|
Name |
Accession |
Description |
Interval |
E-value |
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
3-551 |
0e+00 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 979.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 3 WLLEPSPVEPRGRAEMEPNRRGwpKTRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGT 82
Cdd:cd00764 215 WIFIPERPPEDGWEDQMCRRLS--EHRSRGKRLNIIIVAEGAIDDQLKPITSEDVKDLVVERLGLDTRVTTLGHVQRGGT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 83 PSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNI 162
Cdd:cd00764 293 PSAFDRILASLMGVEAVMALLEATPDTPACVVSLNGNKAVRLPLMECVQLTKDVQKAMDEKRFDEAAALRGKSFDKNWNL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 163 YKLLAHQKPPK--EKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRG 240
Cdd:cd00764 373 YKLLAIELPQPlpEKTNLNIAIVNVGAPAAGMNAAVRSAVRYGLAHGHRPYAIYDGFEGLAKGQIVELGWIDVGGWTGRG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 241 GSMLGTKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSD 320
Cdd:cd00764 453 GSELGTKRTLPKKDLETIAYNFQKYGIDGLIIVGGFEAYKGLLQLREAREQYEEFCIPMVLIPATVSNNVPGTDFSLGSD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 321 TAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRG 400
Cdd:cd00764 533 TALNALMKYCDRIKQSASGTKRRVFIVETMGGYCGYLATMTGLAVGADAAYVFEEPFNIRDLQENVEHLTEKMKTTIGRG 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 401 LVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFAN 480
Cdd:cd00764 613 LVLRNEKCNENYTTVFTYELYSEEGKGVFDCRTNVLGHVQQGGAPSPFDRNFGTKFAVKAMKWIEQKLKENYAAGNEFAN 692
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768020939 481 APDSACVIGLKKKAVAFSPVTELKKDTdFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRT 551
Cdd:cd00764 693 DPDFNCVNGVKKYAVLFEPVEELKQTT-FEHRIPKEQWWLSLRPLLKILAKYKISADISDHGQLEHVTRGQ 762
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
19-533 |
0e+00 |
|
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 769.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 19 EPNRRGWP--------KTRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRIL 90
Cdd:TIGR02478 218 RPPEEGWEdqlchklkRNRKAGKRKTIVIVAEGAIDRDLNPITSEDVKDVLVERLGLDTRITVLGHVQRGGAPSAFDRIL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 91 SSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNIYKLLAHQK 170
Cdd:TIGR02478 298 ATRQGVEAVLAVLESTPETPSPVISLRGNKIVRKPLVEAVAQTKTVAKAIEEKDFDEAMRLRGREFAENLETFLFLSIPD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 171 PPK-----EKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLG 245
Cdd:TIGR02478 378 DDKklvpsEASRLRIAIIHVGAPAGGMNAATRSAVRYALARGHTVIAIHNGFSGLARHDVRELTWSDVEGWVGEGGSELG 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 246 TKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNA 325
Cdd:TIGR02478 458 TNRSLPGDDLGTIAYYFQQHKIDGLIIIGGFEAFEALYQLDAAREKYPAFRIPMVVIPATISNNVPGTEYSLGSDTALNE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 326 AMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRGLVLRN 405
Cdd:TIGR02478 538 ITEYCDNIKQSASASKRRVFVVETMGGYSGYLATMAGLATGADAAYIPEEGISLKDLQEDIEHLKETFAEGRAGKLILRN 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 406 EKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANaPDSA 485
Cdd:TIGR02478 618 EKASKVYTTDFIARIISEEGKGRFDARTAVLGHMQQGGSPSPFDRVRATRLAIRAVDFIEEKIKANKHADKLSAD-DTSA 696
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 768020939 486 CVIGLKKKAVAFSPV-TELKKDTDFEHRMPREQWWLSLRLMLKMLAQYR 533
Cdd:TIGR02478 697 VVIGIRGSNVLFTPVkQLLANETDFEHRRPKNQWWLQLRPLVRILAGRD 745
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
180-461 |
6.25e-127 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 372.44 E-value: 6.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLES-- 257
Cdd:pfam00365 2 IGILTSGGDAPGMNAAIRAVVRTAIYRGHEVYGIRNGYEGLVEGDIDELTWRDVSGILNRGGTILGTSRSKPFKTEEGre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 258 -IVENIRIYGIHALLVVGGFEAYEGVLQLVEARGryeelcIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQS 336
Cdd:pfam00365 82 kIAENLKKLGIDALVVIGGDGSLTGANKLSEERG------IPVVGIPKTIDNDIPGTDYTIGFDTALNTIVEAIDRIRDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 337 ASGTkRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTeKMKTDIqrgLVLRNEKCHDyytTEF 416
