|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
1-309 |
0e+00 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 636.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 1 MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPV 80
Cdd:PRK10294 1 MVRIYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 81 ATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQNQG 160
Cdd:PRK10294 81 ATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 161 IRCIIDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQ 240
Cdd:PRK10294 161 IRCIIDSSGDALSAALAIGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKRVVVSLGPQGALGVDSENCIQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1531036277 241 VVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR 309
Cdd:PRK10294 241 VVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR 309
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
4-304 |
2.42e-128 |
|
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: 367.67 E-value: 2.42e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 4 IYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 84 EAKDWTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLE-IESGAILVISGSLPPGVKLEKLTQLISAAQNQGIR 162
Cdd:TIGR03168 81 EVKGETRINVKI-KESSGEETELNEPGPEISEEELEQLLEKLRElLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 163 CIIDSSGEALSAALAiGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVV 242
Cdd:TIGR03168 160 VILDTSGEALREALA-AKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRG-AENVLVSLGADGALLVTKEGALKAT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1531036277 243 PPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIY 304
Cdd:TIGR03168 238 PPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELL 299
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
4-305 |
2.26e-124 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 357.91 E-value: 2.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 4 IYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 84 EAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLE-IESGAILVISGSLPPGVKLEKLTQLISAAQNQGIR 162
Cdd:COG1105 81 PIEGETRINIKIVDPSDGTETEINEPGPEISEEELEALLERLEElLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 163 CIIDSSGEALSAALAiGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVV 242
Cdd:COG1105 161 VVLDTSGEALKAALE-AGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERG-AENVVVSLGADGALLVTEDGVYRAK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1531036277 243 PPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYA 305
Cdd:COG1105 239 PPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLA 301
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
3-292 |
7.42e-110 |
|
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: 320.25 E-value: 7.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 3 RIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVAT 82
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 83 VEAKDWTRQNLHVHvEASGEQYRFVMPGAALNEDEFRQLEEQVLEI-ESGAILVISGSLPPGVKLEKLTQLISAAQNQGI 161
Cdd:cd01164 81 VEVAGETRINVKIK-EEDGTETEINEPGPEISEEELEALLEKLKALlKKGDIVVLSGSLPPGVPADFYAELVRLAREKGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 162 RCIIDSSGEALSAALAiGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQV 241
Cdd:cd01164 160 RVILDTSGEALLAALA-AKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERG-AENVLVSLGADGALLVTKDGVYRA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1531036277 242 VPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGT 292
Cdd:cd01164 238 SPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGT 288
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
4-304 |
1.55e-79 |
|
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: 243.65 E-value: 1.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 4 IYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 84 EAKDWTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLE-IESGAILVISGSLPPGVKLEKLTQLISAAQNQGIR 162
Cdd:TIGR03828 81 RVPGETRINVKI-KEPSGTETKLNGPGPEISEEELEALLEKLRAqLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 163 CIIDSSGEALSAALAIgNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVV 242
Cdd:TIGR03828 160 VILDTSGEALRDGLKA-KPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLG-AENVLISLGADGALLVTKEGALFAQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1531036277 243 PPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIY 304
Cdd:TIGR03828 238 PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELL 299
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-294 |
1.00e-66 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 210.66 E-value: 1.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 9 LAPSLDSATITPQIYPEGKL----RCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGAT-GEHLVSLLADENVPVATV 83
