|
Name |
Accession |
Description |
Interval |
E-value |
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-286 |
1.33e-135 |
|
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: 385.35 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 1 MIYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKGLDCHF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 81 TPIADDTRINVKIHAEE--ETELNGAGPDITAKEIEAFYTELANLTP-NDVVVMSGSLAPSLPDSFYYDIIQKVEAAGAN 157
Cdd:cd01164 81 VEVAGETRINVKIKEEDgtETEINEPGPEISEEELEALLEKLKALLKkGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 158 FVIDTTGEALKKTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAP 237
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489740500 238 KGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSEDIA 286
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-299 |
4.96e-131 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 374.47 E-value: 4.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 2 IYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKGLDCHFT 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 82 PIADDTRINVKIHAE---EETELNGAGPDITAKEIEAFYTELANL-TPNDVVVMSGSLAPSLPDSFYYDIIQKVEAAGAN 157
Cdd:COG1105 81 PIEGETRINIKIVDPsdgTETEINEPGPEISEEELEALLERLEELlKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 158 FVIDTTGEALKKTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAP 237
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489740500 238 KGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSED--IATRAKIDEILPLIN 299
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGtgLPDREDVEELLAQVE 304
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-296 |
1.50e-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: 368.06 E-value: 1.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 2 IYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKGLDCHFT 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 82 PIADDTRINVKIH--AEEETELNGAGPDITAKEIEAFYTELANLTPN-DVVVMSGSLAPSLPDSFYYDIIQKVEAAGANF 158
Cdd:TIGR03168 81 EVKGETRINVKIKesSGEETELNEPGPEISEEELEQLLEKLRELLASgDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 159 VIDTTGEALKKTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPK 238
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 239 GQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSED--IATRAKIDEILP 296
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGtgLPDPEDVEELLD 300
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-300 |
5.30e-127 |
|
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: 364.22 E-value: 5.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 2 IYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKGLDCHFT 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 82 PIADDTRINVKIH--AEEETELNGAGPDITAKEIEAFYTEL-ANLTPNDVVVMSGSLAPSLPDSFYYDIIQKVEAAGANF 158
Cdd:TIGR03828 81 RVPGETRINVKIKepSGTETKLNGPGPEISEEELEALLEKLrAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 159 VIDTTGEALKKTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPK 238
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489740500 239 GQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSED--IATRAKIDEILPLINI 300
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGtgLPDPEDIEELLPQVTI 304
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-300 |
8.96e-57 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 185.67 E-value: 8.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 4 TITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIG-----GFTGTFisdalKAKGLDC 78
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGkdnqdGFQQLF-----SELGIAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 79 HFTPIADDTRINVKIhAEEE---TELNGAGPDITAKEIEAFYTE-LANLTPNDVVVMSGSLAPSL-PDSFYyDIIQKVEA 153
Cdd:PRK09513 82 RFQVVQGRTRINVKL-TEKDgevTDFNFSGFEVTPADWERFVTDsLSWLGQFDMVAVSGSLPRGVsPEAFT-DWMTRLRS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 154 AGANFVIDTTGEALKKTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYF 233
Cdd:PRK09513 160 QCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 234 SPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACgSATAFSED---IATRAKIDEILPLINI 300
Cdd:PRK09513 240 AKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAV-SALAVSQSnvgITDRPQLAAMMARVDL 308
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-254 |
1.69e-52 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 174.53 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 1 MIYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKgLDCHF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ-IKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 81 TPIADDTRINVKI-HAEEETELNGAGPDITAKEIEAFYTELANLTPN-DVVVMSGSLAPSLPDSFYYDIIQKVEAAGANF 158
Cdd:PRK13508 80 YKIKGETRNCIAIlHEGQQTEILEKGPEISVQEADGFLHHFKQLLESvEVVAISGSLPAGLPVDYYAQLIELANQAGKPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 159 VIDTTGEALKKTL--PSHPLVVKPNNHELADYYHTTFNSQADII-AAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSP 235
Cdd:PRK13508 160 VLDCSGAALQAVLesPYKPTVIKPNIEELSQLLGKEVSEDLDELkEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYKVD 239
|
250
....*....|....*....
