|
Name |
Accession |
Description |
Interval |
E-value |
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-300 |
1.26e-135 |
|
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: 386.17 E-value: 1.26e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 2 IYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEGIDTDFV 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVKIK--ADQETEINGLGPIVTDIQLAEL-EMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGAQV 158
Cdd:TIGR03828 81 RVPGETRINVKIKepSGTETKLNGPGPEISEEELEALlEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIK 238
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 656223598 239 GTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATAFSDD--LASIEFIKEIYEKVEV 300
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPEDIEELLPQVTI 304
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-299 |
2.18e-134 |
|
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: 382.69 E-value: 2.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 2 IYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEGIDTDFV 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVKIK--ADQETEINGLGPIVTDIQLAELEMVLAGLTKE-DTVVFAGSAPASLGNEVYNRLIPVAKKAGAQV 158
Cdd:TIGR03168 81 EVKGETRINVKIKesSGEETELNEPGPEISEEELEQLLEKLRELLASgDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIK 238
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 656223598 239 GTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATAFSDDL--ASIEFIKEIYEKVE 299
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTglPDPEDVEELLDQVT 303
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-299 |
3.70e-133 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 379.86 E-value: 3.70e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 2 IYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEGIDTDFV 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVKIKAD---QETEINGLGPIVTDIQLAEL-EMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGAQ 157
Cdd:COG1105 81 PIEGETRINIKIVDPsdgTETEINEPGPEISEEELEALlERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 158 VVCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPI 237
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 656223598 238 KGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATAFSDD--LASIEFIKEIYEKVE 299
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGtgLPDREDVEELLAQVE 304
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-286 |
2.94e-132 |
|
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: 376.87 E-value: 2.94e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 1 MIYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEGIDTDF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 81 VQVNQDTRINVKIKAD--QETEINGLGPIVTDIQLAELEMVLAGLTKE-DTVVFAGSAPASLGNEVYNRLIPVAKKAGAQ 157
Cdd:cd01164 81 VEVAGETRINVKIKEEdgTETEINEPGPEISEEELEALLEKLKALLKKgDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 158 VVCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPI 237
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 656223598 238 KGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATAFSDDLA 286
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-280 |
2.32e-53 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 175.99 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 7 LNPAID----YIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGG-FTGQFIKDGLIAEGIDTDFV 81
Cdd:pfam00294 1 KVVVIGeaniDLIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVK---IKADQETEINGLGPIVTDIQLAELEMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGA-- 156
Cdd:pfam00294 81 VIDEDTRTGTAlieVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGTfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 157 QVVCDFEGQTL--LDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFA 234
Cdd:pfam00294 161 PNLLDPLGAAReaLLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 656223598 235 KPI-KGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATA 280
Cdd:pfam00294 241 PAVpKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVV 287
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-254 |
4.69e-51 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 170.65 E-value: 4.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 4 TVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLG-----GFTGQFIKDGliaegIDT 78
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGkdnqdGFQQLFSELG-----IAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 79 DFVQVNQDTRINVKIkadqeTEINGlgpIVTDIQLAELEMV-----------LAGLTKEDTVVFAGSAPASLGNEVYNRL 147
Cdd:PRK09513 82 RFQVVQGRTRINVKL-----TEKDG---EVTDFNFSGFEVTpadwerfvtdsLSWLGQFDMVAVSGSLPRGVSPEAFTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 148 IPVAKKAGAQVVCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVT 227
Cdd:PRK09513 154 MTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVN 233
|
250 260
....*....|....*....|....*..
