|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02548 |
PLN02548 |
adenosine kinase |
27-296 |
1.37e-150 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 424.90 E-value: 1.37e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 27 WMIQQPHkAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEK 106
Cdd:PLN02548 64 WMLQIPG-ATSYMGCIGKDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 107 NWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQ 186
Cdd:PLN02548 142 NWALVEKAKFYYIAGFFLTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALPYVDFLFGNETEARTFAKVQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 187 GFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDK 266
Cdd:PLN02548 222 GWETEDVEEIALKISALPKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGK 301
|
250 260 270
....*....|....*....|....*....|
gi 1034566520 267 PLTECIRAGHYAASIIIRRTGCTFPEKPDF 296
Cdd:PLN02548 302 DIEECVRAGNYAANVIIQRSGCTYPEKPDF 331
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
27-296 |
1.94e-129 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 371.67 E-value: 1.94e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 27 WMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEK 106
Cdd:PTZ00247 74 WMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 107 NWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQ 186
Cdd:PTZ00247 153 VQEAIKTAQLYYLEGFFLTVSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPYVDILFGNEEEAKTFAKAM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 187 GFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDK 266
Cdd:PTZ00247 233 KWDTEDLKEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGK 312
|
250 260 270
....*....|....*....|....*....|
gi 1034566520 267 PLTECIRAGHYAASIIIRRTGCTFPEKPDF 296
Cdd:PTZ00247 313 DIDRCVEAGHYSAQVIIQHNGCTYPEKPPF 342
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
29-291 |
9.86e-107 |
|
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: 312.63 E-value: 9.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 29 IQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekN 107
Cdd:cd01168 65 AAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----D 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 108 WMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREqg 187
Cdd:cd01168 140 WSLLAKAKYLYLEGYLLTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEA-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 188 fETKDIKEIAKKTQALpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKP 267
Cdd:cd01168 218 -ETTDDLEAALKLLAL------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEP 288
|
250 260
....*....|....*....|....
gi 1034566520 268 LTECIRAGHYAASIIIRRTGCTFP 291
Cdd:cd01168 289 LEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
36-290 |
1.07e-64 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 204.88 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 36 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEK 113
Cdd:pfam00294 51 VAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLEN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 114 ARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISqfYKESLMKVMPYVDILFGNETEAATFAREQgfetkdI 193
Cdd:pfam00294 128 ADLLYISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLGA--AREALLELLPLADLLKPNEEELEALTGAK------L 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 194 KEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIR 273
Cdd:pfam00294 200 DDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALR 277
|
250
....*....|....*..
gi 1034566520 274 AGHYAASIIIRRTGCTF 290
Cdd:pfam00294 278 FANAAAALVVQKSGAQT 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
36-289 |
1.28e-39 |
|
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: 140.40 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 36 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 113
Cdd:COG0524 53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 114 ARVCYIAGFFLT--VSPESVLKVAHHASENNR--IFTLNLSAPFISQfYKESLMKVMPYVDILFGNETEAATFareqgFE 189
Cdd:COG0524 128 ADILHLGGITLAsePPREALLAALEAARAAGVpvSLDPNYRPALWEP-ARELLRELLALVDILFPNEEEAELL-----TG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 190 TKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDK 266
Cdd:COG0524 202 ETDPEEAAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGL 269
|
250 260
....*....|....*....|...
gi 1034566520 267 PLTECIRAGHYAASIIIRRTGCT 289
Cdd:COG0524 270 DLEEALRFANAAAALVVTRPGAQ 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-287 |
4.35e-32 |
|
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: 120.35 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 37 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTcaACIT----GDNRslIANLAAANcykkeKHL---DLEKNW 108
Cdd:cd01174 54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENR--IVVVPGAN-----GELtpaDVDAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 109 MLVEKARVCYIAgffLTVSPESVLKVAHHASENNRIFTLNlSAPFISQFYKeslmkVMPYVDILFGNETEAATFAREQGF 188
Cdd:cd01174 125 ELIAAADVLLLQ---LEIPLETVLAALRAARRAGVTVILN-PAPARPLPAE-----LLALVDILVPNETEAALLTGIEVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 189 ETKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATESEVT---AFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSD 265
Cdd:cd01174 196 DEEDAEKAARLLLAKGV------KNVIVTLGAKGALLASGGEVEhvpAFKV------KAVDTTGAGDTFIGALAAALARG 263
|
250 260
....*....|....*....|..
