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Q9HGZ1 (PFKA1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase 1

Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 1
Gene names
Name:pfkA
ORF Names:AO090003001390
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 785785ATP-dependent 6-phosphofructokinase 1 HAMAP-Rule MF_03184
PRO_0000112036

Regions

Nucleotide binding86 – 872ATP By similarity
Nucleotide binding116 – 1194ATP By similarity
Region1 – 389389N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region162 – 1643Substrate binding By similarity
Region206 – 2083Substrate binding By similarity
Region297 – 3004Substrate binding By similarity
Region390 – 40314Interdomain linker HAMAP-Rule MF_03184
Region404 – 785382C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region537 – 5415Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region582 – 5843Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region674 – 6774Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1641Proton acceptor By similarity
Metal binding1171Magnesium; catalytic By similarity
Binding site231ATP; via amide nitrogen By similarity
Binding site1991Substrate; shared with dimeric partner By similarity
Binding site2631Substrate By similarity
Binding site2911Substrate; shared with dimeric partner By similarity
Binding site4801Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6421Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6681Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7491Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HGZ1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B6BD92CBFF928954

FASTA78585,970
        10         20         30         40         50         60 
MATTHAPAEP PKRRRIGVLT SGGDAPGMNG AVRAVVRMAI YSGCEAYAVY EGYEGLVHGG 

        70         80         90        100        110        120 
DMIRQVHWED VRGWLSRGGT LIGSARSMAF RERAGRLKAA KNMIVRGIDA LVVCGGDGSL 

       130        140        150        160        170        180 
TGADLFRSEW PGLLEELVKT GELTEEQIVP YKVLNIVGLV GSIDNDMSGT DATIGCYSSL 

       190        200        210        220        230        240 
TRICDAVDDV FDTAYSHQRG FVIEVMGRHC GWLALMSAIS TGADWLFIPE MPPREGWEDD 

       250        260        270        280        290        300 
MCDIITKNRQ ERGKRRTIVI VAEGAHDRQL NKITSSKIKD ILTNRLDLDT RVTVLGHTQR 

       310        320        330        340        350        360 
GGAACAYDRT LSTLQGVEAV RAVLDMTPES PSPVITVREN KLLRTPLMDA VKATKEVADL 

       370        380        390        400        410        420 
IHERKFDEAM HLRDSEFKEY HFAYKNTATP DHPKLILPEN KRMRIAIIHV GAPAGGMNQA 

       430        440        450        460        470        480 
TRAAVAYCQT RGHTALAVHN GFPGLCRHHA DTPVSSVREV SWEEQDTWVN EGGSDIGTNR 

       490        500        510        520        530        540 
SLPSEDFETT AKCFEKFKFD GLFVVGGFEA FTAVSQLRQA REKYPAFKIP MVVLPATISN 

       550        560        570        580        590        600 
NVPGTEYSLG SDTCLNTLID FCDAIRQSAS SSRRRVFVVE TQGGKSGYVA TTAGLAVGAS 

       610        620        630        640        650        660 
AVYIPEEGID IKMLARDIDF LRNNFAHDKG ANRAGKIILR NETASSTYTT QVIADMIKEE 

       670        680        690        700        710        720 
AKGRFESRAA VPGHFQQGGK PSPMDRIRAL RMAIRCMQHI ETFSGKSADE IAADELSATV 

       730        740        750        760        770        780 
IGVKGSQVLF SQMGGPNGLE ATETDWARRR PKDEFWLDLQ STVNILSGRA SFGEGKTGWS 


CYENC 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032270 mRNA. Translation: BAB12230.1.
AP007155 Genomic DNA. Translation: BAE58448.1.
RefSeqXP_001820450.2. XM_001820398.2.

3D structure databases

ProteinModelPortalQ9HGZ1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00001912; CADAORAP00001882; CADAORAG00001912.
GeneID5992433.
KEGGaor:AOR_1_2444154.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAVQHGITN.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA1_ASPOR
AccessionPrimary (citable) accession number: Q9HGZ1
Secondary accession number(s): Q2UJ17
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways