|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
5-293 |
5.65e-106 |
|
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: 310.25 E-value: 5.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 5 DLLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTV 84
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 85 GVLVGRD-PTGVALITVDPSGDNSIVVSPGANSRLLPADVRAATSLFHASRVVSAQLEIPLETVVEVVR-NLAPGGRFVL 162
Cdd:cd01174 81 YVEVVVGaPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRaARRAGVTVIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 163 NPSPPRELPAEVLAACDPLIVNEHEARVILGAACVSEDPADW-ARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAV 241
Cdd:cd01174 161 NPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKaARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2015363443 242 DAVDTTGAGDAFTAALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPT 293
Cdd:cd01174 241 KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
10-298 |
3.18e-91 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 272.94 E-value: 3.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 10 GSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVG 89
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 90 RD-PTGVALITVDPSGDNSIVVSPGANSRLLPADVRAATSLFHASRVVSAQLEIPLETVVEVVRNL-APGGRFVLNPSPP 167
Cdd:TIGR02152 81 KDtPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAkKHGVKVILNPAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 168 RE-LPAEVLAACDPLIVNEHEARVILGAACVSEDPADWA-RLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVD 245
Cdd:TIGR02152 161 IKdLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAaEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2015363443 246 TTGAGDAFTAALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPTAAEVD 298
Cdd:TIGR02152 241 TTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-297 |
2.58e-73 |
|
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: 227.46 E-value: 2.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 5 DLLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTV 84
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 85 GVLVGRD-PTGVALITVDPSGDNSIVVSPGANSRLLPADVRAAtsLFHASRVV-----SAQLEIPLETVVEVVRNL-APG 157
Cdd:COG0524 81 GVRRDPGaPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEA--LLAGADILhlggiTLASEPPREALLAALEAArAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 158 GRFVLNPS-------PPRELPAEVLAACDPLIVNEHEARVILGaacvSEDPADWARLLLAKGPRSVVVTLGAEGALVGDA 230
Cdd:COG0524 159 VPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTG----ETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015363443 231 SGVTRVPSVAVDAVDTTGAGDAFTAALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPTAAEV 297
Cdd:COG0524 235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
2-299 |
1.01e-72 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 226.93 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 2 YDYDLLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGV 81
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 82 DTVGVLVGRD-PTGVALITVDP-SGDNSIVVSPGANSRLLPADVRAATSL-FHASRVVSAQLEIPLETVVEVVRNLAPGG 158
Cdd:PTZ00292 94 NTSFVSRTENsSTGLAMIFVDTkTGNNEIVIIPGANNALTPQMVDAQTDNiQNICKYLICQNEIPLETTLDALKEAKERG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 159 RF-VLNPSP-PRELPAEVLAAC----DPLIVNEHEARVILGAACVSEDPADWA-RLLLAKGPRSVVVTLGAEG-ALVGDA 230
Cdd:PTZ00292 174 CYtVFNPAPaPKLAEVEIIKPFlkyvSLFCVNEVEAALITGMEVTDTESAFKAsKELQQLGVENVIITLGANGcLIVEKE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015363443 231 SGVTRVPSVAVDAVDTTGAGDAFTAALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPTAAEVDA 299
Cdd:PTZ00292 254 NEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPA 322
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
6-299 |
3.22e-72 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 224.75 E-value: 3.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 6 LLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVG 85
Cdd:PRK11142 5 LVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 86 V-LVGRDPTGVALITVDPSGDNSIVVSPGANSRLLPADVRAATSLFHASRVVSAQLEIPLETVVEVVRnLAP--GGRFVL 162
Cdd:PRK11142 85 VsVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAK-IAKqhGTKVIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 163 NPSPPRELPAEVLAACDPLIVNEHEARVILGAACVSEDPADWA-RLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAV 241
Cdd:PRK11142 164 NPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAaQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015363443 242 DAVDTTGAGDAFTAALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPTAAEVDA 299
Cdd:PRK11142 244 QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDA 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-258 |
1.48e-52 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 173.68 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 5 DLLVVGSANADLVIDVERRPaaGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTV 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 85 GVLV-GRDPTGVALITVDPSGDNSIVVSPGANSRLLPADVRAATSLFHASRVV----SAQLEIPLETVVEVVRNLAPGGR 159
Cdd:pfam00294 79 YVVIdEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 160 FVLNPSPP----RELPAEVLAACDPLIVNEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVT 234
Cdd:pfam00294 159 FDPNLLDPlgaaREALLELLPLADLLKPNEEELEALTGAKLDDiEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260
....*....|....*....|....*
gi 2015363443 235 RVPSV-AVDAVDTTGAGDAFTAALA 258
Cdd:pfam00294 239 HVPAVpKVKVVDTTGAGDSFVGGFL 263
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-257 |
2.00e-42 |
|
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: 147.07 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 5 DLLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTV 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 85 GV-LVGRDPTGVALITVDPsGDNSIVVS-PGANSRLLPADVRAATSLFhasRVVSAQLEIPLETVVEVVRnlAPGGRFVL 162
Cdd:cd01942 81 HVrVVDEDSTGVAFILTDG-DDNQIAYFyPGAMDELEPNDEADPDGLA---DIVHLSSGPGLIELARELA--AGGITVSF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 163 NPSP-----PRELPAEVLAACDPLIVNEHEARVILGAacvsedpADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVP 237
Cdd:cd01942 155 DPGQelprlSGEELEEILERADILFVNDYEAELLKER-------TGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVP 227
|
250 260
....*....|....*....|.
gi 2015363443 238 SV-AVDAVDTTGAGDAFTAAL 257
Cdd:cd01942 228 AVpAVKVVDTTGAGDAFRAGF 248
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
7-257 |
7.33e-36 |
|
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: 130.45 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 7 LVVGSANADLVIDVERRPAAgetvlggdLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGV 86
Cdd:cd01167 3 VCFGEALIDFIPEGSGAPET--------FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 87 -LVGRDPTGVALITVDPSGDNS--IVVSPGAN----SRLLPADVRAATsLFHASRVvsAQLEIPL-ETVVEVVRNLAPGG 158
Cdd:cd01167 75 qFDPAAPTTLAFVTLDADGERSfeFYRGPAADllldTELNPDLLSEAD-ILHFGSI--ALASEPSrSALLELLEAAKKAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 159 RFVL-----------NPSPPRELPAEVLAACDPLIVNEHEARVILGaacvSEDPADWARLLLAKGPRSVVVTLGAEGALV 227
Cdd:cd01167 152 VLISfdpnlrpplwrDEEEARERIAELLELADIVKLSDEELELLFG----EEDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260 270
....*....|....*....|....*....|
gi 2015363443 228 GDASGVTRVPSVAVDAVDTTGAGDAFTAAL 257
Cdd:cd01167 228 YTKGGVGEVPGIPVEVVDTTGAGDAFVAGL 257
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
24-257 |
1.00e-35 |
|
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: 130.00 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 24 PAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRD-PTGVALITVDP 102
Cdd:cd01166 15 PGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGLYFLEIGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 103 SGDNSIV--VSPGANSRLLPADVRAA----TSLFHASRVVSAQLEIPLETVVEVVRNLAPGGRFV---LNPSP------- 166
Cdd:cd01166 95 GGERRVLyyRAGSAASRLTPEDLDEAalagADHLHLSGITLALSESAREALLEALEAAKARGVTVsfdLNYRPklwsaee 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 167 PRELPAEVLAACDPLIVNEHEARVILGAAcVSEDPADwARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDT 246
Cdd:cd01166 175 AREALEELLPYVDIVLPSEEEAEALLGDE-DPTDAAE-RALALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDT 252
|
250
....*....|.
gi 2015363443 247 TGAGDAFTAAL 257
Cdd:cd01166 253 TGAGDAFAAGF 263
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
38-256 |
5.00e-27 |
|
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: 107.31 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 38 HPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTGVALITVDPSGDNSIVVSPGANSR 117
Cdd:cd01168 53 IAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 118 LLPADVraATSLFHASRVV---SAQLEIPLETVVEVVRNL-APGGRFVLNPSPP------RELPAEVLAACDPLIVNEHE 187
Cdd:cd01168 133 LSPDDL--DWSLLAKAKYLyleGYLLTVPPEAILLAAEHAkENGVKIALNLSAPfivqrfKEALLELLPYVDILFGNEEE 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 188 ARVILGAAcvSEDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVD-AVDTTGAGDAFTAA 256
Cdd:cd01168 211 AEALAEAE--TTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGG 278
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
39-259 |
1.91e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 97.31 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLvgRDP---TGVALITVDPSGDNSI--VVSPG 113
Cdd:PRK09434 27 PGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLR--LDPahrTSTVVVDLDDQGERSFtfMVRPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 114 ANSRLLPADV---RAATSLFHASRVVSAqlEIPLETVVEVVRNLAPGGRFVL-----------NPSPPRELPAEVLAACD 179
Cdd:PRK09434 105 ADLFLQPQDLppfRQGEWLHLCSIALSA--EPSRSTTFEAMRRIKAAGGFVSfdpnlredlwqDEAELRECLRQALALAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 180 PLIVNEHEARVILGAACVSEDPADWARLLlakGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAALAW 259
Cdd:PRK09434 183 VVKLSEEELCFLSGTSQLEDAIYALADRY---PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLA 259
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
6-257 |
3.55e-23 |
|
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: 95.95 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 6 LLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGvDTVG 85
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGG-DKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 86 VLVGRDPTGVALITVDPSGDNSIVVSPGANSRLLP-ADVRAATSLFHASRVVSAQLEIPLETVVEVVRNLAPGGRFvlnp 164
Cdd:cd01947 81 VAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKwPILDEGDGVFITAAAVDKEAIRKCRETKLVILQVTPRVRV---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 165 spprELPAEVLAACDPLIVNEHEarvilgaaCVSEDPADwarLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAV 244
Cdd:cd01947 157 ----DELNQALIPLDILIGSRLD--------PGELVVAE---KIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVP 221
|
250
....*....|...
gi 2015363443 245 DTTGAGDAFTAAL 257
Cdd:cd01947 222 DSTGAGDSFAAGF 234
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-258 |
1.77e-22 |
|
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: 94.30 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 6 LLVVGSANADLVIDVErrpaaGETVLGGDLAVH----PGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGV 81
Cdd:cd01941 2 IVVIGAANIDLRGKVS-----GSLVPGTSNPGHvkqsPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 82 DTVGVLVGRDPTGVALITVDPSGDNSIVVS-PGANSRLLPADVRAATSLFHASRVVSAQLEIPLETVVEVVRnLAPGGRF 160
Cdd:cd01941 77 NVRGIVFEGRSTASYTAILDKDGDLVVALAdMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLA-LAAKHGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 161 VLNPSPPREL----PAEVLAACDPLIVNEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALV--GDASGV 233
Cdd:cd01941 156 PVAFEPTSAPklkkLFYLLHAIDLLTPNRAELEALAGALIENnEDENKAAKILLLPGIKNVIVTLGAKGVLLssREGGVE 235
|
250 260
....*....|....*....|....*..
gi 2015363443 234 TRV--PSVAVDAVDTTGAGDAFTAALA 258
Cdd:cd01941 236 TKLfpAPQPETVVNVTGAGDAFVAGLV 262
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
7-259 |
1.82e-22 |
|
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: 94.28 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 7 LVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGV 86
Cdd:cd01945 3 LGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 87 LVGRDPTGVALITVDPSGDNSIV----VSPGANSRLLPADVRAATSLFHA-SRVVSAQLEIpletvVEVVRNLAPGGRFV 161
Cdd:cd01945 83 VVAPGARSPISSITDITGDRATIsitaIDTQAAPDSLPDAILGGADAVLVdGRQPEAALHL-----AQEARARGIPIPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 162 LNPSPPRELpAEVLAACDPLIVNEHEARVILGAAcvSEDPADWARLLlakGPRSVVVTLGAEGAL-VGDASGVTRVPSVA 240
Cdd:cd01945 158 LDGGGLRVL-EELLPLADHAICSENFLRPNTGSA--DDEALELLASL---GIPFVAVTLGEAGCLwLERDGELFHVPAFP 231
|
250
....*....|....*....
gi 2015363443 241 VDAVDTTGAGDAFTAALAW 259
Cdd:cd01945 232 VEVVDTTGAGDVFHGAFAH 250
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
15-259 |
5.69e-21 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 90.58 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 15 DLVIDVERrPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDgHGRLLIDSLRAAGVDTVGVLVgRDPTG 94
Cdd:COG1105 11 DRTYEVDE-LEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGF-TGEFIEELLDEEGIPTDFVPI-EGETR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 95 VALITVDP-SGDNSIVVSPGAnsRLLPADVRAATSLF-----HASRVV---SAQLEIPLETVVEVVRNL-APGGRFVLNP 164
Cdd:COG1105 88 INIKIVDPsDGTETEINEPGP--EISEEELEALLERLeellkEGDWVVlsgSLPPGVPPDFYAELIRLArARGAKVVLDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 165 SppRELPAEVLAACdPLIV--NEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAV 241
Cdd:COG1105 166 S--GEALKAALEAG-PDLIkpNLEELEELLGRPLETlEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKV 242
|
250
....*....|....*...
