|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-303 |
4.06e-93 |
|
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: 278.31 E-value: 4.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 9 IAFFGECMVEISGSP---------LTKKFGGDTLNTALYLSRLTqhqnLSVHYATGLGSDELSQNMIDSWQLEGIQTNFV 79
Cdd:cd01166 2 VVTIGEVMVDLSPPGggrleqadsFRKFFGGAEANVAVGLARLG----HRVALVTAVGDDPFGRFILAELRREGVDTSHV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 80 ERIPNKLPGLYMVETDETGERHFHYWRNDAAVkSYFQTDDLNKLEIAltekQVDAVYISGISIAILDDTsRERLLKAIGV 159
Cdd:cd01166 78 RVDPGRPTGLYFLEIGAGGERRVLYYRAGSAA-SRLTPEDLDEAALA----GADHLHLSGITLALSESA-REALLEALEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 160 FSNQGGKLIFDNNYRPQLWTTEQAQHWYAKLLPLVDIALITEDDDLLVWGNGESVQQ----RCLRLGCQEIVIKRGCEPC 235
Cdd:cd01166 152 AKARGVTVSFDLNYRPKLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAaeraLALALGVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515637963 236 KIVQVEQgdvvESYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAI 303
Cdd:cd01166 232 LVYTGGG----RVFVPAYPV-EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-312 |
2.65e-62 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 199.73 E-value: 2.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 8 NIAFFGECMVEIS--------------GSPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEG 73
Cdd:COG0524 1 DVLVIGEALVDLVarvdrlpkggetvlAGSFRRSPGGAAANVAVALARL----GARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 74 IQTNFVERIPNKLPGLYMVETDETGERHFHYWRNDAAvksYFQTDDLNKLEIAltekQVDAVYISGISIAilDDTSRERL 153
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANA---ELTPEDLDEALLA----GADILHLGGITLA--SEPPREAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 154 LKAIGVFSNQGGKLIFDNNYRPQLWttEQAQHWYAKLLPLVDIALITEDDDLLVWGNG--ESVQQRCLRLGCQEIVIKRG 231
Cdd:COG0524 148 LAALEAARAAGVPVSLDPNYRPALW--EPARELLRELLALVDILFPNEEEAELLTGETdpEEAAAALLARGVKLVVVTLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 232 CEPCKIVqvEQGDVVEsyVSATRVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAIIPMSAMSQ 311
Cdd:COG0524 226 AEGALLY--TGGEVVH--VPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREE 300
|
.
gi 515637963 312 L 312
Cdd:COG0524 301 V 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
8-304 |
8.64e-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: 159.43 E-value: 8.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 8 NIAFFGECMVEISG------------SPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEGIQ 75
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvrvSTVEKGPGGKGANVAVALARL----GGDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 76 TNFVERIPNKLPGLYMVETDETGERHFHYWRNDAAVKsYFQTDDLNKLEIAltekQVDAVYISGIsiaiLDDTSRERLLK 155
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADL-TPEELEENEDLLE----NADLLYISGS----LPLGLPEATLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 156 AIGVFSNQGGKliFDNNYRPQLWTTEQAqhwYAKLLPLVDIALITEDDDLLVWG-NGESVQ------QRCLRLGCQEIVI 228
Cdd:pfam00294 148 ELIEAAKNGGT--FDPNLLDPLGAAREA---LLELLPLADLLKPNEEELEALTGaKLDDIEealaalHKLLAKGIKTVIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515637963 229 KRGCEPCKIVQVEQgdvvESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAII 304
Cdd:pfam00294 223 TLGADGALVVEGDG----EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
8-303 |
4.50e-35 |
|
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: 128.91 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 8 NIAFFGECMVEI------SGSPLTKKFGGDTLNTALYLSRLTQHqnlsVHYATGLGSDELSQNMIDSWQLEGIQTNFVER 81
Cdd:cd01167 1 KVVCFGEALIDFipegsgAPETFTKAPGGAPANVAVALARLGGK----AAFIGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 82 IPNKLPGLYMVETDETGERHFHYWRNDAAvkSYFQTDDLNKLEIalteKQVDAVYISgiSIAILDDTSRERLLKAIGVFS 161
