|
Name |
Accession |
Description |
Interval |
E-value |
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-326 |
4.63e-56 |
|
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: 184.32 E-value: 4.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPERGWLVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARL--GARVALVGAVGDDPFGDFLLAELRAEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQRTFFHSPGANRLLDLPAFEP-LDAPLKIFHLGYLLLLESLDRpdevygTRSARLLAQ 164
Cdd:COG0524 80 SGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEaLLAGADILHLGGITLASEPPR------EALLAALEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 165 MRERGYEVSLDLVSRKG-DPRYRPLVLPALKHLDYLTINELEASEFSGLEirlpngephvaNIARAASALLDAGVRQRVV 243
Cdd:COG0524 154 ARAAGVPVSLDPNYRPAlWEPARELLRELLALVDILFPNEEEAELLTGET-----------DPEEAAAALLARGVKLVVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 244 IHCPEGAWGVSRTEAGRwVPSwrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANAIDGAKTL 323
Cdd:COG0524 223 TLGAEGALLYTGGEVVH-VPA---FPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTR 298
|
...
gi 490281904 324 PEL 326
Cdd:COG0524 299 EEV 301
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-319 |
1.22e-42 |
|
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: 149.69 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 3 RKGIIAAGNMLVDHVHQIGqWPERGWLVEIVHSERATGGAPLNVLLTLAKMHA---GLPLQAVGLIGE-DNDGDYITAML 78
Cdd:cd01168 1 RYDVLGLGNALVDILAQVD-DAFLEKLGLKKGDMILADMEEQEELLAKLPVKYiagGSAANTIRGAAAlGGSAAFIGRVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 79 DQYHINRQLVQRTSSAPTSMTQVMTDAE-GQRTFFHSPGANRLL--DLPA---FEPLDAPLKIFhlgylllleslDRPDE 152
Cdd:cd01168 80 DDKLGDFLLKDLRAAGVDTRYQVQPDGPtGTCAVLVTPDAERTMctYLGAaneLSPDDLDWSLL-----------AKAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 153 VY--------GTRSARLLAQM-RERGYEVSLDLVSRKGDPRYRPLVLPALKHLDYLTINELEASEFSGLEIRlpngephv 223
Cdd:cd01168 149 LYlegylltvPPEAILLAAEHaKENGVKIALNLSAPFIVQRFKEALLELLPYVDILFGNEEEAEALAEAETT-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 224 aNIARAASALLDAGVRQRVVIHCPEGAWGVSRTEAgRWVPSWrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLA 303
Cdd:cd01168 221 -DDLEAALKLLALRCRIVVITQGAKGAVVVEGGEV-YPVPAI--PVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLG 296
|
330
....*....|....*.
gi 490281904 304 HACARASLQAANAIDG 319
Cdd:cd01168 297 SYAAAEVIQQLGPRLP 312
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
29-318 |
9.49e-34 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 125.92 E-value: 9.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 29 LVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINRQLVQRTSSAPTSMTQVMTDAEGQ 108
Cdd:pfam00294 23 LVRVSTVEKGPGGKGANVAVALARL--GGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 109 RTF-FHSPGANRLLDLPAFEPLDAPLKIfhlgyllllesldrpDEVYgtRSARLLAQMRERGYEVSLDLVSRKG--DPRY 185
Cdd:pfam00294 101 RTIvFNRGAAADLTPEELEENEDLLENA---------------DLLY--ISGSLPLGLPEATLEELIEAAKNGGtfDPNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 186 RP---LVLPALKHL----DYLTINELEASEFSGLEIrlpngePHVANIARAASALLDAGVRQRVVIHCPEGAWGVSRTEA 258
Cdd:pfam00294 164 LDplgAAREALLELlplaDLLKPNEEELEALTGAKL------DDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 259 GRWVPswrLPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANAID 318
Cdd:pfam00294 238 VHVPA---VPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-314 |
3.82e-28 |
|
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: 110.80 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPERgwlveivhSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:cd01167 2 VVCFGEALIDFIPEGSGAPET--------FTKAPGGAPANVAVALARL--GGKAAFIGKVGDDEFGDFLLETLKEAGVDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQR--TFFHSPGANRLLDLPAFEPLDAPLKIFHlgyllllesldrpdevYGT------- 156
Cdd:cd01167 72 RGIQFDPAAPTTLAFVTLDADGERsfEFYRGPAADLLLDTELNPDLLSEADILH----------------FGSialasep 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 157 -RSA--RLLAQMRERGYEVSLDLVSRK----GDPRYRPLVLPALKHLDYLTINELEASEFSGLEirlpngephvaNIARA 229
Cdd:cd01167 136 sRSAllELLEAAKKAGVLISFDPNLRPplwrDEEEARERIAELLELADIVKLSDEELELLFGEE-----------DPEEI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 230 ASALLDAGvRQRVVIHC-PEGAWgVSRTEAGRWVPSwrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACAR 308
Cdd:cd01167 205 AALLLLFG-LKLVLVTRgADGAL-LYTKGGVGEVPG---IPVEVVDTTGAGDAFVAGLLAQLLSRGLLALDEDELAEALR 279
|
....*.
gi 490281904 309 ASLQAA 314
Cdd:cd01167 280 FANAVG 285
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-307 |
2.81e-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: 105.47 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPERGWLVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKL--GLSPGLVAAVGEDFHGRLYLEELREEGVDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQRTFFHSPGANRLLDLPAFEPLDAPLKIFHLGylllleslDRPDEVYGTRSARllaqm 165
Cdd:cd01942 80 SHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPDGLADIVHLS--------SGPGLIELARELA----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 166 rERGYEVSLDLvSRKGDPRYRPLVLPALKHLDYLTINELEASEFSGLEirlpnGEPhvaniaraaSALLDAGVRQRVVIH 245
Cdd:cd01942 147 -AGGITVSFDP-GQELPRLSGEELEEILERADILFVNDYEAELLKERT-----GLS---------EAELASGVRVVVVTL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490281904 246 CPEGAWGVSRTEAGRwVPswRLPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACA 307
Cdd:cd01942 211 GPKGAIVFEDGEEVE-VP--AVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA 269
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-307 |
7.52e-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: 101.88 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHqigqwPERGWLVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:cd01166 2 VVTIGEVMVDLSP-----PGGGRLEQADSFRKFFGGAEANVAVGLARL--GHRVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQRTFFH--SPGANRLLDLPAFEPLD-APLKIFHLGYLLLLESLDRPDEVYgtrsaRLL 162
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYyrAGSAASRLTPEDLDEAAlAGADHLHLSGITLALSESAREALL-----EAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 163 AQMRERGYEVSLDLVSRK---GDPRYRPLVLPALKHLDYLTINELEASEFSGLEirlpnGEPHVANIARAasalLDAGVR 239
Cdd:cd01166 150 EAAKARGVTVSFDLNYRPklwSAEEAREALEELLPYVDIVLPSEEEAEALLGDE-----DPTDAAERALA----LALGVK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490281904 240 QRVVIHCPEGAWGVSRTEAGRwVPSwrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACA 307
Cdd:cd01166 221 AVVVKLGAEGALVYTGGGRVF-VPA---YPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAA 284
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-319 |
6.86e-20 |
|
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: 87.99 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 5 GIIAAGNMLVDHVHQIGQWPERGwlvEIVHSERAT---GGAPLNVLLTLAKmhAGLPLQAVGLIGEDNDGDYITAMLDQY 81
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPG---ETVLGSSFEtgpGGKGANQAVAAAR--LGARVAMIGAVGDDAFGDELLENLREE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 82 HINRQLVQRTSSAPTSMTQVMTDAEGQRTFFHSPGANRLLDLPAFEPLDAPLKifhlgyllllesldrpdevygtRSARL 161
Cdd:cd01174 76 GIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIA----------------------AADVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 162 LAQMrergyEVSLDLV-------SRKG-----DP-RYRPLVLPALKHLDYLTINELEASEFSGLEIrlpngePHVANIAR 228
Cdd:cd01174 134 LLQL-----EIPLETVlaalraaRRAGvtvilNPaPARPLPAELLALVDILVPNETEAALLTGIEV------TDEEDAEK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 229 AASALLDAGVRQRVVIHCPEGAWGVSRTEAGrWVPSwrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACAR 308
Cdd:cd01174 203 AARLLLAKGVKNVIVTLGAKGALLASGGEVE-HVPA---FKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
|
330
....*....|.