gi 2015363443 242 DAVDTTGAGDAFTAALAW 259
Cdd:COG1105 243 EVVSTVGAGDSMVAGFLA 260
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
40-300 |
5.24e-20 |
|
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: 88.04 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 40 GGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRD-PTGVALITVDPSGDNSIVV--SPGANS 116
Cdd:TIGR04382 34 GGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGrRTSLVFLEIKPPDEFPLLFyrENAADL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 117 RLLPADV-----RAATSL------FHASRVVSAQLeipleTVVEVVRNLapGGRFVL----------NPSPPRELPAEVL 175
Cdd:TIGR04382 114 ALTPDDVdedyiASARALlvsgtaLSQEPSREAVL-----KALEYARAA--GVRVVLdidyrpylwkSPEEAGIYLRLVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 176 AACDPLIVNEHEARVILGaacvSEDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVT-RVPSVAVDAVDTTGAGDAFT 254
Cdd:TIGR04382 187 PLVDVIIGTREEFDIAGG----EGDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEGvEVPGFPVEVLNVLGAGDAFA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2015363443 255 AALAWKLGAGAALAEAAAYAARVGAAAVTRRGAQESYPTAAEVDAL 300
Cdd:TIGR04382 263 SGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLEELEAF 308
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
6-257 |
1.32e-19 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 86.71 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 6 LLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGkGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVG 85
Cdd:cd01944 2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 86 VLVGRDPTGVALITVDPSGDNSIVVSPGA----NSRLLPADVRAATSLFHASRVVSAQLEIPLETVVEVVRNLAPGGRFV 161
Cdd:cd01944 81 PPRGGDDGGCLVALVEPDGERSFISISGAeqdwSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 162 LNPSP-----PRELPAEVLAACDPLIVNEHEARVILGAACVSEDpaDWARLLLAKGPRSVVVTLGAEGALVGDASGVTR- 235
Cdd:cd01944 161 FDPGPrisdiPDTILQALMAKRPIWSCNREEAAIFAERGDPAAE--ASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHi 238
|
250 260
....*....|....*....|..
gi 2015363443 236 VPSVAVDAVDTTGAGDAFTAAL 257
Cdd:cd01944 239 IPGFKVKAVDTIGAGDTHAGGM 260
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
3-258 |
5.54e-19 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 86.81 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 3 DYDLLVVGSANADLVIDVERRPAAG---ETVLGGDLAVHP-------GGKGANQAVAAARLGAGTALLARVGDDGHGRLL 72
Cdd:PLN02341 72 EIDVATLGNLCVDIVLPVPELPPPSreeRKAYMEELAASPpdkksweAGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 73 IDSLRAAGVDTVGVLVGRD---------PTGVALITVDPSGdnsivvSPGANSRL-------------LPADVRAAtslF 130
Cdd:PLN02341 152 LDVLAEEGISVVGLIEGTDagdsssasyETLLCWVLVDPLQ------RHGFCSRAdfgpepafswiskLSAEAKMA---I 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 131 HASRVV----SAQLEIPLETVVEVVRNLA---------PGGR---FVLNPSPPRELPAEVLAACDPLIVNEHEARVILGA 194
Cdd:PLN02341 223 RQSKALfcngYVFDELSPSAIASAVDYAIdvgtavffdPGPRgksLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGI 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015363443 195 AcvseDPADWARLLLAKGPRS--VVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAALA 258
Cdd:PLN02341 303 R----NPILAGQELLRPGIRTkwVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIA 364
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
15-259 |
2.53e-18 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 82.97 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 15 DLVIDVERrPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDgHGRLLIDSLRAAGVDTVGVLVGrDPTG 94
Cdd:cd01164 12 DLTIELDQ-LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVA-GETR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 95 VALITVDPSGDNSIVVSPGANsrLLPADVRA-ATSLFHASR-----VVSAQL--EIPLETVVEVVRNL-APGGRFVLNPS 165
Cdd:cd01164 89 INVKIKEEDGTETEINEPGPE--ISEEELEAlLEKLKALLKkgdivVLSGSLppGVPADFYAELVRLArEKGARVILDTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 166 PPrelPAEVLAACDPLIV--NEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVD 242
Cdd:cd01164 167 GE---ALLAALAAKPFLIkpNREELEELFGRPLGDeEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVK 243
|
250
....*....|....*..
