|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
2-278 |
0e+00 |
|
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: 522.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 2 SLLVVGSVAFDAVETPFGKIDKMLGGSASHFSISASYFTDVRIVGVVGGDFTDAEQKVFDSHNVETSDLERVPDGETFRW 81
Cdd:cd01946 1 SLLVVGSVAFDAIETPFGKVDKALGGSATYFSLSASYFTDVRLVGVVGEDFPEEDYKLLNSHNIVTLGLLSKEDGKTFHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 82 YGRYDYDLNVAHTLDTKLNVFADFKPKLSSQSKSSRLVFLGNIQPDLQREVRQQIPDAELVALDTMNLWIETTRESLMKT 161
Cdd:cd01946 81 AGRYHYDLNEADTLDTDLNVFADFDPQLPEHYKDSEFVFLGNIAPELQREVLEQVKDPKLVVMDTMNFWISIKPEKLKKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 162 IQGVDVVIINDAEARQLTELPNLIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVFDPTGAGDTFAGGF 241
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGF 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 31789445 242 MGYLSSQPTLDEAAMRRAMIFGSVMASFNVEEFGTAR 278
Cdd:cd01946 241 IGYLASQKDTSEANMRRAIIYGSAMASFCVEDFGTKR 277
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
2-287 |
1.39e-46 |
|
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: 158.89 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 2 SLLVVGSVAFDAVETPF-----------GKIDKMLGGSASHFSISASYFT-DVRIVGVVGGD-FTDAEQKVFDSHNVETS 68
Cdd:COG0524 1 DVLVIGEALVDLVARVDrlpkggetvlaGSFRRSPGGAAANVAVALARLGaRVALVGAVGDDpFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 69 DLERVPDGETFRWYGRYDYDLNvaHTLDTKLNVFADFKPKLSSQS--KSSRLVFLG------NIQPDLQREVRQQIPDAE 140
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGE--RTIVFYRGANAELTPEDLDEAllAGADILHLGgitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 141 -LVALDTM---NLWiETTRESLMKTIQGVDVVIINDAEARQLTELPNLIKAARAILSWGPRALIVKRGEYGAALFTNDSY 216
Cdd:COG0524 159 vPVSLDPNyrpALW-EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31789445 217 FAIPAYPLEsVFDPTGAGDTFAGGFMGYLssqptLDEAAMRRAMIFGSVMASFNVEEFGtARVQRLTYDEI 287
Cdd:COG0524 238 VHVPAFPVE-VVDTTGAGDAFAAGFLAGL-----LEGLDLEEALRFANAAAALVVTRPG-AQPALPTREEV 301
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
2-276 |
2.05e-26 |
|
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: 105.09 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 2 SLLVVGSVAFDAV--ETPFGKIDK---------MLGGSASHFSISASYF-TDVRIVGVVGGDFTDAE-QKVFDSHNVETS 68
Cdd:cd01942 1 DVAVVGHLNYDIIlkVESFPGPFEsvlvkdlrrEFGGSAGNTAVALAKLgLSPGLVAAVGEDFHGRLyLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 69 DLERVPDGETFRWYGRYDYDLNvahtldtklNVFADFKPKLSSQSKSSRLVFLGN---IQPDLQREVrqqIPDAE----- 140
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDN---------QIAYFYPGAMDELEPNDEADPDGLadiVHLSSGPGL---IELARelaag 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 141 --LVALDTMNLWIETTRESLMKTIQGVDVVIINDAEARQLTELPNLIKAARAIlswGPRALIVKRGEYGAALFTNDSYFA 218
Cdd:cd01942 149 giTVSFDPGQELPRLSGEELEEILERADILFVNDYEAELLKERTGLSEAELAS---GVRVVVVTLGPKGAIVFEDGEEVE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 31789445 219 IPAYPLESVFDPTGAGDTFAGGFM-GYLSSQPTLDeaamrrAMIFGSVMASFNVEEFGT 276
Cdd:cd01942 226 VPAVPAVKVVDTTGAGDAFRAGFLyGLLRGYDLEE------SLRLGNLAASLKVERRGA 278
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
2-277 |
2.79e-23 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 97.03 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 2 SLLVVGSVAFDAVETPFGKID---------KMLGGSASHFSISASYF-TDVRIVGVVGGDFTDAE-QKVFDSHNVETSDL 70
