|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-309 |
0e+00 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 606.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 1 MILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDDNVKKDFF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQIKHAFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 81 SIQGETRNCIAILHGDNQTEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKPVV 160
Cdd:PRK13508 81 KIKGETRNCIAILHEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 161 LDCSGAALQAVLESPHKPTVIKPNNEELSQLLGREVSEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVDI 240
Cdd:PRK13508 161 LDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEVSEDLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYKVDI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446526941 241 PRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTGHVNMANYQALYDQLIVKEV 309
Cdd:PRK13508 241 PKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQEKQTGHVNMANYDELYNQIEVKEV 309
|
|
| lacC |
TIGR01231 |
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of ... |
1-309 |
1.20e-174 |
|
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: 485.55 E-value: 1.20e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 1 MILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDDN-VKKDF 79
Cdd:TIGR01231 1 MILTVTLNPSVDISYPLETLKIDTVNRVKEVSKTAGGKGLNVTRVLYQSGDKVLASGFLGGKLGEFIESELDQSpIKHAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 80 FSIQGETRNCIAILHGDNQTEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKPV 159
Cdd:TIGR01231 81 YKISGETRNCIAILHEGNQTEILEQGPTISHEEAEGFLDHFENLLKKSEVVAISGSLPKGLPNDYYEQLIQLCSDEGVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 160 VLDCSGAALQAVLESPHKPTVIKPNNEELSQLLGREVSEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVD 239
Cdd:TIGR01231 161 VLDCSGAPLETVLKSSAKPTVIKPNNEELSQLLGKEVTKDIEELKDALKEPLFSGIEWIIVSLGRQGAFAKHGDTFYKVD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 240 IPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTGHVNMANYQALYDQLIVKEV 309
Cdd:TIGR01231 241 IPDIPVVNPVGSGDSTVAGITSALNSKKSDADLLKKANTLGMLNAQETMTGHVNLTNYDTLNSQIEVKEV 310
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-304 |
4.78e-122 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 351.74 E-value: 4.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 2 ILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDD-NVKKDFF 80
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEeGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 81 SIQGETRNCIAILHGDN--QTEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKP 158
Cdd:COG1105 81 PIEGETRINIKIVDPSDgtETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 159 VVLDCSGAALQAVLESphKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKV 238
Cdd:COG1105 161 VVLDTSGEALKAALEA--GPDLIKPNLEELEELLGRPL-ETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446526941 239 DIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTGHVNMANYQALYDQL 304
Cdd:COG1105 238 KPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQV 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-290 |
6.63e-114 |
|
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: 330.65 E-value: 6.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 1 MILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDD-NVKKDF 79
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEeGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 80 FSIQGETRNCIAILHGDNQ-TEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKP 158
Cdd:cd01164 81 VEVAGETRINVKIKEEDGTeTEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 159 VVLDCSGAALQAVLESphKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKV 238
Cdd:cd01164 161 VILDTSGEALLAALAA--KPFLIKPNREELEELFGRPL-GDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446526941 239 DIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTG 290
Cdd:cd01164 238 SPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-303 |
3.48e-112 |
|
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: 326.84 E-value: 3.48e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 2 ILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDD-NVKKDFF 80
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEeGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 81 SIQGETRNCIAILH-GDNQTEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKPV 159
Cdd:TIGR03168 81 EVKGETRINVKIKEsSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 160 VLDCSGAALQAVLESphKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVD 239
Cdd:TIGR03168 161 ILDTSGEALREALAA--KPFLIKPNHEELEELFGREL-KTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKAT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446526941 240 IPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTGHVNMANYQALYDQ 303
Cdd:TIGR03168 238 PPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQ 301
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-273 |
2.90e-77 |
|
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: 237.87 E-value: 2.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 2 ILTVTMNPSIDISYPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENIDDN-VKKDFF 80
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEgIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 81 SIQGETRNCIAILHGDNQ-TEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKPV 159
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGTeTKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 160 VLDCSGAALQAVLESphKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVD 239
Cdd:TIGR03828 161 ILDTSGEALRDGLKA--KPFLIKPNDEELEELFGREL-KTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQ 237
|
250 260 270
....*....|....*....|....*....|....
gi 446526941 240 IPRIQVVNPVGSGDSTVAGISSGLLHKESDAELL 273
Cdd:TIGR03828 238 PPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEAL 271
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-291 |
4.49e-66 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 209.12 E-value: 4.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 7 MNPSIDIS----YPLDELKIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGG-KLGEFLVENIDD-NVKKDFF 80
Cdd:pfam00294 1 KVVVIGEAnidlIGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKeGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 81 SIQGETRNCIAILHGDN--QTEVLEKGPVVLEQEGQDFlEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAG-- 156
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGdgERTIVFNRGAAADLTPEEL-EENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGtf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 157 KPVVLDCSGAALQAVLESPHKPTVIKPNNEELSQLLGREvSEDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFY 236
Cdd:pfam00294 160 DPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAK-LDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446526941 237 KVD-IPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQEKMTGH 291
Cdd:pfam00294 239 HVPaVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-273 |
8.97e-38 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 135.98 E-value: 8.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 2 ILTVTMNPSIDISYPLDELKIDTVNRVvdvtKTAG----GKGLNVTRVLSEFGDSVlatgLVGGKLGEflvENIDD---- 73
Cdd:PRK09513 5 VATITLNPAYDLVGFCPEIERGEVNLV----KTTGlhaaGKGINVAKVLKDLGIDV----TVGGFLGK---DNQDGfqql 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 74 ----NVKKDFFSIQGETRNCIAILHGDNQ-TEVLEKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASL 148
Cdd:PRK09513 74 fselGIANRFQVVQGRTRINVKLTEKDGEvTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 149 VELANQAGKPVVLDCSGAALQAVLESphKPTVIKPNNEELSQLLGREVSEdLDELKEVLQEPLFAGIEWIIVSLGANGAF 228
Cdd:PRK09513 154 MTRLRSQCPCIIFDSSREALVAGLKA--APWLVKPNRRELEIWAGRKLPE-LKDVIEAAHALREQGIAHVVISLGAEGAL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446526941 229 AKHGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELL 273
Cdd:PRK09513 231 WVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTL 275
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-274 |
5.04e-27 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 107.56 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 2 ILTVTMNPSIDIS------YPLDELkidtvnRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKLGEFLVENI-DDN 74
Cdd:PRK10294 4 IYTLTLAPSLDSAtitpqiYPEGKL------RCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLaDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 75 VKKDFFSIQGETRNCIAIlHGD---NQTEVLEKGPVVLEQEGQDFLEHFKKLlESVEVVAISGSLPAGLPVDYYASLVEL 151
Cdd:PRK10294 78 VPVATVEAKDWTRQNLHV-HVEasgEQYRFVMPGAALNEDEFRQLEEQVLEI-ESGAILVISGSLPPGVKLEKLTQLISA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 152 ANQAGKPVVLDCSGAALQAVLESPHKpTVIKPNNEELSQLLGREVSEDlDELKEVLQEPLFAG-IEWIIVSLGANGAFAK 230
Cdd:PRK10294 156 AQKQGIRCIIDSSGDALSAALAIGNI-ELVKPNQKELSALVNRDLTQP-DDVRKAAQELVNSGkAKRVVVSLGPQGALGV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446526941 231 HGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLI 274
Cdd:PRK10294 234 DSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVR 277
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-280 |
4.82e-26 |
|
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: 104.58 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 11 IDISYPLDEL-KIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSV-LATGLVGGKLGEFLVENIDD-NVKKDFFSIQGETR 87
