|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
12-342 |
9.36e-163 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 457.64 E-value: 9.36e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 12 LGNPLLDIVATVDSEFLDKYNLRPDNAILAKDEHMSLYKDLVEKYNPDYIAGGSAQNTLRVCQWILQKPKIAAFFGCVGK 91
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPGATSYMGCIGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 92 DDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLISNGHRSLCAHLAAANEFTVEHLQKPENRELWENARYFYITGFFLV 171
Cdd:PLN02548 81 DKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVEHLKKPENWALVEKAKFYYIAGFFLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 172 INPAAVMQVAQHAYDSKSTFMLNLSASFVMQQFKEPLMAVMPYVKVLFGNVEEAKSFARAYDWETKDLKEIGLKLVALDK 251
Cdd:PLN02548 161 VSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQGWETEDVEEIALKISALPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 252 ENCEGERIVIITQGPRPVLAFQGCAIKEYPVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQIIQH 331
Cdd:PLN02548 241 ASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQR 320
|
330
....*....|.
gi 1939370354 332 SGCTFEGKPSF 342
Cdd:PLN02548 321 SGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
9-343 |
3.30e-151 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 429.06 E-value: 3.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSEFLDKYNLRPDNAILAKDEHMSLYKDLVEKYNPDYIAGGSAQNTLRVCQWILQKPK-IAAFFG 87
Cdd:PTZ00247 8 LLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKgFVCYVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 88 CVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLISNGHRSLCAHLAAANEFTVEHLQKPENRELWENARYFYITG 167
Cdd:PTZ00247 88 CVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAEHMQSHAVQEAIKTAQLYYLEG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 168 FFLVINPAAVMQVAQHAYDSKSTFMLNLSASFVMQQFKEPLMAVMPYVKVLFGNVEEAKSFARAYDWETKDLKEIGLKLV 247
Cdd:PTZ00247 168 FFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAMKWDTEDLKEIAARIA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 248 ALDKENCEGERIVIITQGPRPVLAFQGCAIKEYPVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQ 327
Cdd:PTZ00247 248 MLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQV 327
|
330
....*....|....*.
gi 1939370354 328 IIQHSGCTFEGKPSFR 343
Cdd:PTZ00247 328 IIQHNGCTYPEKPPFL 343
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-337 |
1.47e-122 |
|
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: 355.00 E-value: 1.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSEFLDKYNLRPDNAILAkdeHMSLYKDLVEKYNPDYIAGGSAQNTLRVCQWILQKpkiAAFFGC 88
Cdd:cd01168 4 VLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAALGGS---AAFIGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 89 VGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLISNGH-RSLCAHLAAANEFTVEHLqkpeNRELWENARYFYITG 167
Cdd:cd01168 78 VGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAeRTMCTYLGAANELSPDDL----DWSLLAKAKYLYLEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 168 FFLVINPAAVMQVAQHAYDSKSTFMLNLSASFVMQQFKEPLMAVMPYVKVLFGNVEEAKSFARAydwETKDLKEIGLKLV 247
Cdd:cd01168 154 YLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 248 ALDKencegeRIVIITQGPRPVLAFQGcaIKEYPVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQ 327
Cdd:cd01168 231 ALRC------RIVVITQGAKGAVVVEG--GEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAE 302
|
330
....*....|
gi 1939370354 328 IIQHSGCTFE 337