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAA--DLLLDTELNPDLL----SEADILHFG--SIALASEPSRSALLELLEAAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 162 NQGGKLIFDNNYRPQLWTT-EQAQHWYAKLLPLVDIALITEDDdlLVW----GNGESVQQRCLRLGCQEIVIKRGCEPCk 236
Cdd:cd01167 149 KAGVLISFDPNLRPPLWRDeEEARERIAELLELADIVKLSDEE--LELlfgeEDPEEIAALLLLFGLKLVLVTRGADGA- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515637963 237 IVQVEQGdvvESYVSATRVsNVVDTCAAGDSFAAGYLAA-------RLTGESATDAAEFGHQLASIVIQYSGAI 303
Cdd:cd01167 226 LLYTKGG---VGEVPGIPV-EVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
29-305 |
1.09e-19 |
|
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: 87.28 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 29 GGDTLNTALYLSRLTQhqnlSVHYATGLGSDELSQNMIDSWQLEGIQTNFVerIPNKLP-GLYMVETDETGERHFHywRN 107
Cdd:cd01168 55 GGSAANTIRGAAALGG----SAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQ--VQPDGPtGTCAVLVTPDAERTMC--TY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 108 DAAvKSYFQTDDLNKLEIalteKQVDAVYISGIsiaiLDDTSRERLLKAIGVFSNQGGKLIFD-------NNYRPQLWtt 180
Cdd:cd01168 127 LGA-ANELSPDDLDWSLL----AKAKYLYLEGY----LLTVPPEAILLAAEHAKENGVKIALNlsapfivQRFKEALL-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 181 eqaqhwyaKLLPLVDIALITEDD--DLLVWGNGESVQQ--RCLRLGCQEIVIKRGCEPCKIVQVEQgdvvESYVSATRVS 256
Cdd:cd01168 196 --------ELLPYVDILFGNEEEaeALAEAETTDDLEAalKLLALRCRIVVITQGAKGAVVVEGGE----VYPVPAIPVE 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 515637963 257 NVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAIIP 305
Cdd:cd01168 264 KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-303 |
3.81e-19 |
|
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: 85.44 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 24 LTKKFGGDTLNTALYLSRLTQHqnlSVHYATgLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETDETGER-HF 102
Cdd:cd01942 31 LRREFGGSAGNTAVALAKLGLS---PGLVAA-VGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQiAY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 103 HYWrnDAAvksyfqtDDLNKLEIALTEKQVDAVYISGISIAILDDtsRErllkaigvFSNQGGKLIFDNNYRPQLWTTEQ 182
Cdd:cd01942 107 FYP--GAM-------DELEPNDEADPDGLADIVHLSSGPGLIELA--RE--------LAAGGITVSFDPGQELPRLSGEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 183 AQHWyaklLPLVDIALITEDD-DLLVWGNGESVQQrcLRLGCQEIVIKRGCEPCKIVqvEQGDVVEsyVSATRVSNVVDT 261
Cdd:cd01942 168 LEEI----LERADILFVNDYEaELLKERTGLSEAE--LASGVRVVVVTLGPKGAIVF--EDGEEVE--VPAVPAVKVVDT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 515637963 262 CAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAI 303
Cdd:cd01942 238 TGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
29-302 |
1.44e-17 |
|
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: 80.86 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 29 GGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEGIQTNFVeRIPNKLPGLYMVETDEtGERHFHYWRND 108
Cdd:cd01940 22 GGNALNVAVYAKRL----GHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGLSNKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 109 AAVKSYFQTDDLNKLeialteKQVDAVYISGISiailDDTSRERLLKAIGVfsnQGGKLIFDNNYRpqlWTTEQAQhwya 188
Cdd:cd01940 96 GVAREHPFEADLEYL------SQFDLVHTGIYS----HEGHLEKALQALVG---AGALISFDFSDR---WDDDYLQ---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 189 KLLPLVDIALIT--EDDDLLVwgngESVQQRCLRLGCQEIVIKRGCEPckiVQVEQGDVVesYVSATRVSNVVDTCAAGD 266
Cdd:cd01940 156 LVCPYVDFAFFSasDLSDEEV----KAKLKEAVSRGAKLVIVTRGEDG---AIAYDGAVF--YSVAPRPVEVVDTLGAGD 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 515637963 267 SFAAGYLAARL-TGESATDAAEFGHQLASIVIQYSGA 302