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGelvrvstveKGPGGKGANVAVALARLgGDVAFIGAVGDDNFGEFlLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 71 ERVPDGETFRWYGRYDYDLNvaHTLDTKLNVFADFKPKLSSQS----KSSRLVFLGNIQPD--------LQREVRQQIPD 138
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGE--RTIVFNRGAAADLTPEELEENedllENADLLYISGSLPLglpeatleELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 139 AELVALDTmnLWIetTRESLMKTIQGVDVVIINDAEARQLTELPN-----LIKAARAILSWGPRALIVKRGEYGAALFTN 213
Cdd:pfam00294 159 FDPNLLDP--LGA--AREALLELLPLADLLKPNEEELEALTGAKLddieeALAALHKLLAKGIKTVIVTLGADGALVVEG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31789445 214 DSYFAIPAYPLESVFDPTGAGDTFAGGFMGYLSSQPTLDEAAmrramIFGSVMASFNVEEFGTA 277
Cdd:pfam00294 235 DGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEAL-----RFANAAAALVVQKSGAQ 293
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
162-277 |
1.93e-21 |
|
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: 91.84 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 162 IQGVDVVIINDAEARQLTELP-----NLIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVfDPTGAGDT 236
Cdd:cd01174 173 LALVDILVPNETEAALLTGIEvtdeeDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAV-DTTGAGDT 251
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 31789445 237 FAGGFMGYLSSQPTLdEAAMRRAMIFgsvmASFNVEEFGTA 277
Cdd:cd01174 252 FIGALAAALARGLSL-EEAIRFANAA----AALSVTRPGAQ 287
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
155-276 |
4.10e-21 |
|
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: 91.52 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 155 RESLMKTIQGVDVVIINDAEARQLTELP--NLIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVFDPTG 232
Cdd:cd01168 191 KEALLELLPYVDILFGNEEEAEALAEAEttDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNG 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 31789445 233 AGDTFAGGFM-GYLSSQPtLDEAAMrramiFGSVMASFNVEEFGT 276
Cdd:cd01168 271 AGDAFAGGFLyGLVQGEP-LEECIR-----LGSYAAAEVIQQLGP 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
21-271 |
4.63e-20 |
|
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: 88.02 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 21 IDKMLGGSASHFSISASYF-TDVRIVGVVGGD-FTDAEQKVFDSHNVETSDLERVPDGET---FRWYGR-------YDYD 88
Cdd:cd01166 26 FRKFFGGAEANVAVGLARLgHRVALVTAVGDDpFGRFILAELRREGVDTSHVRVDPGRPTglyFLEIGAggerrvlYYRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 89 LNVAHTLDTKLNVFADFKpklssqskSSRLVFLGNIQPDLQREVRQQIPDA--------ELVALDTM---NLW-IETTRE 156
Cdd:cd01166 106 GSAASRLTPEDLDEAALA--------GADHLHLSGITLALSESAREALLEAleaakargVTVSFDLNyrpKLWsAEEARE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 157 SLMKTIQGVDVVIINDAEARQLTELPNLIKAARAILSW--GPRALIVKRGEYGAALFTNDSYFAIPAYPLEsVFDPTGAG 234
Cdd:cd01166 178 ALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALalGVKAVVVKLGAEGALVYTGGGRVFVPAYPVE-VVDTTGAG 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 31789445 235 DTFAGGFM-GYLSSQPtldeaaMRRAMIFGSVMASFNV 271
Cdd:cd01166 257 DAFAAGFLaGLLEGWD------LEEALRFANAAAALVV 288
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
115-245 |
8.39e-19 |
|
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: 82.53 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 115 SSRLVFLGNIQPDLQReVRQQIPDAE----LVALDTMNLWIETTRESLMKTIQGVDVVIINDAEARQLTELPNL-----I 185
Cdd:cd00287 57 GADAVVISGLSPAPEA-VLDALEEARrrgvPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLevkeaA 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31789445 186 KAARAILSWGPRALIVKRGEYGAALFTND-SYFAIPAYPlESVFDPTGAGDTFAGGFMGYL 245