gi 490281904 309 ASLQAANAIDG 319
Cdd:cd01174 279 LSVTRPGAQPS 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
40-312 |
2.82e-15 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 75.17 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 40 GGAPLNVLLTLAKMhaGLPLQAVGLIGEDNdGDYITAMLDQYHINRQLVQRTSSAPTSMTqVMTDAEGQRTFFHSPGA-- 117
Cdd:COG1105 35 GGKGINVARVLKAL--GVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGETRINIK-IVDPSDGTETEINEPGPei 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 118 -----NRLLDlpAFEPLDAPLKI----------FhlgyllllesldrPDEVYgtrsARLLAQMRERGYEVSLDlVSrkGD 182
Cdd:COG1105 111 seeelEALLE--RLEELLKEGDWvvlsgslppgV-------------PPDFY----AELIRLARARGAKVVLD-TS--GE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 183 P-----RYRPLVLpalKhldyltINELEASEFSGLEIrlpngePHVANIARAASALLDAGVrQRVVIHC-PEGAWGVSRT 256
Cdd:COG1105 169 AlkaalEAGPDLI---K------PNLEELEELLGRPL------ETLEDIIAAARELLERGA-ENVVVSLgADGALLVTED 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490281904 257 EAgrwvpsWRLPPEEI--IGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQ 312
Cdd:COG1105 233 GV------YRAKPPKVevVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAAL 284
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
29-330 |
9.39e-15 |
|
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: 73.79 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 29 LVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINRQLVQRTSSAPTSMTqvmtdaegq 108
Cdd:TIGR04382 23 LEDVTSFAKYLGGSPANIAVGAARL--GLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGRRTSLV--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 109 rtffhspganrLLDLpaFEPLDAPLKIFHLGYLLLLESLDRPDEVY----------GT-------RSARLLA--QMRERG 169
Cdd:TIGR04382 92 -----------FLEI--KPPDEFPLLFYRENAADLALTPDDVDEDYiasarallvsGTalsqepsREAVLKAleYARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 170 YEVSLDLVSRK---GDPRYRPLVLP-ALKHLDYLTINELEasefsgLEIRLPNGEPHvaniaRAASALLDAGVRQRVVIH 245
Cdd:TIGR04382 159 VRVVLDIDYRPylwKSPEEAGIYLRlVLPLVDVIIGTREE------FDIAGGEGDDE-----AAARALLDAGVEILVVKR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 246 CPEGAWGVSRTEAGRWVPSwrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACAR---ASLQAANAIdgaKT 322
Cdd:TIGR04382 228 GPEGSLVYTGDGEGVEVPG---FPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAivvSRHSCSPAM---PT 301
|
....*...
gi 490281904 323 LPELQAFI 330
Cdd:TIGR04382 302 LEELEAFL 309
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
33-312 |
1.31e-13 |
|
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: 70.30 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 33 VHSERAT-GGAPLNVLLTLAKMhaGLPLQAVGLIGEDNdGDYITAMLDQYHINRQLVqrTSSAPTSMTQVMTDAEGQRTF 111
Cdd:TIGR03168 27 VAAVRKDaGGKGINVARVLARL--GAEVVATGFLGGFT-GEFIEALLAEEGIKNDFV--EVKGETRINVKIKESSGEETE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 112 FHSPGA-------NRLLdlpafEPLDAPLKifhlgylllleSLDR-----------PDEVYgtrsARLLAQMRERGYEVS 173
Cdd:TIGR03168 102 LNEPGPeiseeelEQLL-----EKLRELLA-----------SGDIvvisgslppgvPPDFY----AQLIAIARKKGAKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 174 LDlVSrkGDP-----RYRP-LVLPalkhldyltiNELEASEFSGLEIRLPNGephvanIARAASALLDAGVrQRVVIHC- 246
Cdd:TIGR03168 162 LD-TS--GEAlrealAAKPfLIKP----------NHEELEELFGRELKTLEE------IIEAARELLDRGA-ENVLVSLg 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490281904 247 PEGAWGVSRTEAGRWVPswrlPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQ 312
Cdd:TIGR03168 222 ADGALLVTKEGALKATP----PKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAF 283
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-317 |
2.64e-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: 68.98 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPERGWLVEIVHSERATGGAPLNVLLTLAKmhAGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAK--LGNDVRFFSNLGRDEIGIQSLEELESGGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSsaPTSMTQVMTDAEGQRTFFHSPGanrlldlPAFEPLDAPlkifhlgylllleSLDRPDEVYGTRSARL---L 162
Cdd:cd01947 80 TVAWRDK--PTRKTLSFIDPNGERTITVPGE-------RLEDDLKWP-------------ILDEGDGVFITAAAVDkeaI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 163 AQMRERGYeVSLDLVsrkgdPRYRPLVL-PALKHLDYLTINELEASEFSgleirlpngephvaniaraaSALLDAGVRQR 241
Cdd:cd01947 138 RKCRETKL-VILQVT-----PRVRVDELnQALIPLDILIGSRLDPGELV--------------------VAEKIAGPFPR 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490281904 242 VVIhCPEGAWGVSRTEAGRW--VPswrLPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANAI 317
Cdd:cd01947 192 YLI-VTEGELGAILYPGGRYnhVP---AKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
33-312 |
1.37e-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: 66.95 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 33 VHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINRqLVQRTSSAPTSMTQVMTDAEGQrtfF 112
Cdd:cd01941 28 GHVKQSPGGVGRNIAENLARL--GVSVALLSAVGDDSEGESILEESEKAGLNV-RGIVFEGRSTASYTAILDKDGD---L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 113 HSPGAN-RLLDLPAFEPL--------DAPLKIFHLgylllleslDRPDEVYgtrsARLLAQMRERGYEVSLDLVSrkgDP 183
Cdd:cd01941 102 VVALADmDIYELLTPDFLrkirealkEAKPIVVDA---------NLPEEAL----EYLLALAAKHGVPVAFEPTS---AP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 184 RYRPLVLPaLKHLDYLTINELEASEFSGLEIRlpNGEPHVaniaRAASALLDAGVRQRVVIHCPEGAWGVSRTEAgrwVP 263
Cdd:cd01941 166 KLKKLFYL-LHAIDLLTPNRAELEALAGALIE--NNEDEN----KAAKILLLPGIKNVIVTLGAKGVLLSSREGG---VE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490281904 264 SWRLPP---EEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQ 312
Cdd:cd01941 236 TKLFPApqpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
159-289 |
7.97e-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: 63.27 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 159 ARLLAQMRERGYEVSLDLVSRKGDPRYRPLVlPALKHLDYLTINELEASEFSGLEIrlpngePHVANIARAASALLDAGV 238
Cdd:cd00287 74 LDALEEARRRGVPVVLDPGPRAVRLDGEELE-KLLPGVDILTPNEEEAEALTGRRD------LEVKEAAEAAALLLSKGP 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490281904 239 rQRVVIHC-PEGAWGVSRTEAGRWVPSWrlpPEEIIGSVGAGDAFCAGLLYG 289
Cdd:cd00287 147 -KVVIVTLgEKGAIVATRGGTEVHVPAF---PVKVVDTTGAGDAFLAALAAG 194
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
33-312 |
1.76e-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: 63.71 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 33 VHSERAT-GGAPLNVLLTLAkmHAGLPLQAVGLIGEDNdGDYITAMLDQYHINRQLVqrTSSAPTSMTQVMTDAEGQRTF 111
Cdd:cd01164 28 VSSTRKDaGGKGINVARVLK--DLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFV--EVAGETRINVKIKEEDGTETE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 112 FHSPGA-------NRLLDLpafepLDAPLKIFHLGYLLLLESLDRPDEVYgtrsARLLAQMRERGYEVSLDlVSrkGDP- 183
Cdd:cd01164 103 INEPGPeiseeelEALLEK-----LKALLKKGDIVVLSGSLPPGVPADFY----AELVRLAREKGARVILD-TS--GEAl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 184 ----RYRPLVL-PalkhldyltiNELEASEFSGLEIrlpngePHVANIARAASALLDAGVrQRVVIHC-PEGAWGVSRTE 257
Cdd:cd01164 171 laalAAKPFLIkP----------NREELEELFGRPL------GDEEDVIAAARKLIERGA-ENVLVSLgADGALLVTKDG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490281904 258 AgrwvpsWR--LPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQ 312
