSDEEKEAVLQALLF 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 247 VIVTLGARGAMIVRrsSGRTES---SPSTLPCKSLP--------VVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVA 315
Cdd:cd01943 218 SGILQDPGGGVVLR--CGKLGCyvgSADSGPELWLPayhtkstkVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAA 295
|
....*...
gi 223992801 316 SMSVRKRG 323
Cdd:cd01943 296 SFAIEQVG 303
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
41-303 |
1.71e-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: 54.67 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 41 GGKGANQAVAAASIGIVSRtssvhMIGRVGDDDMGRSLLRGLCLRKVCIyeKESVVSDTHTGVAsiTVDTTSGQNTIVVS 120
Cdd:cd01940 22 GGNALNVAVYAKRLGHESA-----YIGAVGNDDAGAHVRSTLKRLGVDI--SHCRVKEGENAVA--DVELVDGDRIFGLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 121 -PGANLSLRPEEvastltrilsstnNDNTQLSrGKDVVLVQLEITPETAHEALKTssrlgaitiLNPAPAPKGWDISNDW 199
Cdd:cd01940 93 nKGGVAREHPFE-------------ADLEYLS-QFDLVHTGIYSHEGHLEKALQA---------LVGAGALISFDFSDRW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 200 LssidilipnESELASLCGFDDVG----GDVTGEGEEAMARSLLERGVRqAVIVTLGARGAMIvrrSSGRTESSPSTLPC 275
Cdd:cd01940 150 D---------DDYLQLVCPYVDFAffsaSDLSDEEVKAKLKEAVSRGAK-LVIVTRGEDGAIA---YDGAVFYSVAPRPV 216
|
250 260
....*....|....*....|....*...
gi 223992801 276 KslpVVDAVGAGDAFCGALAAYLSRGVD 303
Cdd:cd01940 217 E---VVDTLGAGDSFIAGFLLSLLAGGT 241
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
8-318 |
3.94e-08 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 54.17 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 8 VVVGSINQDL-----TTYTPSLPSPGQTLlgtdfvTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRgl 82
Cdd:PRK09954 61 VVVGAINMDIrgmadIRYPQAASHPGTIH------CSAGGVGRNIAHNLALLG-----RDVHLLSAIGDDFYGETLLE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 83 clrkvciyekesvvsdtHTGVASITVDTT---SGQNTIVVSPGAN------LSLRPEEVASTLTRILSSTNNDntqLSRG 153
Cdd:PRK09954 128 -----------------ETRRAGVNVSGCirlHGQSTSTYLAIANrqdetvLAINDTHILQQLTPQLLNGSRD---LIRH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 154 KDVVLVQLEITPETAHEALKTSSRLGaiTILNPAPAPKGWDISNdWLSSIDILIPNESELASLCGfddvgGDVTGEGEEA 233
Cdd:PRK09954 188 AGVVLADCNLTAEALEWVFTLADEIP--VFVDTVSEFKAGKIKH-WLAHIHTLKPTQPELEILWG-----QAITSDADRN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 234 MA-RSLLERGVRQaVIVTLGARGAMIVRRSSgrtESSPSTLPCKSlpVVDAVGAGDAFCGALAAYLSRGVDLERAASMAC 312
Cdd:PRK09954 260 AAvNALHQQGVQQ-IFVYLPDESVFCSEKDG---EQFLLTAPAHT--TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAM 333
|
....*.
gi 223992801 313 GVASMS 318
Cdd:PRK09954 334 ACAAIS 339
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
204-311 |
1.07e-07 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 52.07 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESELASLCGFDDVGGDVTgegeEAMARSLLERGVRQaVIVTlgarGAMIVRRSSGRTE------SSPSTLPCKS 277
Cdd:COG2240 140 DIITPNLTELALLTGRPYETLEEA----LAAARALLALGPKI-VVVT----SVPLDDTPADKIGnlavtaDGAWLVETPL 210
|
90 100 110
....*....|....*....|....*....|....