Cdd:cd01940 227 SFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
19-305 |
1.27e-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: 75.66 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 19 ISGSPLTKKFGGDTLNTALYLSRLTQHqnlsVHYATGLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETDETG 98
Cdd:cd01174 26 VLGSSFETGPGGKGANQAVAAARLGAR----VAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 99 ErhfhywrndaavksyfqtddlNKLEI------ALTEKQVDAV--YISGISIAIL-----DDTSRERLLKAigvfsNQGG 165
Cdd:cd01174 102 E---------------------NRIVVvpgangELTPADVDAAleLIAAADVLLLqleipLETVLAALRAA-----RRAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 166 KL-IFdnNYRPqlwtteqAQHWYAKLLPLVDI--------ALITEDDDLLVwGNGESVQQRCLRLGCQEIVIKRGcepck 236
Cdd:cd01174 156 VTvIL--NPAP-------ARPLPAELLALVDIlvpneteaALLTGIEVTDE-EDAEKAARLLLAKGVKNVIVTLG----- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515637963 237 ivqvEQGDVV-----ESYVSATRVsNVVDTCAAGDSFaAGYLAARLT-GESATDAAEFGHQLASIVIQYSGAI--IP 305
Cdd:cd01174 221 ----AKGALLasggeVEHVPAFKV-KAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAAAALSVTRPGAQpsIP 291
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
19-302 |
2.03e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 66.68 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 19 ISGSPLTKKFGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETD-ET 97
Cdd:PTZ00292 42 LHGTSFHKGFGGKGANQAVMASKL----GAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDtKT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 98 GerhfhywrNDAAVKSYFQTDdlnkleiALTEKQVDAV---YISGISIAIL-DDTSRERLLKAIGVFSNQGGKLIFDNNY 173
Cdd:PTZ00292 118 G--------NNEIVIIPGANN-------ALTPQMVDAQtdnIQNICKYLICqNEIPLETTLDALKEAKERGCYTVFNPAP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 174 RPQLWTTEQAqhwyAKLLPLVDIALITEDDDLLVWG----NGESVQQ---RCLRLGCQEIVIKRGCEPCKIVQVEQGDVv 246
Cdd:PTZ00292 183 APKLAEVEII----KPFLKYVSLFCVNEVEAALITGmevtDTESAFKaskELQQLGVENVIITLGANGCLIVEKENEPV- 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 515637963 247 esYVSATRVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGA 302
Cdd:PTZ00292 258 --HVPGKRV-KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGT 310
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
189-305 |
5.22e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 65.82 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 189 KLLPLVDIALITEDD-----DLLVWGNgESVQQRCLRLGCQE---------IVIKRGCEPCKIVQveqGDVVESY-VSAT 253
Cdd:PTZ00247 210 QVLPYVDILFGNEEEaktfaKAMKWDT-EDLKEIAARIAMLPkysgtrprlVVFTQGPEPTLIAT---KDGVTSVpVPPL 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 515637963 254 RVSNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAIIP 305
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
56-298 |
8.41e-11 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 61.88 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 56 LGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETDETGERHFHYWRNDAAvKSYFQTDDLNKLeialteKQVDAV 135
Cdd:PRK09434 51 VGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSA-DLFLQPQDLPPF------RQGEWL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 136 YISgiSIAILDDTSRERLLKAIGVFSNQGGKLIFDNNYRPQLW-TTEQAQHWYAKLLPLVDIALITEDDDLLVWG---NG 211
Cdd:PRK09434 124 HLC--SIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWqDEAELRECLRQALALADVVKLSEEELCFLSGtsqLE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 212 ESVQQRCLRLGCQEIVIKRGCEpcKIVQVEQGDVveSYVSATRVsNVVDTCAAGDSFAAGYLAarltGESATDAAEFGHQ 291
Cdd:PRK09434 202 DAIYALADRYPIALLLVTLGAE--GVLVHTRGQV--QHFPAPSV-DPVDTTGAGDAFVAGLLA----GLSQAGLWTDEAE 272
|
....*..
