|
Name |
Accession |
Description |
Interval |
E-value |
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-287 |
1.35e-117 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 340.19 E-value: 1.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 2 IHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGGFTGRYIVEELRKQHINVTPA 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 82 WVAEPTRINIFINDGRD--EYKLVNPGARINDEGKEQILHHL-QCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGCE 158
Cdd:COG1105 81 PIEGETRINIKIVDPSDgtETEINEPGPEISEEELEALLERLeELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 159 VILDISHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAP 238
Cdd:COG1105 161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1462009246 239 KIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLG 287
Cdd:COG1105 241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-287 |
3.73e-117 |
|
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: 339.17 E-value: 3.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 2 IHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGGFTGRYIVEELRKQHINVTPA 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 82 WVAEPTRINIFIND-GRDEYKLVNPGARINDEGKEQILHHL-QCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGCEV 159
Cdd:TIGR03168 81 EVKGETRINVKIKEsSGEETELNEPGPEISEEELEQLLEKLrELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 160 ILDISHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPK 239
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1462009246 240 IELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLG 287
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTG 288
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-287 |
7.56e-114 |
|
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: 330.71 E-value: 7.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 2 IHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGGFTGRYIVEELRKQHINVTPA 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 82 WVAEPTRINIFIND-GRDEYKLVNPGARINDEGKEQILHHL-QCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGCEV 159
Cdd:TIGR03828 81 RVPGETRINVKIKEpSGTETKLNGPGPEISEEELEALLEKLrAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 160 ILDISHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPK 239
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1462009246 240 IELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLG 287
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTG 288
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-287 |
4.71e-107 |
|
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: 312.93 E-value: 4.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 1 MIHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGGFTGRYIVEELRKQHINVTP 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 81 AWVAEPTRINIFINDGR-DEYKLVNPGARINDEGKEQILHHL-QCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGCE 158
Cdd:cd01164 81 VEVAGETRINVKIKEEDgTETEINEPGPEISEEELEALLEKLkALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 159 VILDISHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAP 238
Cdd:cd01164 161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1462009246 239 KIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLG 287
Cdd:cd01164 241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
12-287 |
3.70e-42 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 147.10 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 12 DMNIFCDPLQ---PAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGG-FTGRYIVEELRKQHINVTPAWVAEPT 87
Cdd:pfam00294 7 EANIDLIGNVeglPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYVVIDEDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 88 RINIFI--NDGRDEYKLVNPGARINDEGKEQILHHLQCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGCE--VILDI 163
Cdd:pfam00294 87 RTGTALieVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGTFdpNLLDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 164 SHPVLRQLLEW--HPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSA-PKI 240
Cdd:pfam00294 167 LGAAREALLELlpLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKV 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1462009246 241 ELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLG 287