Cdd:cd01164 234 V------YRasPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAF 284
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
33-316 |
3.58e-10 |
|
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: 59.91 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 33 VHSERA-TGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNdGDYITAMLDQYHINRQLVqrTSSAPTSMTQVMTDAEGQRTF 111
Cdd:TIGR03828 27 VESTRIdAGGKGINVSRVLKNL--GVDVVALGFLGGFT-GDFIEALLREEGIKTDFV--RVPGETRINVKIKEPSGTETK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 112 FHSPGA-------NRLLD-----LPAFEPL----DAPLKIfhlgyllllesldrPDEVYgtrsARLLAQMRERGYEVSLD 175
Cdd:TIGR03828 102 LNGPGPeiseeelEALLEklraqLAEGDWLvlsgSLPPGV--------------PPDFY----AELIALAREKGAKVILD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 176 lVSrkGDP-----RYRPLVL-PalkhldyltiNELEASEFSGLEirLPNGEPhvanIARAASALLDAGVRQRVVIHCPEG 249
Cdd:TIGR03828 164 -TS--GEAlrdglKAKPFLIkP----------NDEELEELFGRE--LKTLEE----IIEAARELLDLGAENVLISLGADG 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490281904 250 AWGVSRTEAgrwvpsWR--LPPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANA 316
Cdd:TIGR03828 225 ALLVTKEGA------LFaqPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGT 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-307 |
1.06e-08 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 55.51 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPERGWLVEIVHSERATGGApLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINr 85
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGGG-FNVMVAASRL--GIPTVNAGPLGNGNWADQIRQAMRDEGIE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQRTFFHSPGANRLLDLPAFEPLD-APLKIFHLGYLLLLesldrpdevYGTRSARLLAQ 164
Cdd:cd01944 78 ILLPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTvAPYDYVYLSGYTLA---------SENASKVILLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 165 MRER---GYEVSLDLVSRKGDPrYRPLVLPALKHLDYLTINELEASEFSGleirlpNGEPHVANIARAASALLDAGVrqr 241
Cdd:cd01944 149 WLEAlpaGTTLVFDPGPRISDI-PDTILQALMAKRPIWSCNREEAAIFAE------RGDPAAEASALRIYAKTAAPV--- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490281904 242 VVIHCPEGAWGVSRTEAGRWVPSWrlpPEEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACA 307
Cdd:cd01944 219 VVRLGSNGAWIRLPDGNTHIIPGF---KVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAA 281
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
14-330 |
1.23e-08 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 55.51 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 14 VDHVHQIGqwpergwlvEIVHSE---RATGGAPLNVLLTLAKMHAGLPLqaVGLIGEDNDG-DYITAMLDQyHINRQLVQ 89
Cdd:PTZ00292 32 VDRMPQVG---------ETLHGTsfhKGFGGKGANQAVMASKLGAKVAM--VGMVGTDGFGsDTIKNFKRN-GVNTSFVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 90 RTSSAPTSMTQVMTDAE-GQRTFFHSPGANRLLDlPAFepLDAPLKIFHLGYLLLLESLDRPDEVygtrSARLLAQMRER 168
Cdd:PTZ00292 100 RTENSSTGLAMIFVDTKtGNNEIVIIPGANNALT-PQM--VDAQTDNIQNICKYLICQNEIPLET----TLDALKEAKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 169 GYEVSLDLVSRKgDPRYRPLVLPALKHLDYLTINELEASEFSGLEIRlpNGEphvaNIARAASALLDAGVRQRVVIHCPE 248
Cdd:PTZ00292 173 GCYTVFNPAPAP-KLAEVEIIKPFLKYVSLFCVNEVEAALITGMEVT--DTE----SAFKASKELQQLGVENVIITLGAN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 249 GAWGVSRTEAGRWVPSWRLppeEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANAIDGAKTLPELQA 328
Cdd:PTZ00292 246 GCLIVEKENEPVHVPGKRV---KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPA 322
|
..
