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Conserved domains on  [gi|768020939|ref|XP_011527905|]
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ATP-dependent 6-phosphofructokinase, liver type isoform X7 [Homo sapiens]

Protein Classification

6-phosphofructokinase( domain architecture ID 807)

6-phosphofructokinase catalyzes the conversion of fructose-6-phosphate to fructose-1, 6-diphosphate and is a key regulatory enzyme of glycolysis

Gene Ontology:  GO:0003872|GO:0006002|GO:0046872

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PFK super family cl00204
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 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.


The actual alignment was detected with superfamily member cd00764:

Pssm-ID: 469655 [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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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