Cdd:pfam00294 247 KVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-277 |
2.60e-35 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 129.46 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 1 MIHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGGFTGRYIVEELRKQhinVTP 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ---IKH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 81 AW--VAEPTRINIFINDGRDEYKLVNPGARI-NDEGKEQILHHLQCVTPGDYLVISGSLPPGIESRFYSEILVLCQQKGC 157
Cdd:PRK13508 78 AFykIKGETRNCIAILHEGQQTEILEKGPEIsVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 158 EVILDISHPVLRQLLE--WHPLLIKPNDDELNEIFGLDVSspQRVREAMQTLHQ---LGARNVLLTLGAQGLYFSNGEQL 232
Cdd:PRK13508 158 PVVLDCSGAALQAVLEspYKPTVIKPNIEELSQLLGKEVS--EDLDELKEVLQQplfEGIEWIIVSLGADGAFAKHNDTF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1462009246 233 WFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATG 277
Cdd:PRK13508 236 YKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLG 280
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-255 |
7.02e-35 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 128.36 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 2 IHTLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHyqqpthvMG-----IF--GGFTGRYIVEELRKQ 74
Cdd:PRK10294 4 IYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAH-------LGgsataIFpaGGATGEHLVSLLADE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 75 HINVTPAWVAEPTRINIFIN--DGRDEYKLVNPGARINDEGKEQILHHLQCVTPGDYLVISGSLPPGIESRFYSEILVLC 152
Cdd:PRK10294 77 NVPVATVEAKDWTRQNLHVHveASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 153 QQKGCEVILDISHPVLRQLLEWHPL-LIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLG-ARNVLLTLGAQGLYFSNGE 230
Cdd:PRK10294 157 QKQGIRCIIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkAKRVVVSLGPQGALGVDSE 236
|
250 260
....*....|....*....|....*
gi 1462009246 231 QLWFCSAPKIELVSSACAGDAALGA 255
Cdd:PRK10294 237 NCIQVVPPPVKSQSTVGAGDSMVGA 261
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-285 |
4.28e-31 |
|
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: 118.06 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 8 NTAIDMNIFCDPLQ-PAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFG-GFTGRYIVEELRKQHINVTPAWVAE 85
Cdd:COG0524 7 EALVDLVARVDRLPkGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGdDPFGDFLLAELRAEGVDTSGVRRDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 86 --PTRIN-IFINDGRDEYKLVNPGAriNDE-GKEQILHHLqcVTPGDYLVISGSLPPGIESR-FYSEILVLCQQKGCEVI 160
Cdd:COG0524 87 gaPTGLAfILVDPDGERTIVFYRGA--NAElTPEDLDEAL--LAGADILHLGGITLASEPPReALLAALEAARAAGVPVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 161 LDIS---------HPVLRQLLEWHPLLiKPNDDELNEIFGLDvsspqRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQ 231
Cdd:COG0524 163 LDPNyrpalwepaRELLRELLALVDIL-FPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGGE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1462009246 232 LWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAG 285
Cdd:COG0524 237 VVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
4-292 |
1.16e-29 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 114.41 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 4 TLTLNTAIDMNIFCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHyqqpthvMGI---FGGFTGRYIVEELRK--QHINV 78
Cdd:PRK09513 7 TITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKD-------LGIdvtVGGFLGKDNQDGFQQlfSELGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 79 TPAW--VAEPTRINIFINDGRDEYKLVN-PGARINDEGKEQILH-HLQCVTPGDYLVISGSLPPGIESRFYSEILVLCQQ 154
Cdd:PRK09513 80 ANRFqvVQGRTRINVKLTEKDGEVTDFNfSGFEVTPADWERFVTdSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 155 KGCEVILDISHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWF 234
Cdd:PRK09513 160 QCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1462009246 235 CSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGLGKLNRT 292
Cdd:PRK09513 240 AKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRP 297
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
64-278 |
2.02e-21 |
|
