|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-297 |
1.08e-77 |
|
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: 239.01 E-value: 1.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDipLQPVSKNIFDvdsyPLERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDI 84
Cdd:cd01166 1 DVVTIGEVMVD--LSPPGGGRLE----QADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 85 QSLKQDVSIDTSINVGLVTEDGERTFVTNRNGS-LWKLNIDDVDFARFSQAKLLSLASIFNSPLLDGKALT-EIFTQAKA 162
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSaASRLTPEDLDEAALAGADHLHLSGITLALSESAREALlEALEAAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 163 RQMIICAD-MIKPRLN--ETLDDICEAL-SYVDYLFPNFAEAKLLTGKETLDEIADCFLA--CGVKTVVIKTGKDGCFIK 236
Cdd:cd01166 155 RGVTVSFDlNYRPKLWsaEEAREALEELlPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKLGAEGALVY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111328 237 RGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGAT 297
Cdd:cd01166 235 TGGGRVFVPAYP-VEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-306 |
1.11e-76 |
|
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: 236.70 E-value: 1.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDIplqpvsknIFDVDSYP-------LERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHC 77
Cdd:COG0524 1 DVLVIGEALVDL--------VARVDRLPkggetvlAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 78 RKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNRnGSLWKLNIDDVDFARFSQAKLLSLASIFNSPLLDGKALTEIF 157
Cdd:COG0524 73 RAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYR-GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 158 TQAKARQMIICAD-MIKPRL-NETLDDICEALSYVDYLFPNFAEAKLLTGKETLDEIADCFLACGVKTVVIKTGKDGCFI 235
Cdd:COG0524 152 EAARAAGVPVSLDpNYRPALwEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111328 236 KRGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGATTGVKNRKLV 306
Cdd:COG0524 232 YTGGEVVHVPAFP-VEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-298 |
7.39e-73 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 226.46 E-value: 7.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDipLQPVSKNIFDVDSYPlERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDI 84
Cdd:pfam00294 1 KVVVIGEANID--LIGNVEGLPGELVRV-STVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 85 QSLKQDVSIDTSINVGLVTEDGERTFVTNRNGSLWKLNI-DDVDFARFSQAKLLSLASIFNSPLlDGKALTEIFTQAKAR 163
Cdd:pfam00294 78 DYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEeLEENEDLLENADLLYISGSLPLGL-PEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 164 QmiICADMIKPRLNETLDDICEALSYVDYLFPNFAEAKLLTGKEtLDEIADC------FLACGVKTVVIKTGKDGCFIKR 237
Cdd:pfam00294 157 G--TFDPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAK-LDDIEEAlaalhkLLAKGIKTVIVTLGADGALVVE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111328 238 GDMTMKVPAVAGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGATT 298
Cdd:pfam00294 234 GDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
5-299 |
5.23e-44 |
|
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: 152.77 E-value: 5.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDIplqpvsknIFDVDSYPLERIAMT------------------------TGGDAINEATIISRLGHRTAL 60
Cdd:cd01168 3 DVLGLGNALVDI--------LAQVDDAFLEKLGLKkgdmiladmeeqeellaklpvkyiAGGSAANTIRGAAALGGSAAF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 61 MSRIGKDAAGQFILDHCRKENIDIQS-LKQDVSIDTSINvgLVTEDGERTFVTNRnGSLWKLNIDDVDFARFSQAKLLSL 139
Cdd:cd01168 75 IGRVGDDKLGDFLLKDLRAAGVDTRYqVQPDGPTGTCAV--LVTPDAERTMCTYL-GAANELSPDDLDWSLLAKAKYLYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 140 ASIFNspLLDGKALTEIFTQAKARQMIICADM----IKPRLNETLDDIceaLSYVDYLFPNFAEAKLLTGKETLD--EIA 213
Cdd:cd01168 152 EGYLL--TVPPEAILLAAEHAKENGVKIALNLsapfIVQRFKEALLEL---LPYVDILFGNEEEAEALAEAETTDdlEAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 214 DCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLS 293
Cdd:cd01168 227 LKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQ 306
|
....*.
gi 90111328 294 VGATTG 299
Cdd:cd01168 307 LGPRLP 312
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-296 |
1.65e-41 |
|
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: 145.39 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 37 AMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNR-- 114
Cdd:cd01174 32 ETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPga 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 115 NGSLWKLNIDDVDfARFSQAKLLSLAsiFNSPLldgKALTEIFTQAKARQMIICADM--IKPRLNEtlddiceALSYVDY 192
Cdd:cd01174 112 NGELTPADVDAAL-ELIAAADVLLLQ--LEIPL---ETVLAALRAARRAGVTVILNPapARPLPAE-------LLALVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 193 LFPNFAEAKLLTGKETLDE-----IADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFASGFI 267
Cdd:cd01174 179 LVPNETEAALLTGIEVTDEedaekAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFK-VKAVDTTGAGDTFIGALA 257
|
250 260
....*....|....*....|....*....