gi 2015363443 243 AVDTTGAGDAFTAALAW 259
Cdd:cd01164 244 VVSTVGAGDSMVAGFVA 260
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
39-258 |
2.26e-17 |
|
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: 80.09 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTGVALITVDpSGDNSIVVS-PGANSR 117
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADVELV-DGDRIFGLSnKGGVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 118 LLPADVR----AATSLFHASrVVSAQLEIPletvvEVVRNLAPGGRFVLNPSPPRELPAEVLAACDplivneheaRVILG 193
Cdd:cd01940 100 EHPFEADleylSQFDLVHTG-IYSHEGHLE-----KALQALVGAGALISFDFSDRWDDDYLQLVCP---------YVDFA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015363443 194 AACVSEDPADWARLLLAK----GPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAALA 258
Cdd:cd01940 165 FFSASDLSDEEVKAKLKEavsrGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFL 233
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
37-260 |
2.95e-17 |
|
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: 80.31 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 37 VHPGGKGANQAVAAARLGAGTALLARVGDDgHGRLLIDSLRAAGVDTVGVLVgRDPTGVALITVDPSGDNSIVVSPGAns 116
Cdd:TIGR03168 32 KDAGGKGINVARVLARLGAEVVATGFLGGF-TGEFIEALLAEEGIKNDFVEV-KGETRINVKIKESSGEETELNEPGP-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 117 RLLPADVRA-----ATSLFHASRVV---SAQLEIPLETVVEVVRNLAPGG-RFVLNPSppRELPAEVLAACdPLIV--NE 185
Cdd:TIGR03168 108 EISEEELEQlleklRELLASGDIVVisgSLPPGVPPDFYAQLIAIARKKGaKVILDTS--GEALREALAAK-PFLIkpNH 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015363443 186 HEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAALAWK 260
Cdd:TIGR03168 185 EELEELFGRELKTlEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAG 260
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
16-258 |
7.76e-17 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 79.08 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 16 LVIDVERRpaagETVLGGdlavhpggkGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPT-- 93
Cdd:COG2870 44 PVVRVERE----EERPGG---------AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPtt 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 94 --------GVALITVDpSGDNSIVvsPGANSRLLPADVRAATSLFHAsrVVsaqLE------IPLETVVEVVRNLAPGGR 159
Cdd:COG2870 111 tktrviagGQQLLRLD-FEDRFPL--SAELEARLLAALEAALPEVDA--VI---LSdygkgvLTPELIQALIALARAAGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 160 FVLNPSPPRELpaEVLAACDPLIVNEHEARVILGAACVSEDPADWA--RLLLAKGPRSVVVTLGAEGALVGDASG-VTRV 236
Cdd:COG2870 183 PVLVDPKGRDF--SRYRGATLLTPNLKEAEAAVGIPIADEEELVAAaaELLERLGLEALLVTRGEEGMTLFDADGpPHHL 260
|
250 260
....*....|....*....|..
gi 2015363443 237 PSVAVDAVDTTGAGDAFTAALA 258
Cdd:COG2870 261 PAQAREVFDVTGAGDTVIATLA 282
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
39-257 |
1.32e-15 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 75.81 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVgrDP---TGVALITVDPSGDNSIVV--SPG 113
Cdd:PLN02323 42 PGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRF--DPgarTALAFVTLRSDGEREFMFyrNPS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 114 ANSRLLPAD-----VRAAtSLFH---------ASRvvSAQLEiPLETVVE--VVRNLAPGGRFVLNPSP--PRELPAEVL 175
Cdd:PLN02323 120 ADMLLRESEldldlIRKA-KIFHygsislitePCR--SAHLA-AMKIAKEagALLSYDPNLRLPLWPSAeaAREGIMSIW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 176 AACDPLIVNEHEARVILGaacvSEDPADWARL-LLAKGPRSVVVTLGAEGA--LVGDASGvtRVPSVAVDAVDTTGAGDA 252
Cdd:PLN02323 196 DEADIIKVSDEEVEFLTG----GDDPDDDTVVkLWHPNLKLLLVTEGEEGCryYTKDFKG--RVEGFKVKAVDTTGAGDA 269
|
....*
gi 2015363443 253 FTAAL 257
Cdd:PLN02323 270 FVGGL 274
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
6-259 |
1.99e-15 |
|
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: 73.28 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 6 LLVVGSANADLVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLArvgddghgrllidslraagvdtvg 85
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 86 vlvgrdptgvalitvdpsgdnsivvspgansrllpADVRAATSLFHASRVVSAQLEIPLETVVEVVRNLAPGGRfvlnpS 165
Cdd:cd00287 58 -----------------------------------ADAVVISGLSPAPEAVLDALEEARRRGVPVVLDPGPRAV-----R 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 166 PPRELPAEVLAACDPLIVNEHEARVILGAA-CVSEDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVT-RVPSVAVDA 243
Cdd:cd00287 98 LDGEELEKLLPGVDILTPNEEEAEALTGRRdLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEvHVPAFPVKV 177
|
250
....*....|....*.