gi 1034566520 266 KPLTECIRAGHYAASIIIRRTG 287
Cdd:cd01174 264 LSLEEAIRFANAAAALSVTRPG 285
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
114-263 |
4.28e-29 |
|
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: 109.88 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 114 ARVCYIAGffLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKEsLMKVMPYVDILFGNETEAATFAREQGFETKDI 193
Cdd:cd00287 58 ADAVVISG--LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-LEKLLPGVDILTPNEEEAEALTGRRDLEVKEA 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 194 keiakkTQALPKMNSKRQRIVIFTQGRDDTIMATEsEVTAFAVLDQDqKEIIDTNGAGDAFVGGFLSQLV 263
Cdd:cd00287 135 ------AEAAALLLSKGPKVVIVTLGEKGAIVATR-GGTEVHVPAFP-VKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
33-289 |
4.48e-25 |
|
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: 101.50 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 33 HKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQ-PTGTcAACITGDNRS---LIANLAAANCYKKEKHLDLEknw 108
Cdd:cd01166 46 HRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGGErrvLYYRAGSAASRLTPEDLDEA--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 109 mLVEKARVCYIAGFFLTVSP---ESVLKVAHHASENN--RIFTLNLSAPFIS-QFYKESLMKVMPYVDILFGNETEAATF 182
Cdd:cd01166 121 -ALAGADHLHLSGITLALSEsarEALLEALEAAKARGvtVSFDLNYRPKLWSaEEAREALEELLPYVDIVLPSEEEAEAL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 183 AREQGfeTKDIKEIAKKTQALPKmnskrqrIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAGDAFVGGFLSQL 262
Cdd:cd01166 200 LGDED--PTDAAERALALALGVK-------AVVVKLGAEGALVYTGGGRVFVPAY---PVEVVDTTGAGDAFAAGFLAGL 267
|
250 260
....*....|....*....|....*..
gi 1034566520 263 VSDKPLTECIRAGHYAASIIIRRTGCT 289
Cdd:cd01166 268 LEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
36-288 |
1.65e-20 |
|
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: 88.91 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 36 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTcaACIT---GDNRSLIANLAAANCYKKEKHLDLEKNW--- 108
Cdd:cd01942 53 PGLVAAVGEDFHGRLYLEELREEGVDtSHVRVVDEDSTGV--AFILtdgDDNQIAYFYPGAMDELEPNDEADPDGLAdiv 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 109 ------MLVEKARVCYIAGFFLTVSPesvlkvahhasennriftlnlsAPFISQFYKESLMKVMPYVDILFGNETEAATF 182
Cdd:cd01942 131 hlssgpGLIELARELAAGGITVSFDP----------------------GQELPRLSGEELEEILERADILFVNDYEAELL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 183 AREQGFETKDIkeiakktqalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQL 262
Cdd:cd01942 189 KERTGLSEAEL--------------ASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAV--KVVDTTGAGDAFRAGFLYGL 252
|
250 260
....*....|....*....|....*.
gi 1034566520 263 VSDKPLTECIRAGHYAASIIIRRTGC 288
Cdd:cd01942 253 LRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
36-287 |
2.40e-20 |
|
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: 88.46 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 36 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTCAACITGD-NRS-LIANLAAANCykkekHLDLEKNWMLVE 112
Cdd:cd01167 45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDADgERSfEFYRGPAADL-----LLDTELNPDLLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 113 KARVCYIAGFFLTVSP--ESVLKVAHHASENNRI--FTLNLSAPFISQFY--KESLMKVMPYVDILFGNETEAATFareq 186
Cdd:cd01167 120 EADILHFGSIALASEPsrSALLELLEAAKKAGVLisFDPNLRPPLWRDEEeaRERIAELLELADIVKLSDEELELL---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 187 gFETKDIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMAT---ESEVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLV 263
Cdd:cd01167 196 -FGEEDPEEIAALLLLFG------LKLVLVTRGADGALLYTkggVGEVPGIPV------EVVDTTGAGDAFVAGLLAQLL 262
|
250 260 270
....*....|....*....|....*....|.
gi 1034566520 264 SDK-------PLTECIRAGHYAASIIIRRTG 287
Cdd:cd01167 263 SRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
131-287 |
1.45e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 131 VLKVAHHASennrIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAreqGFETKDIKEIAKKTQALPKMNSkr 210
Cdd:PTZ00292 165 ALKEAKERG----CYTVFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALIT---GMEVTDTESAFKASKELQQLGV-- 235
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034566520 211 qRIVIFTQG-RDDTIMATESEVTAfavLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 287
Cdd:PTZ00292 236 -ENVIITLGaNGCLIVEKENEPVH---VPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
33-289 |
1.29e-12 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 66.85 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 33 HKAAtFFGCIGIDKFGEILKRKAAEAHVDA-HYYEQNEQPTGtcaACITG----DNRSLIanlaaancYKKEKHLDL--- 104
Cdd:TIGR04382 49 LKTA-FITRVGDDQFGRFVRDYLRREGVDTsHVVTDPGRRTS---LVFLEikppDEFPLL--------FYRENAADLalt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 105 --EKNWMLVEKARVCYIAGFFLTVSP--ESVLKVAHHASENNRIFTLNLSapFISQFYKES------LMKVMPYVDILFG 174
Cdd:TIGR04382 117 pdDVDEDYIASARALLVSGTALSQEPsrEAVLKALEYARAAGVRVVLDID--YRPYLWKSPeeagiyLRLVLPLVDVIIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 175 NETEAATFAREqgfetKDIKEIAKKTQALPKmnskrqRIVIFTQGRDDTIMATES----EVTAFAVldqdqkEIIDTNGA 250
Cdd:TIGR04382 195 TREEFDIAGGE-----GDDEAAARALLDAGV------EILVVKRGPEGSLVYTGDgegvEVPGFPV------EVLNVLGA 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034566520 251 GDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 289
Cdd:TIGR04382 258 GDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
36-281 |
1.72e-12 |
|
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: 66.18 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 36 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIAnLAAANCYKKEKHLDLEKNWMLVEKAR 115
Cdd:cd01941 52 VALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGDLVVA-LADMDIYELLTPDFLRKIREALKEAK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 116 V------------------CYIAGFFLTVSPESVLKVAHhasennrIFTLNlsapfisqfykeslmkvmPYVDILFGNET 177
Cdd:cd01941 131 PivvdanlpeealeyllalAAKHGVPVAFEPTSAPKLKK-------LFYLL------------------HAIDLLTPNRA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 178 EAATFAREQGFETKDIKeIAKKTQALPKMNskrqrIVIFTQGRDDTI---MATESEVTAFAVLDQDqkEIIDTNGAGDAF 254
Cdd:cd01941 186 ELEALAGALIENNEDEN-KAAKILLLPGIK-----NVIVTLGAKGVLlssREGGVETKLFPAPQPE--TVVNVTGAGDAF 257
|
250 260
....*....|....*....|....*..
gi 1034566520 255 VGGFLSQLVSDKPLTECIRAGHYAASI 281
Cdd:cd01941 258 VAGLVAGLLEGMSLDDSLRFAQAAAAL 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
37-287 |
9.80e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 64.12 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 37 TFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTcaACI----TGDNRSLIAnlAAANCYKKEKHLdlEKNWMLV 111
Cdd:PRK11142 57 AFIACVGDDSIGESMRQQLAKDGIDtAPVSVIKGESTGV--ALIfvndEGENSIGIH--AGANAALTPALV--EAHRELI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 112 EKARVCYIAgffLTVSPESVLKVAHHASENNRIFTLNlSAPfiSQFYKESLMKVmpyVDILFGNETEAATFAreqGFETK 191
Cdd:PRK11142 131 ANADALLMQ---LETPLETVLAAAKIAKQHGTKVILN-PAP--ARELPDELLAL---VDIITPNETEAEKLT---GIRVE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 192 DIKEIAKKTQALpkmNSKRQRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPL 268
Cdd:PRK11142 199 DDDDAAKAAQVL---HQKGIETVLITLGSRGVWLSENGEgqrVPGFRV------QAVDTIAAGDTFNGALVTALLEGKPL 269
|
250
....*....|....*....
gi 1034566520 269 TECIRAGHYAASIIIRRTG 287
Cdd:PRK11142 270 PEAIRFAHAAAAIAVTRKG 288
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
38-287 |
1.35e-11 |
|
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: 63.60 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 38 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAancykkEKHLDLEknWML---VEK 113
Cdd:cd01944 54 NAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDgERSFISISGA------EQDWSTE--WFAtltVAP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 114 ARVCYIAGFFLTVSPESV--LKVAHHASENNRIFTLNLSaPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETK 191
Cdd:cd01944 126 YDYVYLSGYTLASENASKviLLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMAKRPIWSCNREEAAIFAERGDPAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 192 D-IKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMAtesevtAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTE 270
Cdd:cd01944 205 AsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIP------GFKV------KAVDTIGAGDTHAGGMLAGLAKGMSLAD 272
|
250
....*....|....*..
gi 1034566520 271 CIRAGHYAASIIIRRTG 287
Cdd:cd01944 273 AVLLANAAAAIVVTRSG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
33-282 |
1.89e-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: 60.06 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 33 HKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTG-TCAACITGDNRSLIANLAAAncykkEKHLDLEKNWMLV 111
Cdd:cd01940 37 HESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAvADVELVDGDRIFGLSNKGGV-----AREHPFEADLEYL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 112 EKARVCYIAGFFLTVSPESVLKVAHHASennriftLNLSAPFISQFYKESLMKVMPYVDILFgneteaatFAREqGFETK 191
Cdd:cd01940 111 SQFDLVHTGIYSHEGHLEKALQALVGAG-------ALISFDFSDRWDDDYLQLVCPYVDFAF--------FSAS-DLSDE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 192 DIKEIAKKTQalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAGDAFVGGFL-SQLVSDKPLTE 270
Cdd:cd01940 175 EVKAKLKEAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEVVDTLGAGDSFIAGFLlSLLAGGTAIAE 245
|
250
....*....|...
gi 1034566520 271 CIRAG-HYAASII 282
Cdd:cd01940 246 AMRQGaQFAAKTC 258
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
159-270 |
6.49e-07 |
|
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: 49.77 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 159 KESLMKVMPYVDILFGNETEAatfareqgfetKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVtaFAVLD 238
Cdd:cd01946 154 PEKLKKVLAKVDVVIINDGEA-----------RQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGY--FAAPA 220
|
90 100 110
....*....|....*....|....*....|..
gi 1034566520 239 QDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTE 270
Cdd:cd01946 221 YPLESVFDPTGAGDTFAGGFIGYLASQKDTSE 252
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
37-289 |
2.84e-06 |
|
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: 47.80 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 37 TFFGCIGIDKFGE-ILKRkaAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLaaancykKEKHLDLEKNWMLVEkar 115
Cdd:cd01947 54 RFFSNLGRDEIGIqSLEE--LESGGDKHTVAWRDKPTRKTLSFIDPNGERTITVP-------GERLEDDLKWPILDE--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 116 vcyIAGFFLTvsPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMkvmpYVDILFGNETEAAtfarEQGFETKDIKe 195
Cdd:cd01947 122 ---GDGVFIT--AAAVDKEAIRKCRETKLVILQVTPRVRVDELNQALI----PLDILIGSRLDPG----ELVVAEKIAG- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 196 iakktqalpkmnsKRQRIVIFTQGRDDTIMATESE---VTAFavldqdQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECI 272
Cdd:cd01947 188 -------------PFPRYLIVTEGELGAILYPGGRynhVPAK------KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEAL 248
|
250
....*....|....*..
