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E6U0M2 (E6U0M2_BACCJ) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 22. 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:Bcell_3225 EMBL ADU31467.1
OrganismBacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) [Complete proteome] [HAMAP] EMBL ADU31467.1
Taxonomic identifier649639 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length319 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. SAAS SAAS022953 HAMAP-Rule MF_00339

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
Region249 – 2524Substrate 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 site2431Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E6U0M2 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: A5308D9387DB66E2

FASTA31934,353
        10         20         30         40         50         60 
MKRIGVLTSG GDSPGMNAAI RAVVRKAIFH NLEVYGIYYG YAGLISGDIK KLEIGSVGDI 

        70         80         90        100        110        120 
IHRGGTMLYT ARCEEFKTLE GQKKGIEQLK KFGIEALVVI GGDGSFQGAK KLTEHGFPTI 

       130        140        150        160        170        180 
GVPGTIDNDI PGTDFTIGFD TALNTVIDAV DKIRDTATSH ERTYVIEVMG RDAGDIALWA 

       190        200        210        220        230        240 
GLADGAESIL IPEDDFSMDD IIDRLEKGHK RGKKHSIIVV AEGCGSGVEI GKTIEERTKL 

       250        260        270        280        290        300 
DTRVTVLGHI QRGGSPTASD RVLASRLGAY AVELLLDGEA GKMVGIEKNQ LVSHDIDEAL 

       310 
SRKHTIDLNM YKLSKELSI 

« Hide

References

[1]"Complete sequence of Bacillus cellulosilyticus DSM 2522."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Brumm P., Mead D., Woyke T.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002394 Genomic DNA. Translation: ADU31467.1.
RefSeqYP_004096198.1. NC_014829.1.

3D structure databases

ProteinModelPortalE6U0M2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU31467; ADU31467; Bcell_3225.
GeneID10089805.
KEGGbco:Bcell_3225.
PATRIC45162508. VBIBacCel7049_3319.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.

Enzyme and pathway databases

BioCycBCEL649639:GHTT-3313-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 nameE6U0M2_BACCJ
AccessionPrimary (citable) accession number: E6U0M2
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: July 9, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)