gi 515637963 292 LASIVIQ 298
Cdd:PRK09434 273 LAEIIAQ 279
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
56-302 |
1.21e-10 |
|
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: 61.08 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 56 LGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETDETGErhfhywrN----DAAVKSYFQTDDLNKLEIALTEKQ 131
Cdd:TIGR02152 54 VGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGE-------NrivvVAGANAELTPEDIDAAEALIAESD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 132 VdavyisgisIAILDDTSRERLLKAIGVFSNQGGKLIFdnNYRPQLWTTEQAqhwyakLLPLVDI--------ALITEDD 203
Cdd:TIGR02152 127 I---------VLLQLEIPLETVLEAAKIAKKHGVKVIL--NPAPAIKDLDDE------LLSLVDIitpneteaEILTGIE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 204 dllvWGNGESVQ---QRCLRLGCQEIVIKRGCEPCKIVqvEQGDVVesYVSATRVsNVVDTCAAGDSFAAGYLAARLTGE 280
Cdd:TIGR02152 190 ----VTDEEDAEkaaEKLLEKGVKNVIITLGSKGALLV--SKDESK--LIPAFKV-KAVDTTAAGDTFNGAFAVALAEGK 260
|
250 260
....*....|....*....|..
gi 515637963 281 SATDAAEFGHQLASIVIQYSGA 302
Cdd:TIGR02152 261 SLEDAIRFANAAAAISVTRKGA 282
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
24-302 |
4.50e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.28 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 24 LTKKF-GGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEGIQTNfveripnklpglymvetdetgerHF 102
Cdd:PRK09813 17 LGKAFsGGNAVNVAVYCTRY----GIQPGCITWVGDDDYGTKLKQDLARMGVDIS-----------------------HV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 103 HYWRNDAAVkSYFQTDDLNKL----------EIALTEKQVDavYISGISI---AILDDTsrERLLKAIgvfsNQGGKLI- 168
Cdd:PRK09813 70 HTKHGVTAQ-TQVELHDNDRVfgdytegvmaDFALSEEDYA--WLAQYDIvhaAIWGHA--EDAFPQL----HAAGKLTa 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 169 FDNNYRPQ--LWTTeqaqhwyakLLPLVDIALITEDDDllvwgngesvqQRCLRLGCQEIViKRGCEPCKIVQVEQG--- 243
Cdd:PRK09813 141 FDFSDKWDspLWQT---------LVPHLDYAFASAPQE-----------DEFLRLKMKAIV-ARGAGVVIVTLGENGsia 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 244 -DVVESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGA 302
Cdd:PRK09813 200 wDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
16-273 |
5.43e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 56.76 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 16 MVEISGSPLTKKF---GGDTlNTALYLSRLTQHQNLSVHyatgLGSDELSQNMIDSWQLEGIQTnfVERIPNKLPG---- 88
Cdd:PLN02341 104 MEELAASPPDKKSweaGGNC-NFAIAAARLGLRCSTIGH----VGDEIYGKFLLDVLAEEGISV--VGLIEGTDAGdsss 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 89 ------LYMVETDETGeRHFHYWRNDAAVKSYFqtDDLNKL--EIALTEKQVDAVYISGIsiaILDDTSRERLLKAIGVF 160
Cdd:PLN02341 177 asyetlLCWVLVDPLQ-RHGFCSRADFGPEPAF--SWISKLsaEAKMAIRQSKALFCNGY---VFDELSPSAIASAVDYA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 161 SNQGGKLIFDNNYRPQ--LWTTEQAQHWYAKLLPLVDIALITEDDDLLVWGNGESVQ--QRCLRLGC--QEIVIKRGCEP 234
Cdd:PLN02341 251 IDVGTAVFFDPGPRGKslLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILagQELLRPGIrtKWVVVKMGSKG 330
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 515637963 235 CkiVQVEQGDVveSYVSATRVsNVVDTCAAGDSFAA----GYL 273
Cdd:PLN02341 331 S--ILVTRSSV--SCAPAFKV-NVVDTVGCGDSFAAaialGYI 368
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
30-301 |
8.71e-09 |
|
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: 55.51 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 30 GDTLNTALYLSRLTQHQNLSVHYATGLGSDELSQNMIDswqlegiqtnfvERIPNKLPGLY---------MVETDetGER 100
