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E4TIZ2 (E4TIZ2_CALNY) 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
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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:Calni_1216 EMBL ADR19124.1
OrganismCalditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1) [Complete proteome] [HAMAP] EMBL ADR19124.1
Taxonomic identifier768670 [NCBI]
Taxonomic lineageBacteriaDeferribacteresDeferribacteralesDeferribacteraceae

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Molecule processing

Signal peptide1 – 2929 Potential EMBL ADR19124.1
Chain30 – 320291 Potential
PRO_5000662451

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
Region250 – 2534Substrate 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 site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2441Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E4TIZ2 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 12474B17187A3047

FASTA32034,104
        10         20         30         40         50         60 
MKRIAVMTSG GDCPGMNAAI RSVVRTAIAH NLEPFGIEQG YKGLIEGKII PMSNKSVANI 

        70         80         90        100        110        120 
IQRGGTILKS ARSMEFKTDE GQRKAVNNLA ELGIEGLIII GGDGSLTGAK ILSERYGIKT 

       130        140        150        160        170        180 
IGIPGSIDND LCCTDMSIGV DTALNTIVRA VDSINDTASS HDRTFLIEVM GRNCGYLALV 

       190        200        210        220        230        240 
SAIATGAEAV LIPEVQYDIE KIIAKIKKRY EEGKSRSIII IAEGVGSAMD FGKVFGMIGG 

       250        260        270        280        290        300 
FDTRVTVLGH LQRGGSPTVF DRILATRMGT AAVEALLDGV TASMTALQKT KIELVPFKDI 

       310        320 
IGLKKPLDHK LIEIAEVLSR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002347 Genomic DNA. Translation: ADR19124.1.
RefSeqYP_004051287.1. NC_014758.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADR19124; ADR19124; Calni_1216.
GeneID10009238.
KEGGcni:Calni_1216.
PATRIC45190187. VBICalNit163602_1297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAMELREGH.

Enzyme and pathway databases

BioCycCNIT768670:GHD1-1240-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 nameE4TIZ2_CALNY
AccessionPrimary (citable) accession number: E4TIZ2
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)