Cdd:cd01168 303 VIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
47-336 |
3.26e-57 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 187.55 E-value: 3.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 47 SLYKDLVEKYNPDYIAGGSAQNTLRVCQWILQKpkiAAFFGCVGKDDYANILEKKATQDGLSV-FYEYAVDAPTGTCAVL 125
Cdd:pfam00294 18 GLPGELVRVSTVEKGPGGKGANVAVALARLGGD---VAFIGAVGDDNFGEFLLQELKKEGVDTdYVVIDEDTRTGTALIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 126 IS-NGHRSLCAHLAAANEFTVEHLQkpENRELWENARYFYITGFFLVINPAAVMQVAQHAYDSKSTFMLNLSASFVmqQF 204
Cdd:pfam00294 95 VDgDGERTIVFNRGAAADLTPEELE--ENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLG--AA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 205 KEPLMAVMPYVKVLFGNVEEAKSFARAYDWETKDLKEIGLKLVAldkencEGERIVIITQGPRPVLAFQGCaiKEYPVQR 284
Cdd:pfam00294 171 REALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLA------KGIKTVIVTLGADGALVVEGD--GEVHVPA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1939370354 285 FTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQIIQHSGCTF 336
Cdd:pfam00294 243 VPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-344 |
9.18e-43 |
|
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: 150.03 E-value: 9.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSefldkyNLRPDNAILAKDEHMSLykdlvekynpdyiaGGSAQNTLRVCQWiLQKPkiAAFFGC 88
Cdd:COG0524 2 VLVIGEALVDLVARVDR------LPKGGETVLAGSFRRSP--------------GGAAANVAVALAR-LGAR--VALVGA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 89 VGKDDYANILEKKATQDGLSVFY-EYAVDAPTGTCAVLIS-NGHRSLCAHLAAANEFTVEHLqkpeNRELWENARYFYIT 166
Cdd:COG0524 59 VGDDPFGDFLLAELRAEGVDTSGvRRDPGAPTGLAFILVDpDGERTIVFYRGANAELTPEDL----DEALLAGADILHLG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 167 GFFLV--INPAAVMQVAQHAYDSKSTFMLNLSASFVM-QQFKEPLMAVMPYVKVLFGNVEEAKSFaraydWETKDLKEIG 243
Cdd:COG0524 135 GITLAsePPREALLAALEAARAAGVPVSLDPNYRPALwEPARELLRELLALVDILFPNEEEAELL-----TGETDPEEAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 244 LKLVALdkenceGERIVIITQGPRPVLAFQGCAIKEYPVQrftPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIW 323
Cdd:COG0524 210 AALLAR------GVKLVVVTLGAEGALLYTGGEVVHVPAF---PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANA 280
|
330 340
....*....|....*....|.
gi 1939370354 324 AASQIIQHSGCTfEGKPSFRE 344
Cdd:COG0524 281 AAALVVTRPGAQ-PALPTREE 300
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-335 |
3.79e-28 |
|
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: 111.13 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATvdsefldkynlrpdnailakDEHMSLYKDLVEKYnpdyiAGGSAQNTLRVCQwILQKPkiAAFFGC 88
Cdd:cd01166 2 VVTIGEVMVDLSPP--------------------GGGRLEQADSFRKF-----FGGAEANVAVGLA-RLGHR--VALVTA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 89 VGKDDYANILEKKATQDGLSVfyeYAV----DAPTGTCAVLI-SNGHRSLC---AHlAAANEFTVEHLqkpeNRELWENA 160
Cdd:cd01166 54 VGDDPFGRFILAELRREGVDT---SHVrvdpGRPTGLYFLEIgAGGERRVLyyrAG-SAASRLTPEDL----DEAALAGA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 161 RYFYITGFFLVINP---AAVMQVAQHA--YDSKSTFMLNLSASFVM-QQFKEPLMAVMPYVKVLFGNVEEAKSFaraydW 234
Cdd:cd01166 126 DHLHLSGITLALSEsarEALLEALEAAkaRGVTVSFDLNYRPKLWSaEEAREALEELLPYVDIVLPSEEEAEAL-----L 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 235 ETKDLKEIglklVALDKENCEGERIVIITQGPRPVLAFQG---CAIKEYPVQrftpeqIVDTTAAGDAFCGGFLAQYIQS 311
Cdd:cd01166 201 GDEDPTDA----AERALALALGVKAVVVKLGAEGALVYTGggrVFVPAYPVE------VVDTTGAGDAFAAGFLAGLLEG 270
|
330 340
....*....|....*....|....
