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B9E7A4 (PFKA_MACCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 43. 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:MCCL_1365
OrganismMacrococcus caseolyticus (strain JCSC5402) [Complete proteome] [HAMAP]
Taxonomic identifier458233 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesMacrococcus

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. 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 – 319319ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000192376

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Region125 – 1273Substrate binding By similarity
Region169 – 1713Substrate binding By similarity
Region185 – 1873Allosteric activator ADP binding By similarity
Region213 – 2153Allosteric activator ADP binding By similarity
Region249 – 2524Substrate binding By similarity

Sites

Active site1271Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1541Allosteric activator ADP By similarity
Binding site1621Substrate; shared with dimeric partner By similarity
Binding site2111Allosteric activator ADP By similarity
Binding site2221Substrate By similarity
Binding site2431Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
B9E7A4 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 93DC977086228635

FASTA31934,605
        10         20         30         40         50         60 
MKKIAVLTSG GDAPGMNAAV RAVVRKAMYY DIEVYGVYQG YQGLINNNIK KMERGTVGDK 

        70         80         90        100        110        120 
IQRGGTFLQS ARCPEFKDPE VRKQAIANLN NLGIEGLVVI GGDGSYRGAQ RLNEEGIKTI 

       130        140        150        160        170        180 
GIPGTIDNDI NGTDFTIGFD TALNTIVEAI DKIRDTASSH ERTFIVEVMG RDAGDLALWS 

       190        200        210        220        230        240 
GLAGGAETVL CPEHRKDVKV IADKIQQGIE RGKKHSIIVV AEGVMTGEEC GQELKKYINV 

       250        260        270        280        290        300 
DTRISVLGHM QRGGSPSGMD RVLASRLGGY AVELLMNDET GLAVGIQNNS LSKTKFEDIF 

       310 
TSVHHLDEKM YELSNELSI 

« Hide

References

[1]"Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC5402.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009484 Genomic DNA. Translation: BAH18072.1.
RefSeqYP_002560768.1. NC_011999.1.

3D structure databases

ProteinModelPortalB9E7A4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING458233.MCCL_1365.

Proteomic databases

PRIDEB9E7A4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH18072; BAH18072; MCCL_1365.
GeneID7389857.
KEGGmcl:MCCL_1365.
PATRIC22425115. VBIMacCas48391_1498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycMCAS458233:GI03-1378-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_MACCJ
AccessionPrimary (citable) accession number: B9E7A4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 43 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