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Q0AVB9 (Q0AVB9_SYNWW) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 67. 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

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339

Short name=ATP-PFK 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:Swol_2041 EMBL ABI69335.1
OrganismSyntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) [Complete proteome] [HAMAP] EMBL ABI69335.1
Taxonomic identifier335541 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophomonas

Protein attributes

Sequence length318 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 SAAS SAAS022953

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 SAAS SAAS012828

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339 SAAS SAAS022953.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding72 – 732ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP By similarity HAMAP-Rule MF_00339
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region125 – 1273Substrate binding By similarity HAMAP-Rule MF_00339
Region168 – 1703Substrate binding By similarity HAMAP-Rule MF_00339
Region184 – 1863Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region212 – 2143Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region248 – 2514Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1271Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1031Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site111ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1531Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1611Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2101Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2211Substrate By similarity HAMAP-Rule MF_00339
Binding site2421Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
Q0AVB9 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: EE85DD34FFE37912

FASTA31834,255
        10         20         30         40         50         60 
MQKVGILTSG GDASGMNAAI RAVVRTALYH QMEAYGIHLG FEGLMAGNFD PMSRGSVADI 

        70         80         90        100        110        120 
IHRGGTILQT SRSQIFMTGN GREKARDELQ KRGIQNLVII GGNGSLRGGY ELGKLGINVI 

       130        140        150        160        170        180 
GIPATIDNDI VYTRSIGFDT AVNTALEAIN RIRDTATSHG RIFIIEVMGR HCGEIALAAG 

       190        200        210        220        230        240 
VAGGAESILI PEIETDLDEV TRKIKQGTQR GKLHSIIILA EGVYPVMELA QEIEKRTGKD 

       250        260        270        280        290        300 
TRVSILGHTQ RGGTPTAVDR IMASRMGMAA VDFIVEGKRN IMVAEEGDRI LPVPLQEVIR 

       310 
GTRTPELAMF EIARILSI 

« Hide

References

[1]"The genome of Syntrophomonas wolfei: new insights into syntrophic metabolism and biohydrogen production."
Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.
Environ. Microbiol. 12:2289-2301(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2245B / Goettingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000448 Genomic DNA. Translation: ABI69335.1.
RefSeqYP_754706.1. NC_008346.1.

3D structure databases

ProteinModelPortalQ0AVB9.
SMRQ0AVB9. Positions 1-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335541.Swol_2041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI69335; ABI69335; Swol_2041.
GeneID4283264.
KEGGswo:Swol_2041.
PATRIC23859158. VBISynWol51738_2214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSWOL335541:GHL1-2097-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
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 nameQ0AVB9_SYNWW
AccessionPrimary (citable) accession number: Q0AVB9
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)