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPgelvRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNfGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 84 EAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQNQG--I 161
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGtfD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 162 RCIIDSSGEALSAALA-IGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQ 240
Cdd:pfam00294 161 PNLLDPLGAAREALLElLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKG-IKTVIVTLGADGALVVEGDGEVH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1531036277 241 VVP-PPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRL 294
Cdd:pfam00294 240 VPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
1-290 |
7.11e-37 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 133.67 E-value: 7.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 1 MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAifpaGGATG-------EHLVSLL 73
Cdd:PRK09513 2 SRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTV----GGFLGkdnqdgfQQLFSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 74 ADENvPVATVEAKdwTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLE-IESGAILVISGSLPPGVKLEKLTQL 152
Cdd:PRK09513 78 GIAN-RFQVVQGR--TRINVKL-TEKDGEVTDFNFSGFEVTPADWERFVTDSLSwLGQFDMVAVSGSLPRGVSPEAFTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 153 ISAAQNQGIRCIIDSSGEALSAALAiGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAkRVVVSLGPQGALG 232
Cdd:PRK09513 154 MTRLRSQCPCIIFDSSREALVAGLK-AAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIA-HVVISLGAEGALW 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1531036277 233 VDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAgSAATLNQ 290
Cdd:PRK09513 232 VNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAV-SALAVSQ 288
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
17-293 |
6.44e-30 |
|
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: 114.98 E-value: 6.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 17 TITPQIYPEGKLRCTAPVFE--PGGGGINVARAIAHLGGSATAIFPAG-GATGEHLVSLLADENVPVATVEAKD--WTRQ 91
Cdd:COG0524 13 VARVDRLPKGGETVLAGSFRrsPGGAAANVAVALARLGARVALVGAVGdDPFGDFLLAELRAEGVDTSGVRRDPgaPTGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 92 NLhVHVEASGEQYRFVMPGAA--LNEDEFRQLEeqvleIESGAILVISG-SLPPGVKLEKLTQLISAAQNQGIRCIIDSS 168
Cdd:COG0524 93 AF-ILVDPDGERTIVFYRGANaeLTPEDLDEAL-----LAGADILHLGGiTLASEPPREALLAALEAARAAGVPVSLDPN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 169 ---------GEALSAALAigNIELVKPNQKELsalvnRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCI 239
Cdd:COG0524 167 yrpalwepaRELLRELLA--LVDILFPNEEEA-----ELLTGETDPEEAAAALLARG-VKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1531036277 240 QVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTR 293
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
4-277 |
9.85e-30 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 114.82 E-value: 9.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 4 IYTLTLAPSLDSAtitpqiYP--EGKLRCTAPVFE----PGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLaDEN 77
Cdd:PRK13508 2 ILTVTLNPSIDIS------YPldELKLDTVNRVVDvsktAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHL-DDQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 78 VPVATVEAKDWTRQNLHVHVEasGEQYRFVMPGAALNEDEFRQLEEQVLEI-ESGAILVISGSLPPGVKLEKLTQLISAA 156
Cdd:PRK13508 75 IKHAFYKIKGETRNCIAILHE--GQQTEILEKGPEISVQEADGFLHHFKQLlESVEVVAISGSLPAGLPVDYYAQLIELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 157 QNQGIRCIIDSSGEALSAALaIGNIE--LVKPNQKELSALVNRELTQPDDVRKAA--QEIVNSgkAKRVVVSLGPQGALG 232
Cdd:PRK13508 153 NQAGKPVVLDCSGAALQAVL-ESPYKptVIKPNIEELSQLLGKEVSEDLDELKEVlqQPLFEG--IEWIIVSLGADGAFA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1531036277 233 VDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVR 277
Cdd:PRK13508 230 KHNDTFYKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLK 274
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
37-292 |
1.14e-22 |
|
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: 95.31 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 37 PGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVE-AKDWTRQNLHVHVEASGEQYRFVMPGAALN 114
Cdd:cd01174 35 PGGKGANQAVAAARLGARVAMIGAVGDdAFGDELLENLREEGIDVSYVEvVVGAPTGTAVITVDESGENRIVVVPGANGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 115 ---EDEFRQLEEqvleIESGAILVISGSLPPGVKLEKLTqlisAAQNQGIRCIIDSSG-EALSAALaIGNIELVKPNQKE 190
Cdd:cd01174 115 ltpADVDAALEL----IAAADVLLLQLEIPLETVLAALR----AARRAGVTVILNPAPaRPLPAEL-LALVDILVPNETE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 191 LSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENA 270
Cdd:cd01174 186 AALLTGIEVTDEEDAEKAARLLLAKG-VKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGL 264
|
250 260
....*....|....*....|..