Cdd:pfam00365 156 ASSH-NRVFVVEVMGRHCGWLALMAGLAGGADAILIPEIPFDIEELCEKIKELR-KGKRFS---IIVVAEGASD---GEF 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 768020939 417 LYNLYssEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAM 461
Cdd:pfam00365 228 LAKLI--EEGTGIETRVTVLGHVQRGGTPSAFDRILATRLGVKAV 270
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
180-466 |
7.04e-71 |
|
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439975 [Multi-domain] Cd Length: 344 Bit Score: 230.73 E-value: 7.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPK---GQLE 256
Cdd:COG0205 4 IGILTSGGDAPGLNAAIRAVVRTAIKYGIEVYGIRDGYEGLLEGDIIDLTREDVSGILQRGGTILGSSRSKPFkteEGRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 257 SIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGryeelciVMCV-IPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQ 335
Cdd:COG0205 84 KALENLKKLGIDALVVIGGDGSLDGAAKLAEEYG-------IPVVgIPKTIDNDLPGTDYTIGFDTAVNTAAEAIDRLRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 336 SASGTkRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLkvnVEHMTEKMKTDIQRGLVL--------RNEK 407
Cdd:COG0205 157 TAASH-ERVFVVEVMGRHAGWLALAAGLAGGADLILIPEVPFDLDKL---LEKLKERRKRGKGYSIIVvaegagdeDGEA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768020939 408 CHDYYTTEFLYNLYSSEGKGV---------FDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSE 466
Cdd:COG0205 233 VLEADTDAFGHVRLGGIGEYLakeieertgIETRVTVLGHLQRGGSPSAFDRVLASRLGAAAVELLLE 300
|
|
| PRK03202 |
PRK03202 |
ATP-dependent 6-phosphofructokinase; |
180-460 |
1.60e-69 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235111 [Multi-domain] Cd Length: 320 Bit Score: 226.50 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRT----LPKGQL 255
Cdd:PRK03202 4 IGVLTSGGDAPGMNAAIRAVVRTAISEGLEVYGIYDGYAGLLEGDIVKLDLKSVSDIINRGGTILGSARFpefkDEEGRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 256 EsIVENIRIYGIHALLVVGGFEAYEGVLQLVEARgryeelciVMCV-IPATISNNVPGTDFSLGSDTAVNAAMESCDRIK 334
Cdd:PRK03202 84 K-AIENLKKLGIDALVVIGGDGSYMGAKRLTEHG--------IPVIgLPGTIDNDIAGTDYTIGFDTALNTAVEAIDRLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 335 QSASgTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLkvnVEHMTEKMKTDIQRGLVLRNEKCHD--YY 412
Cdd:PRK03202 155 DTAS-SHERVFIVEVMGRHAGDLALHAGIAGGAEVILIPEVPFDIEEL---CAKIKKGRERGKKHAIIVVAEGVMPaeEL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 768020939 413 TTEFlynlyssEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKA 460
Cdd:PRK03202 231 AKEI-------EERTGLETRVTVLGHIQRGGSPTAFDRVLASRMGAHA 271
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
3-551 |
0e+00 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 979.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 3 WLLEPSPVEPRGRAEMEPNRRGwpKTRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGT 82
Cdd:cd00764 215 WIFIPERPPEDGWEDQMCRRLS--EHRSRGKRLNIIIVAEGAIDDQLKPITSEDVKDLVVERLGLDTRVTTLGHVQRGGT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 83 PSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNI 162
Cdd:cd00764 293 PSAFDRILASLMGVEAVMALLEATPDTPACVVSLNGNKAVRLPLMECVQLTKDVQKAMDEKRFDEAAALRGKSFDKNWNL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 163 YKLLAHQKPPK--EKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRG 240
Cdd:cd00764 373 YKLLAIELPQPlpEKTNLNIAIVNVGAPAAGMNAAVRSAVRYGLAHGHRPYAIYDGFEGLAKGQIVELGWIDVGGWTGRG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 241 GSMLGTKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSD 320
Cdd:cd00764 453 GSELGTKRTLPKKDLETIAYNFQKYGIDGLIIVGGFEAYKGLLQLREAREQYEEFCIPMVLIPATVSNNVPGTDFSLGSD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 321 TAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRG 400
Cdd:cd00764 533 TALNALMKYCDRIKQSASGTKRRVFIVETMGGYCGYLATMTGLAVGADAAYVFEEPFNIRDLQENVEHLTEKMKTTIGRG 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 401 LVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFAN 480
Cdd:cd00764 613 LVLRNEKCNENYTTVFTYELYSEEGKGVFDCRTNVLGHVQQGGAPSPFDRNFGTKFAVKAMKWIEQKLKENYAAGNEFAN 692
