|
Name |
Accession |
Description |
Interval |
E-value |
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-266 |
3.29e-99 |
|
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: 292.17 E-value: 3.29e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 2 LELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKMAESSGR 81
Cdd:TIGR03168 19 LTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFVEVKGETRINVKIKESSGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAGPW 161
Cdd:TIGR03168 99 ETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKVILDTSGEALREALAAKPF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 162 LIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:TIGR03168 179 LIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFL 258
|
250 260
....*....|....*....|....*
gi 2505224387 242 HGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:TIGR03168 259 AGLARGLSLEEALRFAVAAGSAAAF 283
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
2-267 |
4.49e-99 |
|
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: 291.36 E-value: 4.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 2 LELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKMAESSGR 81
Cdd:cd01164 20 LQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAGPW 161
Cdd:cd01164 100 ETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGARVILDTSGEALLAALAAKPF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 162 LIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:cd01164 180 LIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFV 259
|
250 260
....*....|....*....|....*.
gi 2505224387 242 HGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01164 260 AGLAQGLSLEEALRLAVAAGSATAFS 285
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-265 |
1.07e-98 |
|
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: 291.03 E-value: 1.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 2 LELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKMAESSGR 81
Cdd:TIGR03828 19 LTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAGPW 161
Cdd:TIGR03828 99 ETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKVILDTSGEALRDGLKAKPF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 162 LIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:TIGR03828 179 LIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAGDSMVAGFL 258
|
250 260
....*....|....*....|....
gi 2505224387 242 HGLIGGHEPQKILRTATAIAAMAV 265
Cdd:TIGR03828 259 AGLESGLSLEEALRLAVAAGSAAA 282
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
1-266 |
1.12e-96 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 285.88 E-value: 1.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 1 ALELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKMAE-SS 79
Cdd:COG1105 18 ELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFVPIEGETRINIKIVDpSD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 80 GRITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAG 159
Cdd:COG1105 98 GTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAKVVLDTSGEALKAALEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 160 PWLIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAG 239
Cdd:COG1105 178 PDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAG 257
|
250 260
....*....|....*....|....*..
gi 2505224387 240 MVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:COG1105 258 FLAGLARGLDLEEALRLAVAAGAAAAL 284
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-267 |
9.45e-86 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 258.09 E-value: 9.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 2 LELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKMAESSGR 81
Cdd:PRK09513 23 IERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAGPW 161
Cdd:PRK09513 103 VTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 162 LIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLI 262
|
250 260
....*....|....*....|....*.
gi 2505224387 242 HGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:PRK09513 263 YGLLMRESSEHTLRLATAVSALAVSQ 288
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-267 |
6.85e-37 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 132.08 E-value: 6.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 4 LGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDN-QQAFEALFERRHFVDEFVRVPGETRSNIKMAE-SSGR 81
Cdd:pfam00294 20 PGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNfGEFLLQELKKEGVDTDYVVIDEDTRTGTALIEvDGDG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPGPQVSEEAQQALFARVEQIAPGfDVVVVAGSLPRGVTPEWLQKLLLM--LKGLGLKVALDSSGLALRAG--LA 157
Cdd:pfam00294 100 ERTIVFNRGAAADLTPEELEENEDLLENA-DLLYISGSLPLGLPEATLEELIEAakNGGTFDPNLLDPLGAAREALleLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 158 AGPWLIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLP-PKVTVASTVGAGDSL 236
Cdd:pfam00294 179 PLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKVKVVDTTGAGDSF 258
|
250 260 270
....*....|....*....|....*....|.
gi 2505224387 237 LAGMVHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:pfam00294 259 VGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-260 |
1.84e-29 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 112.89 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 1 ALELGQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQafealFERRHFVDE----FVRVPGETRSNIKMA 76
Cdd:PRK13508 19 ELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQ-----FIAEHLDDQikhaFYKIKGETRNCIAIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 77 ESsGRITDLNGPGPQVSEEAQQALFARVEQIAPGFDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGL 156
Cdd:PRK13508 94 HE-GQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPVVLDCSGAALQAVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 157 AAG--PWLIKPNTEELADALDAPII-SIAAQAEAAARLHAQGIEHVVISQGSEGV---HWFS-PSVALhslpPKVTVAST 229
Cdd:PRK13508 173 ESPykPTVIKPNIEELSQLLGKEVSeDLDELKEVLQQPLFEGIEWIIVSLGADGAfakHNDTfYKVDI----PKIEVVNP 248
|
250 260 270
....*....|....*....|....*....|.