gi 2015363443 244 VDTTGAGDAFTAALAW 259
Cdd:cd00287 178 VDTTGAGDAFLAALAA 193
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
37-257 |
1.32e-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: 68.97 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 37 VHPGGKGANQAVAAARLGAGTALLARVGDDghgRLLIDSLRAAGVDTVGVLVGRDPTGVALItVDPSGDNSIVVSPGANs 116
Cdd:cd01937 21 VKPGGPATYASLTLSRLGLTVKLVTKVGRD---YPDKWSDLFDNGIEVISLLSTETTTFELN-YTNEGRTRTLLAKCAA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 117 rllpadvRAATSLFHASRVVSAQL--EIPLETVVEVVRNLAPGGR----FVLNPSPPRELPAEVLAACDPLIVNEHEARV 190
Cdd:cd01937 96 -------IPDTESPLSTITAEIVIlgPVPEEISPSLFRKFAFISLdaqgFLRRANQEKLIKCVILKLHDVLKLSRVEAEV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015363443 191 ILgaacvseDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAAL 257
Cdd:cd01937 169 IS-------TPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAF 228
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
38-253 |
3.27e-12 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 66.20 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 38 HPGGKGANQA-VAAARLGAG---TALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTGV--ALITvdpsgdnsivvs 111
Cdd:PTZ00247 60 VPGGSALNTArVAQWMLQAPkgfVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTcaVLVC------------ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 112 pgANSRLLPADVRAATSL----FHASRVVSAQ------------LEIPLETVVEVVRNL-APGGRFVLNPSPPRELPA-- 172
Cdd:PTZ00247 128 --GKERSLVANLGAANHLsaehMQSHAVQEAIktaqlyylegffLTVSPNNVLQVAKHArESGKLFCLNLSAPFISQFff 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 173 ----EVLAACDPLIVNEHEARVI-----LGAACVSEDPADWARLLLAKG--PRSVVVTLGAEGALVGDASGVTRVPSVAV 241
Cdd:PTZ00247 206 erllQVLPYVDILFGNEEEAKTFakamkWDTEDLKEIAARIAMLPKYSGtrPRLVVFTQGPEPTLIATKDGVTSVPVPPL 285
|
250
....*....|....*
gi 2015363443 242 DA---VDTTGAGDAF 253
Cdd:PTZ00247 286 DQekiVDTNGAGDAF 300
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
38-255 |
5.06e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 64.76 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 38 HPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTgvALITVDPSGDNSI----VVSPG 113
Cdd:PRK09813 21 FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT--AQTQVELHDNDRVfgdyTEGVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 114 ANSRLLPADVRAATS--LFHASRVVSAQLEIPletvvevvRNLAPGGR--FVLNPSPPRELPAEVLAACDPLIVNEHear 189
Cdd:PRK09813 99 ADFALSEEDYAWLAQydIVHAAIWGHAEDAFP--------QLHAAGKLtaFDFSDKWDSPLWQTLVPHLDYAFASAP--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 190 vilgaacvseDPADWARLLL----AKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTA 255
Cdd:PRK09813 168 ----------QEDEFLRLKMkaivARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIA 227
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
3-258 |
2.41e-11 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 63.08 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 3 DYdLLVVGSANADlVIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVD 82
Cdd:PRK09850 5 DY-VVIIGSANID-VAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 83 TVGVL-VGRDPTGVALITVDPSGDNSIVVSPGANSRLLPADVRAA-TSLFHASRVVSAQLEIPLETVVEVVRNLAPGGRF 160
Cdd:PRK09850 83 VDKCLiVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQhREFIQRAKVIVADCNISEEALAWILDNAANVPVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 161 VLNPSPPRELPA-EVLAACDPLIVNEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTR-VP 237
Cdd:PRK09850 163 VDPVSAWKCVKVrDRLNQIHTLKPNRLEAETLSGIALSGrEDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGwSA 242
|
250 260
....*....|....*....|.
gi 2015363443 238 SVAVDAVDTTGAGDAFTAALA 258
Cdd:PRK09850 243 PIKTNVINVTGAGDAMMAGLA 263
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
38-258 |
3.30e-11 |
|
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: 62.58 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 38 HPGGkGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTGVAlitvdpsgdNSIVVSpgaNSR 117
Cdd:cd01172 38 RLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPTTTK---------TRVIAR---NQQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 118 LLPADvraatslFHASRVVSAQLEIPLetvVEVVRNLAPG---------GRFVLNPSPPREL-----PAEVLAACDP--- 180
Cdd:cd01172 105 LLRVD-------REDDSPLSAEEEQRL---IERIAERLPEadvvilsdyGKGVLTPRVIEALiaaarELGIPVLVDPkgr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 181 ----------LIVNEHEARVILGAACVSEDPADWA--RLLLAKGPRSVVVTLGAEG-ALVGDASGVTRVPSVAVDAVDTT 247
Cdd:cd01172 175 dyskyrgatlLTPNEKEAREALGDEINDDDELEAAgeKLLELLNLEALLVTLGEEGmTLFERDGEVQHIPALAKEVYDVT 254
|
250
....*....|.