gi 90111328 268 AALLEGKNLRECARFANATAAISVLSVGA 296
Cdd:cd01174 258 AALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-296 |
4.18e-40 |
|
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: 141.68 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDIplqpvsknIFDVDSYPLERIAMTT-------GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHC 77
Cdd:cd01942 1 DVAVVGHLNYDI--------ILKVESFPGPFESVLVkdlrrefGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 78 RKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNRNGSLWKLNIDDVDfaRFSQAKLLSLASifnsplldGKALTEIF 157
Cdd:cd01942 73 REEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEAD--PDGLADIVHLSS--------GPGLIELA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 158 TQAKARQMIICAD---MIKPRLNETLDDIceaLSYVDYLFPNFAEAKLLTGKETLDEIAdcfLACGVKTVVIKTGKDGCF 234
Cdd:cd01942 143 RELAAGGITVSFDpgqELPRLSGEELEEI---LERADILFVNDYEAELLKERTGLSEAE---LASGVRVVVVTLGPKGAI 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111328 235 IKRGDMTMKVPAVAGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGA 296
Cdd:cd01942 217 VFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-296 |
2.59e-37 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 134.69 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 6 VICIGAAIVD-IPLQPVSKNIFDvdSYPleriamttGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDI 84
Cdd:cd01167 2 VVCFGEALIDfIPEGSGAPETFT--KAP--------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 85 QSLKQDVSIDTSINVGLVTEDGERTFVTNRNGS---LWKLNIDDvdfARFSQAKLLSLASIfnsPLLDG---KALTEIFT 158
Cdd:cd01167 72 RGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAadlLLDTELNP---DLLSEADILHFGSI---ALASEpsrSALLELLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 159 QAKARQMIICAD------MIKPRlNETLDDICEALSYVDYLFPNFAEAKLLTGKETLDEIADCFLACGVKTVVIKTGKDG 232
Cdd:cd01167 146 AAKKAGVLISFDpnlrppLWRDE-EEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111328 233 CFIKRGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKN-------LRECARFANATAAISVLSVGA 296
Cdd:cd01167 225 ALLYTKGGVGEVPGIP-VEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAGA 294
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
41-312 |
2.52e-27 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 108.42 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNrNGSLWK 120
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIH-AGANAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 121 LNIDDVD--FARFSQAK--LLSLASIFNSPLLDGKalteiftQAKARQmiicadmIKPRLN----ETLDDicEALSYVDY 192
Cdd:PRK11142 118 LTPALVEahRELIANADalLMQLETPLETVLAAAK-------IAKQHG-------TKVILNpapaRELPD--ELLALVDI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 193 LFPNFAEAKLLTGKETLDE-----IADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFASGFI 267
Cdd:PRK11142 182 ITPNETEAEKLTGIRVEDDddaakAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFR-VQAVDTIAAGDTFNGALV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 90111328 268 AALLEGKNLRECARFANATAAISVLSVGATTGVKNRKLVEQLLEE 312
Cdd:PRK11142 261 TALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQE 305
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-293 |
1.26e-26 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 105.86 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 6 VICIGAAIVDIPLQpVSKNIFDVDSYPlERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKenIDIQ 85
Cdd:cd01941 2 IVVIGAANIDLRGK-VSGSLVPGTSNP-GHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEK--AGLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 86 SLKQDVS-IDTSINVGLVTEDGERTFVTNRNGSLWKLNIDDVDFAR--FSQAKLLSLASifNSPLLDGKALTEIFTQAKA 162
Cdd:cd01941 78 VRGIVFEgRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIReaLKEAKPIVVDA--NLPEEALEYLLALAAKHGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 163 RQMIICADMIKprlnetLDDICEALSYVDYLFPNFAEAKLLTG---KETLDEIADC--FLACGVKTVVIKTGKDGCFI-- 235
Cdd:cd01941 156 PVAFEPTSAPK------LKKLFYLLHAIDLLTPNRAELEALAGaliENNEDENKAAkiLLLPGIKNVIVTLGAKGVLLss 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111328 236 -KRGDMTMKVPAVAGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLS 293
Cdd:cd01941 230 rEGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-299 |
1.32e-24 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 100.45 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDIplqpvsknIFDVDSYPL--ERIAMTT-----GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHC 77
Cdd:cd01945 1 RVLGVGLAVLDL--------IYLVASFPGgdGKIVATDyavigGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 78 RKENIDIQSLKQDVSIDTSIN-VGLVTEDGERTFVTNRNGSLWKLNIDDVDFARFSqakllslASIFNSPLLDgkALTEI 156
Cdd:cd01945 73 AAEGVDTSFIVVAPGARSPISsITDITGDRATISITAIDTQAAPDSLPDAILGGAD-------AVLVDGRQPE--AALHL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 157 FTQAKAR--QMIICADMIKPRLNEtlddicEALSYVDYLFP--NFAEAklLTGkETLDEIADCFLACGVKTVVIKTGKDG 232
Cdd:cd01945 144 AQEARARgiPIPLDLDGGGLRVLE------ELLPLADHAICseNFLRP--NTG-SADDEALELLASLGIPFVAVTLGEAG 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111328 233 C-FIKRGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGATTG 299
Cdd:cd01945 215 ClWLERDGELFHVPAFP-VEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAG 281
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
41-312 |
3.19e-23 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 97.13 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAaGQFILDHCRKENIDIQSLKqdVSIDTSINVGLVTEDGERTFVTNRNGslwk 120
Cdd:COG1105 35 GGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVP--IEGETRINIKIVDPSDGTETEINEPG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 121 LNIDDVDFARFsQAKLLSLA----------SIfnSPLLDGKALTEIFTQAKARQMIICADMIKPRLNEtlddiceALSY- 189
Cdd:COG1105 108 PEISEEELEAL-LERLEELLkegdwvvlsgSL--PPGVPPDFYAELIRLARARGAKVVLDTSGEALKA-------ALEAg 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 190 VDYLFPNFAEAKLLTGKE--TLDEIADC---FLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFAS 264
Cdd:COG1105 178 PDLIKPNLEELEELLGRPleTLEDIIAAareLLERGAENVVVSLGADGALLVTEDGVYRAKPPK-VEVVSTVGAGDSMVA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 90111328 265 GFIAALLEGKNLRECARFANATAAISVLSVGatTGVKNRKLVEQLLEE 312
Cdd:COG1105 257 GFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
28-296 |
5.27e-23 |
|
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: 95.88 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 28 VDSYPLERIaMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQdvsIDTSINVGLVTE-DG 106
Cdd:cd01940 10 VDKYLHLGK-MYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV---KEGENAVADVELvDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 107 ERTFVTNRNGSLWKLNIDDVDFARFSQAKLlslasIFNSPLLDGKALTEIFTQAKARQMIICADMikpRLNETLDDICEA 186
Cdd:cd01940 86 DRIFGLSNKGGVAREHPFEADLEYLSQFDL-----VHTGIYSHEGHLEKALQALVGAGALISFDF---SDRWDDDYLQLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 187 LSYVDYLFPNFAEAKLLTGKETLDEiadcFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFASGF 266
Cdd:cd01940 158 CPYVDFAFFSASDLSDEEVKAKLKE----AVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRP-VEVVDTLGAGDSFIAGF 232
|
250 260 270
....*....|....*....|....*....|.