Cdd:cd00287 136 EAAALLLSKGPKVVIVTLGEKGAIVATRGgTEVHVPAFP-VKVVDTTGAGDAFLAALAAGL 195
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
163-287 |
1.06e-14 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 73.31 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 163 QGVDVVIINDAEARQLTELP-----NLIKAARAILS-WGPRALIVKRGEYGAALFTND-SYFAIPAYPLEsVFDPTGAGD 235
Cdd:COG2870 197 RGATLLTPNLKEAEAAVGIPiadeeELVAAAAELLErLGLEALLVTRGEEGMTLFDADgPPHHLPAQARE-VFDVTGAGD 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 31789445 236 TFAGGFMGYLSSQPTLDEAAmrramIFGSVMASFNVEEFGTARVqrlTYDEI 287
Cdd:COG2870 276 TVIATLALALAAGASLEEAA-----ELANLAAGIVVGKLGTATV---SPEEL 319
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
142-290 |
1.33e-14 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 72.86 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 142 VALDTmnlwietTRESLMKTIQ-GVDVVIINDAEARQLTELP-----NLIKAARAILSWGPRALIVKRGEYGAALFTNDS 215
Cdd:COG1105 161 VVLDT-------SGEALKAALEaGPDLIKPNLEELEELLGRPletleDIIAAARELLERGAENVVVSLGADGALLVTEDG 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31789445 216 YFAIPAYPLESVfDPTGAGDTFAGGFMGYLSSQPTLDEAAmRRAMIFGSVmasfNVEEFGTARVQRLTYDEINER 290
Cdd:COG1105 234 VYRAKPPKVEVV-STVGAGDSMVAGFLAGLARGLDLEEAL-RLAVAAGAA----AALSPGTGLPDREDVEELLAQ 302
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-268 |
3.48e-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: 71.51 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 4 LVVGSVAFDAVETPFGKID---KMLGGSASHFSISASYF-TDVRIVGVVGGD-FTDAEQKVFDSHNVETSDLERVP---- 74
Cdd:cd01167 3 VCFGEALIDFIPEGSGAPEtftKAPGGAPANVAVALARLgGKAAFIGKVGDDeFGDFLLETLKEAGVDTRGIQFDPaapt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 75 ---------DGE-TFRWYGRYDYDLNvahtLDTKLNvfadfKPKLSSqsksSRLVFLGNI---QPDLQREVRQQIPDAE- 140
Cdd:cd01167 83 tlafvtldaDGErSFEFYRGPAADLL----LDTELN-----PDLLSE----ADILHFGSIalaSEPSRSALLELLEAAKk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 141 ---LVALDT---MNLW--IETTRESLMKTIQGVDVVIINDAEARQLTELPNLIKAARAILSWGPRALIVKRGEYGAALFT 212
Cdd:cd01167 150 agvLISFDPnlrPPLWrdEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 31789445 213 NDSYFAIPAYPLESVfDPTGAGDTFAGGFMGYLSSQP--TLDEAAMRRAMIFGSVMAS 268
Cdd:cd01167 230 KGGVGEVPGIPVEVV-DTTGAGDAFVAGLLAQLLSRGllALDEDELAEALRFANAVGA 286
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
4-279 |
4.57e-14 |
|
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: 71.44 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 4 LVVGSVAFD-----AVE----------TPFGKIDKMLGGS---ASHFsisASYFTDVRIVGVVGGDfTDAE--QKVFDSH 63
Cdd:cd01172 3 LVVGDVILDeylygDVErispeapvpvVKVEREEIRLGGAanvANNL---ASLGAKVTLLGVVGDD-EAGDllRKLLEKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 64 NVETsDLERVPDGETfrwygrydydlnvahtlDTKLNVFADFKpKLSSQSKSSRLVFLGNIQPDLQREVRQQIPDAELVA 143
Cdd:cd01172 79 GIDT-DGIVDEGRPT-----------------TTKTRVIARNQ-QLLRVDREDDSPLSAEEEQRLIERIAERLPEADVVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 144 L-DTMN-LWIETTRESLMKTI--QGVDVVI-----------------INDAEARQLTELP-----NLIKAARAILS-WGP 196
Cdd:cd01172 140 LsDYGKgVLTPRVIEALIAAAreLGIPVLVdpkgrdyskyrgatlltPNEKEAREALGDEindddELEAAGEKLLElLNL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 197 RALIVKRGEYGAALFT-NDSYFAIPAYPLEsVFDPTGAGDTFAGGFMGYLSSQPTLDEAAMrramiFGSVMASFNVEEFG 275
Cdd:cd01172 220 EALLVTLGEEGMTLFErDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAF-----LANAAAGVVVGKVG 293
|
....