gi 490281904 329 FI 330
Cdd:PTZ00292 323 DV 324
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
40-307 |
2.60e-08 |
|
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: 54.28 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 40 GGAPLNVLLTLAKmhAGLPLQAVGLIGEDNDGDYITAMLDQYHINRQLVqRTSSAPTSMTQVMTDaEGQRTFFHS----- 114
Cdd:cd01940 22 GGNALNVAVYAKR--LGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELV-DGDRIFGLSnkggv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 115 ----PGANRLLDLPAFEpldaplkIFHLGyllllesldrpdeVYGtRSARLLAQMRERGYE---VSLDlVSRKGDPRYRP 187
Cdd:cd01940 98 arehPFEADLEYLSQFD-------LVHTG-------------IYS-HEGHLEKALQALVGAgalISFD-FSDRWDDDYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 188 LVLPalkHLDYLTINeleASEFSGLEIRlpngephvaniaRAASALLDAGVRQRVVIHCPEGAWGvsrtEAGRWVPSWRL 267
Cdd:cd01940 156 LVCP---YVDFAFFS---ASDLSDEEVK------------AKLKEAVSRGAKLVIVTRGEDGAIA----YDGAVFYSVAP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490281904 268 PPEEIIGSVGAGDAFCAGLLYG-SHERWPLTASLQLAHACA 307
Cdd:cd01940 214 RPVEVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQGAQFA 254
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
40-306 |
1.17e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 52.63 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 40 GGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINRQLVQRTSSAPTSMTQVMTDAEGQR--TFFHSPGA 117
Cdd:PRK09434 28 GGAPANVAVGIARL--GGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERsfTFMVRPSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 118 NRLL---DLPAFEPLDaplkIFHLGYLLLLeslDRPdevygTRSARLLA--QMRERGYEVSLDLVSR----KGDPRYRPL 188
Cdd:PRK09434 106 DLFLqpqDLPPFRQGE----WLHLCSIALS---AEP-----SRSTTFEAmrRIKAAGGFVSFDPNLRedlwQDEAELREC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 189 VLPALKHLDYLtineleasEFSGLEIRLPNGEPHVANIARAASALLdaGVRQRVVIHCPEGAWGVSRTEagrwVPSWRLP 268
Cdd:PRK09434 174 LRQALALADVV--------KLSEEELCFLSGTSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQ----VQHFPAP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490281904 269 PEEIIGSVGAGDAFCAGLLYG--SHERWPLTASL----QLAHAC 306
Cdd:PRK09434 240 SVDPVDTTGAGDAFVAGLLAGlsQAGLWTDEAELaeiiAQAQAC 283
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
221-328 |
4.60e-07 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 50.85 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 221 PHVANIARAASALLDAGVRQRVVIHCPEGAWGVSrtEAGRWVPSwrlPPE-EIIGSVGAGDAFCAGLLYGSHERWPLTAS 299
Cdd:PRK09513 200 PELKDVIEAAHALREQGIAHVVISLGAEGALWVN--ASGEWIAK---PPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHT 274
|
90 100
....*....|....*....|....*....
gi 490281904 300 LQLAHACARASLQAANAidGAKTLPELQA 328
Cdd:PRK09513 275 LRLATAVSALAVSQSNV--GITDRPQLAA 301
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
162-316 |
1.81e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 48.58 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 162 LAQMRERGYEVSLDLVSRKGDPryrpLVLPALKHLDYLTINELEASEFsgLEIRLpngephvaniaraaSALLDAGVRQR 241
Cdd:PRK09813 129 FPQLHAAGKLTAFDFSDKWDSP----LWQTLVPHLDYAFASAPQEDEF--LRLKM--------------KAIVARGAGVV 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490281904 242 VVIHCPEG--AWGVSRTeagrwvpsWRLPPE--EIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANA 316
Cdd:PRK09813 189 IVTLGENGsiAWDGAQF--------WRQAPEpvTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
189-331 |
3.75e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 48.10 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 189 VLPALKHLDYLTINELEASEFSGlEIRLPNGEphVANIARAASALLDA-GVRQRVVIHC--PEGAWGVSRTEAgRWVPSW 265
Cdd:PTZ00247 208 LLQVLPYVDILFGNEEEAKTFAK-AMKWDTED--LKEIAARIAMLPKYsGTRPRLVVFTqgPEPTLIATKDGV-TSVPVP 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490281904 266 RLPPEEIIGSVGAGDAFCAGLL--YGSHErwPLTASLQLAHACARASLQAanaiDGAkTLPELQAFIQ 331