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: 91.84 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 64 GRYIVEELRKQHINVTPAWVAEPTR---INIFINDGRDEYKLVNPGAriNDE-GKEQILHHLQCVTPGDYLVISGSLP-P 138
Cdd:cd01174 65 GDELLENLREEGIDVSYVEVVVGAPtgtAVITVDESGENRIVVVPGA--NGElTPADVDAALELIAAADVLLLQLEIPlE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 139 GIEsrfysEILVLCQQKGCEVILDIS--HPVLRQLLEWHPLLIkPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVL 216
Cdd:cd01174 143 TVL-----AALRAARRAGVTVILNPApaRPLPAELLALVDILV-PNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVI 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1462009246 217 LTLGAQG-LYFSNGEQLWFcSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGA 278
Cdd:cd01174 217 VTLGAKGaLLASGGEVEHV-PAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
20-285 |
5.63e-15 |
|
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: 73.76 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 20 LQPAAVNRTRQTEYC---PNGKGVNVSLVLHHYQQPTHVMGIFG--GFtGRYIVEELRKQHINVT--PAWVAEPTRINIF 92
Cdd:cd01166 12 LSPPGGGRLEQADSFrkfFGGAEANVAVGLARLGHRVALVTAVGddPF-GRFILAELRREGVDTShvRVDPGRPTGLYFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 93 INDGRDEYKLVN-----PGARIN-DEGKEQILHhlqcvtPGDYLVISGSLPPGIES--RFYSEILVLCQQKGCEVILDIS 164
Cdd:cd01166 91 EIGAGGERRVLYyragsAASRLTpEDLDEAALA------GADHLHLSGITLALSESarEALLEALEAAKARGVTVSFDLN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 165 H-PVLRQLLEWHPLLIK---------PNDDELNEIFGLdvSSPQRVREAMQTLHqLGARNVLLTLGAQGLYFSNGEQLWF 234
Cdd:cd01166 165 YrPKLWSAEEAREALEEllpyvdivlPSEEEAEALLGD--EDPTDAAERALALA-LGVKAVVVKLGAEGALVYTGGGRVF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1462009246 235 CSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAG 285
Cdd:cd01166 242 VPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
18-275 |
1.04e-12 |
|
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: 66.95 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 18 DPLQPAAVN--RTRQTeycPNGKGVNVSLVLHHYQQPTHVMGIFGG-FTGRYIVEELRKQHINVTPAWVA-EPTRINIFI 93
Cdd:cd01941 18 GSLVPGTSNpgHVKQS---PGGVGRNIAENLARLGVSVALLSAVGDdSEGESILEESEKAGLNVRGIVFEgRSTASYTAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 94 NDGRDEYKLVNPGARINDEGKEQIL-HHLQCVTPGDYLVISGSLPPGIESRfyseILVLCQQKGCEVILDI-SHPVLRQL 171
Cdd:cd01941 95 LDKDGDLVVALADMDIYELLTPDFLrKIREALKEAKPIVVDANLPEEALEY----LLALAAKHGVPVAFEPtSAPKLKKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 172 LEW-HPL-LIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQG-LYFSNGEQLWFCSAPKI---ELVSS 245
Cdd:cd01941 171 FYLlHAIdLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGvLLSSREGGVETKLFPAPqpeTVVNV 250
|
250 260 270
....*....|....*....|....*....|
gi 1462009246 246 ACAGDAALGAFLSRWLNAGDIPQALALASA 275
Cdd:cd01941 251 TGAGDAFVAGLVAGLLEGMSLDDSLRFAQA 280
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
127-261 |
2.09e-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: 64.81 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 127 GDYLVISGSLPPGiesRFYSEILVLCQQKGCEVILD-------ISHPVLRQLLEwHPLLIKPNDDELNEIFGLDVSSPQR 199
Cdd:cd00287 58 ADAVVISGLSPAP---EAVLDALEEARRRGVPVVLDpgpravrLDGEELEKLLP-GVDILTPNEEEAEALTGRRDLEVKE 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1462009246 200 VREAMQTLHQLGARNVLLTLGAQG-LYFSNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWL 261
Cdd:cd00287 134 AAEAAALLLSKGPKVVIVTLGEKGaIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
178-285 |
2.37e-11 |
|
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: 63.04 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 178 LIKPNDDELNEIFGLDvsSPQRVReamQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPKIELVSSACAGDAALGAFL 257
Cdd:cd01167 184 IVKLSDEELELLFGEE--DPEEIA---ALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLL 258
|
90 100 110
....*....|....*....|....*....|....*
gi 1462009246 258 SRWLNAGD-------IPQALALASATGADVAASAG 285
Cdd:cd01167 259 AQLLSRGLlaldedeLAEALRFANAVGALTCTKAG 293
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
196-280 |
1.20e-10 |
|
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: 60.83 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 196 SPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWLNAGD-IPQALALAS 274
Cdd:cd01940 172 SDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGGTaIAEAMRQGA 251
|
....*.