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGARVaLVGAVGDDPFGDFLLAELRAeGVDTSGVRRDPGAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 88 NCIAIL----HGDNQTEVLekgPVVLEQEGQDFLEhfKKLLESVEVVAISGSLPAG-LPVDYYASLVELANQAGKPVVLD 162
Cdd:COG0524 90 TGLAFIlvdpDGERTIVFY---RGANAELTPEDLD--EALLAGADILHLGGITLASePPREALLAALEAARAAGVPVSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 163 csgAALQAVLESPHKP---------TVIKPNNEELSQLLGREvseDLDELKEVLQEplfAGIEWIIVSLGANGAFAKHGD 233
Cdd:COG0524 165 ---PNYRPALWEPAREllrellalvDILFPNEEEAELLTGET---DPEEAAAALLA---RGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446526941 234 TFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLG 280
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
11-285 |
7.07e-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: 87.63 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 11 IDIsYPLDELKIDTVNRVvdvTKTAGGKGLNVTRVLSEFGDSV-LATGLVGGKLGEFLV-----ENIDDN-VKKDffsiq 83
Cdd:cd01166 10 VDL-SPPGGGRLEQADSF---RKFFGGAEANVAVGLARLGHRVaLVTAVGDDPFGRFILaelrrEGVDTShVRVD----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 84 getrnciailhGDNQTevlekGPVVLEQEGQD----------------FLEHF-KKLLESVEVVAISGSLPAGLPVDYYA 146
Cdd:cd01166 81 -----------PGRPT-----GLYFLEIGAGGerrvlyyragsaasrlTPEDLdEAALAGADHLHLSGITLALSESAREA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 147 SL--VELANQAGKPVVLDC-------SGAALQAVLES--PHKpTVIKPNNEELSQLLGREVSEDLDE-LKEVLqeplfAG 214
Cdd:cd01166 145 LLeaLEAAKARGVTVSFDLnyrpklwSAEEAREALEEllPYV-DIVLPSEEEAEALLGDEDPTDAAErALALA-----LG 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446526941 215 IEWIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLGMLNAQ 285
Cdd:cd01166 219 VKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVT 289
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
31-285 |
3.43e-17 |
|
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: 80.05 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 31 VTKTAGGKGLNVTRVLSEFGDSVLATGLVGGKL-GEFLVEN---IDDNVKKDFFSiQGETRNCIAILHGDNQTEVLEKGP 106
Cdd:cd01941 30 VKQSPGGVGRNIAENLARLGVSVALLSAVGDDSeGESILEEsekAGLNVRGIVFE-GRSTASYTAILDKDGDLVVALADM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 107 VVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLpvdyYASLVELANQAGKPVVLD-CSGAALQAVLESPHKPTVIKPNN 185
Cdd:cd01941 109 DIYELLTPDFLRKIREALKEAKPIVVDANLPEEA----LEYLLALAAKHGVPVAFEpTSAPKLKKLFYLLHAIDLLTPNR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 186 EELSQLLGREVSEDLDELKEVlQEPLFAGIEWIIVSLGANGAFAKHGDT-FYKVDIPRIQVVNPV---GSGDSTVAGISS 261
Cdd:cd01941 185 AELEALAGALIENNEDENKAA-KILLLPGIKNVIVTLGAKGVLLSSREGgVETKLFPAPQPETVVnvtGAGDAFVAGLVA 263
|
250 260
....*....|....*....|....
gi 446526941 262 GLLHKESDAELLIkanvLGMLNAQ 285
Cdd:cd01941 264 GLLEGMSLDDSLR----FAQAAAA 283
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
89-264 |
7.34e-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: 71.74 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 89 CIAILHGDNQTEVLEKGPVVLEQEG---QDFLEHFKKLLESVEVVAISGSLPAGL--PVDYYASLVELANQAGKPVVLDC 163
Cdd:cd00287 12 VILRVDALPLPGGLVRPGDTEERAGggaANVAVALARLGVSVTLVGADAVVISGLspAPEAVLDALEEARRRGVPVVLDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 164 SGAA----LQAVLESPHKPTVIKPNNEELSQLLGREVSEDLDELkEVLQEPLFAGIEWIIVSLGANGAFAKH-GDTFYKV 238
Cdd:cd00287 92 GPRAvrldGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAA-EAAALLLSKGPKVVIVTLGEKGAIVATrGGTEVHV 170
|
170 180
....*....|....*....|....*.