Cdd:cd01944 36 GGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRD------------EGIEILLPPRGgddggclvaLVEPD--GER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 101 HFHYWrndAAVKSYFQTDDLNKLEIALTekqvDAVYISGISIAilDDTSRERLLKAIGVFSNQGGKLIFDnnYRPQLwtT 180
Cdd:cd01944 102 SFISI---SGAEQDWSTEWFATLTVAPY----DYVYLSGYTLA--SENASKVILLEWLEALPAGTTLVFD--PGPRI--S 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 181 EQAQHWYAKLLPLVDIALITEDDDLLVWGNGES-VQQRCLRLGCQE---IVIKRGCEPCKIVQVEQGDvveSYVSATRVS 256
Cdd:cd01944 169 DIPDTILQALMAKRPIWSCNREEAAIFAERGDPaAEASALRIYAKTaapVVVRLGSNGAWIRLPDGNT---HIIPGFKVK 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515637963 257 nVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSG 301
Cdd:cd01944 246 -AVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
132-277 |
5.74e-08 |
|
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: 52.10 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 132 VDAVYISGISIAilddtsRERLLKAIGVFSNQGGKLIFDNNYRPQLWTTEQaqhwYAKLLPLVDI--------ALITEDD 203
Cdd:cd00287 58 ADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE----LEKLLPGVDIltpneeeaEALTGRR 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515637963 204 DLLVWGNGESVQQRcLRLGCQEIVIKRGcepckivqvEQGDVV----ESYVSA-TRVSNVVDTCAAGDSFAAGYLAARL 277
Cdd:cd00287 128 DLEVKEAAEAAALL-LSKGPKVVIVTLG---------EKGAIVatrgGTEVHVpAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
226-305 |
9.07e-08 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 52.79 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 226 IVIKRGCEPckIVQVEQGDVVESYVSATRVSNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAIIP 305
Cdd:PLN02548 249 VVITQGADP--TVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYP 326
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
28-302 |
1.72e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 48.71 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 28 FGGDTLNTALYLSRLTQHqnlsVHYATGLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETDETGErhfhywrn 107
Cdd:PRK11142 38 FGGKGANQAVAAARLGAD----IAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGE-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 108 daavksyfqtddlNKLEI------ALTEKQVDAVY--ISGISIAILD-DTSRERLLKAIGVFSNQGGKLIFdnNYRPqlw 178
Cdd:PRK11142 106 -------------NSIGIhaganaALTPALVEAHRelIANADALLMQlETPLETVLAAAKIAKQHGTKVIL--NPAP--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 179 tteqAQHWYAKLLPLVDIalIT--EDDDLLVWG----NGESVQQRCLRL---GCQEIVIKRGCEPCKIVQVEQGDVVESY 249
Cdd:PRK11142 168 ----ARELPDELLALVDI--ITpnETEAEKLTGirveDDDDAAKAAQVLhqkGIETVLITLGSRGVWLSENGEGQRVPGF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515637963 250 vsatRVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGA 302
Cdd:PRK11142 242 ----RV-QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
17-273 |
7.94e-06 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 46.92 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 17 VEISGSPLTKKF-GGDTLNTALYLSRLTQhqnlSVHYATGLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGLYMVETD 95
Cdd:PLN02323 30 VSLAEAPAFKKApGGAPANVAVGISRLGG----SSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 96 ETGERHFHYWRNDAAvKSYFQTDDLNkleIALTEKQvdAVYISGiSIAILDDTSRERLLKAIGVFSNQGGKLIFDNNYRP 175
Cdd:PLN02323 106 SDGEREFMFYRNPSA-DMLLRESELD---LDLIRKA--KIFHYG-SISLITEPCRSAHLAAMKIAKEAGALLSYDPNLRL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 176 QLW-TTEQAQHWYAKLLPLVDIALITEDDDLLVWGNGESVQQRCLRL---GCQEIVIKRGCEPCKIVQVEQGDVVESYvs 251
Cdd:PLN02323 179 PLWpSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVKLwhpNLKLLLVTEGEEGCRYYTKDFKGRVEGF-- 256
|
250 260
....*....|....*....|..