gi 1462009246 275 ATGADV 280
Cdd:cd01940 252 QFAAKT 257
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
64-278 |
5.69e-10 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 59.11 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 64 GRYIVEELRKQHINVTPAWVA--EPTRIN-IFINDGRDEYKLVNPGAriNDEGKEQILH-HLQCVTPGDYLVISGSLP-P 138
Cdd:PRK11142 68 GESMRQQLAKDGIDTAPVSVIkgESTGVAlIFVNDEGENSIGIHAGA--NAALTPALVEaHRELIANADALLMQLETPlE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 139 GIEsrfysEILVLCQQKGCEVILD------ISHpvlrQLLEWHPLlIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGA 212
Cdd:PRK11142 146 TVL-----AAAKIAKQHGTKVILNpapareLPD----ELLALVDI-ITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGI 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1462009246 213 RNVLLTLGAQGLYFSNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGA 278
Cdd:PRK11142 216 ETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAA 281
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
127-279 |
4.04e-09 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 127 GDYLVISGSLPpgIESRFysEILVLCQQKGCEVILDIS-------HPVLRQLLEWHPLLIkPNDDELNEIFGLDVSSPQR 199
Cdd:PTZ00292 148 CKYLICQNEIP--LETTL--DALKEAKERGCYTVFNPApapklaeVEIIKPFLKYVSLFC-VNEVEAALITGMEVTDTES 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 200 VREAMQTLHQLGARNVLLTLGAQG-LYFSNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGA 278
Cdd:PTZ00292 223 AFKASKELQQLGVENVIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAA 302
|
.
gi 1462009246 279 D 279
Cdd:PTZ00292 303 I 303
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
178-285 |
1.63e-08 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 54.87 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 178 LIKPNDDELNEIFGLDVSSPQRVREAMQTL-HQLGARNVLLTLGAQG-LYFSNGEQLWFCSAPKIELVSSACAGDAALgA 255
Cdd:cd01172 184 LLTPNEKEAREALGDEINDDDELEAAGEKLlELLNLEALLVTLGEEGmTLFERDGEVQHIPALAKEVYDVTGAGDTVI-A 262
|
90 100 110
....*....|....*....|....*....|.
gi 1462009246 256 FLSRWLNAG-DIPQALALASATGADVAASAG 285
Cdd:cd01172 263 TLALALAAGaDLEEAAFLANAAAGVVVGKVG 293
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
14-285 |
3.40e-08 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 53.58 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 14 NIFCD-------PLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGG-FTGRYIVEELRKQHINVTPAWVAE 85
Cdd:cd01947 7 HVEWDiflsldaPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRdEIGIQSLEELESGGDKHTVAWRDK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 86 PTRINIFINDGRDEYKLVNPGARINDEGKEQILhhlqcvTPGDYLVISGSLPPgiesrfySEILVLCQQKGCeVILDISH 165
Cdd:cd01947 87 PTRKTLSFIDPNGERTITVPGERLEDDLKWPIL------DEGDGVFITAAAVD-------KEAIRKCRETKL-VILQVTP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 166 PV----LRQLLEWHPLLIKPNDDelneiFGLDVSSPqrvREAMqtlhqLGARNVLLTLGAQGLYFSNGEQLWFCSAPKIE 241
Cdd:cd01947 153 RVrvdeLNQALIPLDILIGSRLD-----PGELVVAE---KIAG-----PFPRYLIVTEGELGAILYPGGRYNHVPAKKAK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1462009246 242 LVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAG 285
Cdd:cd01947 220 VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
202-278 |
5.54e-08 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 53.07 E-value: 5.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1462009246 202 EAMQTLHQLGARNVLLTLGAQG-LYFSNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGA 278
Cdd:cd01945 193 EALELLASLGIPFVAVTLGEAGcLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAA 270
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
155-276 |
5.99e-08 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 52.59 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 155 KGCEVILDIsHPVLRQLLEWHPLLIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLT------LGAQGLYFSN 228