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768020939 481 APDSACVIGLKKKAVAFSPVTELKKDTdFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRT 551
Cdd:cd00764 693 DPDFNCVNGVKKYAVLFEPVEELKQTT-FEHRIPKEQWWLSLRPLLKILAKYKISADISDHGQLEHVTRGQ 762
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
19-533 |
0e+00 |
|
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 769.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 19 EPNRRGWP--------KTRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRIL 90
Cdd:TIGR02478 218 RPPEEGWEdqlchklkRNRKAGKRKTIVIVAEGAIDRDLNPITSEDVKDVLVERLGLDTRITVLGHVQRGGAPSAFDRIL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 91 SSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNIYKLLAHQK 170
Cdd:TIGR02478 298 ATRQGVEAVLAVLESTPETPSPVISLRGNKIVRKPLVEAVAQTKTVAKAIEEKDFDEAMRLRGREFAENLETFLFLSIPD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 171 PPK-----EKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLG 245
Cdd:TIGR02478 378 DDKklvpsEASRLRIAIIHVGAPAGGMNAATRSAVRYALARGHTVIAIHNGFSGLARHDVRELTWSDVEGWVGEGGSELG 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 246 TKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNA 325
Cdd:TIGR02478 458 TNRSLPGDDLGTIAYYFQQHKIDGLIIIGGFEAFEALYQLDAAREKYPAFRIPMVVIPATISNNVPGTEYSLGSDTALNE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 326 AMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRGLVLRN 405
Cdd:TIGR02478 538 ITEYCDNIKQSASASKRRVFVVETMGGYSGYLATMAGLATGADAAYIPEEGISLKDLQEDIEHLKETFAEGRAGKLILRN 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 406 EKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANaPDSA 485
Cdd:TIGR02478 618 EKASKVYTTDFIARIISEEGKGRFDARTAVLGHMQQGGSPSPFDRVRATRLAIRAVDFIEEKIKANKHADKLSAD-DTSA 696
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 768020939 486 CVIGLKKKAVAFSPV-TELKKDTDFEHRMPREQWWLSLRLMLKMLAQYR 533
Cdd:TIGR02478 697 VVIGIRGSNVLFTPVkQLLANETDFEHRRPKNQWWLQLRPLVRILAGRD 745
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
180-461 |
6.25e-127 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 372.44 E-value: 6.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLES-- 257
Cdd:pfam00365 2 IGILTSGGDAPGMNAAIRAVVRTAIYRGHEVYGIRNGYEGLVEGDIDELTWRDVSGILNRGGTILGTSRSKPFKTEEGre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 258 -IVENIRIYGIHALLVVGGFEAYEGVLQLVEARGryeelcIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQS 336
Cdd:pfam00365 82 kIAENLKKLGIDALVVIGGDGSLTGANKLSEERG------IPVVGIPKTIDNDIPGTDYTIGFDTALNTIVEAIDRIRDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 337 ASGTkRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTeKMKTDIqrgLVLRNEKCHDyytTEF 416
Cdd:pfam00365 156 ASSH-NRVFVVEVMGRHCGWLALMAGLAGGADAILIPEIPFDIEELCEKIKELR-KGKRFS---IIVVAEGASD---GEF 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 768020939 417 LYNLYssEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAM 461
Cdd:pfam00365 228 LAKLI--EEGTGIETRVTVLGHVQRGGTPSAFDRILATRLGVKAV 270
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
180-466 |
7.04e-71 |
|
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439975 [Multi-domain] Cd Length: 344 Bit Score: 230.73 E-value: 7.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPK---GQLE 256
Cdd:COG0205 4 IGILTSGGDAPGLNAAIRAVVRTAIKYGIEVYGIRDGYEGLLEGDIIDLTREDVSGILQRGGTILGSSRSKPFkteEGRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 257 SIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGryeelciVMCV-IPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQ 335
Cdd:COG0205 84 KALENLKKLGIDALVVIGGDGSLDGAAKLAEEYG-------IPVVgIPKTIDNDLPGTDYTIGFDTAVNTAAEAIDRLRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 336 SASGTkRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLkvnVEHMTEKMKTDIQRGLVL--------RNEK 407
Cdd:COG0205 157 TAASH-ERVFVVEVMGRHAGWLALAAGLAGGADLILIPEVPFDLDKL---LEKLKERRKRGKGYSIIVvaegagdeDGEA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768020939 408 CHDYYTTEFLYNLYSSEGKGV---------FDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSE 466
Cdd:COG0205 233 VLEADTDAFGHVRLGGIGEYLakeieertgIETRVTVLGHLQRGGSPSAFDRVLASRLGAAAVELLLE 300
|
|
