|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-308 |
1.54e-157 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 442.24 E-value: 1.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 1 MILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTlKNINNKF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLD-DQIKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 81 YTIKGDTRNCIAILHEGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIPV 160
Cdd:PRK13508 80 YKIKGETRNCIAILHEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 161 VLDTSGESLKQVLLSNNIPYMIKPNIDELTVLLNNKVVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVD 240
Cdd:PRK13508 160 VLDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEVSEDLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYKVD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1325393571 241 IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQINVK 308
Cdd:PRK13508 240 IPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQEKQTGHVNMANYDELYNQIEVK 307
|
|
| lacC |
TIGR01231 |
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of ... |
1-308 |
5.29e-136 |
|
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of lactose degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273515 [Multi-domain] Cd Length: 310 Bit Score: 387.71 E-value: 5.29e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 1 MILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKNINNKF 80
Cdd:TIGR01231 1 MILTVTLNPSVDISYPLETLKIDTVNRVKEVSKTAGGKGLNVTRVLYQSGDKVLASGFLGGKLGEFIESELDQSPIKHAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 81 YTIKGDTRNCIAILHEGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIPV 160
Cdd:TIGR01231 81 YKISGETRNCIAILHEGNQTEILEQGPTISHEEAEGFLDHFENLLKKSEVVAISGSLPKGLPNDYYEQLIQLCSDEGVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 161 VLDTSGESLKQVLLSNNIPYMIKPNIDELTVLLNNKVVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVD 240
Cdd:TIGR01231 161 VLDCSGAPLETVLKSSAKPTVIKPNNEELSQLLGKEVTKDIEELKDALKEPLFSGIEWIIVSLGRQGAFAKHGDTFYKVD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1325393571 241 IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQINVK 308
Cdd:TIGR01231 241 IPDIPVVNPVGSGDSTVAGITSALNSKKSDADLLKKANTLGMLNAQETMTGHVNLTNYDTLNSQIEVK 308
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-306 |
3.85e-118 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 342.12 E-value: 3.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 2 ILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKNINNKFY 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 82 TIKGDTRNCIAILHE--GHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIP 159
Cdd:COG1105 81 PIEGETRINIKIVDPsdGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 160 VVLDTSGESLKQVLLSNniPYMIKPNIDELTVLLnNKVVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQV 239
Cdd:COG1105 161 VVLDTSGEALKAALEAG--PDLIKPNLEELEELL-GRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325393571 240 DIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQIN 306
Cdd:COG1105 238 KPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQVE 304
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-291 |
2.08e-108 |
|
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: 316.78 E-value: 2.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 1 MILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKNINNKF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 81 YTIKGDTRNCIAILH-EGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIP 159
Cdd:cd01164 81 VEVAGETRINVKIKEeDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 160 VVLDTSGESLKQVLLSNniPYMIKPNIDELTVLLnNKVVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQV 239
Cdd:cd01164 161 VILDTSGEALLAALAAK--PFLIKPNREELEELF-GRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1325393571 240 DIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTG 291
Cdd:cd01164 238 SPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-305 |
1.22e-106 |
|
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: 312.59 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 2 ILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKNINNKFY 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 82 TIKGDTRNCIAILH-EGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIPV 160
Cdd:TIGR03168 81 EVKGETRINVKIKEsSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 161 VLDTSGESLKQVLLSNniPYMIKPNIDELTVLLNNKvVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVD 240
Cdd:TIGR03168 161 ILDTSGEALREALAAK--PFLIKPNHEELEELFGRE-LKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKAT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1325393571 241 IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQI 305
Cdd:TIGR03168 238 PPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQV 302
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-307 |
2.28e-81 |
|
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: 248.27 E-value: 2.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 2 ILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKNINNKFY 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 82 TIKGDTRNCIAILHEGHQ-TEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGLPSDYYRYLIEIADSLDIPV 160
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGTeTKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 161 VLDTSGESLKQVLLSNniPYMIKPNIDELTVLLNNKvVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVD 240