gi 1939370354 312 KDLDVCIRCGIWAASQIIQHSGCT 335
Cdd:cd01166 271 WDLEEALRFANAAAALVVTRPGDI 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
84-326 |
5.34e-23 |
|
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: 96.85 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 84 AFFGCVGKDDYANILEKKATQDGLSVFYEYAV-DAPTGTCAVLIS-NGHRSLCAHLAAANEFTVEHLQKpeNRELWENAR 161
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVVvGAPTGTAVITVDeSGENRIVVVPGANGELTPADVDA--ALELIAAAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 162 yfyitgfFLV----INPAAVMQVAQHAYDSKSTFMLNLSAsfvmqqFKEPLMAVMPYVKVLFGNVEEAKSFARAYDWETK 237
Cdd:cd01174 132 -------VLLlqleIPLETVLAALRAARRAGVTVILNPAP------ARPLPAELLALVDILVPNETEAALLTGIEVTDEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 238 DLKEIGLKLVALdkenceGERIVIITQGPRPVLAFQGCAIKEYPvqrFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVC 317
Cdd:cd01174 199 DAEKAARLLLAK------GVKNVIVTLGAKGALLASGGEVEHVP---AFKVKAVDTTGAGDTFIGALAAALARGLSLEEA 269
|
....*....
gi 1939370354 318 IRCGIWAAS 326
Cdd:cd01174 270 IRFANAAAA 278
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-334 |
5.38e-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: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSEfldkynlrPDnailakdEHMS-LYKDLVEKYnpdyiaGGSAQNTLRVCQWILQKPKIAaffG 87
Cdd:cd01942 2 VAVVGHLNYDIILKVESF--------PG-------PFESvLVKDLRREF------GGSAGNTAVALAKLGLSPGLV---A 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 88 CVGKDDYANILEKKATQDGLSVFY-EYAVDAPTGTcAVLISNGHRS--LCAHLAAANEFTVEHLQKPENrelweNARYFY 164
Cdd:cd01942 58 AVGEDFHGRLYLEELREEGVDTSHvRVVDEDSTGV-AFILTDGDDNqiAYFYPGAMDELEPNDEADPDG-----LADIVH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 165 ITGFFLVINpaavMQVAQHAYDSKSTF-----MLNLSasfvmqqfKEPLMAVMPYVKVLFGNveeaksfarayDWETKDL 239
Cdd:cd01942 132 LSSGPGLIE----LARELAAGGITVSFdpgqeLPRLS--------GEELEEILERADILFVN-----------DYEAELL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 240 KEI-GLKLVALDKenceGERIVIITQGPRPVLAFQGCaiKEYPVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCI 318
Cdd:cd01942 189 KERtGLSEAELAS----GVRVVVVTLGPKGAIVFEDG--EEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESL 262
|
330
....*....|....*.
