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F4CD21 (F4CD21_SPHS2) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:pfkA HAMAP-Rule MF_00339
Ordered Locus Names:Sph21_1062 EMBL ADZ77632.1
OrganismSphingobacterium sp. (strain 21) [Complete proteome] [HAMAP] EMBL ADZ77632.1
Taxonomic identifier743722 [NCBI]
Taxonomic lineageBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaeSphingobacterium

Protein attributes

Sequence length324 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 SAAS SAAS022953 HAMAP-Rule MF_00339.

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 binding75 – 762ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding105 – 1084ATP By similarity HAMAP-Rule MF_00339
Region24 – 285Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region129 – 1313Substrate binding By similarity HAMAP-Rule MF_00339
Region173 – 1753Substrate binding By similarity HAMAP-Rule MF_00339
Region189 – 1913Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region216 – 2183Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region255 – 2584Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1311Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1061Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site141ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1581Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1661Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2251Substrate By similarity HAMAP-Rule MF_00339
Binding site2491Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
F4CD21 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: E270CCCE1B5FD1D6

FASTA32434,525
        10         20         30         40         50         60 
MSTIKNIAVF TSGGDSPGMN AAIRAVVRTS LHYNLNVFGI QRGYDGMVNG DIFPMDAKSV 

        70         80         90        100        110        120 
ANIIQRGGTI LKTARSKEFR TVEGRQQAYE QIRKFQIDGL VAIGGDGTFT GAAKFIEEHD 

       130        140        150        160        170        180 
IPVMGLPGTI DNDLAGTDFT IGYDTAINTV ISAVDKIRDT AESHDRLFII EVMGRDSGLI 

       190        200        210        220        230        240 
ALRSGIGTGA EAILIPESAT NSKALLEKLA HGRKDKSSKI VLVAEGDEEG GAFAIAELVK 

       250        260        270        280        290        300 
KHFPNYDTRV SILGHIQRGG SPTCMDRVLA SRLGVAAVEA LLAGRKGEMA GVINGDIAFT 

       310        320 
PFNKAIKHID SLTPSLLKIV DILS 

« Hide

References

[1]"Complete sequence of Sphingobacterium sp. 21."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K., Allgaier M. expand/collapse author list , Thelen M.P., Hugenholtz P., Woyke T.
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002584 Genomic DNA. Translation: ADZ77632.1.
RefSeqYP_004316302.1. NC_015277.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ77632; ADZ77632; Sph21_1062.
GeneID10346804.
KEGGshg:Sph21_1062.
PATRIC47235888. VBISphSp165585_1138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.
OMAMELREGH.

Enzyme and pathway databases

BioCycSSP743722:GH04-1077-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 nameF4CD21_SPHS2
AccessionPrimary (citable) accession number: F4CD21
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)