| PRK03202 |
PRK03202 |
ATP-dependent 6-phosphofructokinase; |
180-460 |
1.60e-69 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235111 [Multi-domain] Cd Length: 320 Bit Score: 226.50 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRT----LPKGQL 255
Cdd:PRK03202 4 IGVLTSGGDAPGMNAAIRAVVRTAISEGLEVYGIYDGYAGLLEGDIVKLDLKSVSDIINRGGTILGSARFpefkDEEGRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 256 EsIVENIRIYGIHALLVVGGFEAYEGVLQLVEARgryeelciVMCV-IPATISNNVPGTDFSLGSDTAVNAAMESCDRIK 334
Cdd:PRK03202 84 K-AIENLKKLGIDALVVIGGDGSYMGAKRLTEHG--------IPVIgLPGTIDNDIAGTDYTIGFDTALNTAVEAIDRLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 335 QSASgTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLkvnVEHMTEKMKTDIQRGLVLRNEKCHD--YY 412
Cdd:PRK03202 155 DTAS-SHERVFIVEVMGRHAGDLALHAGIAGGAEVILIPEVPFDIEEL---CAKIKKGRERGKKHAIIVVAEGVMPaeEL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 768020939 413 TTEFlynlyssEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKA 460
Cdd:PRK03202 231 AKEI-------EERTGLETRVTVLGHIQRGGSPTAFDRVLASRMGAHA 271
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
179-503 |
1.33e-63 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
Pssm-ID: 238216 [Multi-domain] Cd Length: 338 Bit Score: 211.77 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 179 SLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRT----LPKGQ 254
Cdd:cd00363 2 KIGVLTSGGDAPGMNAAIRGVVRSAIAEGLEVYGIYEGYAGLVEGDIKELDWESVSDIINRGGTIIGSARCkefrTEEGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 255 LESIvENIRIYGIHALLVVGGFEAYEGVLQLVE-ARGRYEELCIVMCviPATISNNVPGTDFSLGSDTAVNAAMESCDRI 333
Cdd:cd00363 82 AKAA-ENLKKHGIDALVVIGGDGSYTGADLLTEeWPSKYQGFNVIGL--PGTIDNDIKGTDYTIGFDTALKTIVEAIDRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 334 KQSASgTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNihdlKVNVEHMTEKMKTDIQRG----LVLRNEKch 409
Cdd:cd00363 159 RDTAS-SHQRTFVVEVMGRHCGDIALEAGLATGADIIFIPEEPAA----DEWEEEMVDVIKKRRERGkrhgIVIVAEG-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 410 dyyTTEFLYNLYSSEG-------KGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVyrkgrvfanap 482
Cdd:cd00363 232 ---AIDFIPKPITEKLlaklveeRLGFDTRATVLGHVQRGGTPTAFDRILASRLGAEAVELLLEGTGGT----------- 297
|
330 340
....*....|....*....|.
gi 768020939 483 dSACVIGLKKKAVAFSPVTEL 503
Cdd:cd00363 298 -PVGIQNLNENQVVRHPLTEA 317
|
|
| Bacterial_PFK |
cd00763 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
180-460 |
4.80e-61 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include bacterial ATP-dependent phosphofructokinases. These are allosrterically regulated homotetramers; the subunits are of about 320 amino acids.
Pssm-ID: 238388 [Multi-domain] Cd Length: 317 Bit Score: 204.18 E-value: 4.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKR----TLPKGQL 255
Cdd:cd00763 3 IGVLTSGGDAPGMNAAIRGVVRSAIAEGLEVYGIRDGYAGLIAGDIVPLDRYSVSDIINRGGTFLGSARfpefKDEEGQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 256 ESIvENIRIYGIHALLVVGGFEAYEGVLQLVEARgryeelciVMCV-IPATISNNVPGTDFSLGSDTAVNAAMESCDRIK 334
Cdd:cd00763 83 KAI-EQLKKHGIDALVVIGGDGSYMGAMRLTEHG--------FPCVgLPGTIDNDIPGTDYTIGFDTALNTVVEAIDRIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 335 QSASgTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKtdiQRGLVLRNEkcHDYYTT 414
Cdd:cd00763 154 DTSS-SHQRISVVEVMGRHCGDIALAAGIAGGAEFIVIPEAEFDREEVANRIKAGIERGK---KHAIVVVAE--GVYDVD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 768020939 415 EFLYNLyssEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKA 460
Cdd:cd00763 228 ELAKEI---EEATGFETRATVLGHIQRGGSPTAFDRILASRMGAYA 270
|
|
| PFK |
cd00363 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
27-161 |
8.82e-54 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to PFK family that includes ATP- and pyrophosphate (PPi)- dependent phosphofructokinases. Some members evolved by gene duplication and thus have a large C-terminal/N-terminal extension comprising a second PFK domain. Generally, ATP-PFKs are allosteric homotetramers, and PPi-PFKs are dimeric and nonallosteric except for plant PPi-PFKs which are allosteric heterotetramers.