gi 1034566520 273 RAGHYAASIIIRRTGCT 289
Cdd:cd01947 249 ELGAQCGAICVSHFGPY 265
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
159-287 |
3.21e-06 |
|
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: 47.72 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 159 KESLMKVMPYVDILFGNETEAATFAREQGFETKDIKE------IAKKTQALPKMNSkrqrIVIFTQGRDDTIMATESEVT 232
Cdd:cd01943 171 LEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEkeavlqALLFSGILQDPGG----GVVLRCGKLGCYVGSADSGP 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034566520 233 AF---AVlDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 287
Cdd:cd01943 247 ELwlpAY-HTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
164-283 |
3.39e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 47.42 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 164 KVMPYVDILFGNETEAATFAREQgfeTKDIKEIAKKTqalpkmnskrqriVIFTQGRDDTIMATESEVTAFAVldqDQKE 243
Cdd:PRK09813 154 TLVPHLDYAFASAPQEDEFLRLK---MKAIVARGAGV-------------VIVTLGENGSIAWDGAQFWRQAP---EPVT 214
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034566520 244 IIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 283
Cdd:PRK09813 215 VVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
175-275 |
8.51e-06 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 46.28 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 175 NETEAATFAreqGFETKDIKEIAKKTQALPKMNSkrqRIVIFTQGRDDTIMATESEVTAFAVLDQdqkEIIDTNGAGDAF 254
Cdd:COG1105 184 NLEELEELL---GRPLETLEDIIAAARELLERGA---ENVVVSLGADGALLVTEDGVYRAKPPKV---EVVSTVGAGDSM 254
|
90 100
....*....|....*....|.
gi 1034566520 255 VGGFLSQLVSDKPLTECIRAG 275
Cdd:COG1105 255 VAGFLAGLARGLDLEEALRLA 275
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
245-270 |
1.17e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 46.15 E-value: 1.17e-05
10 20
....*....|....*....|....*.
gi 1034566520 245 IDTNGAGDAFVGGFLSQLVSDKPLTE 270
Cdd:PLN02323 261 VDTTGAGDAFVGGLLSQLAKDLSLLE 286
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
40-287 |
5.61e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 44.01 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 40 GCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAaCITGD--NRSLIANLAAA-----NCYKKEkhlDLE-KNWMLV 111
Cdd:PLN02379 108 GACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCV-CLVDAlgNRTMRPCLSSAvklqaDELTKE---DFKgSKWLVL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 112 EkarvcYiaGFFltvSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPY--VDILFGNETEAATFAReqGFE 189
Cdd:PLN02379 184 R-----Y--GFY---NLEVIEAAIRLAKQEGLSVSLDLASFEMVRNFRSPLLQLLESgkIDLCFANEDEARELLR--GEQ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 190 TKDIKEiakktqALpKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQdqKEIIDTNGAGDAFVGGFLSQLVSDKPLT 269
Cdd:PLN02379 252 ESDPEA------AL-EFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGE--TNAVDATGAGDLFASGFLYGLIKGLSLE 322
|
250
....*....|....*...
gi 1034566520 270 ECIRAGHYAASIIIRRTG 287
Cdd:PLN02379 323 ECCKVGACSGGSVVRALG 340
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
191-275 |
7.89e-05 |
|
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: 43.29 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 191 KDIKEIAKKtqalpkMNSKRQRIVIFTQGRDDTIMATESEV---TAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKP 267
Cdd:cd01164 200 EDVIAAARK------LIERGAENVLVSLGADGALLVTKDGVyraSPPKV------KVVSTVGAGDSMVAGFVAGLAQGLS 267
|
....*...