gi 90111328 267 IAALLEGK-NLRECARFANATAAISVLSVGA 296
Cdd:cd01940 233 LLSLLAGGtAIAEAMRQGAQFAAKTCGHEGA 263
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
41-298 |
9.28e-23 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 96.34 E-value: 9.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTS---INVGLVTEDGERTFVTNRNGS 117
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGlamIFVDTKTGNNEIVIIPGANNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 118 LwklNIDDVDFAR---FSQAKLLSLASifNSPLldgKALTEIFTQAKARQMIIC---ADMIKPRLNETLDDIceaLSYVD 191
Cdd:PTZ00292 132 L---TPQMVDAQTdniQNICKYLICQN--EIPL---ETTLDALKEAKERGCYTVfnpAPAPKLAEVEIIKPF---LKYVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 192 YLFPNFAEAKLLTGKETLDE-----IADCFLACGVKTVVIKTGKDGCFI-KRGDMTMKVPAVAgITAIDTIGAGDNFASG 265
Cdd:PTZ00292 201 LFCVNEVEAALITGMEVTDTesafkASKELQQLGVENVIITLGANGCLIvEKENEPVHVPGKR-VKAVDTTGAGDCFVGS 279
|
250 260 270
....*....|....*....|....*....|...
gi 90111328 266 FIAALLEGKNLRECARFANATAAISVLSVGATT 298
Cdd:PTZ00292 280 MAYFMSRGKDLKESCKRANRIAAISVTRHGTQS 312
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
41-312 |
1.10e-20 |
|
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: 89.94 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAaGQFILDHCRKENIDIQSLKqdVSIDTSINVGLVTEDGERTfvtnrngslwK 120
Cdd:TIGR03168 35 GGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVE--VKGETRINVKIKESSGEET----------E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 121 LN-----IDDVDFARFsQAKLLSLasifnspLLDGKAL-----------TEIFTQ--AKARQ---MIICaDMIKPRLNEt 179
Cdd:TIGR03168 102 LNepgpeISEEELEQL-LEKLREL-------LASGDIVvisgslppgvpPDFYAQliAIARKkgaKVIL-DTSGEALRE- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 180 lddiceALSYVDYLF-PNFAEAKLLTGKE--TLDEIADC---FLACGVKTVVIKTGKDGCFIKRGDMTMKVPAvAGITAI 253
Cdd:TIGR03168 172 ------ALAAKPFLIkPNHEELEELFGRElkTLEEIIEAareLLDRGAENVLVSLGADGALLVTKEGALKATP-PKVEVV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111328 254 DTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGatTGVKNRKLVEQLLEE 312
Cdd:TIGR03168 245 NTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDVEELLDQ 301
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
41-303 |
2.84e-19 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 86.14 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVTEDGER--TFVTNRNGSL 118
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 119 WkLNIDDVdfARFSQAKLLSLASIfnsplldgkALT---------EIFTQAKARQMIICADmikPRLNETL--------D 181
Cdd:PRK09434 108 F-LQPQDL--PPFRQGEWLHLCSI---------ALSaepsrsttfEAMRRIKAAGGFVSFD---PNLREDLwqdeaelrE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 182 DICEALSYVDYLFPNFAEAKLLTGKETLDEIADCFLA-CGVKTVVIKTGKDG-CFIKRGDMTmKVPAVAgITAIDTIGAG 259
Cdd:PRK09434 173 CLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADrYPIALLLVTLGAEGvLVHTRGQVQ-HFPAPS-VDPVDTTGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 90111328 260 DNFASGFIAALLEGKN------LRECARFANATAAISVLSVGATTGVKNR 303
Cdd:PRK09434 251 DAFVAGLLAGLSQAGLwtdeaeLAEIIAQAQACGALATTAKGAMTALPNR 300
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-291 |
3.45e-19 |
|
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: 85.55 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 6 VICIGAAIVDIplqpvsknIFDVDSYP-------LERIAMTTGGdAINEATIISRLGHRTALMSRIGKDAAGQFILDHCR 78
Cdd:cd01944 2 VLVIGAAVVDI--------VLDVDKLPasggdieAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 79 KENIDIqsLKQDVSIDTSIN-VGLVTEDGERTFVTNRNG-SLWKLNiddvDFARFSQAK----LLSLASIFNSPLLDGkA 152