gi 489740500 236 APKGQVINSVGAGDSMIGG 254
Cdd:PRK13508 240 IPKIEVVNPVGSGDSTVAG 258
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
1-280 |
1.44e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.97 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 1 MIYTITVNPSIDYVVQLPqmtlGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGG-FTGTFISDALKAKGLDCH 79
Cdd:pfam00294 3 VVIGEANIDLIGNVEGLP----GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 80 FTPIADDTRINVKIH---AEEETELNGAGPDITAKEIEAFYTELANLTPNDVVVMSGSLAPSLPDsFYYDIIQKVEAAGA 156
Cdd:pfam00294 79 YVVIDEDTRTGTALIevdGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPE-ATLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 157 NFV---IDTTGEALKK--TLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAV 231
Cdd:pfam00294 158 TFDpnlLDPLGAAREAllELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489740500 232 YF-SPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATA 280
Cdd:pfam00294 238 VHvPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVV 287
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-278 |
4.54e-31 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 118.35 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 2 IYTITVNPSIDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIGGFTGTFISDALKAKGLDCHFT 81
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 82 PIADDTRINVKIHAE---EETELNGAGPDITAKEIEAFYTELANLTPNDVVVMSGSLAPSLPDSFYYDIIQKVEAAGANF 158
Cdd:PRK10294 84 EAKDWTRQNLHVHVEasgEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 159 VIDTTGEALKKTLPSHPL-VVKPNNHELADYYHTTFNSQADIIAAGQRMLAEG-AQHVLISMAGDGGLLITKDA-VYFSP 235
Cdd:PRK10294 164 IIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSENcIQVVP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489740500 236 AP-KGQviNSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSA 278
Cdd:PRK10294 244 PPvKSQ--STVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSA 285
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-280 |
2.57e-23 |
|
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: 97.26 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 11 IDYVVQLPQMTLGSVNRLAHT-AKLPGGKGINVSQILNDLDQPNKALGFIG-GFTGTFISDALKAKGLDCHFTPIADDTR 88
Cdd:COG0524 10 VDLVARVDRLPKGGETVLAGSfRRSPGGAAANVAVALARLGARVALVGAVGdDPFGDFLLAELRAEGVDTSGVRRDPGAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 89 I---NVKIHAEEETELN---GAGPDITAKEIEAfytelANLTPNDVVVMSG-SLAPSLPDSFYYDIIQKVEAAGANFVID 161
Cdd:COG0524 90 TglaFILVDPDGERTIVfyrGANAELTPEDLDE-----ALLAGADILHLGGiTLASEPPREALLAALEAARAAGVPVSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 162 T---------TGEALKKTLPSHPlVVKPNNHELADYYHTTfnsqaDIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVY 232
Cdd:COG0524 165 PnyrpalwepARELLRELLALVD-ILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489740500 233 FSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATA 280
Cdd:COG0524 239 HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
180-279 |
9.40e-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: 70.27 E-value: 9.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 180 PNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTF 259
Cdd:cd01174 181 PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAAL 260
|
90 100
....*....|....*....|
gi 489740500 260 AKTHDAVESFRYGLACGSAT 279
Cdd:cd01174 261 ARGLSLEEAIRFANAAAALS 280
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
156-260 |
7.22e-12 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 63.27 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 156 ANFVIDTTGEALKKTLPsHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFS- 234
Cdd:cd00287 92 GPRAVRLDGEELEKLLP-GVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHv 170
|
90 100
....*....|....*....|....*.
gi 489740500 235 PAPKGQVINSVGAGDSMIGGFVGTFA 260
Cdd:cd00287 171 PAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
64-277 |
3.00e-10 |
|
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: 59.90 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 64 GTFISDALKAKGLDCHFTPIADDTRIN---VKIHAEEETEL-----NGAGPDITAKEIEAFYTELAnltpnDVVVMSGSl 135
Cdd:cd01166 60 GRFILAELRREGVDTSHVRVDPGRPTGlyfLEIGAGGERRVlyyraGSAASRLTPEDLDEAALAGA-----DHLHLSGI- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 136 APSLPDSFY---YDIIQKVEAAGANFVIDTtgeALKKTLPSHPlVVKPNNHELADYYH------------TTFNSQADII 200
Cdd:cd01166 134 TLALSESARealLEALEAAKARGVTVSFDL---NYRPKLWSAE-EAREALEELLPYVDivlpseeeaealLGDEDPTDAA 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489740500 201 AAGqRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGS 277
Cdd:cd01166 210 ERA-LALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAA 285
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
130-280 |
6.70e-10 |
|
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: 58.63 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 130 VMSGSLAPSLPDSfyydIIQKVEAA------GANFVIDTTGEALKKTLPSHPLVVkpnnheLADYYHTTFNSQADIIAAG 203
Cdd:cd01946 118 VFLGNIAPELQRE----VLEQVKDPklvvmdTMNFWISIKPEKLKKVLAKVDVVI------INDGEARQLTGAANLVKAA 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489740500 204 QRMLAEGAQHVLISMAGDGGLLITKDAVYFSPA-PKGQVINSVGAGDSMIGGFVGTFAKTHDAVES-FRYGLACGSATA 280
Cdd:cd01946 188 RLILAMGPKALIIKRGEYGALLFTDDGYFAAPAyPLESVFDPTGAGDTFAGGFIGYLASQKDTSEAnMRRAIIYGSAMA 266
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
197-295 |
6.90e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 59.46 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 197 ADIIAAGQRMLAEG--AQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLA 274
Cdd:PLN02341 303 RNPILAGQELLRPGirTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANA 382
|
90 100
....*....|....*....|....*
gi 489740500 275 CGSATAFS----EDIATRAKIDEIL 295
Cdd:PLN02341 383 VGAATAMGcgagRNVATLEKVLELL 407
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
197-295 |
8.68e-08 |
|
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: 52.60 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 197 ADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFS-PAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLAC 275
Cdd:TIGR04382 206 GDDEAAARALLDAGVEILVVKRGPEGSLVYTGDGEGVEvPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNAC 285
|
90 100
....*....|....*....|....