gi 1531036277 271 SLEEMVRFGVAAGSAATLNQGT 292
Cdd:cd01174 265 SLEEAIRFANAAAALSVTRPGA 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
22-291 |
1.26e-20 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 89.62 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 22 IYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIfpagGATGE-----HLVSLLADENVPVATVEAKDW--TRQNLh 94
Cdd:cd01167 12 FIPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFI----GKVGDdefgdFLLETLKEAGVDTRGIQFDPAapTTLAF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 95 VHVEASGE-QYRFVMPGAAlneDEFRQLEEQVLEIESGAILVIsGSL----PPGVklEKLTQLISAAQNQGIRCIID--- 166
Cdd:cd01167 87 VTLDADGErSFEFYRGPAA---DLLLDTELNPDLLSEADILHF-GSIalasEPSR--SALLELLEAAKKAGVLISFDpnl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 167 ----SSGEALSAALAIGNIE---LVKPNQKELsalvnRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCI 239
Cdd:cd01167 161 rpplWRDEEEARERIAELLEladIVKLSDEEL-----ELLFGEEDPEEIAALLLLFG-LKLVLVTRGADGALLYTKGGVG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1531036277 240 QVVPPPVKSQSTVGAGDSMVGAMTLKLAEN-------ASLEEMVRFGVAAGSAATLNQG 291
Cdd:cd01167 235 EVPGIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
35-286 |
7.56e-20 |
|
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: 87.37 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 35 FEPGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLL--ADENVPVATVEAKDwTRQNLHVHvEASGEQYrfvmpgA 111
Cdd:cd01941 32 QSPGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESekAGLNVRGIVFEGRS-TASYTAIL-DKDGDLV------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 112 ALNE-DEFRQLEEQVLE-----IESGAILVISGSLPPGVkLEKLTQLisaAQNQGIR--CIIDSSGEALSAALAIGNIEL 183
Cdd:cd01941 104 ALADmDIYELLTPDFLRkireaLKEAKPIVVDANLPEEA-LEYLLAL---AAKHGVPvaFEPTSAPKLKKLFYLLHAIDL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 184 VKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSEN--CIQVVPPPVkSQSTV---GAGDSM 258
Cdd:cd01941 180 LTPNRAELEALAGALIENNEDENKAAKILLLPG-IKNVIVTLGAKGVLLSSREGgvETKLFPAPQ-PETVVnvtGAGDAF 257
|
250 260
....*....|....*....|....*...
gi 1531036277 259 VGAMTLKLAENASLEEMVRFGVAAGSAA 286
Cdd:cd01941 258 VAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
37-286 |
8.84e-18 |
|
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: 81.85 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 37 PGGGGINVARAIAHLGGSATAI--FPAgGATGEHLVSLLADENVPVATVEAKDWTRQNL-HVHVEASGEQyRFVM--PGA 111
Cdd:cd01166 30 FGGAEANVAVGLARLGHRVALVtaVGD-DPFGRFILAELRREGVDTSHVRVDPGRPTGLyFLEIGAGGER-RVLYyrAGS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 112 AlnedeFRQLEEQVLE---IESGAILVISGSLP--PGVKLEKLTQLISAAQNQGIRCIID--------SSGEA---LSAA 175
Cdd:cd01166 108 A-----ASRLTPEDLDeaaLAGADHLHLSGITLalSESAREALLEALEAAKARGVTVSFDlnyrpklwSAEEAreaLEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 176 LAIGNIELvkPNQKELSALVNRELtqPDDVRKAAQEIvnSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAG 255
Cdd:cd01166 183 LPYVDIVL--PSEEEAEALLGDED--PTDAAERALAL--ALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAG 256
|
250 260 270
....*....|....*....|....*....|.
gi 1531036277 256 DSMVGAMTLKLAENASLEEMVRFGVAAGSAA 286
Cdd:cd01166 257 DAFAAGFLAGLLEGWDLEEALRFANAAAALV 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
39-299 |
2.57e-17 |
|
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: 80.68 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 39 GGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEAKDW-----TR---QNLHVhVEASGEQYRfvmp 109
Cdd:cd01172 40 GGAANVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGIVDEGRptttkTRviaRNQQL-LRVDREDDS---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 110 gaALNEDEFRQLEEQVLEIESGAILVI-----SGSLPPGVklekLTQLISAAQNQGIRCIIDSSGEALSAALaigNIELV 184
Cdd:cd01172 115 --PLSAEEEQRLIERIAERLPEADVVIlsdygKGVLTPRV----IEALIAAARELGIPVLVDPKGRDYSKYR---GATLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 185 KPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVP----PPVksqSTVGAGDSMVG 260
Cdd:cd01172 186 TPNEKEAREALGDEINDDDELEAAGEKLLELLNLEALLVTLGEEGMTLFERDGEVQHIPalakEVY---DVTGAGDTVIA 262
|
250 260 270
....*....|....*....|....*....|....*....