gi 31789445 276 TARV 279
Cdd:cd01172 294 TAPV 297
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
3-272 |
1.42e-13 |
|
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: 69.35 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 3 LLVVGSVAFDAVETPfGKIDKMLGGSASHFSISASYFT-DVRIVGVVGGDFTDAEQKVFDSHNVETSDlervPDGETFRW 81
Cdd:cd01937 2 IVIIGHVTIDEIVTN-GSGVVKPGGPATYASLTLSRLGlTVKLVTKVGRDYPDKWSDLFDNGIEVISL----LSTETTTF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 82 YGRYDYDLNvahtlDTKLNVFADFKPKLSSQSK--SSRLVFLGNIQPDLQREVRQQIpdaELVALDTMNLW--IETTRES 157
Cdd:cd01937 77 ELNYTNEGR-----TRTLLAKCAAIPDTESPLStiTAEIVILGPVPEEISPSLFRKF---AFISLDAQGFLrrANQEKLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 158 LMKTIQGVDVVIINDAEARQLTELpnlIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVfDPTGAGDTF 237
Cdd:cd01937 149 KCVILKLHDVLKLSRVEAEVISTP---TELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVV-DPTGAGDVF 224
|
250 260 270
....*....|....*....|....*....|....*
gi 31789445 238 AGGFMGYLSSQPTLDEAAMrramiFGSVMASFNVE 272
Cdd:cd01937 225 LAAFLYSRLSGKDIKEAAE-----FAAAAAAKFIE 254
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-275 |
8.69e-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: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 3 LLVVGSVAFDAvetpFGKIDKMLG-GSASHFSISASYF---------------TDVRIVGVVGGDFtDAEQKVFDSHNVE 66
Cdd:cd01947 2 IAVVGHVEWDI----FLSLDAPPQpGGISHSSDSRESPgggganvavqlaklgNDVRFFSNLGRDE-IGIQSLEELESGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 67 TSDLERVPDGETFRWYGRYDYDLNVAhTLDTKLNVFADFKPklsSQSKSSRLVFLGNIQPDlqREVRQQIPDAELVALDT 146
Cdd:cd01947 77 DKHTVAWRDKPTRKTLSFIDPNGERT-ITVPGERLEDDLKW---PILDEGDGVFITAAAVD--KEAIRKCRETKLVILQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 147 mnlwieTTRESLM---KTIQGVDVVIINDAEARQLTelpnlikAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYP 223
Cdd:cd01947 151 ------TPRVRVDelnQALIPLDILIGSRLDPGELV-------VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 31789445 224 lESVFDPTGAGDTFAGGFMGYLSSQPTLDEaamrrAMIFGSVMASFNVEEFG 275
Cdd:cd01947 218 -AKVPDSTGAGDSFAAGFIYGLLKGWSIEE-----ALELGAQCGAICVSHFG 263
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
24-291 |
8.70e-13 |
|
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: 67.75 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 24 MLGGSASHFSISASYFT----DVRIVGVV--GGDFTDAEQKVFDSHNVETSdLERVPDGETFRWYGRYDY-DLNVAHTLD 96
Cdd:cd01943 24 VLGGAGTYAILGARLFLppplSRSISWIVdkGSDFPKSVEDELESWGTGMV-FRRDPGRLTTRGLNIYDGnDRRFFKYLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 97 TKL-----NVFADFKPKLSSQ-----SKSSRLVFLGNIQPDLQREVRQQIPDAELVALDTMNLWIETTRESLMKTIQGVD 166
Cdd:cd01943 103 PKKridvsDDLNSTPLIRSSCihlicSPERCASIVDDIINLFKLLKGNSPTRPKIVWEPLPDSCDPENLEDLLQALPRVD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 167 VVIINDAEARQLTELP--------------NLIKAARAILSWGPrALIVKRGEYGAALFTNDS--YFAIPAY--PLESVF 228
Cdd:cd01943 183 VFSPNLEEAARLLGLPtsepssdeekeavlQALLFSGILQDPGG-GVVLRCGKLGCYVGSADSgpELWLPAYhtKSTKVV 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31789445 229 DPTGAGDTFAGGFMGYLSSQPTLDEAAmrramIFGSVMASFNVEEFGtarVQRLTYDEINERF 291
Cdd:cd01943 262 DPTGGGNSFLGGFAAGLALTKSIDEAC-----IYGSVAASFAIEQVG---LPRLTKVEGEELW 316
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
151-268 |
1.19e-11 |
|
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: 64.09 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 151 IETTRESLMKTIQ-GVDVVIINDAEARQLTELPN-----LIKAARAILSWGPRALIVKRGEYGAALFTND-SYFAIPayP 223
Cdd:cd01164 163 LDTSGEALLAALAaKPFLIKPNREELEELFGRPLgdeedVIAAARKLIERGAENVLVSLGADGALLVTKDgVYRASP--P 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 31789445 224 LESVFDPTGAGDTFAGGFMGYLSSQPTLDEAAmRRAMIFGSVMAS 268
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEAL-RLAVAAGSATAF 284
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
166-259 |
8.54e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 62.54 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 166 DVVIINDAEARQLTELPNLIKAARAILSWGPRA--LIVKRGEYGAALFTNDSYFAIPAYPLEsVFDPTGAGDTFAGGF-M 242
Cdd:PLN02341 287 DVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVN-VVDTVGCGDSFAAAIaL 365
|
90
....*....|....*..