gi 489740500 276 G----SATAFSEDIATRAKIDEIL 295
Cdd:TIGR04382 286 GaivvSRHSCSPAMPTLEELEAFL 309
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
160-285 |
7.99e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 49.93 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 160 IDTTGE--ALK-KTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYF-SP 235
Cdd:PRK09954 216 VDTVSEfkAGKiKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFlLT 295
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489740500 236 APKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSEDI 285
Cdd:PRK09954 296 APAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRASGSL 345
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
35-279 |
2.11e-06 |
|
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: 48.46 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 35 PGGKGINVSQILNDLDQPNKALGFIGG-FTGTFISDALKAKGLDCHFTPIAD-DTRINVKIHaEEETELNGAGPDITAKE 112
Cdd:cd01941 34 PGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESEKAGLNVRGIVFEGrSTASYTAIL-DKDGDLVVALADMDIYE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 113 I--EAFYTELANLTPN-DVVVMSGSLAPSLpdsfyydiIQKV-EAAGANFVIDT-----TGEALKKTLPSHPL-VVKPNN 182
Cdd:cd01941 113 LltPDFLRKIREALKEaKPIVVDANLPEEA--------LEYLlALAAKHGVPVAfeptsAPKLKKLFYLLHAIdLLTPNR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 183 HELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKD-AVYFSPAPKGQ---VINSVGAGDSMIGGFVGT 258
Cdd:cd01941 185 AELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREgGVETKLFPAPQpetVVNVTGAGDAFVAGLVAG 264
|
250 260
....*....|....*....|.
gi 489740500 259 FAKTHDAVESFRYGLACGSAT 279
Cdd:cd01941 265 LLEGMSLDDSLRFAQAAAALT 285
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
177-280 |
3.99e-06 |
|
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: 47.63 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 177 VVKPNNHELAdyyhtTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFV 256
Cdd:cd01167 184 IVKLSDEELE-----LLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLL 258
|
90 100 110
....*....|....*....|....*....|.
gi 489740500 257 GTFAKT-------HDAVESFRYGLACGSATA 280
Cdd:cd01167 259 AQLLSRgllaldeDELAEALRFANAVGALTC 289
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
178-283 |
8.40e-06 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 46.52 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 178 VKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGgllitkdaVYFS---------PAPKGQVINSVGAG 248
Cdd:PRK09850 184 LKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG--------VYYSdisgesgwsAPIKTNVINVTGAG 255
|
90 100 110
....*....|....*....|....*....|....*
gi 489740500 249 DSMIGGFVGTFAKTHDAVESFRYGLACGSATAFSE 283
Cdd:PRK09850 256 DAMMAGLASCWVDGMPFAESVRFAQGCSSMALSCE 290
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
169-288 |
1.27e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 169 KTLPSHPLVVKPNNHELADYYHTTFNSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDA--VYFsPAPKGQVINSVG 246
Cdd:PTZ00292 193 KPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEKENepVHV-PGKRVKAVDTTG 271
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489740500 247 AGDSmiggFVGTFAkthdavesfrYGLACGSATAFSEDIATR 288
Cdd:PTZ00292 272 AGDC----FVGSMA----------YFMSRGKDLKESCKRANR 299
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
181-277 |
2.78e-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: 41.83 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 181 NNHELADYYHTTFNsqaDIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPA-PKGQVINSVGAGDSMIGGFVGTF 259
Cdd:cd01168 207 NEEEAEALAEAETT---DDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAiPVEKIVDTNGAGDAFAGGFLYGL 283
|
90
....*....|....*...
gi 489740500 260 AKTHDAVESFRYGLACGS 277
Cdd:cd01168 284 VQGEPLEECIRLGSYAAA 301
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
194-284 |
3.02e-04 |
|
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: 41.63 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 194 NSQADIIAAGQRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGL 273
Cdd:cd01947 173 RLDPGELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGA 252
|
90
....*....|.