gi 1531036277 261 AMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDD 299
Cdd:cd01172 263 TLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKE 301
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
36-293 |
2.92e-14 |
|
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: 71.57 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 36 EPGGGGINVARAIAHLGGSATAIFPAGGAT-GEHLVSLLADENVPVATVeakdWTRQNLH-----VHVEASGEQYRFVMP 109
Cdd:cd01942 34 EFGGSAGNTAVALAKLGLSPGLVAAVGEDFhGRLYLEELREEGVDTSHV----RVVDEDStgvafILTDGDDNQIAYFYP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 110 GAAlneDEFRQLEEQVLEIESGAILVISGSlppgvkleKLTQLISAAQNQGIRCIID-------SSGEALSAALaiGNIE 182
Cdd:cd01942 110 GAM---DELEPNDEADPDGLADIVHLSSGP--------GLIELARELAAGGITVSFDpgqelprLSGEELEEIL--ERAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 183 LVKPNQKELSALVnrELTQPDDVRKAAqeivnsgKAKRVVVSLGPQGALGVDSENCIQVVP-PPVKSQSTVGAGDSMVGA 261
Cdd:cd01942 177 ILFVNDYEAELLK--ERTGLSEAELAS-------GVRVVVVTLGPKGAIVFEDGEEVEVPAvPAVKVVDTTGAGDAFRAG 247
|
250 260 270
....*....|....*....|....*....|..
gi 1531036277 262 MTLKLAENASLEEMVRFGVAAGSAATLNQGTR 293
Cdd:cd01942 248 FLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
181-294 |
4.18e-09 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 181 IELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENC-IQVVPPPVKSQSTVGAGDSMV 259
Cdd:PTZ00292 199 VSLFCVNEVEAALITGMEVTDTESAFKASKELQQLG-VENVIITLGANGCLIVEKENEpVHVPGKRVKAVDTTGAGDCFV 277
|
90 100 110
....*....|....*....|....*....|....*
gi 1531036277 260 GAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRL 294
Cdd:PTZ00292 278 GSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQS 312
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
37-298 |
4.47e-09 |
|
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: 56.21 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 37 PGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEAKDwtRQNLHVHVEASGEQYRF------VMP 109
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNdDAGAHVRSTLKRLGVDISHCRVKE--GENAVADVELVDGDRIFglsnkgGVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 110 GAALNEDEFRQLeeqvleieSGAILVISGSLPPGVKLEKLTQLISAAqnqGIRCIIDSSGEALS--AALAIGNIELVKPN 187
Cdd:cd01940 99 REHPFEADLEYL--------SQFDLVHTGIYSHEGHLEKALQALVGA---GALISFDFSDRWDDdyLQLVCPYVDFAFFS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 188 QKELSalvnreltqPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMV-GAMTLKL 266
Cdd:cd01940 168 ASDLS---------DEEVKAKLKEAVSRG-AKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIaGFLLSLL 237
|
250 260 270
....*....|....*....|....*....|..