gi 1939370354 319 RCGIWAASQIIQHSGC 334
Cdd:cd01942 263 RLGNLAASLKVERRGA 278
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
83-333 |
7.35e-15 |
|
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: 73.54 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 83 AAFFGCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLISNGHRSLcahlAAANEFTVEhlqkpenRELWENARY 162
Cdd:cd01940 39 SAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELVDGDRIF----GLSNKGGVA-------REHPFEADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 163 FYITGFFLVinPAAVMQVAQHAYDSKSTFMLN---LSASFVMQQFKEPLMAVMPYVKVLFGNVEEAKSFARaydwetkdl 239
Cdd:cd01940 108 EYLSQFDLV--HTGIYSHEGHLEKALQALVGAgalISFDFSDRWDDDYLQLVCPYVDFAFFSASDLSDEEV--------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 240 keiglkLVALDKENCEGERIVIITQGPRPVLAFQGCAIKEypvQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDV-CI 318
Cdd:cd01940 177 ------KAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYS---VAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAIAeAM 247
|
250
....*....|....*
gi 1939370354 319 RCGIWAASQIIQHSG 333
Cdd:cd01940 248 RQGAQFAAKTCGHEG 262
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
62-333 |
2.65e-14 |
|
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: 72.28 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 62 AGGSAQNTLRVcqwiLQKPKI-AAFFGCVGKDDYANILEKKATQDGLSVFYEYA-VDAPTGTCAV-LISNGHRS-LCAHL 137
Cdd:cd01167 27 PGGAPANVAVA----LARLGGkAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPAAPTTLAFVtLDADGERSfEFYRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 138 AAANEFTVEHLQKPenreLWENARYFYITGFFLVINP--AAVMQVAQHAYDSKST--FMLNLSASFV--MQQFKEPLMAV 211
Cdd:cd01167 103 PAADLLLDTELNPD----LLSEADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWrdEEEARERIAEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 212 MPYVKVLFGNVEEAKSFARAYDWETKD--LKEIGLKLValdkencegerivIITQGPRPVLAFQGCAIKEYPVqrfTPEQ 289
Cdd:cd01167 179 LELADIVKLSDEELELLFGEEDPEEIAalLLLFGLKLV-------------LVTRGADGALLYTKGGVGEVPG---IPVE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1939370354 290 IVDTTAAGDAFCGGFLAQYIQSKD-------LDVCIRCGIWAASQIIQHSG 333
Cdd:cd01167 243 VVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAG 293
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
160-309 |
4.67e-13 |
|
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: 67.12 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 160 ARYFYITGFFLviNPAAVMQVAQHAYDSKSTFMLNLSASFVMQqFKEPLMAVMPYVKVLFGNVEEAKSFARAYDWETKDL 239
Cdd:cd00287 58 ADAVVISGLSP--APEAVLDALEEARRRGVPVVLDPGPRAVRL-DGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEA 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939370354 240 KEiglklvALDKENCEGERIVIITQGPR-PVLAFQGCAIKEYPVQrftPEQIVDTTAAGDAFCGGFLAQYI 309
Cdd:cd00287 135 AE------AAALLLSKGPKVVIVTLGEKgAIVATRGGTEVHVPAF---PVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
83-331 |
2.46e-11 |
|
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: 63.49 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 83 AAFFGCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTC-AVLISNGHRSL-CAHLAAANEFTVEHLQKpeNRELWENA 160
Cdd:cd01941 52 VALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYtAILDKDGDLVVaLADMDIYELLTPDFLRK--IREALKEA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 161 RYfyitgffLVI---NPAAVMQ---------VAQHAYDSKSTFMLnlsasfvmqqfkEPLMAVMPYVKVLFGNVEEAKSF 228
Cdd:cd01941 130 KP-------IVVdanLPEEALEyllalaakhGVPVAFEPTSAPKL------------KKLFYLLHAIDLLTPNRAELEAL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 229 ARAYDWETKDLKEiglklvALDKENCEGERIVIITQGPRPVLAFQGCA---IKEYPVQrfTPEQIVDTTAAGDAFCGGFL 305
Cdd:cd01941 191 AGALIENNEDENK------AAKILLLPGIKNVIVTLGAKGVLLSSREGgveTKLFPAP--QPETVVNVTGAGDAFVAGLV 262
|
250 260
....*....|....*....|....*.
