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D3EA68 (D3EA68_GEOS4) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 31. 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:GYMC10_4612 EMBL ACX66833.1
OrganismGeobacillus sp. (strain Y412MC10) [Complete proteome] [HAMAP] EMBL ACX66833.1
Taxonomic identifier481743 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length323 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 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
Region128 – 1303Substrate binding By similarity HAMAP-Rule MF_00339
Region172 – 1743Substrate binding By similarity HAMAP-Rule MF_00339
Region188 – 1903Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region216 – 2183Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region253 – 2564Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1301Proton 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 site1571Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1651Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2141Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2251Substrate By similarity HAMAP-Rule MF_00339
Binding site2471Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
D3EA68 [UniParc].

Last modified March 23, 2010. Version 1.
Checksum: 61F6FC3987687F4B

FASTA32334,709
        10         20         30         40         50         60 
MAEVKKIAVL TSGGDSQGMN AALRAVVRSG LYYGLEVYGI QRGYQGLLEN DIIKMDLRSV 

        70         80         90        100        110        120 
GDIIQRGGTI LRSARCEEFK TAEGQQKGAD ILNQHGIDGL VVIGGDGSYQ GANKLSKLGI 

       130        140        150        160        170        180 
KTMGLPGTID NDISFTDYTI GFDTAVSVVV DAVNKLRDTM SSHARSSVVE VMGRHCGDIA 

       190        200        210        220        230        240 
LHAGLASGAE TILVPEVEYN LDEVATRLRE NFAKGKRHSI IIVAEGVGRG EDVVHDLKEC 

       250        260        270        280        290        300 
HASIDARVTV LGHIQRGGAP TPFDRNLASR LGDFAVRSLI DGQSDKGCGI IKGELVLTDI 

       310        320 
DKVVNTKKEF DRDLYDLALR LSQ 

« Hide

References

[1]"Complete sequence of Geobacillus sp. Y412MC10."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Brumm P., Mead D.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y412MC10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001793 Genomic DNA. Translation: ACX66833.1.
RefSeqYP_003244640.1. NC_013406.1.

3D structure databases

ProteinModelPortalD3EA68.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX66833; ACX66833; GYMC10_4612.
GeneID8518798.
KEGGgym:GYMC10_4612.
PATRIC32157725. VBIGeoSp56627_4572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAMELREGH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycPSP481743:GH8K-4661-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 nameD3EA68_GEOS4
AccessionPrimary (citable) accession number: D3EA68
Entry history
Integrated into UniProtKB/TrEMBL: March 23, 2010
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)