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Conserved domains on  [gi|2499511|sp|Q12471|]
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RecName: Full=6-phosphofructo-2-kinase 2; Short=6PF-2-K 2; AltName: Full=Phosphofructokinase 2 II

Protein Classification

shikimate kinase( domain architecture ID 10482710)

shikimate kinase catalyzes the specific phosphorylation of the 3-hydroxylgroup of shikimic acid using ATP as a cosubstrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
84-324 8.83e-93

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


:

Pssm-ID: 396253  Cd Length: 223  Bit Score: 278.07  E-value: 8.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511     84 NADPTYTNGKVNKFMIVLIGLPATGKSTISSHLIQCLKnnplTNSLRCKVFNAGKIRRQISCAtiskpllLSNTSSEDLF 163
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLN----WLGVPTKVFNVGEYRRSAVKA-------YSNYEFFRPD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    164 NPKNNDKKETYARITLQKLFHEINNDECDVGIFDATNSTIERRRFIFEEVCsfntdelsSFNLVPIILQVSCFNRSFIKY 243
Cdd:pfam01591  70 NPEAMKIREQCALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAE--------ENGLKVFFLESICNDPEIIAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    244 NIHNKSFN-EDYLDKPYELAIKDFAKRLKHYYSQFTPFSlDEFNQIHRYISQHeEIDTSLFFFNVIN--AGVVEPHSLNQ 320
Cdd:pfam01591 142 NIKLVKFSsPDYKGKPPEEAIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMI-NVGQSIVVNNVQGylQSRIVYYLMNI 219

                  ....
gi 2499511    321 SHYP 324
Cdd:pfam01591 220 HVTP 223
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
84-324 8.83e-93

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 278.07  E-value: 8.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511     84 NADPTYTNGKVNKFMIVLIGLPATGKSTISSHLIQCLKnnplTNSLRCKVFNAGKIRRQISCAtiskpllLSNTSSEDLF 163
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLN----WLGVPTKVFNVGEYRRSAVKA-------YSNYEFFRPD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    164 NPKNNDKKETYARITLQKLFHEINNDECDVGIFDATNSTIERRRFIFEEVCsfntdelsSFNLVPIILQVSCFNRSFIKY 243
Cdd:pfam01591  70 NPEAMKIREQCALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAE--------ENGLKVFFLESICNDPEIIAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    244 NIHNKSFN-EDYLDKPYELAIKDFAKRLKHYYSQFTPFSlDEFNQIHRYISQHeEIDTSLFFFNVIN--AGVVEPHSLNQ 320
Cdd:pfam01591 142 NIKLVKFSsPDYKGKPPEEAIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMI-NVGQSIVVNNVQGylQSRIVYYLMNI 219

                  ....
gi 2499511    321 SHYP 324
Cdd:pfam01591 220 HVTP 223
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
84-324 8.83e-93

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 278.07  E-value: 8.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511     84 NADPTYTNGKVNKFMIVLIGLPATGKSTISSHLIQCLKnnplTNSLRCKVFNAGKIRRQISCAtiskpllLSNTSSEDLF 163
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLN----WLGVPTKVFNVGEYRRSAVKA-------YSNYEFFRPD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    164 NPKNNDKKETYARITLQKLFHEINNDECDVGIFDATNSTIERRRFIFEEVCsfntdelsSFNLVPIILQVSCFNRSFIKY 243
Cdd:pfam01591  70 NPEAMKIREQCALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAE--------ENGLKVFFLESICNDPEIIAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499511    244 NIHNKSFN-EDYLDKPYELAIKDFAKRLKHYYSQFTPFSlDEFNQIHRYISQHeEIDTSLFFFNVIN--AGVVEPHSLNQ 320
Cdd:pfam01591 142 NIKLVKFSsPDYKGKPPEEAIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMI-NVGQSIVVNNVQGylQSRIVYYLMNI 219

                  ....
gi 2499511    321 SHYP 324
Cdd:pfam01591 220 HVTP 223
 
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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