gi 1939370354 306 AQYIQSKDLDVCIRCGIWAASQIIQH 331
Cdd:cd01941 263 AGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
84-326 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 84 AFFGCVGKDDYANILEKKATQDGLSVFYEYAV-DAPTGTCAVLI-SNGHRSLCAHLAAANEFTVEHLQKPENreLWENAR 161
Cdd:TIGR02152 49 SMIGKVGDDAFGDELLENLKSNGIDTEYVGTVkDTPTGTAFITVdDTGENRIVVVAGANAELTPEDIDAAEA--LIAESD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 162 YFYITgffLVINPAAVMQVAQHAYDSKSTFMLN-------LSASFVMqqfkeplmavmpYVKVLFGNVEEAKSFARAYDW 234
Cdd:TIGR02152 127 IVLLQ---LEIPLETVLEAAKIAKKHGVKVILNpapaikdLDDELLS------------LVDIITPNETEAEILTGIEVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 235 ETKDLKEIGLKLVALdkenceGERIVIITQGPrpvlafQGCAIKEYPVQRFTPE---QIVDTTAAGDAFCGGFLAQYIQS 311
Cdd:TIGR02152 192 DEEDAEKAAEKLLEK------GVKNVIITLGS------KGALLVSKDESKLIPAfkvKAVDTTAAGDTFNGAFAVALAEG 259
|
250
....*....|....*
gi 1939370354 312 KDLDVCIRCGIWAAS 326
Cdd:TIGR02152 260 KSLEDAIRFANAAAA 274
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
205-333 |
9.73e-10 |
|
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: 58.89 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 205 KEPLMAVMPYVKVLFGNVEEAKSFARAYDWETKDLKEiglKLVALDKENCEG-----ERIVIITQGPRPVLAFQGCAIKE 279
Cdd:cd01943 171 LEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEE---KEAVLQALLFSGilqdpGGGVVLRCGKLGCYVGSADSGPE 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939370354 280 Y--PVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQIIQHSG 333
Cdd:cd01943 248 LwlPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
58-333 |
9.29e-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: 55.89 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 58 PDYIAGGSaqntLRVCQwILQKPKI-AAFFGCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLIS-NGHRSLCA 135
Cdd:cd01944 31 KSYVIGGG----FNVMV-AASRLGIpTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEpDGERSFIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 136 HLAAANEFTVEHLQKPENRElwenARYFYITGFFLViNPAAVMQV---AQHAYDSKSTFMLNlsASFVMQQFKEPLM-AV 211
Cdd:cd01944 106 ISGAEQDWSTEWFATLTVAP----YDYVYLSGYTLA-SENASKVIlleWLEALPAGTTLVFD--PGPRISDIPDTILqAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 212 MPYVKVLFGNVEEAKSFAraydwETKDLKEiglkLVALDKENCEGERIVIITQGPRpvlafqGCAIKEYPVQRFT----P 287
Cdd:cd01944 179 MAKRPIWSCNREEAAIFA-----ERGDPAA----EASALRIYAKTAAPVVVRLGSN------GAWIRLPDGNTHIipgfK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1939370354 288 EQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQIIQHSG 333
Cdd:cd01944 244 VKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
16-333 |
2.30e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 55.18 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 16 LLDIVATVDSEFLDKYNLRPDNAILAKDEHMSLYKDLVEKY---NPDY------IAGGSAQNTLRvcqwilqkpKIAAFF 86
Cdd:PLN02379 30 LVDHVARVDWSLLDQIPGDRGGSIRVTIEELEHILREVNAHilpSPDDlspiktMAGGSVANTIR---------GLSAGF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 87 -------GCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLI-SNGHRSL--CAHLAA---ANEFTVEHLQKPEn 153
Cdd:PLN02379 101 gvstgiiGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVdALGNRTMrpCLSSAVklqADELTKEDFKGSK- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 154 relWENARYfyitGFFlvinpaaVMQVAQHAYDSKSTFMLNLS---ASFVM-QQFKEPLMAVMPYVKV--LFGNVEEAKS 227
Cdd:PLN02379 180 ---WLVLRY----GFY-------NLEVIEAAIRLAKQEGLSVSldlASFEMvRNFRSPLLQLLESGKIdlCFANEDEARE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 228 FARAydwETKDLKEIGLKLVAldkENCEGeriVIITQGPRPVLAFQGCAIKEYPVQRFTpeQIVDTTAAGDAFCGGFLAQ 307
Cdd:PLN02379 246 LLRG---EQESDPEAALEFLA---KYCNW---AVVTLGSKGCIARHGKEVVRVPAIGET--NAVDATGAGDLFASGFLYG 314
|
330 340
....*....|....*....|....*.