gi 31789445 243 GYLSSQPTLDEAAMRRA 259
Cdd:PLN02341 366 GYIHNLPLVNTLTLANA 382
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-272 |
9.68e-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: 61.56 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 3 LLVVGSVAFDAvetpFGKIDKMLGGSASH-----FSI----------SASYFTDVRIVGVVGgdfTDAEQKVFDSHnVET 67
Cdd:cd01941 2 IVVIGAANIDL----RGKVSGSLVPGTSNpghvkQSPggvgrniaenLARLGVSVALLSAVG---DDSEGESILEE-SEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 68 SDLERVPDGETFRWYGRY------DYDLNVAhtldtklnvFADfkpklssqskssrLVFLGNIQPDLQREVRQQIPDAEL 141
Cdd:cd01941 74 AGLNVRGIVFEGRSTASYtaildkDGDLVVA---------LAD-------------MDIYELLTPDFLRKIREALKEAKP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 142 VALD------TMNLWIETTRESLMKT----------------IQGVDVVIINDAEARQLTELP-----NLIKAARAILSW 194
Cdd:cd01941 132 IVVDanlpeeALEYLLALAAKHGVPVafeptsapklkklfylLHAIDLLTPNRAELEALAGALienneDENKAAKILLLP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 195 GPRALIVKRGEYGAALF---TNDSYFAIPAYPLESVFDPTGAGDTFAGGFMGYLSSQPTLDEAAmrramIFGSVMASFNV 271
Cdd:cd01941 212 GIKNVIVTLGAKGVLLSsreGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSL-----RFAQAAAALTL 286
|
.
gi 31789445 272 E 272
Cdd:cd01941 287 E 287
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
151-277 |
1.81e-10 |
|
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: 60.50 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 151 IETTRESLMKTIQGVDVVII----------NDAEARQLTELPNLIKAARAILSWGpralivkrgEYGA-ALFTNDSYFAI 219
Cdd:cd01939 166 VEKPREELLELAAYCDVVFVskdwaqsrgyKSPEECLRGEGPRAKKAALLVCTWG---------DQGAgALGPDGEYVHS 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 31789445 220 PAYPLESVFDPTGAGDTFAGGFMGYLSSQPTldeaAMRRAMIFGSVMASFNVEEFGTA 277
Cdd:cd01939 237 PAHKPIRVVDTLGAGDTFNAAVIYALNKGPD----DLSEALDFGNRVASQKCTGVGFD 290
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
23-262 |
6.97e-10 |
|
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: 58.52 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 23 KMLGGSASHFsisasyftdvrivGVVGGDftDAEQKVFD---SHNVETSDLeRVPDGETfrwygrydydlnvAHTLDT-- 97
Cdd:cd01940 33 KRLGHESAYI-------------GAVGND--DAGAHVRStlkRLGVDISHC-RVKEGEN-------------AVADVElv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 98 ---------KLNVFADFKPKLSSQS--KSSRLVFLG--NIQPDLQREVRQQIPDAELVALDTMNLWietTRESLMKTIQG 164
Cdd:cd01940 84 dgdrifglsNKGGVAREHPFEADLEylSQFDLVHTGiySHEGHLEKALQALVGAGALISFDFSDRW---DDDYLQLVCPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 165 VDVVIINdaeARQLTElPNLIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVfDPTGAGDTFAGGFMGY 244
Cdd:cd01940 161 VDFAFFS---ASDLSD-EEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVV-DTLGAGDSFIAGFLLS 235
|
250
....*....|....*...