gi 656223598 228 PAATYFAKPIKGTVKNSVGAGDSMVAG 254
Cdd:PRK09513 234 ASGEWIAKPPACDVVSTVGAGDSMVGG 260
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-270 |
5.09e-44 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 152.18 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 1 MIYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEgIDTDF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ-IKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 81 VQVNQDTRINVKI-KADQETEINGLGPIVTDIQLAE-LEMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGAQV 158
Cdd:PRK13508 80 YKIKGETRNCIAIlHEGQQTEILEKGPEISVQEADGfLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCDFEGQTLLDSL--AHQPLLVKPNNHELEAIFNVEL-NGIADIETYAKKILDMGAQNVIISMAGDGAlLVTPAATYFAK 235
Cdd:PRK13508 160 VLDCSGAALQAVLesPYKPTVIKPNIEELSQLLGKEVsEDLDELKEVLQQPLFEGIEWIIVSLGADGA-FAKHNDTFYKV 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 656223598 236 PI-KGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALK 270
Cdd:PRK13508 239 DIpKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLK 274
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
10-276 |
1.09e-33 |
|
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: 125.00 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 10 AIDYIVRLEHVET-GSVNRMESDDKYAGGKGINVSRVLKRLGYPntaTGFLG----GFTGQFIKDGLIAEGIDTDFVQVN 84
Cdd:COG0524 9 LVDLVARVDRLPKgGETVLAGSFRRSPGGAAANVAVALARLGAR---VALVGavgdDPFGDFLLAELRAEGVDTSGVRRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 85 QDTRI---NVKIKADQETEINGLGPIVTDIQLAELEmvLAGLTKEDTVVFAGSAPAS-LGNEVYNRLIPVAKKAGAQVVC 160
Cdd:COG0524 86 PGAPTglaFILVDPDGERTIVFYRGANAELTPEDLD--EALLAGADILHLGGITLASePPREALLAALEAARAAGVPVSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 161 DF--------EGQTLLDSLAHQPLLVKPNNHELEAIFnvelnGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATY 232
Cdd:COG0524 164 DPnyrpalwePARELLRELLALVDILFPNEEEAELLT-----GETDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 656223598 233 FAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACG 276
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-295 |
3.43e-29 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 112.96 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 2 IYTVTLNPAIDYIVRLEHVETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLGGFTGQFIKDGLIAEGIDTDFV 81
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVKIKADQETEINGL---GPIVTDIQLAELEMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGAQV 158
Cdd:PRK10294 84 EAKDWTRQNLHVHVEASGEQYRFvmpGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCDFEGQTLLDSLAHQPL-LVKPNNHELEAIFNVELNGIADIETYAKKILDMG-AQNVIISMAGDGALLVTPAATYFAKP 236
Cdd:PRK10294 164 IIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 656223598 237 IKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATAFSD--DLASIEFIKEIY 295
Cdd:PRK10294 244 PPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQgtRLCSHDDTQKIY 304
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
32-276 |
2.28e-20 |
|
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: 88.79 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 32 DKYAGGKGINVSRVLKRLGYPntaTGFLGGF----TGQFIKDGLIAEGIDTDFVQVNQDTRINVKIKadqETEINGLGPI 107
Cdd:cd01166 27 RKFFGGAEANVAVGLARLGHR---VALVTAVgddpFGRFILAELRREGVDTSHVRVDPGRPTGLYFL---EIGAGGERRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 108 VTDI------QLAELEMVLAGLTKEDTVVFAGSAPASLGN--EVYNRLIPVAKKAGAQVVCDF----------EGQTLLD 169
Cdd:cd01166 101 LYYRagsaasRLTPEDLDEAALAGADHLHLSGITLALSESarEALLEALEAAKARGVTVSFDLnyrpklwsaeEAREALE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 170 SLAHQPLLVKPNNHELEAIFNVElnGIADIETYAKKiLDMGAQNVIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAGD 249
Cdd:cd01166 181 ELLPYVDIVLPSEEEAEALLGDE--DPTDAAERALA-LALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGD 257
|
250 260
....*....|....*....|....*..