gi 2015363443 248 GAGDAFTAALA 258
Cdd:cd01172 255 GAGDTVIATLA 265
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
17-257 |
6.93e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 62.52 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 17 VIDVERRPAAGETVLGGDLAVHPGGKGANQAVAAARLGAGT--------ALLARVGDDGHGRLLIDSLRAAGVDTVGVLV 88
Cdd:PLN02813 103 VINHEERGKVLRALDGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANVHFLSQPV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 89 GRDPTGVALITVDPSGDNSIVVSPGANSRL-LPADVRAATSlfhASRVVSAQ---LEIP--LETVVEVVRNLAPGGRFV- 161
Cdd:PLN02813 183 KDGTTGTVIVLTTPDAQRTMLSYQGTSSTVnYDSCLASAIS---KSRVLVVEgylWELPqtIEAIAQACEEAHRAGALVa 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 162 LNPSPP------RELPAEVLAAC-DPLIVNEHEARVILGAAcVSEDPADWARLLLAKGPRsVVVTLGAEGALVGDASGVT 234
Cdd:PLN02813 260 VTASDVscierhRDDFWDVMGNYaDILFANSDEARALCGLG-SEESPESATRYLSHFCPL-VSVTDGARGSYIGVKGEAV 337
|
250 260
....*....|....*....|...
gi 2015363443 235 RVPSVAVDAVDTTGAGDAFTAAL 257
Cdd:PLN02813 338 YIPPSPCVPVDTCGAGDAYAAGI 360
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
173-253 |
1.15e-08 |
|
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: 55.16 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 173 EVLAACDPLIVNEHEARVILGAACVSEDpadwARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAV-DTTGAGD 251
Cdd:cd01946 159 KVLAKVDVVIINDGEARQLTGAANLVKA----ARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGD 234
|
..
gi 2015363443 252 AF 253
Cdd:cd01946 235 TF 236
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
40-253 |
1.75e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 54.80 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 40 GGKGANQAVA-AARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGVLVGRDPTGVALITVDPSGDN------SIVVSP 112
Cdd:PLN02379 86 GGSVANTIRGlSAGFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVDALGNRtmrpclSSAVKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 113 GANsRLLPADVRAATSL-----FHASRVVSAQLEIPLETVVEVVRNLApGGRFVLNPSPP--RELPAEVLAACdplIVNE 185
Cdd:PLN02379 166 QAD-ELTKEDFKGSKWLvlrygFYNLEVIEAAIRLAKQEGLSVSLDLA-SFEMVRNFRSPllQLLESGKIDLC---FANE 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015363443 186 HEARVILGAACVSeDPaDWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVA-VDAVDTTGAGDAF 253
Cdd:PLN02379 241 DEARELLRGEQES-DP-EAALEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGeTNAVDATGAGDLF 307
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
39-253 |
2.13e-05 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 45.48 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGANQA-VAAARLGA--GTALLARVGDDGHGRLLIDSLRAAGVdTVGVLVGRD-PTGV-ALITVDpsGDNSIVVSPG 113
Cdd:PLN02548 51 AGGATQNSIrVAQWMLQIpgATSYMGCIGKDKFGEEMKKCATAAGV-NVHYYEDEStPTGTcAVLVVG--GERSLVANLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 114 ANSRLLPADVRAATS--LFHASRVV-SAQ--LEIPLETVVEVVRNLAPGGR-FVLNPSPP------RELPAEVLAACDPL 181
Cdd:PLN02548 128 AANCYKVEHLKKPENwaLVEKAKFYyIAGffLTVSPESIMLVAEHAAANNKtFMMNLSAPficeffKDQLMEALPYVDFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 182 IVNEHEARVI-----LGAACVSEDPADWARLLLAKG--PRSVVVTLGAEGALVGDASGVTRVPSVAV---DAVDTTGAGD 251
Cdd:PLN02548 208 FGNETEARTFakvqgWETEDVEEIALKISALPKASGthKRTVVITQGADPTVVAEDGKVKEFPVIPLpkeKLVDTNGAGD 287
|
..