gi 31789445 245 LSSQPTLDEAAMRRAMIF 262
Cdd:cd01940 236 LLAGGTAIAEAMRQGAQF 253
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
26-278 |
1.17e-09 |
|
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: 58.07 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 26 GGSASHFSISASYF-TDVRIVGVVGGDFTDAEQKVFD-SHNVETSDLERVPDGETFRWYGRYDydlnvAHTLDTKLNVFA 103
Cdd:cd01945 36 GGNAANAAVAVARLgGQARLIGVVGDDAIGRLILAELaAEGVDTSFIVVAPGARSPISSITDI-----TGDRATISITAI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 104 DFKPKLSSQS----KSSRLVFLGNIQPD----LQREVRQQ-IPDaeLVALDTmnlWIETTRESLMKTiqgVDVVIINDAE 174
Cdd:cd01945 111 DTQAAPDSLPdailGGADAVLVDGRQPEaalhLAQEARARgIPI--PLDLDG---GGLRVLEELLPL---ADHAICSENF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 175 ARQLTELPnLIKAARAILSWGPRALIVKRGEYGA-ALFTNDSYFAIPAYPLESVfDPTGAGDTFAGGFM-GYLSSQPTld 252
Cdd:cd01945 183 LRPNTGSA-DDEALELLASLGIPFVAVTLGEAGClWLERDGELFHVPAFPVEVV-DTTGAGDVFHGAFAhALAEGMPL-- 258
|
250 260
....*....|....*....|....*.
gi 31789445 253 eaamRRAMIFGSVMASFNVEEFGTAR 278
Cdd:cd01945 259 ----REALRFASAAAALKCRGLGGRA 280
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
4-290 |
1.30e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 58.28 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 4 LVVGSVAFDAVETPFGKIDKMLGGSASHFSisasyftdvrivgvvggdftdaeqKVFDSHNVETSDLERVpdGETFRWyg 83
Cdd:PLN02630 15 LIVGNYCHDVLIQNGSVTAESLGGAASFIS------------------------NVLDALSVECELVSKV--GPDFLY-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 84 RYDYDLNVAHTLDTKLnVFADFKPKLSSQSKSSRLVFLGNIQ--------PDLQREVRQQIPDAELVALDTMNLWIETTR 155
Cdd:PLN02630 67 QVSHPPIVIPDSKTTE-FHADFDQGIDGNGHEDRVLKRVCACdpiepsdiPDMRYEFGMAVGVAGEILPETLERMVEICD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 156 ------ESLMKTIQGVDVVI----INDAEARQLTELPNLIKAARA---------ILSWgpRALIVKRGEYGAALFTNDSY 216
Cdd:PLN02630 146 vvvvdiQALIRVFDPVDGTVklvkLEETGFYDMLPRIGFLKASSEealfidveeVRQK--CCVIVTNGKKGCRIYWKDGE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31789445 217 FAIPAYPLESVfDPTGAGDTFAGGFMGYLssqptLDEAAMRRAMIFGSVMASFNVEEFG----TARVQRLTYDEINER 290
Cdd:PLN02630 224 MRVPPFPAIQV-DPTGAGDSFLGGFVAGL-----VQGLAVPDAALLGNYFGSLAVEQVGipkfDLRQLQRVKDEVQRR 295
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
155-261 |
2.06e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 54.56 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 155 RESLMKTIQGVDVVIINDAEARQLTELPNLIKAARAILS-WGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVfDPTGA 233
Cdd:PRK09434 171 RECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADrYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPV-DTTGA 249
|
90 100
....*....|....*....|....*...
