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I6SPL1 (I6SPL1_ENTCL) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 13. 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:pfkA HAMAP-Rule MF_00339
ORF Names:A3UG_22510 EMBL AFM62201.1
OrganismEnterobacter cloacae subsp. dissolvens SDM [Complete proteome] EMBL AFM62201.1
Taxonomic identifier1104326 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length320 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 binding73 – 742ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding103 – 1064ATP By similarity HAMAP-Rule MF_00339
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region55 – 606Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region126 – 1283Substrate binding By similarity HAMAP-Rule MF_00339
Region170 – 1723Substrate binding By similarity HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region250 – 2534Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1281Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1041Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site121ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1551Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2121Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2441Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
I6SPL1 [UniParc].

Last modified October 3, 2012. Version 1.
Checksum: FBB76628CFE6F10C

FASTA32034,887
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRAALT EGLEVFGIYD GYLGLYEDRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDE HVREVAIENM KKRGLDALVV IGGDGSYMGA KRLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IKGTDYTIGY FTALGTVVEA IDRLRDTSSS HQRISIVEVM GRYCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFV VVPEVEFSRE DLVAEIKAGI AKGKKHAIVA ITEHICDVDE LAKYIEAETK 

       250        260        270        280        290        300 
RETRATVLGH IQRGGSPGPY DRILASRMGA YAIELLLQGH GGRCVGIQNE KLVHHDIIDA 

       310        320 
IENMKRPFKG DWLDCAKKLY 

« Hide

References

[1]"Genome sequence of Enterobacter cloacae subsp. dissolvens SDM, an efficient biomass-utilizing producer of platform chemical 2,3-butanediol."
Xu Y., Wang A., Tao F., Su F., Tang H., Ma C., Xu P.
J. Bacteriol. 194:897-898(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDM EMBL AFM62201.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003678 Genomic DNA. Translation: AFM62201.1.
RefSeqYP_006479903.1. NC_018079.1.

3D structure databases

ProteinModelPortalI6SPL1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFM62201; AFM62201; A3UG_22510.
GeneID13166366.
KEGGenl:A3UG_22510.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

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 nameI6SPL1_ENTCL
AccessionPrimary (citable) accession number: I6SPL1
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)