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Protein

ATP-dependent 6-phosphofructokinase 2

Gene

pfkB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathway: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgiA)
  3. ATP-dependent 6-phosphofructokinase 2 (pfkB), ATP-dependent 6-phosphofructokinase 1 (pfkA)
  4. Fructose-bisphosphate aldolase (fbaA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251ATP; via amide nitrogenUniRule annotation
Metal bindingi119 – 1191Magnesium; catalyticUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei201 – 2011Substrate; shared with dimeric partnerUniRule annotation
Binding sitei264 – 2641SubstrateUniRule annotation
Binding sitei292 – 2921Substrate; shared with dimeric partnerUniRule annotation
Binding sitei640 – 6401Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892ATPUniRule annotation
Nucleotide bindingi118 – 1214ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 2UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 2UniRule annotation
Short name:
Phosphofructokinase 2UniRule annotation
Alternative name(s):
Phosphohexokinase 2UniRule annotation
Gene namesi
Name:pfkB
ORF Names:AO090010000444
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 8

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775ATP-dependent 6-phosphofructokinase 2PRO_0000112037Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi5062.CADAORAP00004429.

Structurei

3D structure databases

ProteinModelPortaliQ9HGZ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 390390N-terminal catalytic PFK domain 1Add
BLAST
Regioni164 – 1663Substrate bindingUniRule annotation
Regioni208 – 2103Substrate bindingUniRule annotation
Regioni298 – 3014Substrate bindingUniRule annotation
Regioni391 – 40414Interdomain linkerAdd
BLAST
Regioni405 – 775371C-terminal regulatory PFK domain 2Add
BLAST
Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni672 – 6754Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
KOiK00850.
OMAiKEANASM.
OrthoDBiEOG7Q5HPV.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HGZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNTILDTYS SRRKPRRIGI LTSGGDAPGM NGAIRAVVRT AIQNGCEAWA
60 70 80 90 100
IHEGYEGLIQ GGAMMHPLYW EDVRGFLSRG GTLIGSVRCD RFREREGRLQ
110 120 130 140 150
AARNMVLFGI DALVVCGGDG SLTGADLFRS EWPELLNELV STGVLTVAQV
160 170 180 190 200
APHQNLNIVG LLGSIDNDFS GTDATIGCYS ALTRICEAVD AVFDTASSHR
210 220 230 240 250
RGFVVEVMGR HCGWLALMAA IATGADWLFI PERPPRDGWE DDMCSIITKN
260 270 280 290 300
RNRGKRRTIV ILAEGAQDSN LDRISSSAVK DVLSKRLGLD TRVTVLGHIQ
310 320 330 340 350
RGGSPCAYDR WLSTLQGIHA VKAVLSMTPE SPSPVVIIQE NRIRTSSLAE
360 370 380 390 400
TVALTKEANA SMHAKEFEKA ATLRDPEFME YHSAYRHLNT SDHPKMVLPE
410 420 430 440 450
DKRMRVAIIH VGAPAAGMNP ATRAVVAYCL TRGHTPIAIH NGFPGLCRHH
460 470 480 490 500
DDTPGSVREM HWLESGDWIN DGGSDIGTNA GLPLDDIETT AQCFERYKFD
510 520 530 540 550
ALFVIGGFEA FTAVSQLRKA RKQYLAFRIP LVLLPASMSN NVPGTEYSLG
560 570 580 590 600
SDTSLNTLVY FCDVVRQSAS SSGHSVFVVE AQGAEYQATA AALAAGAMTV
610 620 630 640 650
YTPERGITLQ SLSNDIEYLR QQFSKDHGAN RSGKLIIRND QTSTIYSTTE
660 670 680 690 700
IANIIKHEAK NRFDAQGVVP GHFQQGGKVS PIDRIRAFRL AVKCMEHLET
710 720 730 740 750
FAGQSPEEIM NDENSATVIS IKQSRILLLP MGGPTGVEAT DTDWKRQRPK
760 770
TQNWLEIQEA VDSLSGRSSL YAIPN
Length:775
Mass (Da):84,727
Last modified:March 1, 2001 - v1
Checksum:iB5A78C4F7EE43848
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032271 mRNA. Translation: BAB12231.1.
AP007175 Genomic DNA. Translation: BAE66301.1.
RefSeqiXP_001827434.1. XM_001827382.2.

Genome annotation databases

EnsemblFungiiCADAORAT00004509; CADAORAP00004429; CADAORAG00004509.
GeneIDi5999568.
KEGGiaor:AOR_1_724024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032271 mRNA. Translation: BAB12231.1.
AP007175 Genomic DNA. Translation: BAE66301.1.
RefSeqiXP_001827434.1. XM_001827382.2.

3D structure databases

ProteinModelPortaliQ9HGZ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00004429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00004509; CADAORAP00004429; CADAORAG00004509.
GeneIDi5999568.
KEGGiaor:AOR_1_724024.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
KOiK00850.
OMAiKEANASM.
OrthoDBiEOG7Q5HPV.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of glycolytic gene from Aspergillus oryzae."
    Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 42149 / RIB 40.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiPFKA2_ASPOR
AccessioniPrimary (citable) accession number: Q9HGZ0
Secondary accession number(s): Q2TWS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.