gi 656223598 250 SMVAGFTGEYVRSQDPIAALKWGVACG 276
Cdd:cd01166 258 AFAAGFLAGLLEGWDLEEALRFANAAA 284
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
11-279 |
5.96e-20 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 87.61 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 11 IDYIVRLEHV----ETGSVNRMEsddKYAGGKGINVSRVLKRLGYPNTATGFLG--GFtGQFIKDGLIAEGIDTDFVQVN 84
Cdd:cd01174 10 VDLVTRVDRLpkpgETVLGSSFE---TGPGGKGANQAVAAARLGARVAMIGAVGddAF-GDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 85 QDTR-----INVkikadqetEINGLGPIVTD------IQLAELEMVLAGLTKEDTVVFAGSAPAslgnEVYNRLIPVAKK 153
Cdd:cd01174 86 VGAPtgtavITV--------DESGENRIVVVpgangeLTPADVDAALELIAAADVLLLQLEIPL----ETVLAALRAARR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 154 AGAQVVcdF-------EGQTLLDSLAHqplLVkPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLV 226
Cdd:cd01174 154 AGVTVI--LnpaparpLPAELLALVDI---LV-PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 656223598 227 TPAATYFAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTAT 279
Cdd:cd01174 228 SGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALS 280
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
33-280 |
1.04e-19 |
|
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: 86.92 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 33 KYAGGKGINVSRVLKRLGYPntaTGFLGG----FTGQFIKDGLIAEGIDTDFVQVNQD--TRI-NVKIKADQETEINGLG 105
Cdd:cd01167 25 KAPGGAPANVAVALARLGGK---AAFIGKvgddEFGDFLLETLKEAGVDTRGIQFDPAapTTLaFVTLDADGERSFEFYR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 106 PIVTDIQLAELemVLAGLTKEDTVVFAGSAPA--SLGNEVYNRLIPVAKKAGAQVVCD-------FEGQTLLDSLAHQPL 176
Cdd:cd01167 102 GPAADLLLDTE--LNPDLLSEADILHFGSIALasEPSRSALLELLEAAKKAGVLISFDpnlrpplWRDEEEARERIAELL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 177 ----LVKPNNHELEAIFnvelnGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAGDSMV 252
Cdd:cd01167 180 eladIVKLSDEELELLF-----GEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFV 254
|
250 260 270
....*....|....*....|....*....|....*
gi 656223598 253 AGF------TGEYVRSQDPIA-ALKWGVACGTATA 280
Cdd:cd01167 255 AGLlaqllsRGLLALDEDELAeALRFANAVGALTC 289
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
5-276 |
6.67e-16 |
|
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: 76.48 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 5 VTLNPAiDYIVRLEHVEtgsvnrmeSDDKYAGGKGINVSRVLKRLGypnTATGFLGGFT----GQFIKDGLIAEGIDTDF 80
Cdd:TIGR04382 12 VDLYPQ-QIGVPLEDVT--------SFAKYLGGSPANIAVGAARLG---LKTAFITRVGddqfGRFVRDYLRREGVDTSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 81 VQVNQDTRINVKIkadqeTEINGLG--PIV------TDIQLAELEMVLAGLTKEDTVVFAGSA-PASLGNEVYNRLIPVA 151
Cdd:TIGR04382 80 VVTDPGRRTSLVF-----LEIKPPDefPLLfyrenaADLALTPDDVDEDYIASARALLVSGTAlSQEPSREAVLKALEYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 152 KKAGAQVVCDFE------------GQTLLDSLAHQPLLVKpNNHELEAifnveLNGIADIETYAKKILDMGAQNVIISMA 219
Cdd:TIGR04382 155 RAAGVRVVLDIDyrpylwkspeeaGIYLRLVLPLVDVIIG-TREEFDI-----AGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 656223598 220 GDGALLVTPAATYF-AKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACG 276
Cdd:TIGR04382 229 PEGSLVYTGDGEGVeVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACG 286
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
127-257 |
4.46e-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: 72.13 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 127 DTVVFAGSAPASlgnEVYNRLIPVAKKAGAQVVCDFEGQ------TLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIE 200
Cdd:cd00287 59 DAVVISGLSPAP---EAVLDALEEARRRGVPVVLDPGPRavrldgEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAA 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 656223598 201 TYAKKILDMGAQNVIISMAGDGALLVTPAATYF-AKPIKGTVKNSVGAGDSMVAGFTG 257
Cdd:cd00287 136 EAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVhVPAFPVKVVDTTGAGDAFLAALAA 193
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
35-279 |
5.70e-15 |
|
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: 73.50 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 35 AGGKGINVSRVLKRLGYPNTATGFLGG-FTGQFIKDGLIAEGIDTDFVQV-NQDT--------RINVKIKADQETEINGL 104
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESEKAGLNVRGIVFeGRSTasytaildKDGDLVVALADMDIYEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 105 GPIVTDIQLAELemvlagLTKEDTVVFAGSAPAslgnEVYNRLIPVAKKAGAQVVCD----FEGQTLLDSLaHQPLLVKP 180
Cdd:cd01941 114 LTPDFLRKIREA------LKEAKPIVVDANLPE----EALEYLLALAAKHGVPVAFEptsaPKLKKLFYLL-HAIDLLTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 181 NNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPA----ATYFAKPIKGTVKNSVGAGDSMVAGFT 256
Cdd:cd01941 183 NRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREggveTKLFPAPQPETVVNVTGAGDAFVAGLV 262
|
250 260
....*....|....*....|...
