Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6LFS9 (A6LFS9_PARD8) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. Feed History...

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

Names and origin

Protein namesRecommended name:
6-phosphofructokinase 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
Ordered Locus Names:BDI_2830
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP] EMBL ABR44543.1
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Parabacteroides ›

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 SAAS SAAS012003

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase family. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding20 – 245ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding160 – 1645ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding177 – 19317ATP By similarity HAMAP-Rule MF_00339

Sites

Active site1331Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1911Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_00339
Metal binding1931Magnesium By similarity HAMAP-Rule MF_00339
Binding site1681Substrate By similarity HAMAP-Rule MF_00339
Binding site2551Substrate By similarity HAMAP-Rule MF_00339
Binding site2611Substrate By similarity HAMAP-Rule MF_00339
Binding site2641Substrate By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
A6LFS9 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 3BC7F98AD7D94DD5

FASTA33736,075
        10         20         30         40         50         60 
MKIGILSSGG DCPGINATIR GVGKTAIMHY GMEVIGIHSG FIGLLNKDVQ VFDERSLSGI 

        70         80         90        100        110        120 
LNLGGTILGT SREKPFRKLL ASGDSEKPEI IKKNYEELGL DCLVCIGGNG TQKTANLLSQ 

       130        140        150        160        170        180 
IGLNVIGVPK TIDNDIWGTD ITFGFNTAVN IATESIDRLH STASSHKRVM VVEVMGHHAG 

       190        200        210        220        230        240 
WIALYAGMAG GADVILLPEL GYDIDKVNEA ILDRARRGKP YSIVVVAEGI ETPDKKRPSD 

       250        260        270        280        290        300 
YITRAIEAGT GIETRDTVLG YTQRGGNPSP FDRNLATRLG GHATELIANG EFGRMVCIKG 

       310        320        330 
DRVESIPLLE VAGKLKLVTP DHDLIVQGKR MGVTFGK

« Hide

References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8503 / DSM 20701 / NCTC 11152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000140 Genomic DNA. Translation: ABR44543.1.
RefSeqYP_001304165.1. NC_009615.1.

3D structure databases

ProteinModelPortalA6LFS9.
ModBaseSearch...

Protein-protein interaction databases

STRING435591.BDI_2830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR44543; ABR44543; BDI_2830.
GeneID5307979.
KEGGpdi:BDI_2830.
PATRIC22848872. VBIParDis29947_2799.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMANGTQKTA.
ProtClustDBPRK03202.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. Ppfruckinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA6LFS9_PARD8
AccessionPrimary (citable) accession number: A6LFS9
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: July 24, 2007
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info