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C5W020 (C5W020_STRSE) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339

Short name=ATP-PFK HAMAP-Rule MF_00339
Short name=Phosphofructokinase HAMAP-Rule MF_00339
EC=2.7.1.11 HAMAP-Rule MF_00339
Alternative name(s):
Phosphohexokinase HAMAP-Rule MF_00339
Gene names
Name:pfk EMBL CAR45106.1
Synonyms:pfkA HAMAP-Rule MF_00339
Ordered Locus Names:SSU0494 EMBL CAR45106.1
OrganismStreptococcus suis (strain P1/7) [Complete proteome] [HAMAP] EMBL CAR45106.1
Taxonomic identifier218494 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 SAAS SAAS022953

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339 SAAS SAAS012828

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339 SAAS SAAS022953.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding72 – 732ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP By similarity HAMAP-Rule MF_00339
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region125 – 1273Substrate binding By similarity HAMAP-Rule MF_00339
Region169 – 1713Substrate binding By similarity HAMAP-Rule MF_00339
Region185 – 1873Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region213 – 2153Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region250 – 2534Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1271Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1031Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site111ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1541Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1621Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2111Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2221Substrate By similarity HAMAP-Rule MF_00339
Binding site2441Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
C5W020 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: E17587F515A638AA

FASTA33635,491
        10         20         30         40         50         60 
MKRIAVLTSG GDAPGMNAAI RAVVRQAISE GMEVYGINEG YAGMVAGDIH ELSARSVGDI 

        70         80         90        100        110        120 
ISRGGTFLCS ARYPEFAKLE GQLKGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAI 

       130        140        150        160        170        180 
GVPGTIDNDI VGTDFTIGFD TAVTTAMDAI DKIRDTSSSH RRTFVVEVMG RHAGDIALWA 

       190        200        210        220        230        240 
GIASGADVIV VPEEDFNIND VVDRIKAGYD KGKKHSIIVL AEGVMPAAQF AEELKAAGDT 

       250        260        270        280        290        300 
SDLRVTELGH IQRGGSPTAR DRVLASRMGA HAVKLLKEGR GGLAVGIRNE QMVENPILGT 

       310        320        330 
AEEGALFSLT TDGKIVVNNP HKADLELADL NRNLSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946016 Genomic DNA. Translation: CAR45106.1.
RefSeqYP_003026420.1. NC_012925.1.

3D structure databases

ProteinModelPortalC5W020.
SMRC5W020. Positions 1-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218494.SSU0494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR45106; CAR45106; SSU0494.
GeneID8151156.
KEGGssi:SSU0494.
PATRIC19785940. VBIStrSui84581_0479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSSUI218494:GJDS-550-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC5W020_STRSE
AccessionPrimary (citable) accession number: C5W020
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)