gi 2505224387 230 VGAGDSLLAGMVHGLIGGHEPQKILRTATAI 260
Cdd:PRK13508 249 VGSGDSTVAGIASGLLHQEDDADLLKKANVL 279
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-267 |
4.55e-18 |
|
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: 81.85 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 5 GQVNRSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDN--QQAFEALfeRRHFVD-EFVRVPGETRSNIKMAESSG- 80
Cdd:COG0524 23 GETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPfgDFLLAEL--RAEGVDtSGVRRDPGAPTGLAFILVDPd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 81 ---RITDLNGPGPQVSEEAQQalfarvEQIAPGFDVVVVAGSLPRGVTP-EWLQKLLLMLKGLGLKVALDssgLALRAGL 156
Cdd:COG0524 101 gerTIVFYRGANAELTPEDLD------EALLAGADILHLGGITLASEPPrEALLAALEAARAAGVPVSLD---PNYRPAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 157 --AAGPWL---------IKPNTEELADALDapiisIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVT 225
Cdd:COG0524 172 wePARELLrellalvdiLFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVVHVPAFPVE 246
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2505224387 226 VASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:COG0524 247 VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTR 288
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
9-241 |
1.43e-17 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 80.60 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 9 RSNAMLTHAAGKGLNVAQVLADLGHELTVAGFLGIDNQQAFEALFERRHFVDEFVRVPGETRSNIKM-AESSGRITDLNG 87
Cdd:PRK10294 29 RCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVhVEASGEQYRFVM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 88 PGPQVSEEAQQALFARVEQIAPGfDVVVVAGSLPRGVTPEWLQKLLLMLKGLGLKVALDSSGLALRAGLAAGPW-LIKPN 166
Cdd:PRK10294 109 PGAALNEDEFRQLEEQVLEIESG-AILVISGSLPPGVKLEKLTQLISAAQKQGIRCIIDSSGDALSAALAIGNIeLVKPN 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505224387 167 TEELADALDAPIISIAAQAEAAARLHAQGIEH-VVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:PRK10294 188 QKELSALVNRDLTQPDDVRKAAQELVNSGKAKrVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMT 263
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
151-267 |
2.77e-14 |
|
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: 71.04 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 151 ALRAGLAAGPWLIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTV 230
Cdd:cd01174 167 PLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTT 246
|
90 100 110
....*....|....*....|....*....|....*..
gi 2505224387 231 GAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01174 247 GAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTR 283
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
190-266 |
2.02e-12 |
|
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: 65.68 E-value: 2.02e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2505224387 190 RLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:cd01166 213 LALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVT 289
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
154-265 |
2.94e-10 |
|
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: 59.25 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 154 AGLAAGPWLIKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFS--PSVALHSLPPKV--TVAST 229
Cdd:cd01941 171 FYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSreGGVETKLFPAPQpeTVVNV 250
|
90 100 110
....*....|....*....|....*....|....*.
gi 2505224387 230 VGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAV 265
Cdd:cd01941 251 TGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
162-267 |
4.42e-10 |
|
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: 58.80 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 162 LIKPNTEELAdaldaPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMV 241
Cdd:cd01167 184 IVKLSDEELE-----LLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLL 258
|
90 100 110
....*....|....*....|....*....|...