Cdd:cd01944 73 DEGIEI--LLPPRGGDDGGClVALVEPDGERSFISISGAeQDWSTE----WFATLTVAPydyvYLSGYTLASENASKV-I 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 153 LTEIFTQAKARQMIICAdmIKPRLNETLDDICEALSYVDYLFP-NFAEAKLLTGKETLDEIADCfLACGVKT---VVIKT 228
Cdd:cd01944 146 LLEWLEALPAGTTLVFD--PGPRISDIPDTILQALMAKRPIWScNREEAAIFAERGDPAAEASA-LRIYAKTaapVVVRL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111328 229 GKDGCFIK-RGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISV 291
Cdd:cd01944 223 GSNGAWIRlPDGNTHIIPGFK-VKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVV 285
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
41-297 |
8.87e-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: 81.81 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAaGQFILDHCRKENIDIQSLKqdVSIDTSINVGLVTEDGERTfvtnrngslwK 120
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVE--VAGETRINVKIKEEDGTET----------E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 121 LN-----IDDVDFARFsQAKLLSLASIFN--------SPLLDGKALTEIFTQAKARQMIICADMIKPRLNETLDdiceal 187
Cdd:cd01164 103 INepgpeISEEELEAL-LEKLKALLKKGDivvlsgslPPGVPADFYAELVRLAREKGARVILDTSGEALLAALA------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 188 SYVDYLFPNFAEAKLLTGKE--TLDEIADC---FLACGVKTVVIKTGKDGCFIKRGDMTMKVPAvAGITAIDTIGAGDNF 262
Cdd:cd01164 176 AKPFLIKPNREELEELFGRPlgDEEDVIAAarkLIERGAENVLVSLGADGALLVTKDGVYRASP-PKVKVVSTVGAGDSM 254
|
250 260 270
....*....|....*....|....*....|....*
gi 90111328 263 ASGFIAALLEGKNLRECARFANATAAISVLSVGAT 297
Cdd:cd01164 255 VAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
29-311 |
7.14e-17 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 80.22 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 29 DSYPLERIAmttGGDAINEATIISR-LGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQdVSIDTSINVGLVTEDGE 107
Cdd:PLN02379 77 DLSPIKTMA---GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRA-KKGPTAQCVCLVDALGN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 108 RTFVTNRNGSLwKLNIDDVDFARFSQAKLLSLA-SIFNSPLLDgkaltEIFTQAKARQMIICADM--------IKPRLNE 178
Cdd:PLN02379 153 RTMRPCLSSAV-KLQADELTKEDFKGSKWLVLRyGFYNLEVIE-----AAIRLAKQEGLSVSLDLasfemvrnFRSPLLQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 179 TLDDicealSYVDYLFPNFAEAK-LLTGKETLD-EIADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAGITAIDTI 256
Cdd:PLN02379 227 LLES-----GKIDLCFANEDEAReLLRGEQESDpEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDAT 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90111328 257 GAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGATTGVKNRKLVEQLLE 311
Cdd:PLN02379 302 GAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGEVTPENWQWMYKQMQ 356
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
28-296 |
1.48e-16 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 77.86 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 28 VDSYPLERIAMTtGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVteDGE 107
Cdd:PRK09813 11 VDIYPQLGKAFS-GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELH--DND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 108 RTFVTNRNGSLWKLNIDDVDFaRFSQAKLLSLASIFnsplldGKAlTEIFTQAKARQMIIC---ADMIKPRLNETLddic 184
Cdd:PRK09813 88 RVFGDYTEGVMADFALSEEDY-AWLAQYDIVHAAIW------GHA-EDAFPQLHAAGKLTAfdfSDKWDSPLWQTL---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 185 eaLSYVDYLFpnfAEAKLLTG--KETLDEIADCflacGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNF 262
Cdd:PRK09813 156 --VPHLDYAF---ASAPQEDEflRLKMKAIVAR----GAGVVIVTLGENGSIAWDGAQFWRQAPEP-VTVVDTMGAGDSF 225
|
250 260 270
....*....|....*....|....*....|....