gi 2015363443 252 AF 253
Cdd:PLN02548 288 AF 289
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
199-257 |
2.71e-05 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 45.07 E-value: 2.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015363443 199 EDPADWARLLLAKGPRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAAL 257
Cdd:PRK09513 203 KDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGL 261
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
39-260 |
6.28e-05 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 44.00 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGANQAVAAARLGAG-TALLARVGddGHGRLLIDSLRAAGVdTVGVLVGRDPTGVAL-ITVDPSGDNSIVVSPGA-- 114
Cdd:PRK10294 37 PGGGGINVARAIAHLGGSaTAIFPAGG--ATGEHLVSLLADENV-PVATVEAKDWTRQNLhVHVEASGEQYRFVMPGAal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 115 ---NSRLLPADVRAATSlfHASRVVSAQLE--IPLETVVEVVRNLAPGG-RFVLNPSPPRELPAEVLAACDPLIVNEHEA 188
Cdd:PRK10294 114 nedEFRQLEEQVLEIES--GAILVISGSLPpgVKLEKLTQLISAAQKQGiRCIIDSSGDALSAALAIGNIELVKPNQKEL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015363443 189 RVILGAACVSEDPA-DWARLLLAKG-PRSVVVTLGAEGALVGDASGVTRVPSVAVDAVDTTGAGDAFTAALAWK 260
Cdd:PRK10294 192 SALVNRDLTQPDDVrKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLK 265
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
184-258 |
3.20e-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: 41.67 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 184 NEHEARVILGAACVSEDPA-DWARLLLAKGPRSVVVT--------LGAEGALVGDASGVTRVPSVAVDaVDTTGAGDAFT 254
Cdd:COG2240 145 NLTELALLTGRPYETLEEAlAAARALLALGPKIVVVTsvplddtpADKIGNLAVTADGAWLVETPLLP-FSPNGTGDLFA 223
|
....
gi 2015363443 255 AALA 258
Cdd:COG2240 224 ALLL 227
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
7-82 |
1.28e-03 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 39.91 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015363443 7 LVVGSANADL--VIDVERRPAAGETvlgGDLAVHPGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVD 82
Cdd:PRK09954 61 VVVGAINMDIrgMADIRYPQAASHP---GTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVN 135
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
39-86 |
1.96e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 39.51 E-value: 1.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2015363443 39 PGGKGANQAVAAARLGAGTALLARVGDDGHGRLLIDSLRAAGVDTVGV 86
Cdd:PLN02543 171 PGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAV 218
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
137-258 |
2.12e-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: 38.72 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 137 SAQLEIPLETVVEVvRNLAPGGRFVLNP---------SPPRELPAEVLAACDPL--IV--NEHEARVILGAACVS-EDPA 202
Cdd:cd01173 84 AEQVEAVAEIVKRL-KEKNPNLLYVCDPvmgdngklyVVAEEIVPVYRDLLVPLadIItpNQFELELLTGKKINDlEDAK 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015363443 203 DWARLLLAKGPRSVVVT---LGAEG-----ALVGDASGVTRVPSVAVDAvDTTGAGDAFTAALA 258
Cdd:cd01173 163 AAARALHAKGPKTVVVTsveLADDDriemlGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLL 225
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
39-258 |
2.31e-03 |
|
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: 39.25 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 39 PGGKGAnQAVAAARLGAGTALLARVG---DDGHG--RLLIDSLRAAGVDTVgvlVGRDP---TGVALITVDPSGDNSIVV 110
Cdd:cd01943 25 LGGAGT-YAILGARLFLPPPLSRSISwivDKGSDfpKSVEDELESWGTGMV---FRRDPgrlTTRGLNIYDGNDRRFFKY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 111 S----PGANSRLLPADVRAATSLFH----ASRVVSAQLEI--PLETVVEvvrNLAPGGRFVLNPSP----PRELP--AEV 174
Cdd:cd01943 101 LtpkkRIDVSDDLNSTPLIRSSCIHlicsPERCASIVDDIinLFKLLKG---NSPTRPKIVWEPLPdscdPENLEdlLQA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 175 LAACDPLIVNEHEARVILGAACVSE------DPADWARLLLAKGPRS---VVVTLGAEGALVGDASGVTR--VPSVAVDA 243
Cdd:cd01943 178 LPRVDVFSPNLEEAARLLGLPTSEPssdeekEAVLQALLFSGILQDPgggVVLRCGKLGCYVGSADSGPElwLPAYHTKS 257
|
250
....*....|....*...
gi 2015363443 244 ---VDTTGAGDAFTAALA 258
Cdd:cd01943 258 tkvVDPTGGGNSFLGGFA 275
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
184-258 |
4.38e-03 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 38.10 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015363443 184 NEHEARVILGAACVS-EDPADWARLLLAKGPRSVVVTLG-AEGALVGD----ASGVTRVPSVAVDAVDTTGAGDAFTAAL 257
Cdd:COG0351 133 NLPEAEALLGIEITTlDDMREAAKALLELGAKAVLVKGGhLPGDEAVDvlydGDGVREFSAPRIDTGNTHGTGCTLSSAI 212
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.
gi 2015363443 258 A 258
Cdd:COG0351 213 A 213
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