Cdd:cd01173 117 KLYVVAEEI-VPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGST 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1462009246 229 GEQLWFCSAPKIELVSSAC-AGDAALGAFLSRWLNAGDIPQALALASAT 276
Cdd:cd01173 196 ATEAWLVQRPKIPFPAYFNgTGDLFAALLLARLLKGKSLAEALEKALNF 244
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
175-282 |
1.48e-06 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 48.58 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 175 HPLLIK--PNDDELneiFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPKIELVSSACAGDAA 252
Cdd:PRK09813 149 SPLWQTlvPHLDYA---FASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSF 225
|
90 100 110
....*....|....*....|....*....|
gi 1462009246 253 LGAFLSRWLNAGDIPQALalasATGADVAA 282
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAM----AQGTACAA 251
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
147-285 |
1.77e-06 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 48.76 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 147 EILVLCQQKGCEVILDIS--------HPVLRQLLEWHPLLIKpNDDELNEIFGLDVSSpqrVREAMQTLHQLGARNVLLT 218
Cdd:cd01168 165 LAAEHAKENGVKIALNLSapfivqrfKEALLELLPYVDILFG-NEEEAEALAEAETTD---DLEAALKLLALRCRIVVIT 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1462009246 219 LGAQGLYFSNGEQLWFCSAPKIE-LVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAG 285
Cdd:cd01168 241 QGAKGAVVVEGGEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
179-262 |
2.79e-06 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 48.06 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 179 IKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFS--NGEQLWfcSAP-KIELVSSACAGDAALGA 255
Cdd:PRK09850 184 LKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSdiSGESGW--SAPiKTNVINVTGAGDAMMAG 261
|
....*..
gi 1462009246 256 FLSRWLN 262
Cdd:PRK09850 262 LASCWVD 268
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
155-275 |
3.45e-06 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 47.56 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 155 KGCEVILDISHPVLRQLLewhPL--LIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLT--------LGAQGL 224
Cdd:PRK05756 119 KGCIVAPGVAEFLRDRAL---PAadIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTslaragypADRFEM 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1462009246 225 YFSNGEQLWFCSAPKIELVSSAC-AGDAALGAFLSRWLNAGDIPQALALASA 275
Cdd:PRK05756 196 LLVTADGAWHISRPLVDFMRQPVgVGDLTSALFLARLLQGGSLEEALEHTTA 247
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
179-278 |
5.61e-06 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 47.24 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 179 IKPNDDELNEIFGLDvsspqRVREAMQTL-HQLGARNVLLTLGAQG-LYFSNGEQLWFcSAPKIELVSSACAGDAALGAF 256
Cdd:PRK09434 184 VKLSEEELCFLSGTS-----QLEDAIYALaDRYPIALLLVTLGAEGvLVHTRGQVQHF-PAPSVDPVDTTGAGDAFVAGL 257
|
90 100
....*....|....*....|....*...
gi 1462009246 257 L------SRWLNAGDIPQALALASATGA 278
Cdd:PRK09434 258 LaglsqaGLWTDEAELAEIIAQAQACGA 285
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
8-285 |
1.13e-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: 46.15 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 8 NTAIDMNIFCDPL--QPAAVNRTRQTEYCPnGKGVNVSLVLHHYQQPTHVMGIFGG-FTGRYIVEELRKQHINVTPAWVA 84
Cdd:cd01942 7 HLNYDIILKVESFpgPFESVLVKDLRREFG-GSAGNTAVALAKLGLSPGLVAAVGEdFHGRLYLEELREEGVDTSHVRVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 85 EPTRIN-IFI-NDGRDE-----YKLVNPGARINDEGKEQILhhLQCVTPGDYlvisgslppgiesrfySEILVLCQQK-- 155