gi 223992801 278 LPVvDAVGAGDAFCGALAAYLSRGVDLERAASMA 311
Cdd:COG2240 211 LPF-SPNGTGDLFAALLLAHLLRGKSLEEALERA 243
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
110-318 |
1.35e-06 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 49.01 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 110 TTSGQNTIVVSPGANLSlrPEEVASTLTRILsstnndntQLSRGKDVVL---VQLEITPETAHEALKTSSRLGAITILnp 186
Cdd:PRK10294 98 EASGEQYRFVMPGAALN--EDEFRQLEEQVL--------EIESGAILVIsgsLPPGVKLEKLTQLISAAQKQGIRCII-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 187 apapkgwDISNDWLSS------IDILIPNESELASLcgfddVGGDVTGEGE-EAMARSLLERGVRQAVIVTLGARGAMIV 259
Cdd:PRK10294 166 -------DSSGDALSAalaignIELVKPNQKELSAL-----VNRDLTQPDDvRKAAQELVNSGKAKRVVVSLGPQGALGV 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 223992801 260 RRSSGRTESSPstlPCKSLpvvDAVGAGDAFCGALAAYLSRGVDLERAASMacGVASMS 318
Cdd:PRK10294 234 DSENCIQVVPP---PVKSQ---STVGAGDSMVGAMTLKLAENASLEEMVRF--GVAAGS 284
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
204-324 |
1.52e-06 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 49.44 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESElaslcgFDDVGGDVTGEGE-EAMARSLLERGVRQAVIVTLGARGAMIVRRssgrtESSPSTLPCKSLPVVD 282
Cdd:PRK11316 190 TLLTPNLSE------FEAVVGKCKDEAElVEKGMKLIADYDLSALLVTRSEQGMTLLQP-----GKAPLHLPTQAREVYD 258
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 223992801 283 AVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGA 324
Cdd:PRK11316 259 VTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT 300
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
183-323 |
1.85e-06 |
|
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: 48.62 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 183 ILNPAPAPK--GWDISNDWLSS-----------IDILIPNESELASLCGFDDVggdvtgegeEAMARSLLERGVRqAVIV 249
Cdd:cd01946 131 VLEQVKDPKlvVMDTMNFWISIkpeklkkvlakVDVVIINDGEARQLTGAANL---------VKAARLILAMGPK-ALII 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 250 TLGARGAMIVrrssgrTESSPSTLPCKSLP-VVDAVGAGDAFCGALAAYLSRGVD-----LERAASMACGVASMSVRKRG 323
Cdd:cd01946 201 KRGEYGALLF------TDDGYFAAPAYPLEsVFDPTGAGDTFAGGFIGYLASQKDtseanMRRAIIYGSAMASFCVEDFG 274
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
203-324 |
5.01e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 47.71 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 203 IDILIPNESELASLCgfDDVGGDVTGEGEEAMARSLLER--GVRQAVIV-TLGARGAMIVRRSSGRTESSPSTLPCKslp 279
Cdd:PTZ00247 215 VDILFGNEEEAKTFA--KAMKWDTEDLKEIAARIAMLPKysGTRPRLVVfTQGPEPTLIATKDGVTSVPVPPLDQEK--- 289
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 223992801 280 VVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGA 324
Cdd:PTZ00247 290 IVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGC 334
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
247-316 |
1.16e-05 |
|
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: 45.86 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 247 VIVTLGARGAMIVRRSSGRTESSPSTlpckslPVVDAVGAGDAFCGALAAYLSRGVDLERAASMACGVAS 316
Cdd:cd01937 187 IIVTDGEEGGYIFDGNGKYTIPASKK------DVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAA 250
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
200-314 |
1.56e-05 |
|
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: 45.65 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 200 LSSIDILIPNESELASLCGFDDVggdvTGEGEEAMARSLLERGVRQAVI--VTLG--ARGAMIVrrsSGRTESSPSTLPC 275
Cdd:cd01173 134 VPLADIITPNQFELELLTGKKIN----DLEDAKAAARALHAKGPKTVVVtsVELAddDRIEMLG---STATEAWLVQRPK 206
|
90 100 110
....*....|....*....|....*....|....*....
gi 223992801 276 KSLPVvDAVGAGDAFCGALAAYLSRGVDLERAASMACGV 314
Cdd:cd01173 207 IPFPA-YFNGTGDLFAALLLARLLKGKSLAEALEKALNF 244
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
204-307 |
3.04e-05 |
|
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: 44.82 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESELASLCGFddvggDVTGEGEE-AMARSLLERGVRQAVIVTLGARGA-------MIVRRSSGRTESSPSTLPC 275
Cdd:TIGR00687 140 DIITPNQFELELLTGR-----RINTEEEAlAAADALIAMGPDIVLVTHLIRAGSqrdrsfeGLVATQEGRWHISRPLAVF 214
|
90 100 110
....*....|....*....|....*....|..