gi 656223598 257 GEYVRSQDPIAALKWGVACGTAT 279
Cdd:cd01941 263 AGLLEGMSLDDSLRFAQAAAALT 285
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
31-279 |
6.34e-11 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 61.68 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 31 DDKYAGGKGINVSRVLKRLGYPNTATGFLGGFT-GQFIKDGLIAEGIDTDFVQVNQDtrinvkIKADQETEINGLGPIVT 109
Cdd:PRK09813 18 GKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKHG------VTAQTQVELHDNDRVFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 110 DIQlaelEMVLAG----------LTKEDTVVFA--GSAPASLgnevynrliPVAKKAGAQVVCDFEGQtlLDSlahqPLL 177
Cdd:PRK09813 92 DYT----EGVMADfalseedyawLAQYDIVHAAiwGHAEDAF---------PQLHAAGKLTAFDFSDK--WDS----PLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 178 VKPNNHeLEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAGDSMVAGFTG 257
Cdd:PRK09813 153 QTLVPH-LDYAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLC 231
|
250 260
....*....|....*....|..
gi 656223598 258 EYVRSQDPIAALKWGVACGTAT 279
Cdd:PRK09813 232 GWLAGMTLPQAMAQGTACAAKT 253
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
31-280 |
2.65e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 60.62 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 31 DDKY--AGGKgINVSRVLKRLGYPNTATGFLGG-FTGQFIKDGLIAEGIDTdfVQVNQDTRINVKIKADQETEI-----N 102
Cdd:PLN02341 113 DKKSweAGGN-CNFAIAAARLGLRCSTIGHVGDeIYGKFLLDVLAEEGISV--VGLIEGTDAGDSSSASYETLLcwvlvD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 103 GLG-------------PIVTDIQL--AELEMVLagltKEDTVVFA-GSAPASLGNEVYNRLIPVAKKAGAQVVCDF--EG 164
Cdd:PLN02341 190 PLQrhgfcsradfgpePAFSWISKlsAEAKMAI----RQSKALFCnGYVFDELSPSAIASAVDYAIDVGTAVFFDPgpRG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 165 QTLLD-------SLAHqpLL-----VKPNNHELEAifnveLNGIADIETYAKKIL--DMGAQNVIISMAGDGALLVTPAA 230
Cdd:PLN02341 266 KSLLVgtpderrALEH--LLrmsdvLLLTSEEAEA-----LTGIRNPILAGQELLrpGIRTKWVVVKMGSKGSILVTRSS 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 656223598 231 TYFAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACGTATA 280
Cdd:PLN02341 339 VSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATA 388
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
178-300 |
1.36e-08 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 54.99 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 178 VKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLV-TPAATYFAKPIKGTVKNSVGAGDSMVAGFT 256
Cdd:PRK09850 184 LKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSdISGESGWSAPIKTNVINVTGAGDAMMAGLA 263
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 656223598 257 GEYVRSQDPIAALKWGVACGTATAFSD-----DLaSIEFIKEIYEKVEV 300
Cdd:PRK09850 264 SCWVDGMPFAESVRFAQGCSSMALSCEytnnpDL-SIANVISLVENAEC 311
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
25-256 |
4.48e-08 |
|
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: 53.33 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 25 VNRMESDDKYAGGKGiNVSRVLKRLGYPNTATGFLGGFT-GQFIKDGLIAEGIDTDFVQVNQ-----DTRI---NVKI-K 94
Cdd:cd01172 29 VVKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDDEaGDLLRKLLEKEGIDTDGIVDEGrptttKTRViarNQQLlR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 95 ADQETEinglGPIVTDIQLAELEMVLAGLTKEDTVVFAGSAPASLGNEVYNRLIPVAKKAGAQVVCD--------FEGQT 166
Cdd:cd01172 108 VDREDD----SPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIAAARELGIPVLVDpkgrdyskYRGAT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 167 LLdslahqpllvKPNNHELEAIFNVELNGIADIETYAKKILDM-GAQNVIISMAGDGALLV--------TPAatyFAKPi 237
Cdd:cd01172 184 LL----------TPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFerdgevqhIPA---LAKE- 249
|
250
....*....|....*....
