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P47860

- PFKAP_RAT

UniProt

P47860 - PFKAP_RAT

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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene
Pfkp, Pfkc
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Magnesium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341ATP; via amide nitrogen By similarity
Metal bindingi128 – 1281Magnesium; catalytic By similarity
Active sitei175 – 1751Proton acceptor By similarity
Binding sitei210 – 2101Substrate; shared with dimeric partner By similarity
Binding sitei273 – 2731Substrate By similarity
Binding sitei301 – 3011Substrate; shared with dimeric partner By similarity
Binding sitei481 – 4811Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei576 – 5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei639 – 6391Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei744 – 7441Allosteric activator fructose 2,6-bisphosphate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 982ATP By similarity
Nucleotide bindingi127 – 1304ATP By similarity

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. ATP binding Source: RGD
  3. fructose-6-phosphate binding Source: RGD
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 1,6-bisphosphate metabolic process Source: RGD
  3. fructose 6-phosphate metabolic process Source: RGD
  4. glycolytic process Source: RGD
  5. protein homotetramerization Source: RGD
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

SABIO-RKP47860.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, platelet type (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
Phosphohexokinase
Gene namesi
Name:Pfkp
Synonyms:Pfkc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi61893. Pfkp.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 788788ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotationPRO_0000112027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei12 – 121Phosphoserine By similarity
Modified residuei386 – 3861Phosphoserine By similarity
Modified residuei395 – 3951N6-acetyllysine By similarity
Modified residuei486 – 4861N6-acetyllysine By similarity
Glycosylationi540 – 5401O-linked (GlcNAc) By similarity
Modified residuei651 – 6511Phosphotyrosine By similarity
Modified residuei688 – 6881N6-acetyllysine By similarity

Post-translational modificationi

GlcNAcylation decreases enzyme activity By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP47860.
PRIDEiP47860.

2D gel databases

World-2DPAGE0004:P47860.

PTM databases

PhosphoSiteiP47860.

Expressioni

Tissue specificityi

Expressed at high level in neuroendocrine tissues.

Gene expression databases

GenevestigatoriP47860.

Interactioni

Subunit structurei

Homo- and heterotetramers By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi248822. 2 interactions.
IntActiP47860. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP47860.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 399399N-terminal catalytic PFK domain 1UniRule annotationAdd
BLAST
Regioni173 – 1753Substrate binding By similarity
Regioni217 – 2193Substrate binding By similarity
Regioni307 – 3104Substrate binding By similarity
Regioni400 – 41112Interdomain linkerUniRule annotationAdd
BLAST
Regioni412 – 788377C-terminal regulatory PFK domain 2UniRule annotationAdd
BLAST
Regioni538 – 5425Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni583 – 5853Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni671 – 6744Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47860.
KOiK00850.
PhylomeDBiP47860.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47860-1 [UniParc]FASTAAdd to Basket

« Hide

MSDQDSSTSS TSFPKYLEHL SGDGKAIGVL TSGGDAQGMN AAVRAVVRMG    50
IYTGAKVYFI YEGYQGMVDG GSNIVEAKWE CVSSILQVGG TIIGSARCQA 100
FRSREGRLKA ACNLVRLGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAK 150
NGEIDSDTVK KHAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA 200
IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE 250
EMCLKLSENR ARKKRLNIII VSEGAIDTQN KPITSEKIKE LVVTNLGFDT 300
RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLRGN 350
QAVRLPLMEC VQMTQDVQKA MDERRFDEAV KLRGRSFEGN LNTYKRLAIK 400
EPDDKIPKSN CNVAIINVGA PAAGMNAAVR SAVRVGIAEG HKMFAIYDGF 450
DGLANGQIKE IGWGDVGGWT GQGGSILGTK RTLPGKYLEK IAEQMHSKNI 500
NALLIIGGFE AYLGLLELAA ARNKHEAFCV PMVMVPATVS NNVPGSDFSI 550
GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 600
DAAYIFEEQF DIRDLQSNVM HLTEKMKTSI QRGLVLRNEN CSVNYTTDFI 650
YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS AKAMEWISAK 700
LKGSHGTGKK FVSDDSICVL GIQKRDLLFK PVAELRKATD FEHRIPKQQW 750
WLKLRPIMKI LAKYEASYDM SDVGKLEPVH NHGELSAI 788
Length:788
Mass (Da):85,720
Last modified:December 20, 2005 - v2
Checksum:i16FEB963C3297CA6
GO

Sequence cautioni

The sequence AAA17757.1 differs from that shown. Reason: Frameshift at position 27.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 362DA → ES in AAA17757. 1 Publication
Sequence conflicti51 – 511I → M in AAA17757. 1 Publication
Sequence conflicti56 – 561K → Q in AAA17757. 1 Publication
Sequence conflicti111 – 1111A → T in AAA17757. 1 Publication
Sequence conflicti220 – 2201H → Y in AAA17757. 1 Publication
Sequence conflicti600 – 6001A → R in AAA17757. 1 Publication
Sequence conflicti755 – 7551R → L in AAA17757. 1 Publication
Sequence conflicti758 – 7581M → S in AAA17757. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC088847 mRNA. Translation: AAH88847.1.
L25387 mRNA. Translation: AAA17757.1. Frameshift.
PIRiA53047.
RefSeqiNP_996729.1. NM_206847.1.
UniGeneiRn.2278.

Genome annotation databases

GeneIDi60416.
KEGGirno:60416.
UCSCiRGD:61893. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC088847 mRNA. Translation: AAH88847.1 .
L25387 mRNA. Translation: AAA17757.1 . Frameshift.
PIRi A53047.
RefSeqi NP_996729.1. NM_206847.1.
UniGenei Rn.2278.

3D structure databases

ProteinModelPortali P47860.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248822. 2 interactions.
IntActi P47860. 2 interactions.

PTM databases

PhosphoSitei P47860.

2D gel databases

World-2DPAGE 0004:P47860.

Proteomic databases

PaxDbi P47860.
PRIDEi P47860.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 60416.
KEGGi rno:60416.
UCSCi RGD:61893. rat.

Organism-specific databases

CTDi 5214.
RGDi 61893. Pfkp.

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi P47860.
KOi K00850.
PhylomeDBi P47860.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P47860.

Miscellaneous databases

NextBioi 612122.

Gene expression databases

Genevestigatori P47860.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Structure, distribution, and functional expression of the phosphofructokinase C isozyme."
    Gekakis N., Johnson R.C., Jerkins A., Mains R.E., Sul H.S.
    J. Biol. Chem. 269:3348-3355(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-788.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiPFKAP_RAT
AccessioniPrimary (citable) accession number: P47860
Secondary accession number(s): Q5HZX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

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