gi 90111328 263 ASGFIAALLEGKNLRECARFANATAAISVLSVGA 296
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
41-312 |
8.99e-16 |
|
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: 76.09 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAaGQFILDHCRKENIDIQSLKqdVSIDTSINVGLVTEDGErtfVTNRNGSLWK 120
Cdd:TIGR03828 35 GGKGINVSRVLKNLGVDVVALGFLGGFT-GDFIEALLREEGIKTDFVR--VPGETRINVKIKEPSGT---ETKLNGPGPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 121 LNIDDVD------FARFSQAKLLSLA-SIfnSPLLDGKALTEIFTQAKARQMIICADMIKPRLNEtlddiceALSYVDYL 193
Cdd:TIGR03828 109 ISEEELEalleklRAQLAEGDWLVLSgSL--PPGVPPDFYAELIALAREKGAKVILDTSGEALRD-------GLKAKPFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 194 F-PNFAEAKLLTGKE--TLDEIADC---FLACGVKTVVIKTGKDGCFIKRGDMTMKVPAvAGITAIDTIGAGDNFASGFI 267
Cdd:TIGR03828 180 IkPNDEELEELFGRElkTLEEIIEAareLLDLGAENVLISLGADGALLVTKEGALFAQP-PKGEVVSTVGAGDSMVAGFL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 90111328 268 AALLEGKNLRECARFANATAAISVLSVGatTGVKNRKLVEQLLEE 312
Cdd:TIGR03828 259 AGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLPQ 301
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
32-298 |
1.72e-15 |
|
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: 75.29 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 32 PLERIAMTTGGdAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQslkqdvsidtsinvgLVTEDGERTFV 111
Cdd:cd01172 31 KVEREEIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTD---------------GIVDEGRPTTT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 112 TNR----NGSLWKLN-IDDVDFARFSQAKLLslasifnsplldgKALTEIFTQAKArqmIICAD----MIKPRLNETLDD 182
Cdd:cd01172 95 KTRviarNQQLLRVDrEDDSPLSAEEEQRLI-------------ERIAERLPEADV---VILSDygkgVLTPRVIEALIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 183 ICEALS--------------Y--VDYLFPNFAEAKLLTG-----KETLDEIADCFLA-CGVKTVVIKTGKDGC-FIKRGD 239
Cdd:cd01172 159 AARELGipvlvdpkgrdyskYrgATLLTPNEKEAREALGdeindDDELEAAGEKLLElLNLEALLVTLGEEGMtLFERDG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111328 240 MTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGATT 298
Cdd:cd01172 239 EVQHIPALA-KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAP 296
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
5-312 |
1.46e-13 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 70.63 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 5 DVICIGAAIVDI-----PLQPVSKNifDVDSYpLERIAMT--------TGGDAiNEATIISRLGHRTALMSRIGKDAAGQ 71
Cdd:PLN02341 74 DVATLGNLCVDIvlpvpELPPPSRE--ERKAY-MEELAASppdkksweAGGNC-NFAIAAARLGLRCSTIGHVGDEIYGK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 72 FILDHCRKENIDIQSLKQDVSIDTSINVG--------LVTEDGERTFVTNRNGSLWKLNIDDVDFARFSQAKLLSLASIF 143
Cdd:PLN02341 150 FLLDVLAEEGISVVGLIEGTDAGDSSSASyetllcwvLVDPLQRHGFCSRADFGPEPAFSWISKLSAEAKMAIRQSKALF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 144 nsplLDGKALTEIFTQAKArQMIICAdmIK----------PR----LNETLDD---ICEALSYVDYLFPNFAEAKLLTGK 206
Cdd:PLN02341 230 ----CNGYVFDELSPSAIA-SAVDYA--IDvgtavffdpgPRgkslLVGTPDErraLEHLLRMSDVLLLTSEEAEALTGI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 207 ETLDEIADCFL--ACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFASGFIAALLEGKNLRECARFAN 284
Cdd:PLN02341 303 RNPILAGQELLrpGIRTKWVVVKMGSKGSILVTRSSVSCAPAFK-VNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLAN 381
|
330 340
....*....|....*....|....*...
gi 90111328 285 ATAAISVLSVGATTGVKNRKLVEQLLEE 312
Cdd:PLN02341 382 AVGAATAMGCGAGRNVATLEKVLELLRA 409
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
28-297 |
1.54e-13 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 70.13 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 28 VDSYPLERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKqDVSIDTSiNVGLVTEDGE 107
Cdd:PLN02548 42 ASKYNVEYIAGGATQNSIRVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVNVHYYE-DESTPTG-TCAVLVVGGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 108 RTFVTNRNGSLwKLNIDDVD----FARFSQAKLLSLASIF--NSPlldgKALTEIFTQAKARQMIICADMIKPRLNETL- 180
Cdd:PLN02548 120 RSLVANLSAAN-CYKVEHLKkpenWALVEKAKFYYIAGFFltVSP----ESIMLVAEHAAANNKTFMMNLSAPFICEFFk 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 181 DDICEALSYVDYLFPNFAEAKLLT---GKETLD------EIADCFLACGV--KTVVIKTGKDGCFIKRGDMTMKVP--AV 247
Cdd:PLN02548 195 DQLMEALPYVDFLFGNETEARTFAkvqGWETEDveeialKISALPKASGThkRTVVITQGADPTVVAEDGKVKEFPviPL 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 90111328 248 AGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGAT 297
Cdd:PLN02548 275 PKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCT 324
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
129-301 |
4.32e-13 |
|
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: 68.26 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 129 ARFSQAKLLSLASIfnSPLLDgkalTEIFTQAKARQMIICADM-----IKPrlnetlDDICEALSYVDYLFPNFAEAKLL 203
Cdd:cd01946 110 EHYKDSEFVFLGNI--APELQ----REVLEQVKDPKLVVMDTMnfwisIKP------EKLKKVLAKVDVVIINDGEARQL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 204 TGKETLDEIADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAGITAIDTIGAGDNFASGFIAALLEGKNLREcarfA 283
Cdd:cd01946 178 TGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDTSE----A 253
|
170
....*....|....*...