Pssm-ID: 238216 [Multi-domain] Cd Length: 338 Bit Score: 185.58 E-value: 8.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 27 KTRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEAT 106
Cdd:cd00363 215 KRRERGKRHGIVIVAEGAIDFIPKPITEKLLAKLVEERLGFDTRATVLGHVQRGGTPTAFDRILASRLGAEAVELLLEGT 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 768020939 107 PDTPACVVTLSGNQSVRLPLMECVQMTKEVQkamddkrfdeaTQLRGGSFENNWN 161
Cdd:cd00363 295 GGTPVGIQNLNENQVVRHPLTEAVNMTKRVG-----------VDLEGRPFKKFAK 338
|
|
| 6PF1K_euk |
TIGR02478 |
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ... |
180-513 |
3.16e-51 |
|
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).
Pssm-ID: 274152 [Multi-domain] Cd Length: 746 Bit Score: 187.55 E-value: 3.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 180 LAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQ--VQEVGWHDVAGWLGRGGSMLGTKRTLP----KG 253
Cdd:TIGR02478 3 IAVLTSGGDAQGMNAAVRAVVRMAIYVGCRVYAIREGYQGLVDGGdnIEEAQWEDVRGILSLGGTIIGTARCKEfrerPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 254 QLESiVENIRIYGIHALLVVGGFEAYEG-----------VLQLV-------EARGRYEELCIVMCVipATISNNVPGTDF 315
Cdd:TIGR02478 83 RLKA-ARNLVSNGIDALVVIGGDGSLTGadlfreewpslLEELVdtgkitaEQAEEHRHLTIVGLV--GSIDNDMCGTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 316 SLGSDTAVNAAMESCDRIKQSASGTKrRVFIVETMGGYCGYLATVTGIAVGADaaYVF--EDPfnihdLKVN-VEHMTEK 392
Cdd:TIGR02478 160 TIGADSALHRICEAIDAISSTAQSHQ-RAFVVEVMGRHCGYLALMAAIATGAD--YVFipERP-----PEEGwEDQLCHK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 393 MKTDIQRG----LVLRNEKCHD----YYTTEFLYNLYSSEGKgvFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWL 464
Cdd:TIGR02478 232 LKRNRKAGkrktIVIVAEGAIDrdlnPITSEDVKDVLVERLG--LDTRITVLGHVQRGGAPSAFDRILATRQGVEAVLAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 768020939 465 SEKLREvyrkgrvfanAPdsACVIGLKK---------KAVAFS-PVTELKKDTDFEHRM 513
Cdd:TIGR02478 310 LESTPE----------TP--SPVISLRGnkivrkplvEAVAQTkTVAKAIEEKDFDEAM 356
|
|
| Eukaryotic_PFK |
cd00764 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
179-523 |
2.83e-46 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include eukaryotic ATP-dependent phosphofructokinases. These have evolved from the bacterial PFKs by gene duplication and fusion events and exhibit complex allosteric behavior.
Pssm-ID: 238389 [Multi-domain] Cd Length: 762 Bit Score: 173.47 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 179 SLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKG--QVQEVGWHDVAGWLGRGGSMLGTKR----TLPK 252
Cdd:cd00764 5 AIAVLTSGGDAQGMNAAVRAVVRMGIYVGAKVFFVYEGYEGLVKGgdYIKQAEWESVSNWLQEGGTIIGSARckefRERE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 253 GQLESIVeNIRIYGIHALLVVGGFEAYEG-----------VLQLV-------EARGRYEELCIVMCVipATISNNVPGTD 314
Cdd:cd00764 85 GRLQAAY-NLIQRGITNLCVIGGDGSLTGadlfrsewpslLEELVkdgkiteEEVAKYQHLNIVGMV--GSIDNDFCGTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 315 FSLGSDTAVNAAMESCDRIKQSASgTKRRVFIVETMGGYCGYLATVTGIAVGADaaYVF------EDPFNIHDLKVNVEH 388
Cdd:cd00764 162 MTIGTDSALHRICEVVDAITTTAQ-SHQRTFVLEVMGRHCGYLALVSGLATGAD--WIFiperppEDGWEDQMCRRLSEH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 389 MTEKMKTDI---QRGLVLRNEKChdyYTTEFLYNLYSSEGKgvFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLS 465
Cdd:cd00764 239 RSRGKRLNIiivAEGAIDDQLKP---ITSEDVKDLVVERLG--LDTRVTTLGHVQRGGTPSAFDRILASLMGVEAVMALL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768020939 466 EklrevyrkgrvfaNAPDS-ACVIGLKKKAVAFSPVTE---LKKDTDFEHRMPREQWWLSLR 523
Cdd:cd00764 314 E-------------ATPDTpACVVSLNGNKAVRLPLMEcvqLTKDVQKAMDEKRFDEAAALR 362
|
|
| PRK14071 |
PRK14071 |
ATP-dependent 6-phosphofructokinase; |
182-460 |
4.00e-32 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 184487 [Multi-domain] Cd Length: 360 Bit Score: 127.11 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 182 ILNVGAPAAGMNAAVRSAVRTGISH-GHTVYVVHDGFEGLAKG--QVQEVGWHDVAGWLGRGGSMLGTKRT-------LP 251