gi 2505224387 242 HGL-------IGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01167 259 AQLlsrgllaLDEDELAEALRFANAVGALTCTK 291
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
110-245 |
5.24e-10 |
|
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: 57.49 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 110 GFDVVVVAGSLPRGVTPEWLQKLLLMLKGLglkVALDSSGLALRAG------LAAGPWLIKPNTEELADALDAPIISIAA 183
Cdd:cd00287 57 GADAVVISGLSPAPEAVLDALEEARRRGVP---VVLDPGPRAVRLDgeelekLLPGVDILTPNEEEAEALTGRRDLEVKE 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2505224387 184 QAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPP-KVTVASTVGAGDSLLAGMVHGLI 245
Cdd:cd00287 134 AAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAfPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
15-267 |
1.05e-09 |
|
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: 57.96 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 15 THAAGKGLNVAQVLADLGHELTVAGFLGID-NQQAFEALFERRHFVDEFVRVPG-----ETR---SNIKMAessgRITDL 85
Cdd:cd01172 36 EIRLGGAANVANNLASLGAKVTLLGVVGDDeAGDLLRKLLEKEGIDTDGIVDEGrptttKTRviaRNQQLL----RVDRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 86 NGPGpqVSEEAQQALFARVEQIAPGFDVVVVA--GslpRGV-TPEWLQKLLLMLKGLGLKVALDSSGLALRagLAAGPWL 162
Cdd:cd01172 112 DDSP--LSAEEEQRLIERIAERLPEADVVILSdyG---KGVlTPRVIEALIAAARELGIPVLVDPKGRDYS--KYRGATL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 163 IKPNTEELADALDAPIISIAAQAEAAARLHAQ-GIEHVVISQGSEGVHWFSPSVALHSLPPKVT-VASTVGAGDSLLAGM 240
Cdd:cd01172 185 LTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGEVQHIPALAKeVYDVTGAGDTVIATL 264
|
250 260
....*....|....*....|....*..
gi 2505224387 241 VHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01172 265 ALALAAGADLEEAAFLANAAAGVVVGK 291
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
17-266 |
3.40e-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: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 17 AAGKGLNVAQVLADLGHELTVAGFLGIDNQ-QAFEALFERrHFVD--EFVRVPGET--RSNIKMAESSGRITDLNGPGPQ 91
Cdd:cd01945 35 GGGNAANAAVAVARLGGQARLIGVVGDDAIgRLILAELAA-EGVDtsFIVVAPGARspISSITDITGDRATISITAIDTQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 92 VSEEAQQalfarvEQIAPGFDVVVVAGSLPrgvtpewlqklllmlkglglKVALDSSGLALRAGLAA---GPWLIKPNTE 168
Cdd:cd01945 114 AAPDSLP------DAILGGADAVLVDGRQP--------------------EAALHLAQEARARGIPIpldLDGGGLRVLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 169 ELADALD--------APIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLP-PKVTVASTVGAGDSLLAG 239
Cdd:cd01945 168 ELLPLADhaicsenfLRPNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPaFPVEVVDTTGAGDVFHGA 247
|
250 260
....*....|....*....|....*..
gi 2505224387 240 MVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:cd01945 248 FAHALAEGMPLREALRFASAAAALKCR 274
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
2-267 |
7.01e-08 |
|
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: 52.04 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 2 LELGQVNRSNAMLTHAAGKGLNVAQVLADLGHEltVAGFLGIDNQQAFEALFERRHFVDEFVRVpgeTRSNIKMAEsSGR 81
Cdd:cd01947 20 PQPGGISHSSDSRESPGGGGANVAVQLAKLGND--VRFFSNLGRDEIGIQSLEELESGGDKHTV---AWRDKPTRK-TLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 82 ITDLNGPgPQVSEEaQQALFARVEQIAP-GFDVVVvagslprgVTPEWLQKLLLMLKGLGLKVALDssgLALRAGLAAGP 160
Cdd:cd01947 94 FIDPNGE-RTITVP-GERLEDDLKWPILdEGDGVF--------ITAAAVDKEAIRKCRETKLVILQ---VTPRVRVDELN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 161 WLIKPNTEELADALDAPIISIAAQAEAAARlhaqgiEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGM 240
Cdd:cd01947 161 QALIPLDILIGSRLDPGELVVAEKIAGPFP------RYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGF 234
|
250 260
....*....|....*....|....*..
gi 2505224387 241 VHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01947 235 IYGLLKGWSIEEALELGAQCGAICVSH 261
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
18-267 |
7.92e-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: 52.04 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 18 AGKGLNVAQVLADLGHELTVAGFLGidnqQAFEALFERRHFVDEFVRVPGETRSN------IKMAESSGRITDLNGPGPQ 91
Cdd:cd01944 35 IGGGFNVMVAASRLGIPTVNAGPLG----NGNWADQIRQAMRDEGIEILLPPRGGddggclVALVEPDGERSFISISGAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 92 VSEEAQqaLFARVeQIAPGfDVVVVAG------SLPRGVTPEWLQKLLLMLKGLGLKVAL--DSSGLALRAGLAAGPWLI 163
Cdd:cd01944 111 QDWSTE--WFATL-TVAPY-DYVYLSGytlaseNASKVILLEWLEALPAGTTLVFDPGPRisDIPDTILQALMAKRPIWS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 164 KPNTE--ELADALDAPIisiaaqAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSLPP-KVTVASTVGAGDSLLAGM 240
Cdd:cd01944 187 CNREEaaIFAERGDPAA------EASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGfKVKAVDTIGAGDTHAGGM 260
|
250 260
....*....|....*....|....*..