gi 515637963 252 atRVsNVVDTCAAGDSFAAGYL 273
Cdd:PLN02323 257 --KV-KAVDTTGAGDAFVGGLL 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-303 |
1.91e-05 |
|
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: 45.49 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 29 GGDTLNTALYLSRLTQHqnlsVHYATGLGSDELsqnmidswqleGIQtnFVERIPNKLPGLYMVETDETGERHFHYWRND 108
Cdd:cd01947 36 GGGGANVAVQLAKLGND----VRFFSNLGRDEI-----------GIQ--SLEELESGGDKHTVAWRDKPTRKTLSFIDPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 109 ---AAVKSYFQTDDLNKLEIAlteKQVDAVYISGisiAILDDTSRE--RLLKAigVFSNQGGKLIFDNnyrpqlwtteqa 183
Cdd:cd01947 99 gerTITVPGERLEDDLKWPIL---DEGDGVFITA---AAVDKEAIRkcRETKL--VILQVTPRVRVDE------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 184 qhwYAKLLPLVDIaLITEDDDLlvwgNGESVQQRCLRLGCQEIVIKRGCEPCKIvqveqGDVVESYVSATRVSNVVDTCA 263
Cdd:cd01947 159 ---LNQALIPLDI-LIGSRLDP----GELVVAEKIAGPFPRYLIVTEGELGAIL-----YPGGRYNHVPAKKAKVPDSTG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 515637963 264 AGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGAI 303
Cdd:cd01947 226 AGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
28-302 |
2.96e-05 |
|
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: 44.98 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 28 FGGDTLNTALYLSRLtqhqNLSVHYATGLGSDELSQNMIDSWQLEGIQTNFVERIPNKLPGL-YMVETDETGERHFHYWR 106
Cdd:cd01945 35 GGGNAANAAVAVARL----GGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPIsSITDITGDRATISITAI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 107 NDAAVKSYFQTDDLNKLEIALTE-KQVDAVYI-------SGISIAILDDTSR----ERLLKAIGVfsnqggkLIFDNNYR 174
Cdd:cd01945 111 DTQAAPDSLPDAILGGADAVLVDgRQPEAALHlaqearaRGIPIPLDLDGGGlrvlEELLPLADH-------AICSENFL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 175 PQlWTteqaqhwyakllplvdialITEDDDLLVWgngesvqqrcLR-LGCQEIVIKRGCEPCKIVQvEQGDVVEsyVSAT 253
Cdd:cd01945 184 RP-NT-------------------GSADDEALEL----------LAsLGIPFVAVTLGEAGCLWLE-RDGELFH--VPAF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 515637963 254 RVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVIQYSGA 302
Cdd:cd01945 231 PV-EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG 278
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
259-302 |
3.19e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.10 E-value: 3.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 515637963 259 VDTCAAGDSFAAGYLAARLTGES-ATDAAEFGHQLASIVIQYSGA 302
Cdd:PLN02813 347 VDTCGAGDAYAAGILYGLLRGVSdLRGMGELAARVAATVVGQQGT 391
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
197-298 |
4.83e-04 |
|
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: 41.15 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637963 197 ALITEDDDLLVWgngesvQQRCLRLGCQEIVIKRGCEPCKIVQVEQGdVVESYVSATRVSNVVDTCAAGDSFAAGYLAAR 276
Cdd:cd01941 193 ALIENNEDENKA------AKILLLPGIKNVIVTLGAKGVLLSSREGG-VETKLFPAPQPETVVNVTGAGDAFVAGLVAGL 265
|
90 100
....*....|....*....|..
gi 515637963 277 LTGESATDAAEFGHQLASIVIQ 298
Cdd:cd01941 266 LEGMSLDDSLRFAQAAAALTLE 287
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
216-289 |
2.47e-03 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 38.96 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515637963 216 QRCLRLGCQEIVIKRGcepckivqvEQGDVV----ESY-VSATRVsNVVDTCAAGDSFAAGYLAARLTGESATDAAEFG 289
Cdd:COG1105 207 RELLERGAENVVVSLG---------ADGALLvtedGVYrAKPPKV-EVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
242-301 |
4.16e-03 |
|
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: 38.16 E-value: 4.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515637963 242 QGDVVESyvSATRVSNVVDTCAAGDSFAAGYLAARLTGESA-TDAAEFGHQLASIVIQYSG 301
Cdd:cd01939 230 DGEYVHS--PAHKPIRVVDTLGAGDTFNAAVIYALNKGPDDlSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
257-297 |
8.55e-03 |
|
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: 37.00 E-value: 8.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 515637963 257 NVVDTCAAGDSFAAGYLAARLTGESATDAAEFGHQLASIVI 297
Cdd:cd01937 213 DVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| |
