Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2HYU2

- PFKAM_PIG

UniProt

Q2HYU2 - PFKAM_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 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

Magnesium.UniRule annotation

Enzyme regulationi

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

Pathwayi

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 sitei471 – 4711Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei566 – 5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei629 – 6291Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei735 – 7351Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: UniProtKB-UniPathway
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, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKM
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typePRO_0000289804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Glycosylationi530 – 5301O-linked (GlcNAc)By similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei775 – 7751PhosphoserineBy similarity

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ2HYU2.

Interactioni

Subunit structurei

Homo- and heterotetramers. Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).By similarityUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ2HYU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 390389N-terminal catalytic PFK domain 1Add
BLAST
Regioni164 – 1663Substrate bindingUniRule annotation
Regioni208 – 2103Substrate bindingUniRule annotation
Regioni298 – 3014Substrate bindingUniRule annotation
Regioni391 – 40111Interdomain linkerAdd
BLAST
Regioni402 – 780379C-terminal regulatory PFK domain 2Add
BLAST
Regioni528 – 5325Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni573 – 5753Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni661 – 6644Allosteric 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

HOVERGENiHBG000976.
InParanoidiQ2HYU2.
KOiK00850.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2HYU2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTHEEHHAAK SLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIYTGARVFF
60 70 80 90 100
VHEGYQGLVD GGDNIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWGDLLNDLQ KAGKITAEEA
160 170 180 190 200
NKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIIEIVD AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDAWE EHLCRRLSET
260 270 280 290 300
RTRGSRLNII IVAEGAIDKN GQLITSENIK DLVVKRLGYD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME
360 370 380 390 400
CVQVTKDVTK AMNEKRFDEA MKLRGRSFMN NWEVYKLLAH VRPPVTKSGS
410 420 430 440 450
YTVAVMNVGA PTAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE
460 470 480 490 500
AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE
510 520 530 540 550
AYTGGLELME GRKQYDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC
560 570 580 590 600
MTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
610 620 630 640 650
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG
660 670 680 690 700
IFDSRKNVLG HMQQGGSPTP LDRNFATKMG AKAMNWMSGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVTELKEQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSEHAHLEHI TRKRSGEATI
Length:780
Mass (Da):85,327
Last modified:March 7, 2006 - v1
Checksum:iC9E127CBFF6005B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ363336 mRNA. Translation: ABC94908.1.
RefSeqiNP_001038015.1. NM_001044550.1.
UniGeneiSsc.4741.

Genome annotation databases

GeneIDi733601.
KEGGissc:733601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ363336 mRNA. Translation: ABC94908.1 .
RefSeqi NP_001038015.1. NM_001044550.1.
UniGenei Ssc.4741.

3D structure databases

ProteinModelPortali Q2HYU2.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q2HYU2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 733601.
KEGGi ssc:733601.

Organism-specific databases

CTDi 5213.

Phylogenomic databases

HOVERGENi HBG000976.
InParanoidi Q2HYU2.
KOi K00850.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .

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

  1. "Cloning and characterization of porcine phosphofructokinase, muscle (PFKM)."
    Wang J., Deng C.Y., Xiong Y.Z.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPFKAM_PIG
AccessioniPrimary (citable) accession number: Q2HYU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 52 of the entry and version 1 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