gi 1034566520 268 LTECIRAG 275
Cdd:cd01164 268 LEEALRLA 275
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
110-287 |
1.60e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 42.87 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 110 LVEKARVCYIAGFF--LTVSPESVLKVAHHASENNRIFTLNLSAP-FISQFYKESLMKVMPYVDILFGNETEAATFAreq 186
Cdd:PLN02813 221 AISKSRVLVVEGYLweLPQTIEAIAQACEEAHRAGALVAVTASDVsCIERHRDDFWDVMGNYADILFANSDEARALC--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 187 GFETKDIKEIAkkTQALpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQdqkEIIDTNGAGDAFVGGFLSQL---V 263
Cdd:PLN02813 298 GLGSEESPESA--TRYL----SHFCPLVSVTDGARGSYIGVKGEAVYIPPSPC---VPVDTCGAGDAYAAGILYGLlrgV 368
|
170 180
....*....|....*....|....*...
gi 1034566520 264 SDkpltecIR-AGHYA---ASIIIRRTG 287
Cdd:PLN02813 369 SD------LRgMGELAarvAATVVGQQG 390
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
212-264 |
2.99e-04 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 41.85 E-value: 2.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034566520 212 RIVIFTQGRDDTIMATESEVTAFA---VldqdqkEIIDTNGAGDAFVGGFLSQLVS 264
Cdd:PRK09434 214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
200-287 |
6.79e-04 |
|
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: 40.35 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 200 TQALPKMNSKRQRIVIFTQGRDDTIMATES----EVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 275
Cdd:cd01945 192 DEALELLASLGIPFVAVTLGEAGCLWLERDgelfHVPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFA 265
|
90
....*....|..
gi 1034566520 276 HYAASIIIRRTG 287
Cdd:cd01945 266 SAAAALKCRGLG 277
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
159-280 |
7.19e-04 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 40.47 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 159 KESLMKVMPYVDILFgnetEAATFAREQGFETkdikeiAKKTQALPKMNSKRQRIVIFTQGrDDTIMATESEVTAFAVLD 238
Cdd:cd01939 170 REELLELAAYCDVVF----VSKDWAQSRGYKS------PEECLRGEGPRAKKAALLVCTWG-DQGAGALGPDGEYVHSPA 238
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1034566520 239 QDQKEIIDTNGAGDAFVGGFLSQL-VSDKPLTECIRAGHYAAS 280
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALnKGPDDLSEALDFGNRVAS 281
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
158-286 |
4.75e-03 |
|
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: 37.95 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 158 YKESLMkvmPYVDILFGNETEAATFAreqGFETKDIKEIakkTQALPKMNSKRQRIVIFT------QGRDDTIMATESEV 231
Cdd:cd01173 129 YRDLLV---PLADIITPNQFELELLT---GKKINDLEDA---KAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEA 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034566520 232 TAFavldqdQKEIIDT----NGAGDAFVGGFLSQLVSDKPLTEciRAGHYAASI--IIRRT 286
Cdd:cd01173 200 WLV------QRPKIPFpayfNGTGDLFAALLLARLLKGKSLAE--ALEKALNFVheVLEAT 252
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
159-273 |
5.04e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 37.74 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 159 KESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMN---------SKRQRIVIFTQGRDDTIMAtes 229
Cdd:PRK12413 120 RQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAvvikggnrlSQKKAIDLFYDGKEFVILE--- 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034566520 230 evtaFAVLDQDQkeiidtNGAGDAFVGGFLSQLVSDKPLTECIR 273
Cdd:PRK12413 197 ----SPVLEKNN------IGAGCTFASSIASQLVKGKSPLEAVK 230
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
158-281 |
8.67e-03 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 37.00 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566520 158 YKESLMKVMPYVDILFGNETEAAtfareqgfETKDIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMATESE---VTAF 234
Cdd:cd01937 145 EKLIKCVILKLHDVLKLSRVEAE--------VISTPTELARLIKETG------VKEIIVTDGEEGGYIFDGNGkytIPAS 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034566520 235 AvldqdqKEIIDTNGAGDAFVGGFLSQLVSDKpltECIRAGHYAASI 281
Cdd:cd01937 211 K------KDVVDPTGAGDVFLAAFLYSRLSGK---DIKEAAEFAAAA 248
|
|
| |