gi 656223598 238 kgtVKNSVGAGDSMVAGFT 256
Cdd:cd01172 250 ---VYDVTGAGDTVIATLA 265
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
181-276 |
1.40e-06 |
|
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: 48.76 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 181 NNHELEAIFNVELNGIADIetyAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIK-GTVKNSVGAGDSMVAGFTGEY 259
Cdd:cd01168 207 NEEEAEALAEAETTDDLEA---ALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPvEKIVDTNGAGDAFAGGFLYGL 283
|
90
....*....|....*..
gi 656223598 260 VRSQDPIAALKWGVACG 276
Cdd:cd01168 284 VQGEPLEECIRLGSYAA 300
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
149-274 |
1.67e-06 |
|
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: 48.25 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 149 PV-AKKAGAQVVCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVII---SMAGDGA- 223
Cdd:pfam08543 93 PVmVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIkggHLEGEEAv 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 656223598 224 ---LLVTPAATY-FAKPiKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVA 274
Cdd:pfam08543 173 vtdVLYDGGGFYtLEAP-RIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKE 226
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
12-275 |
1.82e-06 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 12 DYIVRLEHV-ETGSVNRMESDDKYAGGKGINVSRVLKRLGYPNTATGFLG--GFTGQFIKDgLIAEGIDTDFVQVNQDTr 88
Cdd:PTZ00292 27 DLIGYVDRMpQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGtdGFGSDTIKN-FKRNGVNTSFVSRTENS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 89 invkikadqeteINGLGPIVTDIQLAELEMVLA-GLTKEDTVVFAGSAPASLGNE----VYNRLIPV---------AKKA 154
Cdd:PTZ00292 105 ------------STGLAMIFVDTKTGNNEIVIIpGANNALTPQMVDAQTDNIQNIckylICQNEIPLettldalkeAKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 155 G-------AQVVCDFEGQTLLDSLAHQPLLVkPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLV- 226
Cdd:PTZ00292 173 GcytvfnpAPAPKLAEVEIIKPFLKYVSLFC-VNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVe 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 656223598 227 TPAATYFAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVAC 275
Cdd:PTZ00292 252 KENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRI 300
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
25-279 |
2.03e-06 |
|
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: 48.12 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 25 VNRMESDDK-YAGGKGINVSRVLKRLGYPntaTGFLGGF----TGQFIKDGLIAEGIDTDFVQV----NQDTRINVKiKA 95
Cdd:cd01940 10 VDKYLHLGKmYPGGNALNVAVYAKRLGHE---SAYIGAVgnddAGAHVRSTLKRLGVDISHCRVkegeNAVADVELV-DG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 96 DQ------ETEINGLGPIVTDIQ-LAELEMVLAGLTKEDtvvfaGSAPASLGNEVYnrlipvakkAGAQVVCDFEGQTLL 168
Cdd:cd01940 86 DRifglsnKGGVAREHPFEADLEyLSQFDLVHTGIYSHE-----GHLEKALQALVG---------AGALISFDFSDRWDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 169 DSLAhqplLVKPnnHELEAIFNVELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAG 248
Cdd:cd01940 152 DYLQ----LVCP--YVDFAFFSASDLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAG 225
|
250 260 270
....*....|....*....|....*....|..
gi 656223598 249 DSMVAGFTGEYVRSQDPIA-ALKWGVACGTAT 279
Cdd:cd01940 226 DSFIAGFLLSLLAGGTAIAeAMRQGAQFAAKT 257
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
192-280 |
2.33e-06 |
|
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: 48.23 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 192 ELNGIADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYF--AKPIKgTVKNSVGAGDSMVAGFTGEYVRSQD-PIAA 268
Cdd:cd01946 176 QLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGYFAapAYPLE-SVFDPTGAGDTFAGGFIGYLASQKDtSEAN 254
|
90
....*....|..