Cdd:PTZ00247 284 PLDQEKIVDTNGAGDAFVGGFLaqYANGK--DIDRCVEAGHYSAQVIIQH----NGC-TYPEKPPFLP 344
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
168-305 |
2.27e-05 |
|
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: 45.27 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 168 RGYEVSLDLVsrkgdPRYRPLVLPalkHLDYLTINELEASEFSGLEIRLpngephVANIARAASALLDAGVRQRVVIHCP 247
Cdd:cd01173 117 KLYVVAEEIV-----PVYRDLLVP---LADIITPNQFELELLTGKKIND------LEDAKAAARALHAKGPKTVVVTSVE 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490281904 248 EG------AWGVSRTEAGRWvpswRLPPEEIIGS-VGAGDAFCAGLLYGSHERWPLTASLQLAHA 305
Cdd:cd01173 183 LAdddrieMLGSTATEAWLV----QRPKIPFPAYfNGTGDLFAALLLARLLKGKSLAEALEKALN 243
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
192-316 |
2.60e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 45.59 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 192 ALKHL----DYLTINELEASEFSGleIRLPngephvaniARAASALLDAGVR-QRVVIHC-PEGAWGVSRTEAGRwVPSW 265
Cdd:PLN02341 278 ALEHLlrmsDVLLLTSEEAEALTG--IRNP---------ILAGQELLRPGIRtKWVVVKMgSKGSILVTRSSVSC-APAF 345
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490281904 266 RLppeEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANA 316
Cdd:PLN02341 346 KV---NVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCGA 393
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
6-306 |
3.26e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.00 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 6 IIAAGNMLVDHVHQIGQWPergwLVEIVHSERATGGAPLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINR 85
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVS----LAEAPAFKKAPGGAPANVAVGISRL--GGSSAFIGKVGDDEFGHMLADILKKNGVNN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 86 QLVQRTSSAPTSMTQVMTDAEGQR--TFFHSPGANRLLDLpafEPLDAPL----KIFHlgyllllesldrpdevYGT--- 156
Cdd:PLN02323 87 EGVRFDPGARTALAFVTLRSDGERefMFYRNPSADMLLRE---SELDLDLirkaKIFH----------------YGSisl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 157 -----RSARLLAqMR---ERGYEVSLdlvsrkgDPRYR-PL----------VLPALKHLDYLTINELEAsEFsgleirLP 217
Cdd:PLN02323 148 itepcRSAHLAA-MKiakEAGALLSY-------DPNLRlPLwpsaeaaregIMSIWDEADIIKVSDEEV-EF------LT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 218 NGEPHVANiarAASALLDAGVRQRVVIHCPEGAWGVSRTEAGRwVPSWRLPPeeiIGSVGAGDAFCAGLL---------Y 288
Cdd:PLN02323 213 GGDDPDDD---TVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGR-VEGFKVKA---VDTTGAGDAFVGGLLsqlakdlslL 285
|
330
....*....|....*...
gi 490281904 289 GSHERwpLTASLQLAHAC 306
Cdd:PLN02323 286 EDEER--LREALRFANAC 301
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
192-317 |
6.87e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 43.94 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 192 ALKHLDYLTINELEASEFS---GLEIRlpngepHVANIARAASALLDA-GVRQRVVIhCPEGAWGVSRTEAGRWV--PSW 265
Cdd:PLN02548 200 ALPYVDFLFGNETEARTFAkvqGWETE------DVEEIALKISALPKAsGTHKRTVV-ITQGADPTVVAEDGKVKefPVI 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490281904 266 RLPPEEIIGSVGAGDAFCAGLLYGsherwpLTASLQLAHaCARASLQAANAI 317
Cdd:PLN02548 273 PLPKEKLVDTNGAGDAFVGGFLSQ------LVQGKDIEE-CVRAGNYAANVI 317
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
186-333 |
7.63e-05 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 43.70 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 186 RPLVLPALKHLDYLTINELEASEFSGLEIRlpngepHVANIARAASALLDAGVrQRVVIHC-PEGAWgVSRTEAGRWVPS 264
Cdd:PRK11142 169 RELPDELLALVDIITPNETEAEKLTGIRVE------DDDDAAKAAQVLHQKGI-ETVLITLgSRGVW-LSENGEGQRVPG 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490281904 265 WRLppeEIIGSVGAGDAFCAGLLYGSHERWPLTASLQLAHACARASLQAANAIDGAKTLPELQAFIQLQ 333
Cdd:PRK11142 241 FRV---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQEQ 306
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
192-307 |
2.82e-04 |
|
