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C6Y444 (C6Y444_PEDHD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 40. 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:Phep_3293 EMBL ACU05487.1
OrganismPedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) [Complete proteome] [HAMAP] EMBL ACU05487.1
Taxonomic identifier485917 [NCBI]
Taxonomic lineageBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter

Protein attributes

Sequence length328 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 binding76 – 772ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding106 – 1094ATP By similarity HAMAP-Rule MF_00339
Region25 – 295Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region130 – 1323Substrate binding By similarity HAMAP-Rule MF_00339
Region174 – 1763Substrate binding By similarity HAMAP-Rule MF_00339
Region190 – 1923Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region218 – 2203Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region257 – 2604Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1321Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1071Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site151ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1591Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1671Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2271Substrate By similarity HAMAP-Rule MF_00339
Binding site2511Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
C6Y444 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 9227CB8DABFC3229

FASTA32835,364
        10         20         30         40         50         60 
MKPNIKNIAV LTSGGDAPGM NACIRAVVRT GIYNGINMFG VLQGYQGLIS NNINPMDARS 

        70         80         90        100        110        120 
VSNIIHLGGT ILKTARCLEF KTDEGMALAY ENMKARDIDG LVVIGGDGTF TGAKRFGEKF 

       130        140        150        160        170        180 
GIRVMGVPGT IDNDLYGSDF TLGYDTAINT VIEAIDKIRD TADSHDRLFF IEVMGRDSGC 

       190        200        210        220        230        240 
IALRSAISSG AEAVLLPEKE TSLNELISML ETGASTKKTS SIVIVSEGHK DGGAYEVAKK 

       250        260        270        280        290        300 
VKERFNHYDT KVTILGHLQR GGSPSSFDRI LGSRLGFAAV NELLKGNTME MVGLRGNEVK 

       310        320 
TTSIEEALTR HTFKLESDLL EMTKVLSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001681 Genomic DNA. Translation: ACU05487.1.
RefSeqYP_003093549.1. NC_013061.1.

3D structure databases

ProteinModelPortalC6Y444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING485917.Phep_3293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU05487; ACU05487; Phep_3293.
GeneID8254412.
KEGGphe:Phep_3293.
PATRIC22883743. VBIPedHep98714_3336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAISEGAFP.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycPHEP485917:GHL9-3329-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 nameC6Y444_PEDHD
AccessionPrimary (citable) accession number: C6Y444
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)