gi 446526941 239 DIPRIQVVNPVGSGDSTVAGISSGLL 264
Cdd:cd00287 171 PAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
149-277 |
1.36e-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: 69.89 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 149 VELANQAGKPVVLDCSGAA--LQAVLEsphKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEWIIVSLGANG 226
Cdd:cd01174 148 LRAARRAGVTVILNPAPARplPAELLA---LVDILVPNETEAALLTGIEV-TDEEDAEKAARLLLAKGVKNVIVTLGAKG 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446526941 227 AFAKHGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKAN 277
Cdd:cd01174 224 ALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFAN 274
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-268 |
2.32e-12 |
|
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: 66.48 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 1 MILTVTMNPSIDISYPLDEL------------------KIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGG- 61
Cdd:cd01168 2 YDVLGLGNALVDILAQVDDAfleklglkkgdmiladmeEQEELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 62 KLGEFLVENIDDN-VKKDFFSIQGETRNCIAILH--GDNQTEVLEKG-PVVLEQEgqdflEHFKKLLESVEVVAISGSLP 137
Cdd:cd01168 82 KLGDFLLKDLRAAgVDTRYQVQPDGPTGTCAVLVtpDAERTMCTYLGaANELSPD-----DLDWSLLAKAKYLYLEGYLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 138 AgLPVDYYASLVELANQAGKPVVLDCS--------GAALQAVLEsphKPTVIKPNNEELSQLLGREVSEDLDELKEVLQE 209
Cdd:cd01168 157 T-VPPEAILLAAEHAKENGVKIALNLSapfivqrfKEALLELLP---YVDILFGNEEEAEALAEAETTDDLEAALKLLAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446526941 210 plfaGIEWIIVSLGANGAFAKHGDTFYKVdiPRIQVVNPV---GSGDSTVAGISSGLLHKES 268
Cdd:cd01168 233 ----RCRIVVITQGAKGAVVVEGGEVYPV--PAIPVEKIVdtnGAGDAFAGGFLYGLVQGEP 288
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
198-274 |
8.35e-09 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 55.44 E-value: 8.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446526941 198 EDLDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLhkESDAELLI 274
Cdd:cd01940 171 LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLL--AGGTAIAE 245
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
28-278 |
8.67e-09 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 55.64 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 28 VVDVTKT---AGGKGlNVTRVLSEFGDSVLATGLVGG-KLGEFLVENIDD-NVKKDFFSIQGETRNC-IAILhGDNQtEV 101
Cdd:cd01172 29 VVKVEREeirLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKeGIDTDGIVDEGRPTTTkTRVI-ARNQ-QL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 102 L----EKGPVVLEQEGQDFLEHFKKLLESVEVVAISGSLPAGLPVDYYASLVELANQAGKPVVLD--CSGAALQAvlesp 175
Cdd:cd01172 106 LrvdrEDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIAAARELGIPVLVDpkGRDYSKYR----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 176 hKPTVIKPNNEELSQLLGREVSEDlDELKEVLQEPL-FAGIEWIIVSLGANGA--FAKHGDTFYkvdIPRI--QVVNPVG 250
Cdd:cd01172 181 -GATLLTPNEKEAREALGDEINDD-DELEAAGEKLLeLLNLEALLVTLGEEGMtlFERDGEVQH---IPALakEVYDVTG 255
|
250 260
....*....|....*....|....*...
gi 446526941 251 SGDSTVAGISSGLLHKESDAELLIKANV 278
Cdd:cd01172 256 AGDTVIATLALALAAGADLEEAAFLANA 283
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
208-280 |
1.14e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 52.91 E-value: 1.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446526941 208 QEPLFAGI--EWIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLG 280
Cdd:PLN02341 310 QELLRPGIrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVG 384
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
93-264 |
2.76e-07 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 50.89 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 93 LHGDNQTEVLEKgpVVLEQEGQDFLEHFkklleSVEVVAISGSLPAGLPVdyyaslvelANQAGKPVVLDCSGAalqavL 172
Cdd:PRK09813 89 VFGDYTEGVMAD--FALSEEDYAWLAQY-----DIVHAAIWGHAEDAFPQ---------LHAAGKLTAFDFSDK-----W 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 173 ESPHKPTVIkpnnEELSQLLGREVSEDlDELKEVLQEPLFAGIEWIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSG 252
Cdd:PRK09813 148 DSPLWQTLV----PHLDYAFASAPQED-EFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAG 222
|
170
....*....|..
gi 446526941 253 DSTVAGISSGLL 264
Cdd:PRK09813 223 DSFIAGFLCGWL 234
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
180-289 |
7.05e-07 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 49.93 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 180 VIKPNNEELSQLLGR-EVSEDLDELKEVLQEPLfagiewIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSGDSTVAG 258
Cdd:PRK09434 183 VVKLSEEELCFLSGTsQLEDAIYALADRYPIAL------LLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAG 256
|
90 100 110
....*....|....*....|....*....|....*....
