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Q5R7V5

- PFKAL_PONAB

UniProt

Q5R7V5 - PFKAL_PONAB

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Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

PFKL

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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. GlcNAcylation by OGT overcomes allosteric regulation (By similarity).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 sitei470 – 4701Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei565 – 5651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei628 – 6281Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei654 – 6541Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei734 – 7341Allosteric 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 1,6-bisphosphate metabolic process Source: UniProtKB
  3. fructose 6-phosphate metabolic process Source: InterPro
  4. glycolytic process Source: UniProtKB
  5. response to glucose Source: UniProtKB
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, liver typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-L
Alternative name(s):
6-phosphofructokinase type B
Phosphofructo-1-kinase isozyme B
Short name:
PFK-B
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKL
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: 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, liver typePRO_0000284441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Glycosylationi529 – 5291O-linked (GlcNAc)By similarity
Modified residuei640 – 6401PhosphotyrosineBy similarity
Modified residuei775 – 7751PhosphoserineBy similarity

Post-translational modificationi

GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ5R7V5.

Interactioni

Subunit structurei

Homo- and heterotetramers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5R7V5.
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 – 40010Interdomain linker
Regioni401 – 780380C-terminal regulatory PFK domain 2Add
BLAST
Regioni527 – 5315Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni572 – 5743Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni660 – 6634Allosteric 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.
InParanoidiQ5R7V5.
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.

Q5R7V5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL
60 70 80 90 100
IHEGYEGLVE GGENIKQANW LSVSNIIQLG GTVIGSARCK AFTTREGRRA
110 120 130 140 150
AAYNLVQHGI TNLCVIGGDG SLTGANIFRS EWGSLLEELV AEGKISETMA
160 170 180 190 200
RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR RCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET
260 270 280 290 300
RSRGSRLNII IIAEGAIDRD GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR VLSSKMAMEA VMALLEATHD TPACVVTLSG NQSVRLPLME
360 370 380 390 400
CVQMTKEVQK AMDDKRFDEA IQLRGGSFEN NWNIYKLLAH QKPPKEKSNF
410 420 430 440 450
SLAILNVGAP AAGMNAAVRS AVRTGISHGH TVYVVHDGFE GLAKGQVQEV
460 470 480 490 500
GWHDVAGWLG RGGSMLGTKR TLPKGQLESI VENIRIYGIH ALLVVGGFEA
510 520 530 540 550
YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME
560 570 580 590 600
SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
610 620 630 640 650
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV
660 670 680 690 700
FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL RDVYRKGRVF
710 720 730 740 750
ANAPDSACVI GLKKKAVAFS PVTELKKDTD FEHRMPREQW WLSLRLMLKM
760 770 780
LAQYRISMAA YVSGELEHVT RRTLSMDKGF
Length:780
Mass (Da):85,067
Last modified:December 21, 2004 - v1
Checksum:i38904F427763072E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860004 mRNA. Translation: CAH92155.1.
RefSeqiNP_001126263.1. NM_001132791.1.

Genome annotation databases

GeneIDi100173235.
KEGGipon:100173235.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860004 mRNA. Translation: CAH92155.1 .
RefSeqi NP_001126263.1. NM_001132791.1.

3D structure databases

ProteinModelPortali Q5R7V5.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R7V5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173235.
KEGGi pon:100173235.

Organism-specific databases

CTDi 5211.

Phylogenomic databases

HOVERGENi HBG000976.
InParanoidi Q5R7V5.
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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiPFKAL_PONAB
AccessioniPrimary (citable) accession number: Q5R7V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 61 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