gi 90111328 284 NATAAISVLSVGATTGVK 301
Cdd:cd01946 254 NMRRAIIYGSAMASFCVE 271
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
41-311 |
8.04e-13 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 68.11 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNRNGS--- 117
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSadm 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 118 LwkLNIDDVDFARFSQAKLLSLASIfnsplldgKALTEIFTQAKARQMIICADM-----IKPRLNETL--------DDIC 184
Cdd:PLN02323 123 L--LRESELDLDLIRKAKIFHYGSI--------SLITEPCRSAHLAAMKIAKEAgallsYDPNLRLPLwpsaeaarEGIM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 185 EALSYVDYLFPNFAEAKLLTGKETL-DEIADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgITAIDTIGAGDNFA 263
Cdd:PLN02323 193 SIWDEADIIKVSDEEVEFLTGGDDPdDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFK-VKAVDTTGAGDAFV 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90111328 264 SGFIAALLEGKN-------LRECARFANATAAISVLSVGATTGVKNRKLVEQLLE 311
Cdd:PLN02323 272 GGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEAVLKLLK 326
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
14-297 |
9.57e-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: 67.06 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 14 VDIPLQPVSKNIFDvdsypleRIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDvsI 93
Cdd:cd01947 16 LDAPPQPGGISHSS-------DSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRD--K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 94 DTSINVGLVTEDGERTFVtnrngslwklNIDDVDFARFSQAKLLSLASIFNSPLLDGKAlteifTQAKARQM---IICAd 170
Cdd:cd01947 87 PTRKTLSFIDPNGERTIT----------VPGERLEDDLKWPILDEGDGVFITAAAVDKE-----AIRKCRETklvILQV- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 171 miKPRlnETLDDICEALSYVDYLFPNFAEAKLLTgketldeIADCFLACGVKTVVIKTGKDGCFIKRGDMTMKVPAVAgI 250
Cdd:cd01947 151 --TPR--VRVDELNQALIPLDILIGSRLDPGELV-------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK-A 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 90111328 251 TAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGAT 297
Cdd:cd01947 219 KVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
181-297 |
9.96e-13 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 67.74 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 181 DDICEALSYVDYLFPNFAEAKLLT-----GKETLDEIADCFLA----CGVK--TVVIKTGKDG--CFIKRGDMTMKVPAV 247
Cdd:PTZ00247 206 ERLLQVLPYVDILFGNEEEAKTFAkamkwDTEDLKEIAARIAMlpkySGTRprLVVFTQGPEPtlIATKDGVTSVPVPPL 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 90111328 248 AGITAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVGAT 297
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCT 335
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
185-271 |
2.37e-12 |
|
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: 64.81 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 185 EALSYVDYLFPNFAEAKLLTGKETLD-----EIADCFLACGVKTVVIKTGKDGCFI-KRGDMTMKVPAVAgITAIDTIGA 258
Cdd:cd00287 105 KLLPGVDILTPNEEEAEALTGRRDLEvkeaaEAAALLLSKGPKVVIVTLGEKGAIVaTRGGTEVHVPAFP-VKVVDTTGA 183
|
90
....*....|...
gi 90111328 259 GDNFASGFIAALL 271
Cdd:cd00287 184 GDAFLAALAAGLA 196
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
8-289 |
3.00e-12 |
|
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: 65.50 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 8 CIGAAIVDIPLQPVSKNIfdvdsypleriamTTGGDAINEATIISRLGHRTALMSRIGKDaagqfildhcrkeNIDIQSL 87
Cdd:cd01937 4 IIGHVTIDEIVTNGSGVV-------------KPGGPATYASLTLSRLGLTVKLVTKVGRD-------------YPDKWSD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 88 KQDVSIDTSINVGLVTEdGERTFVTNRNGSLWKLNIDDVDFARFSQAKLLSLASIFNSPLLD--GKALTEIFTqakarqm 165
Cdd:cd01937 58 LFDNGIEVISLLSTETT-TFELNYTNEGRTRTLLAKCAAIPDTESPLSTITAEIVILGPVPEeiSPSLFRKFA------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 166 IICADM--IKPRLNETLDDICEALSYVDYLFPNFAEAKLLTgkeTLDEIADCFLACGVKTVVIKTGKDGCFIKRGDMTMK 243
Cdd:cd01937 130 FISLDAqgFLRRANQEKLIKCVILKLHDVLKLSRVEAEVIS---TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYT 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 90111328 244 VPAVAGItAIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAI 289
Cdd:cd01937 207 IPASKKD-VVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAK 251
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
36-294 |
9.58e-12 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 64.95 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 36 IAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDIQSLKQDVSIDTSINVGLVTEDGERTFVTNRN 115
Cdd:PRK09954 88 IHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAINDT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 116 GSLWKLNIDDVDFARfsqaKLLSLASIFNSPL-LDGKALTEIFTqakarqmiiCADMIkPRLNETLDD-----ICEALSY 189
Cdd:PRK09954 168 HILQQLTPQLLNGSR----DLIRHAGVVLADCnLTAEALEWVFT---------LADEI-PVFVDTVSEfkagkIKHWLAH 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 190 VDYLFPNFAEAKLLTGKETLDEiADCFLAC------GVKTVVIKTGKDGCFI--KRGDMTMKVPAVAgiTAIDTIGAGDN 261
Cdd:PRK09954 234 IHTLKPTQPELEILWGQAITSD-ADRNAAVnalhqqGVQQIFVYLPDESVFCseKDGEQFLLTAPAH--TTVDSFGADDG 310
|
250 260 270
....*....|....*....|....*....|...