gi 1939370354 308 YIQSKDLDVCIRCGIWAASQIIQHSG 333
Cdd:PLN02379 315 LIKGLSLEECCKVGACSGGSVVRALG 340
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
9-305 |
3.93e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 54.43 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSEFLDKYNL-RPDNAILAKDEHMSLYKDLvEKYNPDYIAGGSAQNTLRV-----CQWILQKPKI 82
Cdd:PLN02813 72 VLGLGQAMVDFSGMVDDEFLERLGLeKGTRKVINHEERGKVLRAL-DGCSYKASAGGSLSNTLVAlarlgSQSAAGPALN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 83 AAFFGCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTCAVLIS-NGHRSLCAHlaaanEFTVEHLQ-KPENRELWENA 160
Cdd:PLN02813 151 VAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTpDAQRTMLSY-----QGTSSTVNyDSCLASAISKS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 161 RYFYITGFFLVINPA--AVMQVAQHAYDSKSTFMLNLSASFVMQQFKEPLMAVMP-YVKVLFGNVEEAKSFARAydwetk 237
Cdd:PLN02813 226 RVLVVEGYLWELPQTieAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGnYADILFANSDEARALCGL------ 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939370354 238 DLKEIGLKLVALDKENCEgerIVIITQGPR-PVLAFQGCAIKEYPvqrfTPEQIVDTTAAGDAFCGGFL 305
Cdd:PLN02813 300 GSEESPESATRYLSHFCP---LVSVTDGARgSYIGVKGEAVYIPP----SPCVPVDTCGAGDAYAAGIL 361
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
43-333 |
5.08e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 53.20 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 43 DEHMSLYKDLVEKYnpdyiAGGSAQNTLRVCQWILQKPkiaAFFGCVGKDDYANILEKKATQDGLSVFYEYAVDAPTGTC 122
Cdd:PRK09813 8 DNCVDIYPQLGKAF-----SGGNAVNVAVYCTRYGIQP---GCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 123 AVLISNGHRSLCAHLaaanEFTVEHLQKPEnrelwENARYfyITGFFLVInpAAVMQVAQHAYDSKSTFMLNLSASFVmQ 202
Cdd:PRK09813 80 QVELHDNDRVFGDYT----EGVMADFALSE-----EDYAW--LAQYDIVH--AAIWGHAEDAFPQLHAAGKLTAFDFS-D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 203 QFKEPLM-AVMPYVKVLFGNVEEAKSFARAYdweTKDLKEIGLKLValdkencegerivIITQGPRPVLAFQGCAIKEYP 281
Cdd:PRK09813 146 KWDSPLWqTLVPHLDYAFASAPQEDEFLRLK---MKAIVARGAGVV-------------IVTLGENGSIAWDGAQFWRQA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1939370354 282 VQrftPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAASQIIQHSG 333
Cdd:PRK09813 210 PE---PVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
9-225 |
3.38e-07 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 51.55 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 9 VVSLGNPLLDIVATVDSEFLDKYNLRPDNAILAKDEHMS-LYKDLVE-KYNPDYIAGGSAQNTLRVCQwILQKPKiAAFF 86
Cdd:PRK15074 36 IVGIDQTLVDIEAKVDDEFLERYGLSKGHSLVIEDDVAEaLYQELKQnNLITHEFAGGTIGNTLHNYS-VLADDR-SVLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 87 GCVGKD----DYA-----NilekkaTQDGLSVFYEYAVDAPTGTCAVLIS-NGHRSLCAHLAAANEFTVEHLqkPEnrEL 156
Cdd:PRK15074 114 GVMSSNieigSYAyrylcN------TSSRTDLNYLQGVDGPIGRCFTLISeDGERTFAISPGHMNQLRPESI--PE--DV 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939370354 157 WENARYFYITGFFLVIN-----PAAVMQVAQHAYDSKSTFMLNLSASFVMQQFKEPLMAVM-PYVKVLFGNVEEA 225
Cdd:PRK15074 184 IAGASALVLTAYLVRCKpgepmPEATMKAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLkEHVSILAMNEDEA 258
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
246-305 |
5.33e-06 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 47.29 E-value: 5.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939370354 246 LVALDKENCegeRIVIITQGPRPVLAFQGCAikeyPVQRFTPEQI--VDTTAAGDAFCGGFL 305