Cdd:PRK14071 9 ILTSGGDCAGLNAVIRAVVHRARGTyGWEVIGIRDATQGLMARppQYIELDLDQVDDLLRMGGTILGTTNKgdpfafpMP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 252 KGQL----ESIVENIRIYGIHALLVVGGfeayEGVLQLVEargryeELC----IVMCVIPATISNNVPGTDFSLGSDTAV 323
Cdd:PRK14071 89 DGSLrdrsQEIIDGYHSLGLDALIGIGG----DGSLAILR------RLAqqggINLVGIPKTIDNDVGATEVSIGFDTAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 324 NAAMESCDRIKQSASgTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIhdlkvnvEHMTEKMKTDIQRG--- 400
Cdd:PRK14071 159 NIATEALDRLHFTAA-SHNRVMILEVMGRDAGHIALAAGIAGGADVILIPEIPYTL-------ENVCKKIRERQEEGknf 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768020939 401 -LVLRNEKCHDY------YTTEFLYNLYSSEGKGVFD---------CRTNVLGHLQQGGAPTPFDRNYGTKLGVKA 460
Cdd:PRK14071 231 cLVVVSEAVRTEegeqvtKTQALGEDRYGGIGQYLAEqiaertgaeTRVTVLGHIQRGGIPSPRDRLLASAFGVAA 306
|
|
| PfkA |
COG0205 |
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part ... |
27-136 |
1.18e-26 |
|
6-phosphofructokinase [Carbohydrate transport and metabolism]; 6-phosphofructokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439975 [Multi-domain] Cd Length: 344 Bit Score: 110.93 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 27 KTRSRGSRLNIIIIAEGAIDRNGKPISSS---------------YVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILS 91
Cdd:COG0205 208 ERRKRGKGYSIIVVAEGAGDEDGEAVLEAdtdafghvrlggigeYLAKEIEERTGIETRVTVLGHLQRGGSPSAFDRVLA 287
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 768020939 92 SKMGMEAVMALLEatpDTPACVVTLSGNQSVRLPLMECVQMTKEV 136
Cdd:COG0205 288 SRLGAAAVELLLE---GKTGVMVGIRRGEIVLVPLEEVANKEKPV 329
|
|
| PRK03202 |
PRK03202 |
ATP-dependent 6-phosphofructokinase; |
29-143 |
9.62e-25 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235111 [Multi-domain] Cd Length: 320 Bit Score: 104.78 E-value: 9.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 29 RSRGSRLNIIIIAEGAIDRNGkpisssyVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPD 108
Cdd:PRK03202 209 RERGKKHAIIVVAEGVMPAEE-------LAKEIEERTGLETRVTVLGHIQRGGSPTAFDRVLASRMGAHAVELLLEGKGG 281
|
90 100 110
....*....|....*....|....*....|....*.
gi 768020939 109 TpacVVTLSGNQSVRLPLMECV-QMTKEVQKAMDDK 143
Cdd:PRK03202 282 R---MVGIQNNKIVHVPIEEAVeNMKHPFDKDLYEL 314
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
27-99 |
1.60e-24 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 103.19 E-value: 1.60e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768020939 27 KTRSRGSRLNIIIIAEGAIDrngkpisSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAV 99
Cdd:pfam00365 205 KELRKGKRFSIIVVAEGASD-------GEFLAKLIEEGTGIETRVTVLGHVQRGGTPSAFDRILATRLGVKAV 270
|
|
| PFKA_ATP |
TIGR02482 |
6-phosphofructokinase; 6-phosphofructokinase (EC 2.7.1.11) catalyzes the addition of phosphate ... |
27-128 |
5.06e-21 |
|
6-phosphofructokinase; 6-phosphofructokinase (EC 2.7.1.11) catalyzes the addition of phosphate from ATP to fructose 6-phosphate to give fructose 1,6-bisphosphate. This represents a key control step in glycolysis. This model hits bacterial ATP-dependent 6-phosphofructokinases which lack a beta-hairpin loop present in TIGR02483 family members. TIGR02483 contains members that are ATP-dependent as well as members that are pyrophosphate-dependent. TIGR02477 represents the pyrophosphate-dependent phosphofructokinase, diphosphate--fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213713 [Multi-domain] Cd Length: 301 Bit Score: 93.57 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 27 KTRSRGSRLNIIIIAEGAIDRNGKPISSSyVKDlvvqRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEat 106
Cdd:TIGR02482 206 EQHEAGKKHSIIIVAEGNIVGSAKEVAKK-IEE----KTGIETRVTVLGHTQRGGSPSAFDRVLASRLGAKAVELLLE-- 278
|
90 100
....*....|....*....|..