gi 90111328 262 FASGFIAALLEGKNLRECARFANATAAISVLSV 294
Cdd:PRK09954 311 FMAGLVYSFLEGYSFRDSARFAMACAAISRASG 343
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
177-313 |
2.37e-11 |
|
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: 63.51 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 177 NETLDDICEALSYVDYLFPNFAEAKLLTG----------KETLDEIADCFLACGVKT---VVIKTGKDGCFI---KRGDM 240
Cdd:cd01943 168 PENLEDLLQALPRVDVFSPNLEEAARLLGlptsepssdeEKEAVLQALLFSGILQDPgggVVLRCGKLGCYVgsaDSGPE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 241 T------MKVPAVagitaIDTIGAGDNFASGFIAALLEGKNLRECARFAN--ATAAISVLSVGATTGVKNRKL-----VE 307
Cdd:cd01943 248 LwlpayhTKSTKV-----VDPTGGGNSFLGGFAAGLALTKSIDEACIYGSvaASFAIEQVGLPRLTKVEGEELwngetVE 322
|
....*.
gi 90111328 308 QLLEEY 313
Cdd:cd01943 323 ERLKEY 328
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
6-295 |
3.16e-11 |
|
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: 62.81 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 6 VICIGAAIVDIplqpVSKnifdVDSYPLE-RIAMTT------GGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCR 78
Cdd:cd01939 2 VLCVGLTVLDF----ITT----VDKYPFEdSDQRTTngrwqrGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 79 KENIDIQS---LKQDVSIDTSInvgLVTEDGERTFVTNRNgSLWKLNIDDVDFARFSQAKLLSLASIFNSPLLDGKALTE 155
Cdd:cd01939 74 SRGIDISHcyrKDIDEPASSYI---IRSRAGGRTTIVNDN-NLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 156 IFTQAKARQMI-ICADMIKPRlnetlDDICEALSYVDYLFPNFAEAKLLtGKETLDEIADCFLA-CGVKTVVIKT-GKDG 232
Cdd:cd01939 150 EHNNRRPEIRItISVEVEKPR-----EELLELAAYCDVVFVSKDWAQSR-GYKSPEECLRGEGPrAKKAALLVCTwGDQG 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111328 233 --CFIKRGDMTmKVPAVAGITAIDTIGAGDNFASGFIAALLEGK-NLRECARFANATAAISVLSVG 295
Cdd:cd01939 224 agALGPDGEYV-HSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPdDLSEALDFGNRVASQKCTGVG 288
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
41-315 |
3.01e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 60.59 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 41 GGDAINEATIISRLGHRTALMSR--------IGKDAAGQFILDHCRKENIDIQSlkQDVSIDTSINV-GLVTEDGERTFV 111
Cdd:PLN02813 126 GGSLSNTLVALARLGSQSAAGPAlnvamagsVGSDPLGDFYRTKLRRANVHFLS--QPVKDGTTGTViVLTTPDAQRTML 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 112 TNRnGSLWKLNIDDVDFARFSQAKLLslasIFNSPLLDGKALTEIFTQA--KARQ-----MIICADM--IKPRLNETLDD 182
Cdd:PLN02813 204 SYQ-GTSSTVNYDSCLASAISKSRVL----VVEGYLWELPQTIEAIAQAceEAHRagalvAVTASDVscIERHRDDFWDV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 183 ICealSYVDYLFPNFAEAKLLTGKETLD--EIADCFLACGVKTVVIKTGKDGCFIK-RGDMTMKVPAVAGitAIDTIGAG 259
Cdd:PLN02813 279 MG---NYADILFANSDEARALCGLGSEEspESATRYLSHFCPLVSVTDGARGSYIGvKGEAVYIPPSPCV--PVDTCGAG 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111328 260 DNFASGFIAALLEG-KNLRECARFANATAAISVLSVGATTGVKN-RKLVEQLLEEYEG 315
Cdd:PLN02813 354 DAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQGTRLRVEDaVELAESFALHLDG 411
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
39-314 |
5.36e-08 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 53.55 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 39 TTG----GDAINEATIISRLGHRTALMSRIGKDAAGQFilDHCRKENiDIQSLKQDVSIDTSINVGLVTEDGErtfVTNR 114
Cdd:PRK09513 33 TTGlhaaGKGINVAKVLKDLGIDVTVGGFLGKDNQDGF--QQLFSEL-GIANRFQVVQGRTRINVKLTEKDGE---VTDF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 115 NGSLWKLNIDDVD-FARFSQAKLLSLASIFNSPLLDGKALTEIFTQAKARQMIICADMIKPRLNETLddiCEALSYVDYL 193
Cdd:PRK09513 107 NFSGFEVTPADWErFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCPCIIFDSSREAL---VAGLKAAPWL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 194 F-PNFAEAKLLTGKE--TLDEI---ADCFLACGVKTVVIKTGKDGCFI--KRGDMTMKVPAVagiTAIDTIGAGDNFASG 265
Cdd:PRK09513 184 VkPNRRELEIWAGRKlpELKDVieaAHALREQGIAHVVISLGAEGALWvnASGEWIAKPPAC---DVVSTVGAGDSMVGG 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 90111328 266 FIAALLEGKNLRECARFANATAAISVLSvgATTGVKNRKLVEQLLEEYE 314
Cdd:PRK09513 261 LIYGLLMRESSEHTLRLATAVSALAVSQ--SNVGITDRPQLAAMMARVD 307
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
186-286 |
6.16e-08 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 52.59 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 186 ALSYVDYLFPNFAEAKLLTGK-----ETLDEIADCFLACGVKTVVIKTgkdgcfIKRGDMTMKVPAVAGITAIDTI---- 256
Cdd:cd01173 133 LVPLADIITPNQFELELLTGKkindlEDAKAAARALHAKGPKTVVVTS------VELADDDRIEMLGSTATEAWLVqrpk 206
|
90 100 110
....*....|....*....|....*....|....*...