Cdd:cd01945 195 LELLASLGI---PFVAVTLGEAGCLWLERDG----ELFHVPAFPVevVDTTGAGDVFHGAFA 249
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
172-315 |
6.29e-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: 47.07 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 172 INPAAVMQVAQHAYDSKSTFMLNLSasFVMQQFKEPLMAVMPYVKVLFGNVEEAKSFARAYDwetkdLKEIGLKLVALdk 251
Cdd:cd01946 123 IAPELQREVLEQVKDPKLVVMDTMN--FWISIKPEKLKKVLAKVDVVIINDGEARQLTGAAN-----LVKAARLILAM-- 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939370354 252 enceGERIVIITQGPRPVLAF---QGCAIKEYPVqrftpEQIVDTTAAGDAFCGGFLAQYIQSKDLD 315
Cdd:cd01946 194 ----GPKALIIKRGEYGALLFtddGYFAAPAYPL-----ESVFDPTGAGDTFAGGFIGYLASQKDTS 251
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
256-315 |
1.12e-05 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 46.47 E-value: 1.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 256 GERIVIITQGPRPVLAFQGCAIKEYPVQRFTPeqiVDTTAAGDAFCGGFLAQYIQSKDLD 315
Cdd:PRK09434 212 PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDP---VDTTGAGDAFVAGLLAGLSQAGLWT 268
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
84-319 |
2.02e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 45.63 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 84 AFFGCVGKDDYANILEKKATQDGLSVfyeYAV----DAPTGTCAVLIS-NGHRSLCAHLAAANEFTVEHLQKpeNRELWE 158
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDT---APVsvikGESTGVALIFVNdEGENSIGIHAGANAALTPALVEA--HRELIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 159 NARYFYITgffLVINPAAVMQVAQHAYDSKSTFMLNLSASfvmQQFKEPLMAVmpyVKVLFGNVEEAKSFA--RAYDWET 236
Cdd:PRK11142 132 NADALLMQ---LETPLETVLAAAKIAKQHGTKVILNPAPA---RELPDELLAL---VDIITPNETEAEKLTgiRVEDDDD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 237 KDLkeiglklvALDKENCEGERIVIITQGPRPVL---AFQGCAIKEYPVQrftpeqIVDTTAAGDAFCGGFLAQYIQSKD 313
Cdd:PRK11142 203 AAK--------AAQVLHQKGIETVLITLGSRGVWlseNGEGQRVPGFRVQ------AVDTIAAGDTFNGALVTALLEGKP 268
|
....*.
gi 1939370354 314 LDVCIR 319
Cdd:PRK11142 269 LPEAIR 274
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
258-332 |
2.71e-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: 45.10 E-value: 2.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939370354 258 RIVIITQGPRPVLAFQGcaiKEYPVQRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCG-IWAASQIIQHS 332
Cdd:cd01947 191 RYLIVTEGELGAILYPG---GRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGaQCGAICVSHFG 263
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
205-328 |
7.96e-05 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 43.97 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 205 KEPLMAVMPY----VKVlfgNVEEAKSFARAYDWETKDLKEIGLKLVAldkencEGERIVIITQGPRPVLAF--QGcaik 278
Cdd:COG1105 167 GEALKAALEAgpdlIKP---NLEELEELLGRPLETLEDIIAAARELLE------RGAENVVVSLGADGALLVteDG---- 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939370354 279 eypVQRFTPEQI--VDTTAAGDAFCGGFLAQYIQSKDLDVCIR----CGIWAASQI 328
Cdd:COG1105 234 ---VYRAKPPKVevVSTVGAGDSMVAGFLAGLARGLDLEEALRlavaAGAAAALSP 286
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
203-315 |
1.51e-04 |
|
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: 42.77 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 203 QFKEPLMAVMPYVKVLFGNVEEAKsfaraydwETKDLKEIGLKLVALdkenceGERIVIITQGPRPVLAFQGCAIkeYPV 282
Cdd:cd01937 144 QEKLIKCVILKLHDVLKLSRVEAE--------VISTPTELARLIKET------GVKEIIVTDGEEGGYIFDGNGK--YTI 207
|
90 100 110
....*....|....*....|....*....|...
