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Q2HYU2

- PFKAM_PIG

UniProt

Q2HYU2 - PFKAM_PIG

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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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

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 sitei25 – 251ATP; via amide nitrogen By similarity
Metal bindingi119 – 1191Magnesium; catalytic By similarity
Active sitei166 – 1661Proton acceptor By similarity
Binding sitei201 – 2011Substrate; shared with dimeric partner By similarity
Binding sitei264 – 2641Substrate By similarity
Binding sitei292 – 2921Substrate; shared with dimeric partner By similarity
Binding sitei471 – 4711Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei566 – 5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei629 – 6291Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei735 – 7351Allosteric activator fructose 2,6-bisphosphate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892ATP By similarity
Nucleotide bindingi118 – 1214ATP By similarity

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 type (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
Phosphohexokinase
Gene namesi
Name:PFKM
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

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
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typeUniRule annotationPRO_0000289804Add
BLAST

Amino acid modifications

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

Post-translational modificationi

GlcNAcylation decreases enzyme activity By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ2HYU2.

Interactioni

Subunit structurei

Homo- and heterotetramers By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ2HYU2.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000976.
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

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MTHEEHHAAK SLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIYTGARVFF    50
VHEGYQGLVD GGDNIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR 100
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWGDLLNDLQ KAGKITAEEA 150
NKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIIEIVD AITTTAQSHQ 200
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDAWE EHLCRRLSET 250
RTRGSRLNII IVAEGAIDKN GQLITSENIK DLVVKRLGYD TRVTVLGHVQ 300
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME 350
CVQVTKDVTK AMNEKRFDEA MKLRGRSFMN NWEVYKLLAH VRPPVTKSGS 400
YTVAVMNVGA PTAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE 450
AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE 500
AYTGGLELME GRKQYDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC 550
MTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 600
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG 650
IFDSRKNVLG HMQQGGSPTP LDRNFATKMG AKAMNWMSGK IKESYRNGRI 700
FANTPDSGCV LGMRKRALVF QPVTELKEQT DFEHRIPKEQ WWLKLRPILK 750
ILAKYEIDLD TSEHAHLEHI TRKRSGEATI 780
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.
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: July 9, 2014
This is version 50 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

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