gi 446526941 259 I-----SSGLLHKESD-AELLIKANVLGMLNAQEK--MT 289
Cdd:PRK09434 257 LlaglsQAGLWTDEAElAEIIAQAQACGALATTAKgaMT 295
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
92-271 |
4.80e-06 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 46.84 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 92 ILHGDNQTEVLEKGP--VVLEQEGQDFLEhFKKLLESVEVVAIsGSlpaGLPVDYYAS-LVELANQAGKPVVLDCSG--- 165
Cdd:cd01171 42 ATPPEAAAVIKSYSPelMVHPLLETDIEE-LLELLERADAVVI-GP---GLGRDEEAAeILEKALAKDKPLVLDADAlnl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 166 AALQAVLESPHKPTVIKPNNEELSQLLGREVSEDLDELKEVLQEplFAGIEWIIVSL-GANGAFAKHGDTFYkvdipriq 244
Cdd:cd01171 117 LADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAARE--AAAKLGATVVLkGAVTVIADPDGRVY-------- 186
|
170 180 190
....*....|....*....|....*....|....*
gi 446526941 245 vVNPV--------GSGDsTVAGISSGLLHKESDAE 271
Cdd:cd01171 187 -VNPTgnpglatgGSGD-VLAGIIAALLAQGLSPL 219
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
11-280 |
7.80e-05 |
|
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: 43.45 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 11 IDISYPLDEL-KIDTVNRVVDVTKTAGGKGLNVTRVLSEFGDSVLATGLVGGK-----LGEFLV-ENIDDnvkkDFFSIQ 83
Cdd:cd01942 10 YDIILKVESFpGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDfhgrlYLEELReEGVDT----SHVRVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 84 GETRNCIAILH---GDNQTEVLEKGPVVLEQEGQDflehfKKLLESVEVVAISGslPAGLPVDYYAslvelANQAGKPVV 160
Cdd:cd01942 86 DEDSTGVAFILtdgDDNQIAYFYPGAMDELEPNDE-----ADPDGLADIVHLSS--GPGLIELARE-----LAAGGITVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 161 LDC-------SGAALQAVLESPHkptVIKPNNEELSQLLGREVSEDLDELKevlqeplfaGIEWIIVSLGANGAFAKHGD 233
Cdd:cd01942 154 FDPgqelprlSGEELEEILERAD---ILFVNDYEAELLKERTGLSEAELAS---------GVRVVVVTLGPKGAIVFEDG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446526941 234 TFYKVD-IPRIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKANVLG 280
Cdd:cd01942 222 EEVEVPaVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA 269
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
158-277 |
1.36e-04 |
|
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: 42.79 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 158 PVVLDCSGAALQAVLEsphKPTVIKPNNEELSQLLGREVSEDLDELKEvLQEPLFAGIewiIVSLGANGAFAKH--GDTF 235
Cdd:cd01944 165 PRISDIPDTILQALMA---KRPIWSCNREEAAIFAERGDPAAEASALR-IYAKTAAPV---VVRLGSNGAWIRLpdGNTH 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446526941 236 YkvdIP--RIQVVNPVGSGDSTVAGISSGLLHKESDAELLIKAN 277
Cdd:cd01944 238 I---IPgfKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLAN 278
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
178-266 |
3.01e-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: 41.62 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 178 PTVIKPNNEELsqllgrEVSEDLDELKEVLQEplfAGIEWIIVSLGANGAFAKHGDTFYKVDIPRIQVVNPVGSGDSTVA 257
Cdd:cd01937 156 HDVLKLSRVEA------EVISTPTELARLIKE---TGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLA 226
|
....*....
gi 446526941 258 GISSGLLHK 266
Cdd:cd01937 227 AFLYSRLSG 235
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
180-278 |
5.52e-04 |
|
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: 41.17 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 180 VIKPNNEELSQLLGREVSED--LDELKEVLQEPLFAGI-----EWIIVSLGANGAFAKhgdtfYKVDIPRIQ-------- 244
Cdd:cd01943 183 VFSPNLEEAARLLGLPTSEPssDEEKEAVLQALLFSGIlqdpgGGVVLRCGKLGCYVG-----SADSGPELWlpayhtks 257
|
90 100 110
....*....|....*....|....*....|....*.