gi 1939370354 283 QRFtPEQIVDTTAAGDAFCGGFLAQYIQSKDLD 315
Cdd:cd01937 208 PAS-KKDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
84-333 |
1.82e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 42.80 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 84 AFFGCVGKDDYANILEKKATQDGLSVFYEYAV-DAPTGtCA---VLISNGHRSLCAHLAAANEFTVEHLqkpenRELWEN 159
Cdd:PTZ00292 70 AMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTeNSSTG-LAmifVDTKTGNNEIVIIPGANNALTPQMV-----DAQTDN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 160 arYFYITGFFLVINP---AAVMQVAQHAYDSKSTFMLNlSASFVMQQFKEPLMAVMPYVKVLFGNVEEAksfARAYDWET 236
Cdd:PTZ00292 144 --IQNICKYLICQNEiplETTLDALKEAKERGCYTVFN-PAPAPKLAEVEIIKPFLKYVSLFCVNEVEA---ALITGMEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 237 KDLKEIGLKLVALdkeNCEGERIVIITQGPrpvlafQGCAIKE---YPVQrfTPEQIV---DTTAAGDAFCGGFLAQYIQ 310
Cdd:PTZ00292 218 TDTESAFKASKEL---QQLGVENVIITLGA------NGCLIVEkenEPVH--VPGKRVkavDTTGAGDCFVGSMAYFMSR 286
|
250 260
....*....|....*....|...
gi 1939370354 311 SKDLDVCIRCGIWAASQIIQHSG 333
Cdd:PTZ00292 287 GKDLKESCKRANRIAAISVTRHG 309
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
205-338 |
3.09e-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: 42.01 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 205 KEPLMAVMPYVKVLFgnveEAKSFARAYDWETkdlkeiGLKLVALDKENCEGERIVIITQGPRPVLAF--QGCAikeYPV 282
Cdd:cd01939 170 REELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWGDQGAGALgpDGEY---VHS 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939370354 283 QRFTPEQIVDTTAAGDAFCGGFL-AQYIQSKDLDVCIRCGIWAASQiiqhsGCTFEG 338
Cdd:cd01939 237 PAHKPIRVVDTLGAGDTFNAAVIyALNKGPDDLSEALDFGNRVASQ-----KCTGVG 288
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
205-326 |
1.47e-03 |
|
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: 39.82 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939370354 205 KEPLMAVMPY----VKVlfgNVEEAKSFARAYDWETKDLKEIGLKLVALdkenceGERIVIITQGPRPVLAFQGCAIkeY 280
Cdd:cd01164 167 GEALLAALAAkpflIKP---NREELEELFGRPLGDEEDVIAAARKLIER------GAENVLVSLGADGALLVTKDGV--Y 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1939370354 281 PVqRFTPEQIVDTTAAGDAFCGGFLAQYIQSKDLDVCIRCGIWAAS 326
Cdd:cd01164 236 RA-SPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGS 280
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
258-314 |
2.87e-03 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 39.22 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939370354 258 RIVIITQGPrpvlafQGCaikeypvQRFTPE----------QIVDTTAAGDAFCGGFLAQYIQSKDL 314
Cdd:PLN02323 231 KLLLVTEGE------EGC-------RYYTKDfkgrvegfkvKAVDTTGAGDAFVGGLLSQLAKDLSL 284
|
|
| |