gi 31789445 234 GDTFAGGFMGYLSSQPTLDEAAMRRAMI 261
Cdd:PRK09434 250 GDAFVAGLLAGLSQAGLWTDEAELAEII 277
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
3-289 |
1.30e-07 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 52.43 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 3 LLVVGSVAFDAV----------ETPFGK-IDKMLGGSASHFSISASYF-TDVRIVGVVGGD-FTDAEQKVFDSHNVETSD 69
Cdd:PTZ00292 18 VVVVGSSNTDLIgyvdrmpqvgETLHGTsFHKGFGGKGANQAVMASKLgAKVAMVGMVGTDgFGSDTIKNFKRNGVNTSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 70 LERVPDGETfrwygrydydlNVAHtldtklnVFADFKpklSSQSKssrLVFLGN----IQPDLQREVRQQIPDAELVALD 145
Cdd:PTZ00292 98 VSRTENSST-----------GLAM-------IFVDTK---TGNNE---IVIIPGannaLTPQMVDAQTDNIQNICKYLIC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 146 TMNLWIETTRESL-------MKTI-------------------QGVDVVIINDAEARQLT-----ELPNLIKAARAILSW 194
Cdd:PTZ00292 154 QNEIPLETTLDALkeakergCYTVfnpapapklaeveiikpflKYVSLFCVNEVEAALITgmevtDTESAFKASKELQQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 195 GPRALIVKRGEYGAALFTNDS-YFAIPAYPLESVfDPTGAGDTFAGGFMGYLSSQPTLDEAAMRRAMIfgsvmASFNVEE 273
Cdd:PTZ00292 234 GVENVIITLGANGCLIVEKENePVHVPGKRVKAV-DTTGAGDCFVGSMAYFMSRGKDLKESCKRANRI-----AAISVTR 307
|
330
....*....|....*.
gi 31789445 274 FGTarvqRLTYDEINE 289
Cdd:PTZ00292 308 HGT----QSSYPHPSE 319
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
149-275 |
1.31e-07 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 52.32 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 149 LW--IETTRESLMKTIQGVDVVIINDAEARQLTELPNlIKAARAILSWGPRA--LIVKRGEYGAALFTNDSYFAIPAYPL 224
Cdd:PLN02323 180 LWpsAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDD-PDDDTVVKLWHPNLklLLVTEGEEGCRYYTKDFKGRVEGFKV 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 31789445 225 ESVfDPTGAGDTFAGGFMGYLSSQPTL--DEAAMRRAMIFGSVMASFNVEEFG 275
Cdd:PLN02323 259 KAV-DTTGAGDAFVGGLLSQLAKDLSLleDEERLREALRFANACGAITTTERG 310
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
151-260 |
3.91e-07 |
|
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: 50.28 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 151 IETTRESLMktiQGVDVVIINDAEARQLTELP-----NLIKAARAILSWGPRALIVK------RGEYGAALFTNDS--YF 217
Cdd:cd01173 126 VPVYRDLLV---PLADIITPNQFELELLTGKKindleDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEawLV 202
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31789445 218 AIPAYPLESVFdpTGAGDTFAGGFMGYLSSQPTLDEAAmRRAM 260
Cdd:cd01173 203 QRPKIPFPAYF--NGTGDLFAALLLARLLKGKSLAEAL-EKAL 242
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
104-305 |
5.43e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 50.58 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 104 DFKPKLSSQSKSSRLV----FLGNIqPDLQREVRQQIPDAE----LVALDTMNL-WIETTRESLMKTI-QGVDVVIINDA 173
Cdd:PLN02813 213 NYDSCLASAISKSRVLvvegYLWEL-PQTIEAIAQACEEAHragaLVAVTASDVsCIERHRDDFWDVMgNYADILFANSD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 174 EARQLTELP---NLIKAARAILSWGPRAlIVKRGEYGAALFTNDSYFAIPAYPLESVfDPTGAGDTFAGGFM-GYLSSQP 249
Cdd:PLN02813 292 EARALCGLGseeSPESATRYLSHFCPLV-SVTDGARGSYIGVKGEAVYIPPSPCVPV-DTCGAGDAYAAGILyGLLRGVS 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 31789445 250 TLdeaamRRAMIFGSVMASFNVEEFGTarvqRLTYDEINERFHAFKEmtHFEEIPF 305
Cdd:PLN02813 370 DL-----RGMGELAARVAATVVGQQGT----RLRVEDAVELAESFAL--HLDGSDM 414
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
156-253 |
1.90e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.79 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 156 ESLMKTIQGVDVVIINDAEARQLTE-----LPNLIKAARAILSWGP------RALIVKRGEYGAALFTNDSYFAIPAYPL 224
Cdd:PTZ00247 206 ERLLQVLPYVDILFGNEEEAKTFAKamkwdTEDLKEIAARIAMLPKysgtrpRLVVFTQGPEPTLIATKDGVTSVPVPPL 285
|
90 100 110
....*....|....*....|....*....|.
