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Q8A624 (PFKA2_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. 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 2

Short name=ATP-PFK 2
Short name=Phosphofructokinase 2
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 2
Gene names
Name:pfkA2
Ordered Locus Names:BT_2062
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length326 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326ATP-dependent 6-phosphofructokinase 2 HAMAP-Rule MF_00339
PRO_0000111938

Regions

Nucleotide binding75 – 762ATP By similarity
Nucleotide binding105 – 1084ATP By similarity
Region24 – 285Allosteric activator ADP binding; shared with dimeric partner By similarity
Region129 – 1313Substrate binding By similarity
Region173 – 1753Substrate binding By similarity
Region189 – 1913Allosteric activator ADP binding By similarity
Region217 – 2193Allosteric activator ADP binding By similarity
Region256 – 2594Substrate binding By similarity

Sites

Active site1311Proton acceptor By similarity
Metal binding1061Magnesium; catalytic By similarity
Binding site141ATP; via amide nitrogen By similarity
Binding site1581Allosteric activator ADP By similarity
Binding site1661Substrate; shared with dimeric partner By similarity
Binding site2151Allosteric activator ADP By similarity
Binding site2261Substrate By similarity
Binding site2501Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A624 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: EEF46D4915E7A082

FASTA32635,257
        10         20         30         40         50         60 
MGTVKCIGIL TSGGDAPGMN AAIRAVTRAA IYNGLQVKGI YRGYKGLVTG EIKEFKSQNV 

        70         80         90        100        110        120 
SNIIQLGGTI LKTARCKEFT TPEGRQLAYD NMKREGIDAL VIIGGDGSLT GARIFAQEFD 

       130        140        150        160        170        180 
VPCIGLPGTI DNDLYGTDTT IGYDTALNTI LDAVDKIRDT ATSHERLFFV EVMGRDAGFL 

       190        200        210        220        230        240 
ALNGAIASGA EAAIIPEFST EVDQLEEFIK NGFRKSKNSS IVLVAESELT GGAMHYAERV 

       250        260        270        280        290        300 
KNEYPQYDVR VTILGHLQRG GSPTAHDRIL ASRLGAAAID AIMEDQRNVM IGIEHDEIVY 

       310        320 
VPFSKAIKND KPVKRDLVNV LKELSI 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO77169.1.
RefSeqNP_810975.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A624.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_2062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO77169; AAO77169; BT_2062.
GeneID1071883.
KEGGbth:BT_2062.
PATRIC21059066. VBIBacThe70966_2120.

Phylogenomic databases

eggNOGCOG0205.
KOK00850.
OMAGIYRGYK.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-2102-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 namePFKA2_BACTN
AccessionPrimary (citable) accession number: Q8A624
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: July 9, 2014
This is version 80 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