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P20275 (PFKA_SPICI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. 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
OrganismSpiroplasma citri
Taxonomic identifier2133 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesEntomoplasmatalesSpiroplasmataceaeSpiroplasma

Protein attributes

Sequence length327 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

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000111975

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP 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
Region251 – 2544Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site121ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2231Substrate By similarity
Binding site2451Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P20275 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 19D9D47E176FE2F6

FASTA32735,197
        10         20         30         40         50         60 
MLKKIGILTS GGDSQGMNAA IAGVIKTAHA KGLETYIIRD GYLGLINNWI EVVDNNFADS 

        70         80         90        100        110        120 
IMLLGGTVIG SARLPEFKDP EVQKKAVDIL KKQEIAALVV IGGDGSYQGA QRLTELGINC 

       130        140        150        160        170        180 
IALPGTIDND ITSSDYTIGF DTAINIVVEA IDRLRDTMQS HNRCSIVEVM GHACGDIALY 

       190        200        210        220        230        240 
AGIAGGADII SINEAALSET EIADRVAMLH QAQKRSVIVV VSEMIYPDVH KLAKLVESKS 

       250        260        270        280        290        300 
GYITRATVLG HTQRGGNPTA MDRYRAFQMA QFAVEQIIAG VGGLAIGNQG DQIIARPIME 

       310        320 
ALSIPRSSRK EIWAKFDQLN QNIYQKS 

« Hide

References

[1]"Organization and nucleotide sequences of the Spiroplasma citri genes for ribosomal protein S2, elongation factor Ts, spiralin, phosphofructokinase, pyruvate kinase, and an unidentified protein."
Chevalier C., Saillard C., Bove J.M.
J. Bacteriol. 172:2693-2703(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27556 / NCPPB 2647 / R8A2.
[2]"Gene organization and transcriptional analysis of the Spiroplasma citri rpsB/tsf/x operon."
Le Dantec L., Bove J.M., Saillard C.
Curr. Microbiol. 37:269-273(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27556 / NCPPB 2647 / R8A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012877 Genomic DNA. Translation: AAB69998.1.
PIRE35270.

3D structure databases

ProteinModelPortalP20275.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_SPICI
AccessionPrimary (citable) accession number: P20275
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 81 of the entry and version 2 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