Cdd:TIGR03828 161 ILDTSGEALRDGLKAK--PFLIKPNDEELEELFGRE-LKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325393571 241 IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQINV 307
Cdd:TIGR03828 238 PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQVTI 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-285 |
7.76e-58 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 187.94 E-value: 7.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 7 LNPSVDIS----YPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGG-KLGEFISEQLTLKNINNKFY 81
Cdd:pfam00294 1 KVVVIGEAnidlIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 82 TIKGDTRNCIAILH--EGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVItISGSLPEGLPSDYYRYLIEIADSLD-- 157
Cdd:pfam00294 81 VIDEDTRTGTALIEvdGDGERTIVFNRGAAADLTPEELEENEDLLENADLLY-ISGSLPLGLPEATLEELIEAAKNGGtf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 158 IPVVLDTSGESLKQVLLSNNIPYMIKPNIDELTVLLNNKVvDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFF 237
Cdd:pfam00294 160 DPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKL-DDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1325393571 238 QVD-IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNT 285
Cdd:pfam00294 239 HVPaVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVV 287
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-310 |
7.69e-37 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 133.67 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 2 ILTVTLNPSVDISYPIKEFKLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTG----GKLGEFISEQltlkNIN 77
Cdd:PRK09513 5 VATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGkdnqDGFQQLFSEL----GIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 78 NKFYTIKGDTRNCIAILH-EGHQTEILESGPTILKLEAEEYLPFFEKLASVSNVITISGSLPEGL-PSDYYRYLIEIaDS 155
Cdd:PRK09513 81 NRFQVVQGRTRINVKLTEkDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVsPEAFTDWMTRL-RS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 156 LDIPVVLDTSGESLKQVLLSNniPYMIKPNIDELTVLLNNKvVDTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKET 235
Cdd:PRK09513 160 QCPCIIFDSSREALVAGLKAA--PWLVKPNRRELEIWAGRK-LPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1325393571 236 FFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKTGHVNLNKFSYIYNQINVKVF 310
Cdd:PRK09513 237 EWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTPF 311
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-290 |
5.97e-28 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 109.87 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 2 ILTVTLNPSVDIS------YPikEFKLddvnRVTDTIKTAGGKGLNVTRVLNDLKKDVIATGFTGGKLGEFISEQLTLKN 75
Cdd:PRK10294 4 IYTLTLAPSLDSAtitpqiYP--EGKL----RCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 76 INNKFYTIKGDTRNCIAILHE--GHQTEILESGPTilkLEAEEYLPFFEKLASVSN--VITISGSLPEGLPSDYYRYLIE 151
Cdd:PRK10294 78 VPVATVEAKDWTRQNLHVHVEasGEQYRFVMPGAA---LNEDEFRQLEEQVLEIESgaILVISGSLPPGVKLEKLTQLIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 152 IADSLDIPVVLDTSGESLKQVLLSNNIPyMIKPNIDELTVLLNNKVVDTlEGIKEALSEELFSG-IEWVVVSRGEKGAVA 230
Cdd:PRK10294 155 AAQKQGIRCIIDSSGDALSAALAIGNIE-LVKPNQKELSALVNRDLTQP-DDVRKAAQELVNSGkAKRVVVSLGPQGALG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 231 KHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTMEEKT 290
Cdd:PRK10294 233 VDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGT 292
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-281 |
1.58e-21 |
|
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: 92.25 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 11 VDISYPIKEF-KLDDVNRVTDTIKTAGGKGLNVTRVLNDLKKDV-IATGFTGGKLGEFISEQLTLKNINNKFYTIKGDTR 88
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGARVaLVGAVGDDPFGDFLLAELRAEGVDTSGVRRDPGAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 89 N--CIAILHEGHQTEILESGPTILKLEAEEYLPffEKLASVSnVITISG-SLPEGLPSDYYRYLIEIADSLDIPVVLDTS 165
Cdd:COG0524 90 TglAFILVDPDGERTIVFYRGANAELTPEDLDE--ALLAGAD-ILHLGGiTLASEPPREALLAALEAARAAGVPVSLDPN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 166 G-----ESLKQVLLSNnIPY--MIKPNIDELTVLLNnkvVDTLEGIKEALSEElfsGIEWVVVSRGEKGAVAKHKETFFQ 238
Cdd:COG0524 167 YrpalwEPARELLREL-LALvdILFPNEEEAELLTG---ETDPEEAAAALLAR---GVKLVVVTLGAEGALLYTGGEVVH 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1325393571 239 VDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACG 281
Cdd:COG0524 240 VPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
34-283 |
2.19e-16 |
|
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: 77.74 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 34 TAGGKGLNVTRVLNDLKKDVIATGFTGGKL-GEFISEQLTLKNINNKFYTIKG-DTRNCIAILHEGHQTEILESGPTILK 111
Cdd:cd01941 33 SPGGVGRNIAENLARLGVSVALLSAVGDDSeGESILEESEKAGLNVRGIVFEGrSTASYTAILDKDGDLVVALADMDIYE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 112 LEAEEYLPFFEKLASVSNVITISGSLPEGLpsdyYRYLIEIADSLDIPVVLD-TSGESLKQVLLSNNIPYMIKPNIDELT 190
Cdd:cd01941 113 LLTPDFLRKIREALKEAKPIVVDANLPEEA----LEYLLALAAKHGVPVAFEpTSAPKLKKLFYLLHAIDLLTPNRAELE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 191 VLLNNKVVDTLEGIKEALSEeLFSGIEWVVVSRGEKGAVAKHKET-----FFQVDIPKiNVINPVGSGDATVAGLALAIS 265
Cdd:cd01941 189 ALAGALIENNEDENKAAKIL-LLPGIKNVIVTLGAKGVLLSSREGgvetkLFPAPQPE-TVVNVTGAGDAFVAGLVAGLL 266
|
250
....*....|....*...