gi 90111328 257 --------GAGDNFASGFIAALLEGKNLRECARFANAT 286
Cdd:cd01173 207 ipfpayfnGTGDLFAALLLARLLKGKSLAEALEKALNF 244
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
224-295 |
9.33e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 52.89 E-value: 9.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111328 224 VVIKTGKDGCFIKRGDMTMKVPAVAGITaIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLSVG 295
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQ-VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
6-293 |
2.16e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 51.53 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 6 VICIGAAIVDIP-LQPVSKNIfdVDSYPlERIAMTTGGDAINEATIISRLGHRTALMSRIGKDAAGQFILDHCRKENIDI 84
Cdd:PRK09850 7 VVIIGSANIDVAgYSHESLNY--ADSNP-GKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 85 QSLKQDVSIDTSINVGLVTEDGERTFVTNrngslwKLNIDDVDFARF--SQAKLLSLASIFNSPL-LDGKALTEIFTQAK 161
Cdd:PRK09850 84 DKCLIVPGENTSSYLSLLDNTGEMLVAIN------DMNISNAITAEYlaQHREFIQRAKVIVADCnISEEALAWILDNAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 162 ARQMiicadMIKPRLNETLDDICEALSYVDYLFPNFAEAKLLTG-----KETLDEIADCFLACGVKTVVIKTGKDGCFI- 235
Cdd:PRK09850 158 NVPV-----FVDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGialsgREDVAKVAAWFHQHGLNRLVLSMGGDGVYYs 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111328 236 -KRGDMTMKVPAVAGItaIDTIGAGDNFASGFIAALLEGKNLRECARFANATAAISVLS 293
Cdd:PRK09850 233 dISGESGWSAPIKTNV--INVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALSC 289
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
178-286 |
2.43e-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: 50.92 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 178 ETLDDICE-ALSYVDYLFPNFAEAKLLTGKE--TLDEI---ADCFLACGVKTVVIkTGkdgcfIKRGDMTMKVPAVAGIT 251
Cdd:COG2240 126 GIAEFIMRrLVPLADIITPNLTELALLTGRPyeTLEEAlaaARALLALGPKIVVV-TS-----VPLDDTPADKIGNLAVT 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 90111328 252 A------------IDTIGAGDNFASGFIAALLEGKNLRECARFANAT 286
Cdd:COG2240 200 AdgawlvetpllpFSPNGTGDLFAALLLAHLLRGKSLEEALERAAAF 246
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
177-283 |
9.54e-07 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 49.29 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 177 NETLDDICEALSYVDYLFPNFAEAKLLTGKE--TLDEI---ADCFLACGVKTVVIKTGK------------DGCFIKrgd 239
Cdd:PRK12413 117 SELRQELIQFFPYVTVITPNLVEAELLSGKEikTLEDMkeaAKKLYDLGAKAVVIKGGNrlsqkkaidlfyDGKEFV--- 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 90111328 240 mTMKVPAVAGitaiDTIGAGDNFASGFIAALLEGKNLRECARFA 283
Cdd:PRK12413 194 -ILESPVLEK----NNIGAGCTFASSIASQLVKGKSPLEAVKNS 232
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
178-268 |
4.75e-06 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 47.38 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 178 ETLDDICEALSYVDYLFPNFAEAKLLTGKETLD-----EIADCFLACGVKTVVIKT-----------------GKDGCFI 235
Cdd:PTZ00344 128 EVVDAYRELIPYADVITPNQFEASLLSGVEVKDlsdalEAIDWFHEQGIPVVVITSfrededpthlrfllscrDKDTKNN 207
|
90 100 110
....*....|....*....|....*....|...
gi 90111328 236 KRgdMTMKVPAVAGitaiDTIGAGDNFASGFIA 268
Cdd:PTZ00344 208 KR--FTGKVPYIEG----RYTGTGDLFAALLLA 234
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
195-290 |
1.26e-03 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 39.72 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111328 195 PNFAEAKLLTGKETLDEIADC------FLACGVKTVVIKTG--------KDGCFIKRGDMTMKVPAVAGItaiDTIGAGD 260
Cdd:PRK06427 139 PNLPEAEALTGLPIADTEDEMkaaaraLHALGCKAVLIKGGhlldgeesVDWLFDGEGEERFSAPRIPTK---NTHGTGC 215
|
90 100 110
....*....|....*....|....*....|...
gi 90111328 261 NFASGfIAALL-EGKNLRECARFANA--TAAIS 290
Cdd:PRK06427 216 TLSAA-IAAELaKGASLLDAVQTAKDyvTRAIR 247
|
|
| |