gi 2505224387 241 VHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:cd01944 261 LAGLAKGMSLADAVLLANAAAAIVVTR 287
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
191-267 |
5.39e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 49.87 E-value: 5.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2505224387 191 LHAQGIEHVVISQGSEGVhWFSPSVALHSLP-PKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:PRK11142 210 LHQKGIETVLITLGSRGV-WLSENGEGQRVPgFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTR 286
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
190-266 |
3.75e-05 |
|
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: 43.93 E-value: 3.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2505224387 190 RLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:cd01937 178 LIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
19-266 |
9.82e-05 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 43.05 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 19 GKGLNVAQVLADLGHELTVAGFLGID--NQQAFEALFERRHFVDEFVRVPGE-TRSNIKMAESSGR----ITDLNgpgpq 91
Cdd:PRK09850 41 GVGRNIAQNLALLGNKAWLLSAVGSDfyGQSLLTQTNQSGVYVDKCLIVPGEnTSSYLSLLDNTGEmlvaINDMN----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 92 VSEEAQQALFARVEQIAPGFDVVVVAGSLPRGvTPEWLQKLLLMLKGLGLKVALDSSGlALRAGLAAGPWLiKPNTEELA 171
Cdd:PRK09850 116 ISNAITAEYLAQHREFIQRAKVIVADCNISEE-ALAWILDNAANVPVFVDPVSAWKCV-KVRDRLNQIHTL-KPNRLEAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 172 DALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALH-SLPPKVTVASTVGAGDSLLAGMVHGLIGGHEP 250
Cdd:PRK09850 193 TLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGwSAPIKTNVINVTGAGDAMMAGLASCWVDGMPF 272
|
250
....*....|....*.
gi 2505224387 251 QKILRTATAIAAMAVT 266
Cdd:PRK09850 273 AESVRFAQGCSSMALS 288
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
190-266 |
1.47e-04 |
|
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: 42.22 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2505224387 190 RLHAQGIEHVVISQGSEGVHWFSPSVALH-SLPPKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:cd01168 228 KLLALRCRIVVITQGAKGAVVVEGGEVYPvPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQ 305
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
197-262 |
1.94e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 42.51 E-value: 1.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505224387 197 EHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAA 262
Cdd:PLN02341 320 KWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
190-262 |
3.18e-04 |
|
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: 41.19 E-value: 3.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2505224387 190 RLHAQGIEHVVISQGSEGVHWFSPSVALHSLPPKVTVASTVGAGDSLLAGMVHG-LIGGHEPQKILRTATAIAA 262
Cdd:cd01940 182 EAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQGAQFAA 255
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
193-266 |
3.57e-04 |
|
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: 41.14 E-value: 3.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2505224387 193 AQGIEHVVISQGSEGVHWFSPSVALHSLP-PKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVT 266
Cdd:cd01942 200 ASGVRVVVVTLGPKGAIVFEDGEEVEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVE 274
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
163-264 |
5.96e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 40.68 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505224387 163 IKPNTEELADALDAPIISIAAQAEAAARLHAQGIEHVVISQGSEGVHWFSPSVALHSL-PPKVTVASTVGAGDSLLAGMV 241
Cdd:PRK09954 237 LKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLtAPAHTTVDSFGADDGFMAGLV 316
|
90 100
....*....|....*....|...
gi 2505224387 242 HGLIGGHEPQKILRTATAIAAMA 264
Cdd:PRK09954 317 YSFLEGYSFRDSARFAMACAAIS 339
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
221-265 |
1.81e-03 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 38.95 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2505224387 221 PPKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAV 265
Cdd:PRK09813 210 PEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
195-267 |
5.42e-03 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 37.79 E-value: 5.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505224387 195 GIEHVVISQGSEG---VHWFSPSVALHSLppKVTVASTVGAGDSLLAGMVHGLIGGHEPQKILRTATAIAAMAVTK 267
Cdd:PTZ00292 234 GVENVIITLGANGcliVEKENEPVHVPGK--RVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTR 307
|
|
| |