gi 446526941 245 --VVNPVGSGDSTVAGISSGLLHKESDAELLIKANV 278
Cdd:cd01943 258 tkVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSV 293
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
151-263 |
8.52e-04 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 40.02 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 151 LANQAGKPVVLD----CSG-------AALQAVLES--PHkPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAGIEW 217
Cdd:COG0351 88 LADYPLVPVVLDpvmvAKSgdrlldeDAVEALRELllPL-ATVVTPNLPEAEALLGIEI-TTLDDMREAAKALLELGAKA 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446526941 218 IIVSLG-ANGAFAKH----GDTFYKVDIPRIQVVNPVGSGDSTVAGISSGL 263
Cdd:COG0351 166 VLVKGGhLPGDEAVDvlydGDGVREFSAPRIDTGNTHGTGCTLSSAIAALL 216
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
148-263 |
1.15e-03 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 39.77 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 148 LVELANQAGKPVVLD-----CSGAAL------QAVLES--PhKPTVIKPNNEELSQLLGREVsEDLDELKEVLQEPLFAG 214
Cdd:pfam08543 78 VAEKLDKYGVPVVLDpvmvaKSGDSLlddeaiEALKEEllP-LATLITPNLPEAEALTGRKI-KTLEDMKEAAKKLLALG 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446526941 215 IEWIIV---SLGANGAFAK----HGDTFYKVDIPRIQVVNPVGSGDSTVAGISSGL 263
Cdd:pfam08543 156 AKAVLIkggHLEGEEAVVTdvlyDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANL 211
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
34-261 |
1.18e-03 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 39.97 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 34 TAGGKGLNVTRVLSEFGDSVLATGLVGGKL-GEFLVENIDD---NVKKDFFsIQGE-TRNCIAILhgDNQTEVLE--KGP 106
Cdd:PRK09850 38 TPGGVGRNIAQNLALLGNKAWLLSAVGSDFyGQSLLTQTNQsgvYVDKCLI-VPGEnTSSYLSLL--DNTGEMLVaiNDM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 107 VVLEQEGQDFLEHFKKLLESVEVVAISGSLPAglpvdyyASLVELANQAGK-PVVLD-CSGAALQAVLESPHKPTVIKPN 184
Cdd:PRK09850 115 NISNAITAEYLAQHREFIQRAKVIVADCNISE-------EALAWILDNAANvPVFVDpVSAWKCVKVRDRLNQIHTLKPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 185 NEELSQLLGREVS--EDLDELKEVLQEplfAGIEWIIVSLGANGAF--AKHGDTFYKVDIpRIQVVNPVGSGDSTVAGIS 260
Cdd:PRK09850 188 RLEAETLSGIALSgrEDVAKVAAWFHQ---HGLNRLVLSMGGDGVYysDISGESGWSAPI-KTNVINVTGAGDAMMAGLA 263
|
.
gi 446526941 261 S 261
Cdd:PRK09850 264 S 264
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
149-264 |
2.21e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.39 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 149 VELANQAGKPVVLDCSG--------AALQAVLESpHKPTVIKPNNEELSQLLGREVSEDLDELKEVLQEplfaGIEWIIV 220
Cdd:PLN02379 197 IRLAKQEGLSVSLDLASfemvrnfrSPLLQLLES-GKIDLCFANEDEARELLRGEQESDPEAALEFLAK----YCNWAVV 271
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446526941 221 SLGANGAFAKHGDTFYKVD-IPRIQVVNPVGSGDSTVAGISSGLL 264
Cdd:PLN02379 272 TLGSKGCIARHGKEVVRVPaIGETNAVDATGAGDLFASGFLYGLI 316
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
178-256 |
5.05e-03 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 38.18 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446526941 178 PTVIKPNNEELSQLLGREVSeDLDELKEVLQEPLFAGIEWIIVSLGANG-AFAKHGDTFYKVDIPRIQVVNPVGSGDSTV 256
Cdd:PTZ00292 199 VSLFCVNEVEAALITGMEVT-DTESAFKASKELQQLGVENVIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFV 277
|
|
| |