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: 42.33 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 192 ALKHLDYLTINELEASEFSGLEIRLPNGEPHVANiarAASALLDAGVRQR----VVIHCpeGAWG-VSRTEAG---RWVP 263
Cdd:cd01943 177 ALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEA---VLQALLFSGILQDpgggVVLRC--GKLGcYVGSADSgpeLWLP 251
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490281904 264 SWRLPPEEIIGSVGAGDAFCAGLLYGSHerwpLTASLQLAHACA 307
Cdd:cd01943 252 AYHTKSTKVVDPTGGGNSFLGGFAAGLA----LTKSIDEACIYG 291
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
192-313 |
6.34e-04 |
|
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: 40.90 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 192 ALKHLDYLTINELEASEFSGLEIRlpngepHVANIARAASALLDAGVRQRVVIHCPEGAWGVSRTE-----AGRwvpSWR 266
Cdd:COG2240 135 LVPLADIITPNLTELALLTGRPYE------TLEEALAAARALLALGPKIVVVTSVPLDDTPADKIGnlavtADG---AWL 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490281904 267 LPPEEIIGS-VGAGDAFCA----GLLYGsherWPLTASLQLAHACARASLQA 313
Cdd:COG2240 206 VETPLLPFSpNGTGDLFAAlllaHLLRG----KSLEEALERAAAFVYEVLER 253
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
1-289 |
9.97e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 40.56 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 1 MERKGIIAAGNMLVDHvhqigqwPERGWLVEIV---HSERATGGAPLNVLLTLAKM---HAGLPLQAV---GLIGEDNDG 71
Cdd:PLN02813 91 LERLGLEKGTRKVINH-------EERGKVLRALdgcSYKASAGGSLSNTLVALARLgsqSAAGPALNVamaGSVGSDPLG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 72 DYITAMLDQYHINrQLVQRTSSAPTSMTQVMTDAEGQRTFFHSPGANRLLDL-PAFEPLDAPLKIFhlgyLLLLESLDRP 150
Cdd:PLN02813 164 DFYRTKLRRANVH-FLSQPVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNYdSCLASAISKSRVL----VVEGYLWELP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 151 DEVYGTRSARLLAqmRERGYEVSLDlvsrKGDP----RYRPLVLPALKH-LDYLTINELEASEFSGLEIrlpngephVAN 225
Cdd:PLN02813 239 QTIEAIAQACEEA--HRAGALVAVT----ASDVscieRHRDDFWDVMGNyADILFANSDEARALCGLGS--------EES 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490281904 226 IARAASALLDAgVRQRVVIHCPEGAWGVSRTEAgRWVPSwrlPPEEIIGSVGAGDAFCAGLLYG 289
Cdd:PLN02813 305 PESATRYLSHF-CPLVSVTDGARGSYIGVKGEA-VYIPP---SPCVPVDTCGAGDAYAAGILYG 363
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
30-314 |
1.46e-03 |
|
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: 39.85 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 30 VEIVHSERATGGApLNVLLTLAKMhaGLPLQAVGLIGEDNDGDYITAMLDQYHINRQLVQRTSSAPTSMTQVMtdAEGQR 109
Cdd:cd01172 30 VKVEREEIRLGGA-ANVANNLASL--GAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTTTKTRVI--ARNQQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 110 TFfhspGANRLLDLPAFEPLDAPLKifhlgyLLLLESLDRPDEV------YGTRSARLLAQMRERGYEVSLDLVsrkGDP 183
Cdd:cd01172 105 LL----RVDREDDSPLSAEEEQRLI------ERIAERLPEADVVilsdygKGVLTPRVIEALIAAARELGIPVL---VDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 184 ------RYRplvlpalkHLDYLTINELEASEFSGLEIrlpngePHVANIARAASALL-DAGVRQRVVIHCPEGAWGVSRT 256
Cdd:cd01172 172 kgrdysKYR--------GATLLTPNEKEAREALGDEI------NDDDELEAAGEKLLeLLNLEALLVTLGEEGMTLFERD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490281904 257 EAGRWVPSWRLPPEEIigsVGAGDAFCAGLLYGsherwpLTASLQLAHACARASLQAA 314
Cdd:cd01172 238 GEVQHIPALAKEVYDV---TGAGDTVIATLALA------LAAGADLEEAAFLANAAAG 286
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
193-314 |
4.02e-03 |
|
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: 38.22 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490281904 193 LKHLDYLTINELEASEFSGLeirlpngephvANIARAASALLDAGVRQRVVihcPEGAWGVSR-TEAGRW-VPSwrLPPE 270
Cdd:cd01946 161 LAKVDVVIINDGEARQLTGA-----------ANLVKAARLILAMGPKALII---KRGEYGALLfTDDGYFaAPA--YPLE 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490281904 271 EIIGSVGAGDAFcAGLLYGSHERWPLTASLQLAHACARASLQAA 314
Cdd:cd01946 225 SVFDPTGAGDTF-AGGFIGYLASQKDTSEANMRRAIIYGSAMAS 267
|
|
| |