gi 223992801 276 KSLPvvdaVGAGDAFCGALAAYLSRGVDLERA 307
Cdd:TIGR00687 215 DPPP----VGTGDLIAALLLATLLHGNSLKEA 242
|
|
| PLN02967 |
PLN02967 |
kinase |
36-218 |
1.19e-04 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 43.88 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 36 FVTSAGGKGANQAVAAASIGivsrtSSVHMIGRVGDDDMGRSLLRGLclrKVCIYEKESVVSDTH--TGVASITVDTTSG 113
Cdd:PLN02967 238 FVRAPGGSAGGVAIALASLG-----GKVAFMGKLGDDDYGQAMLYYL---NVNKVQTRSVCIDGKraTAVSTMKIAKRGR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 114 QNTIVVSPGANLSLRPEEVASTLTR------ILSSTNNDNTQLSrgkdvvlvqleitpeTAHEALKTSSRLGAITI--LN 185
Cdd:PLN02967 310 LKTTCVKPCAEDSLSKSEINIDVLKeakmfyFNTHSLLDPTMRS---------------TTLRAIKISKKLGGVIFydLN 374
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 223992801 186 -PAPApkgWDISNDWLSSI-------DILIPNESELASLCG 218
Cdd:PLN02967 375 lPLPL---WSSSEETKSFIqeawnlaDIIEVTKQELEFLCG 412
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
230-323 |
3.90e-04 |
|
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: 41.62 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 230 GEEAMARSLLERGVRQAVIVTLGARGAMIvRRSSGRTESSPSTLPCKslpVVDAVGAGDAFCGALAAYLS-RGVDLERAA 308
Cdd:cd01939 198 PEECLRGEGPRAKKAALLVCTWGDQGAGA-LGPDGEYVHSPAHKPIR---VVDTLGAGDTFNAAVIYALNkGPDDLSEAL 273
|
90
....*....|....*
gi 223992801 309 SMACGVASMSVRKRG 323
Cdd:cd01939 274 DFGNRVASQKCTGVG 288
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
204-311 |
4.05e-04 |
|
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: 41.31 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESELASLCGFDDVggdvTGEGEEAMARSLLERGVrQAVIVTLG-ARGAMIVRRSSGRTESSPSTLPCKSLPVVD 282
Cdd:pfam08543 121 TLITPNLPEAEALTGRKIK----TLEDMKEAAKKLLALGA-KAVLIKGGhLEGEEAVVTDVLYDGGGFYTLEAPRIPTKN 195
|
90 100
....*....|....*....|....*....
gi 223992801 283 AVGAGDAFCGALAAYLSRGVDLERAASMA 311
Cdd:pfam08543 196 THGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
204-311 |
6.36e-04 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 41.01 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESELASLCGF--DDVGGDVtgegeeAMARSLLERGVRqAVIVT----------------LGARGAMIVRRssgr 265
Cdd:PRK05756 140 DIITPNLFELEWLSGRpvETLEDAV------AAARALIARGPK-IVLVTslaragypadrfemllVTADGAWHISR---- 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 223992801 266 tesspstlpckslPVVD----AVGAGDAFCGALAAYLSRGVDLERAASMA 311
Cdd:PRK05756 209 -------------PLVDfmrqPVGVGDLTSALFLARLLQGGSLEEALEHT 245
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
203-325 |
2.61e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.39 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 203 IDILIPNESELASLcgfddVGGDVTGEGEEAMArsLLERGVRQAViVTLGARGAMIvrRSSGRTESSPSTLPCKslpVVD 282
Cdd:PLN02379 233 IDLCFANEDEAREL-----LRGEQESDPEAALE--FLAKYCNWAV-VTLGSKGCIA--RHGKEVVRVPAIGETN---AVD 299
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 223992801 283 AVGAGDAFCGALAAYLSRGVDLERAASMACGVASMSVRKRGAQ 325
Cdd:PLN02379 300 ATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGE 342
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
231-323 |
7.11e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 37.86 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 231 EEAMARSLLErgVRQ--AVIVTLGARGAMIVRRSSgrtESSPSTLPCKSlpvVDAVGAGDAFCGALAAYLSRGVDLERAA 308
Cdd:PLN02630 190 EEALFIDVEE--VRQkcCVIVTNGKKGCRIYWKDG---EMRVPPFPAIQ---VDPTGAGDSFLGGFVAGLVQGLAVPDAA 261
|
90
....*....|....*
gi 223992801 309 SMACGVASMSVRKRG 323
Cdd:PLN02630 262 LLGNYFGSLAVEQVG 276
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
204-311 |
8.30e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 37.41 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223992801 204 DILIPNESELASLCGFDDVGGDvtgEGEEAMARSLLERGVrQAVIVTLGargamiVRRSSGR------TESSPSTLPCKS 277
Cdd:PRK06427 135 TLITPNLPEAEALTGLPIADTE---DEMKAAARALHALGC-KAVLIKGG------HLLDGEEsvdwlfDGEGEERFSAPR 204
|
90 100 110
....*....|....*....|....*....|....
gi 223992801 278 LPVVDAVGAGDAFCGALAAYLSRGVDLERAASMA 311
Cdd:PRK06427 205 IPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238
|
|
| |