gi 1325393571 266 EEKSDEEILKTAMACGVL 283
Cdd:cd01941 267 EGMSLDDSLRFAQAAAAL 284
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
147-286 |
1.62e-13 |
|
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: 69.53 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 147 RYLIEIADSLDIPVVLDT-------SGESLKQVLLSnnIPYMIK---PNIDELTVLLnnKVVDTLEGIKEALSEELfsGI 216
Cdd:cd01166 146 LEALEAAKARGVTVSFDLnyrpklwSAEEAREALEE--LLPYVDivlPSEEEAEALL--GDEDPTDAAERALALAL--GV 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 217 EWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVLNTM 286
Cdd:cd01166 220 KAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVT 289
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
150-281 |
1.98e-13 |
|
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: 69.12 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 150 IEIADSLDIPVVLDTSG-ESLKQVLLSNniPYMIKPNIDELTVLLNNKVvDTLEGIKEALSEELFSGIEWVVVSRGEKGA 228
Cdd:cd01174 148 LRAARRAGVTVILNPAPaRPLPAELLAL--VDILVPNETEAALLTGIEV-TDEEDAEKAARLLLAKGVKNVIVTLGAKGA 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1325393571 229 VAKHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACG 281
Cdd:cd01174 225 LLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAA 277
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
149-264 |
2.29e-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: 59.03 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 149 LIEIADSLDIPVVLDTSG----ESLKQVLLSNNIPYMIKPNIDELTVLLNnKVVDTLEGIKEALSEELFSGIEWVVVSRG 224
Cdd:cd00287 76 ALEEARRRGVPVVLDPGPravrLDGEELEKLLPGVDILTPNEEEAEALTG-RRDLEVKEAAEAAALLLSKGPKVVIVTLG 154
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1325393571 225 EKGA-VAKHKETFFQVDIPKINVINPVGSGDATVAGLALAI 264
Cdd:cd00287 155 EKGAiVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
151-283 |
5.38e-10 |
|
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: 59.25 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 151 EIADSLDIPVVLDT-------SGESLKQVLlsnNIPYMIKPNIDELTVLLnnkvvdTLEGIKEAlseELFSGIEWVVVSR 223
Cdd:cd01942 143 RELAAGGITVSFDPgqelprlSGEELEEIL---ERADILFVNDYEAELLK------ERTGLSEA---ELASGVRVVVVTL 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325393571 224 GEKGAVAKHKETFFQVD-IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACGVL 283
Cdd:cd01942 211 GPKGAIVFEDGEEVEVPaVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASL 271
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
36-281 |
2.10e-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: 54.53 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 36 GGKGLNVTRVLNDL-KKDVIATGFTGGKLGEFISEQLTLKNINNKFYTIKGDTRNCIAIlheghqTEIL--ESGPTI--- 109
Cdd:TIGR04382 34 GGSPANIAVGAARLgLKTAFITRVGDDQFGRFVRDYLRREGVDTSHVVTDPGRRTSLVF------LEIKppDEFPLLfyr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 110 -----LKLEAEEYLpffEKLASVSNVITISGSLPEGLPSDYYRYL-IEIADSLDIPVVLD------------TSGESLKQ 171
Cdd:TIGR04382 108 enaadLALTPDDVD---EDYIASARALLVSGTALSQEPSREAVLKaLEYARAAGVRVVLDidyrpylwkspeEAGIYLRL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 172 VLlsnniPYM--IKPNIDELTVLLNNKvvDTLEGIKEALSeelfSGIEWVVVSRGEKGAVAKHK-ETFFQVDIPKINVIN 248
Cdd:TIGR04382 185 VL-----PLVdvIIGTREEFDIAGGEG--DDEAAARALLD----AGVEILVVKRGPEGSLVYTGdGEGVEVPGFPVEVLN 253
|
250 260 270
....*....|....*....|....*....|...