gi 31789445 225 --ESVFDPTGAGDTFAGGFMGYLSSQPTLDE 253
Cdd:PTZ00247 286 dqEKIVDTNGAGDAFVGGFLAQYANGKDIDR 316
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
155-272 |
5.31e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 41.31 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 155 RESLMKTIQG--VDVVIINDAEARQLT--ELPNLIKAARAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLESVFDP 230
Cdd:PLN02379 221 RSPLLQLLESgkIDLCFANEDEARELLrgEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDA 300
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 31789445 231 TGAGDTFAGGFMGYLSSQPTLDEAAMRRAMIFGSVMASFNVE 272
Cdd:PLN02379 301 TGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGE 342
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
136-257 |
7.84e-04 |
|
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: 40.48 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 136 IPDAELVALDTMNLWIETTRESLMKTIQGVDVVIinDAEARQLTelpnlikAARAILswgpraLIVKRGEYGAALF-TND 214
Cdd:cd01944 170 IPDTILQALMAKRPIWSCNREEAAIFAERGDPAA--EASALRIY-------AKTAAP------VVVRLGSNGAWIRlPDG 234
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31789445 215 SYFAIPAYPLESVfDPTGAGDTFAGGFMGYLSSQPTLDEAAMR 257
Cdd:cd01944 235 NTHIIPGFKVKAV-DTIGAGDTHAGGMLAGLAKGMSLADAVLL 276
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
189-275 |
1.33e-03 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 39.72 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 189 RAILSWGPRALIVKRGEYGAALFTNDSYFAIPAYPLEsVFDPTGAGDTFAGGFM-GYLSSQPTldEAAMRRamifGSVMA 267
Cdd:PRK09813 178 KAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVT-VVDTMGAGDSFIAGFLcGWLAGMTL--PQAMAQ----GTACA 250
|
....*...
gi 31789445 268 SFNVEEFG 275
Cdd:PRK09813 251 AKTIQYHG 258
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
151-271 |
1.33e-03 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 39.39 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 151 IETTRESLMKTiqgVDVVIINDAEARQLT-----ELPNLIKAARAILSWGPRALIVK----RGEYGAA---LFTNDSYFA 218
Cdd:pfam08543 109 IEALKEELLPL---ATLITPNLPEAEALTgrkikTLEDMKEAAKKLLALGAKAVLIKgghlEGEEAVVtdvLYDGGGFYT 185
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 31789445 219 IPAypleSVFDPT---GAGDTFAGGFMGYLSSQPTLDEAAMR-RAMIFGSVMASFNV 271
Cdd:pfam08543 186 LEA----PRIPTKnthGTGCTLSAAIAANLAKGLSLPEAVREaKEYVTEAIRDALNL 238
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
41-281 |
4.48e-03 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 38.66 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 41 DVRIVGVVGGD-FTDAEQKVFDSHNVEtSDLERVPDGETFrwygrydydlnvahtldTKLNVfadfkpkLSSQSKSSRLV 119
Cdd:PRK11316 66 QARLVGLTGIDeAARALSKLLAAVGVK-CDFVSVPTHPTI-----------------TKLRV-------LSRNQQLIRLD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 120 F---LGNIQPD-LQREVRQQIPDAELV--------ALDTMNLWIETTREslmktiQGVDVVII---NDAE----ARQLTe 180
Cdd:PRK11316 121 FeegFEGVDPQpLLERIEQALPSIGALvlsdyakgALASVQAMIQLARK------AGVPVLIDpkgTDFEryrgATLLT- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31789445 181 lPN----------------LIKAARAILS-WGPRALIVKRGEYGAALFT-NDSYFAIPAYPLEsVFDPTGAGDTFAGGFM 242
Cdd:PRK11316 194 -PNlsefeavvgkckdeaeLVEKGMKLIAdYDLSALLVTRSEQGMTLLQpGKAPLHLPTQARE-VYDVTGAGDTVISVLA 271
|
250 260 270
....*....|....*....|....*....|....*....
gi 31789445 243 GYLSSQPTLDEAAMrramiFGSVMASFNVEEFGTARVQR 281
Cdd:PRK11316 272 AALAAGNSLEEACA-----LANAAAGVVVGKLGTSTVSP 305
|
|
| |
