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B8D1K5 (PFKA_HALOH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:Hore_03210
OrganismHalothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) [Complete proteome] [HAMAP]
Taxonomic identifier373903 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaHalanaerobialesHalanaerobiaceaeHalothermothrix

Protein attributes

Sequence length332 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

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000192374

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region186 – 1883Allosteric activator ADP binding By similarity
Region214 – 2163Allosteric activator ADP binding By similarity
Region262 – 2654Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2561Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
B8D1K5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 12B78E782FFC46BF

FASTA33235,770
        10         20         30         40         50         60 
MKKIGVLTSG GDAPGMNAAI RSVVRTGIYH GLDVVGIRRG YAGLIEGDFY LMDRGSVADI 

        70         80         90        100        110        120 
IQRGGTILLS ARCEEFKTEE GRQKALKKMK EEGIEGLVVI GGDGSFRGAE KVSKELGIPA 

       130        140        150        160        170        180 
IGIPGTIDND LACTDFTIGF DTAMNTIIDT INKIRDTATS HERTFVVETM GRRSGFLTLM 

       190        200        210        220        230        240 
AGLAGGAESI LIPEIDFDLD DVSQKLKKGY ERGKLHSIIL VAEGVGDDFS TNRDINHSKA 

       250        260        270        280        290        300 
FVIGKQIAEK TGLETRVIIL GHIQRGGSPT AMDRILASRM GSKAVELLLA SESNKMVGYV 

       310        320        330 
NNKLVTCDIS EALSKEKQVE KDVYKLANIL SM 

« Hide

References

[1]"Genome analysis of the anaerobic thermohalophilic bacterium Halothermothrix orenii."
Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H., Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.
PLoS ONE 4:E4192-E4192(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H 168 / OCM 544 / DSM 9562.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001098 Genomic DNA. Translation: ACL69082.1.
RefSeqYP_002508077.1. NC_011899.1.

3D structure databases

ProteinModelPortalB8D1K5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373903.Hore_03210.

Proteomic databases

PRIDEB8D1K5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL69082; ACL69082; Hore_03210.
GeneID7314707.
KEGGhor:Hore_03210.
PATRIC22099908. VBIHalOre56292_0341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAAKLERGH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycHORE373903:GHB1-344-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
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 namePFKA_HALOH
AccessionPrimary (citable) accession number: B8D1K5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: July 9, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways