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Q9HGZ0 (PFKA2_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. 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 2

Short name=ATP-PFK 2
Short name=Phosphofructokinase 2
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 2
Gene names
Name:pfkB
ORF Names:AO090010000444
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length775 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 – 775775ATP-dependent 6-phosphofructokinase 2 HAMAP-Rule MF_03184
PRO_0000112037

Regions

Nucleotide binding88 – 892ATP By similarity
Nucleotide binding118 – 1214ATP By similarity
Region1 – 390390N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region164 – 1663Substrate binding By similarity
Region208 – 2103Substrate binding By similarity
Region298 – 3014Substrate binding By similarity
Region391 – 40414Interdomain linker HAMAP-Rule MF_03184
Region405 – 775371C-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
Region672 – 6754Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding1191Magnesium; catalytic By similarity
Binding site251ATP; via amide nitrogen By similarity
Binding site2011Substrate; shared with dimeric partner By similarity
Binding site2641Substrate By similarity
Binding site2921Substrate; shared with dimeric partner By similarity
Binding site6401Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HGZ0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B5A78C4F7EE43848

FASTA77584,727
        10         20         30         40         50         60 
MTNTILDTYS SRRKPRRIGI LTSGGDAPGM NGAIRAVVRT AIQNGCEAWA IHEGYEGLIQ 

        70         80         90        100        110        120 
GGAMMHPLYW EDVRGFLSRG GTLIGSVRCD RFREREGRLQ AARNMVLFGI DALVVCGGDG 

       130        140        150        160        170        180 
SLTGADLFRS EWPELLNELV STGVLTVAQV APHQNLNIVG LLGSIDNDFS GTDATIGCYS 

       190        200        210        220        230        240 
ALTRICEAVD AVFDTASSHR RGFVVEVMGR HCGWLALMAA IATGADWLFI PERPPRDGWE 

       250        260        270        280        290        300 
DDMCSIITKN RNRGKRRTIV ILAEGAQDSN LDRISSSAVK DVLSKRLGLD TRVTVLGHIQ 

       310        320        330        340        350        360 
RGGSPCAYDR WLSTLQGIHA VKAVLSMTPE SPSPVVIIQE NRIRTSSLAE TVALTKEANA 

       370        380        390        400        410        420 
SMHAKEFEKA ATLRDPEFME YHSAYRHLNT SDHPKMVLPE DKRMRVAIIH VGAPAAGMNP 

       430        440        450        460        470        480 
ATRAVVAYCL TRGHTPIAIH NGFPGLCRHH DDTPGSVREM HWLESGDWIN DGGSDIGTNA 

       490        500        510        520        530        540 
GLPLDDIETT AQCFERYKFD ALFVIGGFEA FTAVSQLRKA RKQYLAFRIP LVLLPASMSN 

       550        560        570        580        590        600 
NVPGTEYSLG SDTSLNTLVY FCDVVRQSAS SSGHSVFVVE AQGAEYQATA AALAAGAMTV 

       610        620        630        640        650        660 
YTPERGITLQ SLSNDIEYLR QQFSKDHGAN RSGKLIIRND QTSTIYSTTE IANIIKHEAK 

       670        680        690        700        710        720 
NRFDAQGVVP GHFQQGGKVS PIDRIRAFRL AVKCMEHLET FAGQSPEEIM NDENSATVIS 

       730        740        750        760        770 
IKQSRILLLP MGGPTGVEAT DTDWKRQRPK TQNWLEIQEA VDSLSGRSSL YAIPN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032271 mRNA. Translation: BAB12231.1.
AP007175 Genomic DNA. Translation: BAE66301.1.
RefSeqXP_001827434.1. XM_001827382.2.

3D structure databases

ProteinModelPortalQ9HGZ0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00004509; CADAORAP00004429; CADAORAG00004509.
GeneID5999568.
KEGGaor:AOR_1_724024.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAKEANASM.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA2_ASPOR
AccessionPrimary (citable) accession number: Q9HGZ0
Secondary accession number(s): Q2TWS2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 83 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