gi 1325393571 249 PVGSGDATVAGLALAISEEKSDEEILKTAMACG 281
Cdd:TIGR04382 254 VLGAGDAFASGFLYGLLAGWDLEKALRYGNACG 286
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
199-281 |
8.79e-08 |
|
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: 52.36 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 199 DTLEGIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDeeiLKTAM 278
Cdd:cd01940 171 LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTA---IAEAM 247
|
...
gi 1325393571 279 ACG 281
Cdd:cd01940 248 RQG 250
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
23-285 |
9.54e-08 |
|
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: 52.25 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 23 DDVNRVTDTIKTAGGKGLNVTRVLNDLKKDViatGFTG--GK--LGEFISEQLTLKNINNKFYTIKGDTRNCIAILHEG- 97
Cdd:cd01167 15 EGSGAPETFTKAPGGAPANVAVALARLGGKA---AFIGkvGDdeFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 98 ---HQTEILESGPTILKLEAEEYLPFFEKlASVSNVITISGSLPEGlpSDYYRYLIEIADSLDIPVVLD--------TSG 166
Cdd:cd01167 92 dgeRSFEFYRGPAADLLLDTELNPDLLSE-ADILHFGSIALASEPS--RSALLELLEAAKKAGVLISFDpnlrpplwRDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 167 ESLKQVLLSN----NIpymIKPNIDELTVLLNNKVVDtlegikEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVDIP 242
Cdd:cd01167 169 EEARERIAELlelaDI---VKLSDEELELLFGEEDPE------EIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1325393571 243 KINVINPVGSGDATVAGL--------ALAISEEKSdEEILKTAMACGVLNT 285
Cdd:cd01167 240 PVEVVDTTGAGDAFVAGLlaqllsrgLLALDEDEL-AEALRFANAVGALTC 289
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
181-285 |
1.70e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 51.86 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 181 MIKPNIDELTVLLNNkvvDTLEGIKEALSEELfsGIEWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGL 260
Cdd:PRK09434 183 VVKLSEEELCFLSGT---SQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGL 257
|
90 100 110
....*....|....*....|....*....|.
gi 1325393571 261 --ALAISEEKSDE----EILKTAMACGVLNT 285
Cdd:PRK09434 258 laGLSQAGLWTDEaelaEIIAQAQACGALAT 288
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
191-281 |
5.07e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 50.60 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 191 VLLNNKVVDTLEGI---KEALSEELFSGI--EWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGLALAIS 265
Cdd:PLN02341 289 LLLTSEEAEALTGIrnpILAGQELLRPGIrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYI 368
|
90 100
....*....|....*....|....
gi 1325393571 266 EEKSDEEIL--------KTAMACG 281
Cdd:PLN02341 369 HNLPLVNTLtlanavgaATAMGCG 392
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
8-281 |
3.68e-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: 47.61 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 8 NPSVDISY-----PIKEFKL-------------DDVNRVTDTIKTAGGKGLNVTRVLNDLKKdviATGFTGG----KLGE 65
Cdd:cd01168 9 NALVDILAqvddaFLEKLGLkkgdmiladmeeqEELLAKLPVKYIAGGSAANTIRGAAALGG---SAAFIGRvgddKLGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 66 FISEQLTLKNINNKFYTIKGD-TRNCIAILHEGHQ----TEILESGptilKLEAEEylpFFEKLASVSNVITISGSLPEg 140
Cdd:cd01168 86 FLLKDLRAAGVDTRYQVQPDGpTGTCAVLVTPDAErtmcTYLGAAN----ELSPDD---LDWSLLAKAKYLYLEGYLLT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 141 LPSDYYRYLIEIADSLDIPVVLDtsgeslkqvlLSNniPYMIKPNIDELTVLLNNkvVD---------------TLEGIK 205
Cdd:cd01168 158 VPPEAILLAAEHAKENGVKIALN----------LSA--PFIVQRFKEALLELLPY--VDilfgneeeaealaeaETTDDL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325393571 206 EALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVD-IPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACG 281
Cdd:cd01168 224 EAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPaIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
203-281 |
3.20e-05 |
|
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: 44.72 E-value: 3.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1325393571 203 GIKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMACG 281
Cdd:cd01947 177 GELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCG 255
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
34-284 |
3.95e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 44.54 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 34 TAGGKGLNVTRVLNDLKKDVIATGFTGGKL-GEFISEQLTLK--NINNKFYTIKGDTRNCIAILHEGHQTEILESGPTIL 110
Cdd:PRK09954 91 SAGGVGRNIAHNLALLGRDVHLLSAIGDDFyGETLLEETRRAgvNVSGCIRLHGQSTSTYLAIANRQDETVLAINDTHIL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 111 KLEAEEYLPFFEKLASVSNVITISGSL-PEGLpsdyyRYLIEIADslDIPVVLDTSGEsLKQVLLSNNIPYM--IKPNID 187
Cdd:PRK09954 171 QQLTPQLLNGSRDLIRHAGVVLADCNLtAEAL-----EWVFTLAD--EIPVFVDTVSE-FKAGKIKHWLAHIhtLKPTQP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 188 ELTVLLNNKVVDTLEGIK--EALSEElfsGIEWVVVSRGEKGAVAKHKE-TFFQVDIPKINVINPVGSGDATVAGLALAI 264
Cdd:PRK09954 243 ELEILWGQAITSDADRNAavNALHQQ---GVQQIFVYLPDESVFCSEKDgEQFLLTAPAHTTVDSFGADDGFMAGLVYSF 319
|
250 260
....*....|....*....|
gi 1325393571 265 SEEKSDEEILKTAMACGVLN 284
Cdd:PRK09954 320 LEGYSFRDSARFAMACAAIS 339
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
204-280 |
8.29e-05 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 43.19 E-value: 8.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325393571 204 IKEALSEELFSGIEWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGLALAISEEKSDEEILKTAMAC 280
Cdd:PRK09813 173 LRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTAC 249
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
182-287 |
1.39e-04 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 43.07 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 182 IKPNIDELTVLLNNKVVDTLEGIKealseeLF-SGIEWVVVSRGEKGAVAKHKETFFQVDIPKINVINPVGSGDATVAGL 260
Cdd:PLN02323 201 IKVSDEEVEFLTGGDDPDDDTVVK------LWhPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAGDAFVGGL 274
|
90 100 110
....*....|....*....|....*....|....
gi 1325393571 261 ALAISEEKS---DE----EILKTAMACGVLNTME 287
Cdd:PLN02323 275 LSQLAKDLSlleDEerlrEALRFANACGAITTTE 308
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
173-280 |
8.05e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 40.49 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 173 LLSNNIPY--MIKPNIDELTVLLNNKVVDTLEGIKeALSEELFSGIEWVVVSRGEKGAVAKHKET-FFQVDIPKINVINP 249
Cdd:PTZ00292 191 IIKPFLKYvsLFCVNEVEAALITGMEVTDTESAFK-ASKELQQLGVENVIITLGANGCLIVEKENePVHVPGKRVKAVDT 269
|
90 100 110
....*....|....*....|....*....|.
gi 1325393571 250 VGSGDATVAGLALAISEEKSDEEILKTAMAC 280
Cdd:PTZ00292 270 TGAGDCFVGSMAYFMSRGKDLKESCKRANRI 300
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
184-281 |
3.11e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 38.86 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 184 PNIDELTVLLNNKVVD--TLEGIKEALSEELFSGI-----EWVVVSRGEKGAVAKhketfFQVDIPKI----------NV 246
Cdd:cd01943 186 PNLEEAARLLGLPTSEpsSDEEKEAVLQALLFSGIlqdpgGGVVLRCGKLGCYVG-----SADSGPELwlpayhtkstKV 260
|
90 100 110
....*....|....*....|....*....|....*
gi 1325393571 247 INPVGSGDATVAGLALAISEEKSdeeiLKTAMACG 281
Cdd:cd01943 261 VDPTGGGNSFLGGFAAGLALTKS----IDEACIYG 291
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
33-263 |
7.10e-03 |
|
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: 37.54 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 33 KTAGGKGlNVTRVLNDLKKDVIATGFTGG-KLGEFISEQLTLKNINNKFYTIKGDTRNC-IAILHEGHQteIL----ESG 106
Cdd:cd01172 37 IRLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGIVDEGRPTTTkTRVIARNQQ--LLrvdrEDD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 107 PTILKLEAEEYLPFFEKLASVSNVITIS----GSLPEGLpsdyYRYLIEIADSLDIPVVLDTSGESL---KQVLLsnnip 179
Cdd:cd01172 114 SPLSAEEEQRLIERIAERLPEADVVILSdygkGVLTPRV----IEALIAAARELGIPVLVDPKGRDYskyRGATL----- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325393571 180 ymIKPNIDELTVLLNNKVvDTLEGIkEALSEEL--FSGIEWVVVSRGEKGA--VAKHKEtffQVDIPKIN--VINPVGSG 253
Cdd:cd01172 185 --LTPNEKEAREALGDEI-NDDDEL-EAAGEKLleLLNLEALLVTLGEEGMtlFERDGE---VQHIPALAkeVYDVTGAG 257
|
250
....*....|
gi 1325393571 254 DATVAGLALA 263
Cdd:cd01172 258 DTVIATLALA 267
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