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E1SXU2 (E1SXU2_THESX) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 24. 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:Thet_1716 EMBL ADN55297.1
OrganismThermoanaerobacter sp. (strain X513) [Complete proteome] [HAMAP] EMBL ADN55297.1
Taxonomic identifier573062 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length321 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
Region126 – 1283Substrate binding By similarity HAMAP-Rule MF_00339
Region170 – 1723Substrate binding By similarity HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region251 – 2544Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1281Proton 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 site1551Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2121Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2451Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E1SXU2 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 595F90D4BF423E29

FASTA32135,215
        10         20         30         40         50         60 
MKTIGILTSG GDAPGMNAAI RAVVRTGIYY GLKVKGIMRG YAGLVEDEVI DLNLSSVGDI 

        70         80         90        100        110        120 
LQKGGTILRT ARCEEFKKKE VRKKAYETLQ KHGIEGLVVI GGDGSFRGAQ LLSEEWNVNT 

       130        140        150        160        170        180 
IGIPGTIDND IPCTDYTIGF DTACNTVIDA INKIRDTATS HERANIIEVM GRNAGYIALY 

       190        200        210        220        230        240 
AGLAGGAEMI ILPEVEWSID ELCDKITYGI KRGKLHHIIV LAEGVMSAPE LAKMIKERLP 

       250        260        270        280        290        300 
KLDLRYTILG HIQRGGAPTV MDRVLASQMG ARAVELLLEN KTKRIISIRN NQIVDDDIDE 

       310        320 
ALSMKKEFNR KLYELSKILS I 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter sp. X513."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X513 EMBL ADN55297.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002210 Genomic DNA. Translation: ADN55297.1.
RefSeqYP_003904588.1. NC_014538.1.

3D structure databases

ProteinModelPortalE1SXU2.
SMRE1SXU2. Positions 1-321.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN55297; ADN55297; Thet_1716.
GeneID9761499.
KEGGthx:Thet_1716.
PATRIC42447641. VBITheSp37765_1783.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.

Enzyme and pathway databases

BioCycTSP573062:GHR1-1769-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 nameE1SXU2_THESX
AccessionPrimary (citable) accession number: E1SXU2
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)