gi 656223598 269 LKWGVACGTATA 280
Cdd:cd01946 255 MRRAIIYGSAMA 266
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
167-269 |
7.16e-05 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 43.34 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 167 LLDSLAHqplLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVIIS---MAGDG---ALLVT-PAATYFAKPIKG 239
Cdd:cd01173 132 LLVPLAD---IITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveLADDDrieMLGSTaTEAWLVQRPKIP 208
|
90 100 110
....*....|....*....|....*....|
gi 656223598 240 TVKNSVGAGDSMVAGFTGEYVRSQDPIAAL 269
Cdd:cd01173 209 FPAYFNGTGDLFAALLLARLLKGKSLAEAL 238
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
177-281 |
1.87e-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: 42.06 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 177 LVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQNVII---SMAGD-----GALLVTPA-ATYFAKP-IKGTVknsVG 246
Cdd:COG2240 141 IITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVtsvPLDDTpadkiGNLAVTADgAWLVETPlLPFSP---NG 217
|
90 100 110
....*....|....*....|....*....|....*
gi 656223598 247 AGDSMVAGFTGEYVRSQDPIAALKwgvacgTATAF 281
Cdd:COG2240 218 TGDLFAALLLAHLLRGKSLEEALE------RAAAF 246
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
10-276 |
3.80e-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: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 10 AIDYIVRLEHV--ETGSVN--RMEsddKYAGGKGINVSRVLKRLGypnTATGFLGGFTGQFIKDGLI----AEGIDTDFV 81
Cdd:cd01942 9 NYDIILKVESFpgPFESVLvkDLR---REFGGSAGNTAVALAKLG---LSPGLVAAVGEDFHGRLYLeelrEEGVDTSHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 82 QVNQDTRINVK-IKADQETEInglgpIVTDIQ--LAELEMvlaGLTKEDTVVFAGSAPASLGNEVYNRLipVAKKAGAQV 158
Cdd:cd01942 83 RVVDEDSTGVAfILTDGDDNQ-----IAYFYPgaMDELEP---NDEADPDGLADIVHLSSGPGLIELAR--ELAAGGITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCD-------FEGQTLLDSLAHQPLLVkPNNHELEAIfnVELNGIADIETYAKkildmgAQNVIISMAGDGALLVTPAAT 231
Cdd:cd01942 153 SFDpgqelprLSGEELEEILERADILF-VNDYEAELL--KERTGLSEAELASG------VRVVVVTLGPKGAIVFEDGEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 656223598 232 YFAKPIKGT-VKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACG 276
Cdd:cd01942 224 VEVPAVPAVkVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA 269
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
134-274 |
6.18e-04 |
|
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: 40.46 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 134 SAPASLGNEVYNRLIPVAKKAGAQVVCDFEGQTLLDSLAHQPLLVKPNNHELEAIFNVELNGIADIETYAKKILDMGAQN 213
Cdd:cd01937 107 TAEIVILGPVPEEISPSLFRKFAFISLDAQGFLRRANQEKLIKCVILKLHDVLKLSRVEAEVISTPTELARLIKETGVKE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 656223598 214 VIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVA 274
Cdd:cd01937 187 IIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAA 247
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
197-276 |
3.76e-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: 38.17 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 197 ADIETYAKKILDMGAQNVIISMAGDGALLVTPAATYFAKPIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAALKWGVACG 276
Cdd:cd01947 176 PGELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCG 255
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-269 |
8.98e-03 |
|
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: 37.27 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 9 PAIDYIVRLEHVETGsvnrmesDDKY--------AGGKGINVSRVLKRLGYPNTATGFLGG-FTGQFIKDGLIAEGIDTD 79
Cdd:cd01945 8 AVLDLIYLVASFPGG-------DGKIvatdyaviGGGNAANAAVAVARLGGQARLIGVVGDdAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 80 FVQVNQDTRINVKIKADQETEINGLGPIVTDIQLAELEMVLAGLTKEDTVVFAGSAP-ASLgnevynRLIPVAKKAGAQV 158
Cdd:cd01945 81 FIVVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPeAAL------HLAQEARARGIPI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656223598 159 VCDFEGQTLLDS---LAHQPLLVKPNNheleaiFNVELNGIADIETyAKKILDMGAQNVIISM--AG------DGALLVT 227
Cdd:cd01945 155 PLDLDGGGLRVLeelLPLADHAICSEN------FLRPNTGSADDEA-LELLASLGIPFVAVTLgeAGclwlerDGELFHV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 656223598 228 PAatyfakpIKGTVKNSVGAGDSMVAGFTGEYVRSQDPIAAL 269
Cdd:cd01945 228 PA-------FPVEVVDTTGAGDVFHGAFAHALAEGMPLREAL 262
|
|
| |