gi 768020939 107 pDTPACVVTLSGNQSVRLPLME 128
Cdd:TIGR02482 279 -GKGGVMIGIQNNKIVTHPIEE 299
|
|
| PTZ00286 |
PTZ00286 |
6-phospho-1-fructokinase; Provisional |
172-379 |
2.15e-18 |
|
6-phospho-1-fructokinase; Provisional
Pssm-ID: 185539 Cd Length: 459 Bit Score: 87.79 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 172 PKEKSNFS-----LAILNVGAPAAGMNAAVRSAVRTGIS--HGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSML 244
Cdd:PTZ00286 77 PRKHLYFNpkevkAGIVTCGGLCPGLNVVIRELVMNLINnyGVKTIYGAKYGYKGLYKEDWIKLDPKDVKTIHRLGGTIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 245 GTKRTlpkGQ-LESIVENIRIYGIHALLVVGGFEAYEGVLQL-VEARGRYEELCIvmCVIPATISNNVPGTDFSLGSDTA 322
Cdd:PTZ00286 157 GSSRG---GFdPKVMVDTLIRHGINILFTLGGDGTHRGALAIyKELRRRKLNISV--VGIPKTIDNDIPIIDESFGFQTA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768020939 323 VNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVG-ADAAYVFEDPFNI 379
Cdd:PTZ00286 232 VEEAQNAIRAAYVEAKSAKNGVGIVKLMGRDSGFIALHASVASAdVNVCLIPEFDIPL 289
|
|
| Bacterial_PFK |
cd00763 |
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of ... |
31-140 |
5.30e-18 |
|
Phosphofructokinase, a key regulatory enzyme in glycolysis, catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate. The members belong to a subfamily of the PFKA family (cd00363) and include bacterial ATP-dependent phosphofructokinases. These are allosrterically regulated homotetramers; the subunits are of about 320 amino acids.
Pssm-ID: 238388 [Multi-domain] Cd Length: 317 Bit Score: 85.15 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 31 RGSRLNIIIIAEGAIDRNGkpisssyVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEAtpdTP 110
Cdd:cd00763 210 RGKKHAIVVVAEGVYDVDE-------LAKEIEEATGFETRATVLGHIQRGGSPTAFDRILASRMGAYAVELLLAG---KG 279
|
90 100 110
....*....|....*....|....*....|
gi 768020939 111 ACVVTLSGNQSVRLPLMECVQMTKEVQKAM 140
Cdd:cd00763 280 GLAVGIQNEQLVHHDIIDAIENMKPFKKDW 309
|
|
| PRK14071 |
PRK14071 |
ATP-dependent 6-phosphofructokinase; |
29-137 |
2.84e-14 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 184487 [Multi-domain] Cd Length: 360 Bit Score: 74.34 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 29 RSRGSRLNIIIIAEGAIDRNGKPIS-------------SSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMG 95
Cdd:PRK14071 224 QEEGKNFCLVVVSEAVRTEEGEQVTktqalgedryggiGQYLAEQIAERTGAETRVTVLGHIQRGGIPSPRDRLLASAFG 303
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 768020939 96 MEAVMALLEATPDTpacVVTLSGNQSVRLPLMECVQMTKEVQ 137
Cdd:PRK14071 304 VAAVDLIAQGKFDR---MVAWQNRQVVSVPIAEAIATYRAVD 342
|
|
| PLN02884 |
PLN02884 |
6-phosphofructokinase |
168-392 |
2.47e-12 |
|
6-phosphofructokinase
Pssm-ID: 178472 [Multi-domain] Cd Length: 411 Bit Score: 68.68 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 168 HQKPPKEKSNF-----SLAILNVGAPAAGMNAAVRSAVRT----------GISHGHTvyvvhdGF--EGLA-----KGQV 225
Cdd:PLN02884 39 HRAGPRKKIYFepeevKAAIVTCGGLCPGLNDVIRQIVFTleiygvknivGIPFGYR------GFfeKGLSemplsRKVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 226 QEVGWHdvagwlgrGGSMLGTKRTLPKgqLESIVENIRIYGIHALLVVGGFEAYEGVLQL-VEARGRYEELCIVmCViPA 304
Cdd:PLN02884 113 QNIHLS--------GGSLLGVSRGGAK--TSDIVDSIEARGINMLFVLGGNGTHAGANAIhNECRKRKMKVSVV-GV-PK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 305 TISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVG-ADAAYVFEDPFNIH--- 380
Cdd:PLN02884 181 TIDNDILLMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGIGLVKLMGRSSGFIAMHASLASGqVDICLIPEVPFTLDgpn 260
|
250
....*....|..