Cdd:cd01942 86 DEDSTGvAFIlTDGDDNqiayfYPGAMDELEPNDEADPDGL--ADIVHLSSG----------------PGLIELARELaa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 156 -GCEVILD-------ISHPVLRQLLEwHPLLIKPNDDELNEIFGLDVSSPQRVREamqtlhqlGARNVLLTLGAQG-LYF 226
Cdd:cd01942 148 gGITVSFDpgqelprLSGEELEEILE-RADILFVNDYEAELLKERTGLSEAELAS--------GVRVVVVTLGPKGaIVF 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1462009246 227 SNGEQLWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAG 285
Cdd:cd01942 219 EDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
10-286 |
2.82e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 45.31 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 10 AIDMNI--FCDPLQPAAVNRTRQTEYCPNGKGVNVSLVLHHYQQPTHVMGIFGG-FTGRYIVEELRKQHINVTPA--WVA 84
Cdd:PRK09954 65 AINMDIrgMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDdFYGETLLEETRRAGVNVSGCirLHG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 85 EPTRINIFINDGRDEYKLVnpgarINDEgkeqilHHLQCVTP-------------GDYLVISGSLPPGIEsrfyseiLVL 151
Cdd:PRK09954 145 QSTSTYLAIANRQDETVLA-----INDT------HILQQLTPqllngsrdlirhaGVVLADCNLTAEALE-------WVF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 152 CQQKGCEVILD-ISHPVLRQLLEWHPLL--IKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLGAQGLYFS- 227
Cdd:PRK09954 207 TLADEIPVFVDtVSEFKAGKIKHWLAHIhtLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSe 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 228 -NGEQlWFCSAPKIELVSSACAGDAALGAFLSRWLNAGDIPQALALASATGADVAASAGL 286
Cdd:PRK09954 287 kDGEQ-FLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRASGSL 345
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
178-288 |
5.34e-05 |
|
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: 43.62 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 178 LIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVLLTLG--------AQGLYFSNGEQLWFcSAPKIELVSSACAG 249
Cdd:pfam08543 122 LITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeavVTDVLYDGGGFYTL-EAPRIPTKNTHGTG 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1462009246 250 D---AALGAFLSRWLnagDIPQALALASA--TGAdVAASAGLGK 288
Cdd:pfam08543 201 CtlsAAIAANLAKGL---SLPEAVREAKEyvTEA-IRDALNLGK 240
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
178-278 |
7.59e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 43.16 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 178 LIKPNDDELNEIfgldvSSPqrvREAMQTLHQLGARNVLLTLGAQGLYFSNGEQLWFCSAPKIELVSSACAGDAALGAFL 257
Cdd:cd01937 158 VLKLSRVEAEVI-----STP---TELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFL 229
|
90 100
....*....|....*....|.
gi 1462009246 258 SRWLNAGDIPQALALASATGA 278
Cdd:cd01937 230 YSRLSGKDIKEAAEFAAAAAA 250
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
169-273 |
2.83e-04 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 41.65 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 169 RQLLewhPL--LIKPNDDELNEIFGLDVSSP-QRVREAMQTLHQLGARNVLLTLGAQG-------LYFsNGEQLWFCSAP 238
Cdd:PRK06427 128 ERLL---PLatLITPNLPEAEALTGLPIADTeDEMKAAARALHALGCKAVLIKGGHLLdgeesvdWLF-DGEGEERFSAP 203
|
90 100 110
....*....|....*....|....*....|....*...
gi 1462009246 239 KIELVSSACAGD---AALGAFLSRWLnagDIPQALALA 273
Cdd:PRK06427 204 RIPTKNTHGTGCtlsAAIAAELAKGA---SLLDAVQTA 238
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
153-241 |
3.81e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 38.12 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009246 153 QQKGCEVILDishPVL--------------RQLLEWHPL--LIKPNDDELNEIFGLDVSSPQRVREAMQTLHQLGARNVL 216
Cdd:PRK12413 94 GHPGIPVVLD---PVLvckethdvevselrQELIQFFPYvtVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVV 170
|
90 100 110
....*....|....*....|....*....|..
gi 1462009246 217 LTLG-------AQGLYFsNGEQLWFCSAPKIE 241
Cdd:PRK12413 171 IKGGnrlsqkkAIDLFY-DGKEFVILESPVLE 201
|
|
| |