gi 1531036277 267 AENASLEEMVRFGvaAGSAAtlnqgtRLCSHD 298
Cdd:cd01940 238 AGGTAIAEAMRQG--AQFAA------KTCGHE 261
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
37-294 |
1.60e-08 |
|
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: 54.93 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 37 PGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEAKDwtrqnlhvhvEASGEQYRFVMPGA---- 111
Cdd:cd01168 54 AGGSAANTIRGAAALGGSAAFIGRVGDdKLGDFLLKDLRAAGVDTRYQVQPD----------GPTGTCAVLVTPDAertm 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 112 -----ALNEDEFRQLEEQVleIESGAILVISGSLPPgVKLEKLTQLISAAQNQGIRCIIDSS--------GEALsaALAI 178
Cdd:cd01168 124 ctylgAANELSPDDLDWSL--LAKAKYLYLEGYLLT-VPPEAILLAAEHAKENGVKIALNLSapfivqrfKEAL--LELL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 179 GNIELVKPNQKELSALVNRELTQ-PDDVRKAAQEIVnsgkaKRVVVSLGPQGALGVDSENCIQV-VPPPVKSQSTVGAGD 256
Cdd:cd01168 199 PYVDILFGNEEEAEALAEAETTDdLEAALKLLALRC-----RIVVITQGAKGAVVVEGGEVYPVpAIPVEKIVDTNGAGD 273
|
250 260 270
....*....|....*....|....*....|....*...
gi 1531036277 257 SMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRL 294
Cdd:cd01168 274 AFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
24-291 |
3.90e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 53.79 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 24 PEGK---LRCtapvfePGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEAKDWTRQN-LHVHVE 98
Cdd:PRK09434 17 PEGEnryLKC------PGGAPANVAVGIARLGGESGFIGRVGDdPFGRFMQQTLQDEGVDTTYLRLDPAHRTStVVVDLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 99 ASGEQ-YRF-VMPGAalneDEFRQLEEqvleiesgailvisgsLPPGVKLEKLTQLISAAQNQGIRciiDSSGEALSAAL 176
Cdd:PRK09434 91 DQGERsFTFmVRPSA----DLFLQPQD----------------LPPFRQGEWLHLCSIALSAEPSR---STTFEAMRRIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 177 AIG-------NI-ELVKPNQKELSALVNR-------------ELTQ---PDDVRKAAQEIVNSGKAKRVVVSLGPQGALG 232
Cdd:PRK09434 148 AAGgfvsfdpNLrEDLWQDEAELRECLRQalaladvvklseeELCFlsgTSQLEDAIYALADRYPIALLLVTLGAEGVLV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1531036277 233 VDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLA------ENASLEEMVRFGVAAGSAATLNQG 291
Cdd:PRK09434 228 HTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSqaglwtDEAELAEIIAQAQACGALATTAKG 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
24-294 |
5.85e-08 |
|
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: 53.07 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 24 PEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVA-TVEAKDwTRQNLHVHVEASG 101
Cdd:cd01945 22 GDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDdAIGRLILAELAAEGVDTSfIVVAPG-ARSPISSITDITG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 102 EQ----YRFVMPGAALNEDEFrqleeqvLEIESGAILVISGSLPPGVKLekltqLISAAQNQGIRCIIDSSGEALSAALA 177
Cdd:cd01945 101 DRatisITAIDTQAAPDSLPD-------AILGGADAVLVDGRQPEAALH-----LAQEARARGIPIPLDLDGGGLRVLEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 178 IgnIELVKPNQkeLSALVNRELT--QPDDVRKAAQeivnSGKAKRVVVSLGPQG--ALGVDSENCIqVVPPPVKSQSTVG 253
Cdd:cd01945 169 L--LPLADHAI--CSENFLRPNTgsADDEALELLA----SLGIPFVAVTLGEAGclWLERDGELFH-VPAFPVEVVDTTG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1531036277 254 AGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRL 294
Cdd:cd01945 240 AGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRA 280
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
39-286 |
7.52e-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: 52.81 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 39 GGGINVARAIAHLGGSATAIFPAG-GATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAA--LNE 115
Cdd:cd01944 36 GGGFNVMVAASRLGIPTVNAGPLGnGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDGERSFISISGAEqdWST 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 116 DEFRQLEeqvleIESGAILVISGS--LPPGVKLEKLTQLISAAQNQ-------GIRcIIDSSGEALSAALAigNIELVKP 186
Cdd:cd01944 116 EWFATLT-----VAPYDYVYLSGYtlASENASKVILLEWLEALPAGttlvfdpGPR-ISDIPDTILQALMA--KRPIWSC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 187 NQKELSALVNRELTQPDDVRKAAQEIVNSGkakrVVVSLGPQGALGVDSENCIQVVPP-PVKSQSTVGAGDSMVGAMTLK 265
Cdd:cd01944 188 NREEAAIFAERGDPAAEASALRIYAKTAAP----VVVRLGSNGAWIRLPDGNTHIIPGfKVKAVDTIGAGDTHAGGMLAG 263
|
250 260
....*....|....*....|.