gi 768020939 381 DLKVNVEHMTEK 392
Cdd:PLN02884 261 GVLRHLEHLIET 272
|
|
| PRK06830 |
PRK06830 |
ATP-dependent 6-phosphofructokinase; |
191-380 |
6.30e-11 |
|
ATP-dependent 6-phosphofructokinase;
Pssm-ID: 235869 Cd Length: 443 Bit Score: 64.50 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 191 GMNAAVRSAVRTGishgHTVYVVHD------GFEGLakgqVQEVGwHD--------VAGWLGRGGSMLGTKRtlpkGQ-- 254
Cdd:PRK06830 94 GLNDVIRAIVLEL----HHHYGVRRilgiryGYQGL----IPRYG-HDpveltpevVADIHEFGGTILGSSR----GPqd 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 255 LESIVENIRIYGIHALLVVGGFEAYEGVLQLV-EARGRYEELCIVmcVIPATISNNVPGTDFSLGSDTAVNAAMESCDRI 333
Cdd:PRK06830 161 PEEIVDTLERMNINILFVIGGDGTLRGASAIAeEIERRGLKISVI--GIPKTIDNDINFIQKSFGFETAVEKATEAIRCA 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768020939 334 KQSASGTKRRVFIVETMGGYCGYLATVTGIAVgADAAYVF--EDPFNIH 380
Cdd:PRK06830 239 HVEANGAPNGIGLVKLMGRHSGFIAAYAALAS-KDVNFVLipEVPFDLE 286
|
|
| PLN02564 |
PLN02564 |
6-phosphofructokinase |
239-377 |
5.36e-10 |
|
6-phosphofructokinase
Pssm-ID: 178178 Cd Length: 484 Bit Score: 61.69 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 239 RGGSMLGTKRtlpKGQ-LESIVENIRIYGIHALLVVGGFEAYEG---VLQLVEARGryeeLCIVMCVIPATISNNVPGTD 314
Cdd:PLN02564 151 RGGTILGTSR---GGHdTSKIVDSIQDRGINQVYIIGGDGTQKGasvIYEEIRRRG----LKVAVAGIPKTIDNDIPVID 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768020939 315 FSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAV-GADAAYVFEDPF 377
Cdd:PLN02564 224 KSFGFDTAVEEAQRAINAAHVEAESVENGIGLVKLMGRYSGFIAMYATLASrDVDCCLIPESPF 287
|
|
| PRK14072 |
PRK14072 |
diphosphate--fructose-6-phosphate 1-phosphotransferase; |
186-444 |
2.39e-07 |
|
diphosphate--fructose-6-phosphate 1-phosphotransferase;
Pssm-ID: 237600 [Multi-domain] Cd Length: 416 Bit Score: 53.33 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 186 GAPAAGMNAAVRSAVRTGISHG--HTVYVVHDGFEGLAKGQV---QEVGWHDVAGWLGRGGSMLGTKRTLPKG------Q 254
Cdd:PRK14072 12 GGPTAVINASAAGVIEEARKHKkiGKVYGARNGIIGILDEDLidlSKESDEALAALAHTPSGALGSCRYKLKSleedraE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 255 LESIVENIRIYGIHALLVVGG---FEAYEGVLQLVEARGrYEELCIVmcvIPATISNNVPGTDFSLGSDTAVN----AAM 327
Cdd:PRK14072 92 YERLLEVFKAHDIGYFFYNGGndsMDTALKVSQLAKKMG-YPIRCIG---IPKTIDNDLPGTDHCPGFGSAAKyiatSVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020939 328 E-SCDrikQSASGTKRRVFIVETMGGYCGYLATVTGIA-----VGADAAYVFEDPFNIhdlkvnvehmtEKMKTDIQRgL 401
Cdd:PRK14072 168 EaALD---VAAMANTSKVFILEVMGRHAGWLAAAAALAkqnpdDAPHLIYLPERPFDE-----------EKFLADVRA-I 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 768020939 402 VLRNEKC--------HDyytteflynlysSEGKGVFD--CRTNVLGHLQQGGA 444
Cdd:PRK14072 233 VKRYGYCvvvvsegiRD------------ADGKFIAEagLAEDAFGHAQLGGV 273
|
|
|