gi 489740500 274 ACGSATAFSED 284
Cdd:cd01947 253 QCGAICVSHFG 263
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
56-252 |
3.81e-04 |
|
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: 41.39 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 56 LGFIGGFT-GTFISDALKAKGLDCHFtpIADDTR-INVK------------IHAEEETELNGagpDITAKEIEAFytelA 121
Cdd:cd01172 59 LGVVGDDEaGDLLRKLLEKEGIDTDG--IVDEGRpTTTKtrviarnqqllrVDREDDSPLSA---EEEQRLIERI----A 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 122 NLTPN-DVVVMS----GSLAPSLPDSfyydIIQKVEAAGANFVIDTTGEALKKTlpSHPLVVKPNNHELADYYHTTFNSQ 196
Cdd:cd01172 130 ERLPEaDVVILSdygkGVLTPRVIEA----LIAAARELGIPVLVDPKGRDYSKY--RGATLLTPNEKEAREALGDEINDD 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489740500 197 ADIIAAGQRMLAE-GAQHVLISMAGDGGLLITKD-AVYFSPAPKGQVINSVGAGDSMI 252
Cdd:cd01172 204 DELEAAGEKLLELlNLEALLVTLGEEGMTLFERDgEVQHIPALAKEVYDVTGAGDTVI 261
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
33-279 |
4.92e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 40.88 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 33 KLPGGKGINVSQILNDLDQPNKALGFIGGFT-GTFISDALKAKGLDCHFTPIAD--------DTRINVKIHAEEEtelNG 103
Cdd:PRK09813 20 AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKHgvtaqtqvELHDNDRVFGDYT---EG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 104 AGPDITAKEieafyTELANLTPNDVVVMS--GSLAPSLPdsfyydiiqKVEAAGANFVIDTTgealkkTLPSHPLVVKPN 181
Cdd:PRK09813 97 VMADFALSE-----EDYAWLAQYDIVHAAiwGHAEDAFP---------QLHAAGKLTAFDFS------DKWDSPLWQTLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 182 NHelADYYHTTFNSQADIIAAG-QRMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTFA 260
Cdd:PRK09813 157 PH--LDYAFASAPQEDEFLRLKmKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWL 234
|
250
....*....|....*....
gi 489740500 261 KTHDAVESFRYGLACGSAT 279
Cdd:PRK09813 235 AGMTLPQAMAQGTACAAKT 253
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
140-277 |
5.14e-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: 40.76 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 140 PDSFYYDIIQKVEAA--GANFVIDTTGEALKKTLP------SHPLVVKPNNHELADYYHTTFNSQADiiaagqrmLAEGA 211
Cdd:cd01942 132 LSSGPGLIELARELAagGITVSFDPGQELPRLSGEeleeilERADILFVNDYEAELLKERTGLSEAE--------LASGV 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489740500 212 QHVLISMAGDGGLLITKDAVYFSPA-PKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGS 277
Cdd:cd01942 204 RVVVVTLGPKGAIVFEDGEEVEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAAS 270
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
11-277 |
1.01e-03 |
|
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: 40.10 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 11 IDYVVQLPQMTLGSVNRLAHTAKLPGGKGINVSQILNDLDQPNKALGFIG-GFTGTFISDALKAKGLDCHFTPIADDTRI 89
Cdd:cd01944 10 VDIVLDVDKLPASGGDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGnGNWADQIRQAMRDEGIEILLPPRGGDDGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 90 NVKIHAEEETE-----LNGAGPDITAKEIEAFytelaNLTPNDVVVMSGSlapSLPDSFYYDII----QKVEAAGANFVI 160
Cdd:cd01944 90 CLVALVEPDGErsfisISGAEQDWSTEWFATL-----TVAPYDYVYLSGY---TLASENASKVIllewLEALPAGTTLVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740500 161 DTT-------GEALKKTLPSHPLVvkPNNHELADYYHTTFNSQADiiAAGQRMLAEGAQHVLISMAGDGGLLITKD-AVY 232
Cdd:cd01944 162 DPGprisdipDTILQALMAKRPIW--SCNREEAAIFAERGDPAAE--ASALRIYAKTAAPVVVRLGSNGAWIRLPDgNTH 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489740500 233 FSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVESFRYGLACGS 277
Cdd:cd01944 238 IIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
205-280 |
1.28e-03 |
|
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: 39.64 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489740500 205 RMLAEGAQHVLISMAGDGGLLITKDAVYFSPAPKGQVINSVGAGDSMIGGFVGTFAKTHDAVEsfrYGLACGSATA 280
Cdd:cd01940 182 EAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTAIA---EAMRQGAQFA 254
|
|
| |