gi 1531036277 266 LAENASLEEMVRFGVAAGSAA 286
Cdd:cd01944 264 LAKGMSLADAVLLANAAAAIV 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
36-291 |
1.00e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 52.56 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 36 EPGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEA-KDWTRQNLHVHVEASGEQYRFVMPGA-- 111
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDdSIGESMRQQLAKDGIDTAPVSViKGESTGVALIFVNDEGENSIGIHAGAna 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 112 ALNEDEFRQLEEQVleIESGAILVisgslppgvKLEK-LTQLISAAQ---NQGIRCIIDSS-GEALSAALaIGNIELVKP 186
Cdd:PRK11142 117 ALTPALVEAHRELI--ANADALLM---------QLETpLETVLAAAKiakQHGTKVILNPApARELPDEL-LALVDIITP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 187 NQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKL 266
Cdd:PRK11142 185 NETEAEKLTGIRVEDDDDAAKAAQVLHQKG-IETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTAL 263
|
250 260
....*....|....*....|....*
gi 1531036277 267 AENASLEEMVRFGVAAGSAATLNQG 291
Cdd:PRK11142 264 LEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
130-267 |
2.72e-07 |
|
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: 50.17 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 130 SGAILVISGSLPpgvKLEKLTQLISAAQNQGIRCIIDSSGEALSAALAIGNIEL-----VKPNQKELSALVNRELTQPDD 204
Cdd:cd00287 57 GADAVVISGLSP---APEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKLLpgvdiLTPNEEEAEALTGRRDLEVKE 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1531036277 205 VRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQ-STVGAGDSMVGAMTLKLA 267
Cdd:cd00287 134 AAEAAALLLSKG-PKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVvDTTGAGDAFLAALAAGLA 196
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
199-291 |
1.07e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 49.83 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 199 LTQPDDVRKAAQEIVNSGK-AKRVVVSLGPQGALGVdSENCIQVVPPP-VKSQSTVGAGDSMVGAMTLKLAENASLEEMV 276
Cdd:PLN02341 299 LTGIRNPILAGQELLRPGIrTKWVVVKMGSKGSILV-TRSSVSCAPAFkVNVVDTVGCGDSFAAAIALGYIHNLPLVNTL 377
|
90
....*....|....*
gi 1531036277 277 RFGVAAGSAATLNQG 291
Cdd:PLN02341 378 TLANAVGAATAMGCG 392
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
32-291 |
2.60e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 45.00 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 32 APVFE--PGGGGINVARAIAHLGGSATAIFPAGGAT-GEHLVSLLADENVPVATVEAKDWTRQNL-HVHVEASGEQ---- 103
Cdd:PLN02323 35 APAFKkaPGGAPANVAVGISRLGGSSAFIGKVGDDEfGHMLADILKKNGVNNEGVRFDPGARTALaFVTLRSDGERefmf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 104 YR-----FVMPGAALNEDEFRQ-----------LEE-------QVLEI--ESGAILvisgSLPPGVKLeKLTQLISAAQn 158
Cdd:PLN02323 115 YRnpsadMLLRESELDLDLIRKakifhygsislITEpcrsahlAAMKIakEAGALL----SYDPNLRL-PLWPSAEAAR- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 159 QGIRCIIDSSgealsaalaigniELVKPNQKELSALVNRELTQPDDVRKAAQEivnsgKAKRVVVSLGPQGALGVDSENC 238
Cdd:PLN02323 189 EGIMSIWDEA-------------DIIKVSDEEVEFLTGGDDPDDDTVVKLWHP-----NLKLLLVTEGEEGCRYYTKDFK 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 239 IQVVPPPVKSQSTVGAGDSMVGAMTLKLAENAS-------LEEMVRFGVAAGSAATLNQG 291
Cdd:PLN02323 251 GRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERG 310
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
37-288 |
1.10e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 37 PGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEAS----GEQYRFVMPGA 111
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDdDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELHDNdrvfGDYTEGVMADF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 112 ALNEDEFRQLEEQvlEIESGAILvisgslppGVKLEKLTQLISAaqnqGIRCIIDSSGEALSaalaigniELVKPNQKEL 191
Cdd:PRK09813 102 ALSEEDYAWLAQY--DIVHAAIW--------GHAEDAFPQLHAA----GKLTAFDFSDKWDS--------PLWQTLVPHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 192 SALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENAS 271
Cdd:PRK09813 160 DYAFASAPQEDEFLRLKMKAIVARG-AGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMT 238
|
250
....*....|....*..
gi 1531036277 272 LEEMVRFGvAAGSAATL 288
Cdd:PRK09813 239 LPQAMAQG-TACAAKTI 254
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
23-281 |
1.56e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 43.00 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 23 YPE-----GKLRCTApvfepGGGGINVARAIAHLGGSATAIFPAGGA-TGEHLVslladENVPVATVEAKDWTR---QNL 93
Cdd:PRK09954 78 YPQaashpGTIHCSA-----GGVGRNIAHNLALLGRDVHLLSAIGDDfYGETLL-----EETRRAGVNVSGCIRlhgQST 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 94 HVHVEASGEQYRFVMpgaALNEDE-FRQLEEQVLE-----IESGAILVISGSLPPgvklEKLTQLISAAQnqGIRCIIDS 167
Cdd:PRK09954 148 STYLAIANRQDETVL---AINDTHiLQQLTPQLLNgsrdlIRHAGVVLADCNLTA----EALEWVFTLAD--EIPVFVDT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 168 SGE--ALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPP 245
Cdd:PRK09954 219 VSEfkAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQG-VQQIFVYLPDESVFCSEKDGEQFLLTAP 297
|
250 260 270
....*....|....*....|....*....|....*..
gi 1531036277 246 VKSQ-STVGAGDSMVGAMTLKLAENASLEEMVRFGVA 281
Cdd:PRK09954 298 AHTTvDSFGADDGFMAGLVYSFLEGYSFRDSARFAMA 334
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
178-286 |
4.82e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 41.13 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 178 IGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVSLGPQGALGVDSeNCIQVVPPPVKSQ--STVGAG 255
Cdd:PRK09850 178 LNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHG-LNRLVLSMGGDGVYYSDI-SGESGWSAPIKTNviNVTGAG 255
|
90 100 110
....*....|....*....|....*....|.
gi 1531036277 256 DSMVGAMTLKLAENASLEEMVRFGVAAGSAA 286
Cdd:PRK09850 256 DAMMAGLASCWVDGMPFAESVRFAQGCSSMA 286
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
113-171 |
5.26e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 40.98 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1531036277 113 LNEDEFRqleeqvLEIESG-AILVIS----GSLppgvklEKLTQLISAAQNQGIRCIIDSSGEA 171
Cdd:PRK05105 218 LREPDFQ------FEAEPGvRAIVIKptltGSL------EKCQELIEQAHALGLRAVISSSIES 269
|
|
| PRK14039 |
PRK14039 |
ADP-dependent glucokinase; Provisional |
86-268 |
7.81e-04 |
|
ADP-dependent glucokinase; Provisional
Pssm-ID: 184471 Cd Length: 453 Bit Score: 40.94 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 86 KDW--TRQNLHVHVE----ASGEQYRFVM-------PGAALNEDEFRQLE-------EQVLEIESGAILVISGSLPPGVK 145
Cdd:PRK14039 244 KWWksKNEKLRIHAElghfASKEIANSVFlilagivDSIGMNEDELAMLAnlhgipaEGILEMNAEAIGEAACQLASESG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 146 LEKL-------TQLISAAQNQGIRCIIDSSGEALSAA---LAIGNIELVKPNQKELSalvnrELTQPDDVRKAAQEIVNS 215
Cdd:PRK14039 324 LQRLiihtrefVLCVSKPDVKMAKKKIEAMEFGLKCAgvyAASGSLDGREFVEKEAS-----KLQESDFGREQVELFLKA 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1531036277 216 GKAKRvvvsLGpQGALGVDSENCIQVVPPPVKSQ--STVGAGDSMVGAMTLKLAE 268
Cdd:PRK14039 399 FGGKA----LG-LGAYGLREGYSVCILPTLVSKSpvTTVGLGDTLTAGTFLRLLE 448
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
183-277 |
1.25e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 40.10 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 183 LVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGpqgalGVDSENCIQVV----------PPPVKSQSTV 252
Cdd:PRK08573 133 VVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEELGAEAVVVKGG-----HLEGEEAVDVLyhngtfrefrAPRVESGCTH 207
|
90 100
....*....|....*....|....*
gi 1531036277 253 GAGDSMVGAMTLKLAENASLEEMVR 277
Cdd:PRK08573 208 GTGCSFSAAIAAGLAKGLDPEEAIK 232
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
106-277 |
1.52e-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: 39.49 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 106 FVMPGAALNEDE----FRQLEEQVLEIESGAILviSGSLPPGVKLEKLTQLISA--AQNQGIRCIID-----------SS 168
Cdd:cd01173 45 GTWTGFVLSAEEledlLEGLEALGLLLEYDAVL--TGYLGSAEQVEAVAEIVKRlkEKNPNLLYVCDpvmgdngklyvVA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 169 GEALSA--ALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVVS---LGPQG---ALGVDSENCIQ 240
Cdd:cd01173 123 EEIVPVyrDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKG-PKTVVVTsveLADDDrieMLGSTATEAWL 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 1531036277 241 VVPPPVKSQST-VGAGDSMVGAMTLKLAENASLEEMVR 277
Cdd:cd01173 202 VQRPKIPFPAYfNGTGDLFAALLLARLLKGKSLAEALE 239
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
209-293 |
1.83e-03 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 39.31 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 209 AQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVP--PPVKSQSTVGAGDSMVGAMTLKLAEN-ASLEEMVRFGVAAGSA 285
Cdd:cd01939 203 RGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPahKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQ 282
|
....*...
gi 1531036277 286 ATLNQGTR 293
Cdd:cd01939 283 KCTGVGFD 290
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
34-293 |
2.52e-03 |
|
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: 38.94 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 34 VFEPGGGGINVARAIAHLGGSATAIFPAGG-ATGEHLVSLLADENVPVaTVEAKDWTRQNLHVHVEASGEQYRFVMPGAA 112
Cdd:cd01947 32 RESPGGGGANVAVQLAKLGNDVRFFSNLGRdEIGIQSLEELESGGDKH-TVAWRDKPTRKTLSFIDPNGERTITVPGERL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 113 LNEDEFRQLEE-------------QVLEIESGAILVISGsLPPGVKLEKLTQLisaaqNQGirciidssgealsAALAIG 179
Cdd:cd01947 111 EDDLKWPILDEgdgvfitaaavdkEAIRKCRETKLVILQ-VTPRVRVDELNQA-----LIP-------------LDILIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 180 NielvkpnqkelsalvNRELTQPDDVRKAAQEivnsgKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMV 259
Cdd:cd01947 172 S---------------RLDPGELVVAEKIAGP-----FPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFA 231
|
250 260 270
....*....|....*....|....*....|....
gi 1531036277 260 GAMTLKLAENASLEEMVRFGVAAGSAATLNQGTR 293
Cdd:cd01947 232 AGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
183-277 |
5.37e-03 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 37.85 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1531036277 183 LVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGkAKRVVV---SLGPQGALGVD----SENCIQVVPPPVKSQSTVGAG 255
Cdd:pfam08543 122 LITPNLPEAEALTGRKIKTLEDMKEAAKKLLALG-AKAVLIkggHLEGEEAVVTDvlydGGGFYTLEAPRIPTKNTHGTG 200
|
90 100
....*....|....*....|..
gi 1531036277 256 DSMVGAMTLKLAENASLEEMVR 277
Cdd:pfam08543 201 CTLSAAIAANLAKGLSLPEAVR 222
|
|
| |
