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P00511

- PFKAM_RABIT

UniProt

P00511 - PFKAM_RABIT

Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.

    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
    4. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose 6-phosphate metabolic process Source: InterPro
    3. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP00511.
    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typePRO_0000112019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Glycosylationi530 – 5301O-linked (GlcNAc)By similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Modified residuei775 – 7751Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    GlcNAcylation decreases enzyme activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP00511.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers.

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000014991.

    Structurei

    Secondary structure

    1
    780
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 134
    Beta strandi17 – 215
    Helixi30 – 4314
    Beta strandi47 – 493
    Helixi54 – 596
    Helixi62 – 643
    Helixi71 – 733
    Helixi91 – 933
    Helixi95 – 10814
    Beta strandi112 – 1176
    Helixi119 – 13012
    Helixi133 – 1386
    Turni139 – 1435
    Turni146 – 1483
    Helixi149 – 1513
    Beta strandi157 – 1637
    Helixi178 – 19316
    Beta strandi202 – 2076
    Helixi214 – 22310
    Helixi240 – 25213
    Beta strandi256 – 2605
    Beta strandi269 – 2713
    Helixi276 – 28611
    Beta strandi291 – 2944
    Helixi307 – 32519
    Beta strandi334 – 3396
    Beta strandi342 – 3476
    Helixi348 – 36316
    Helixi367 – 3748
    Helixi377 – 38913
    Beta strandi402 – 4109
    Helixi415 – 42814
    Beta strandi432 – 4387
    Helixi441 – 4455
    Beta strandi448 – 4503
    Turni453 – 4564
    Helixi475 – 4773
    Helixi478 – 48710
    Beta strandi493 – 4986
    Helixi499 – 51416
    Beta strandi522 – 5276
    Helixi542 – 55615
    Turni557 – 5604
    Beta strandi562 – 5643
    Beta strandi566 – 5727
    Helixi579 – 5879
    Beta strandi591 – 5944
    Beta strandi596 – 5983
    Helixi602 – 61615
    Beta strandi621 – 6288
    Beta strandi633 – 6353
    Helixi637 – 64711
    Turni648 – 6514
    Beta strandi653 – 6586
    Helixi670 – 69223
    Beta strandi697 – 7004
    Beta strandi708 – 7147
    Beta strandi717 – 7226
    Helixi723 – 7264
    Helixi727 – 7293
    Turni732 – 7354
    Beta strandi736 – 7394
    Helixi741 – 7444
    Helixi746 – 7516
    Turni752 – 7543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8LX-ray3.20A/B1-762[»]
    3O8NX-ray3.20A/B1-762[»]
    ProteinModelPortaliP00511.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00511.

    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

    eggNOGiCOG0205.
    HOGENOMiHOG000200154.
    HOVERGENiHBG000976.

    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.

    P00511-1 [UniParc]FASTAAdd to Basket

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    MTHEEHHAAR TLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF    50
    VHEGYQGLVD GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR 100
    AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITAEEA 150
    TRSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRITEIVD AITTTAQSHQ 200
    RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDNWE DHLCRRLSET 250
    RTRGSRLNII IVAEGAIDRN GKPITSEGVK DLVVRRLGYD TRVTVLGHVQ 300
    RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME 350
    CVQVTKDVTK AMDEKRFDEA MKLRGRSFMN NWEVYKLLAH IRPPAPKSGS 400
    YTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGPAKGQIEE 450
    AGWSYVGGWT GQGGSKLGSK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE 500
    AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC 550
    TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 600
    TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG 650
    IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMAGK IKESYRNGRI 700
    FANTPDSGCV LGMRKRALVF QPVTELQNQT DFEHRIPKEQ WWLKLRPILK 750
    ILAKYEIDLD TSEHAHLEHI SRKRSGEATV 780
    Length:780
    Mass (Da):85,203
    Last modified:January 23, 2007 - v3
    Checksum:iACDDF38C36F48EDB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691R → S AA sequence (PubMed:6233492)Curated
    Sequence conflicti480 – 50829Missing AA sequence (PubMed:6233492)CuratedAdd
    BLAST
    Sequence conflicti559 – 5591S → I AA sequence (PubMed:6233492)Curated
    Sequence conflicti566 – 5661Missing AA sequence (PubMed:6233492)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14477
    , M14456, M14457, M14458, M14459, M14460, M14461, M14462, M14463, M14464, M14465, M14466, M14467, M14468, M14469, M14470, M14471, M14472, M14473, M14474, M14475, M14476 Genomic DNA. Translation: AAA31441.1.
    PIRiA26550. KIRBF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14477
    , M14456 , M14457 , M14458 , M14459 , M14460 , M14461 , M14462 , M14463 , M14464 , M14465 , M14466 , M14467 , M14468 , M14469 , M14470 , M14471 , M14472 , M14473 , M14474 , M14475 , M14476 Genomic DNA. Translation: AAA31441.1 .
    PIRi A26550. KIRBF.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O8L X-ray 3.20 A/B 1-762 [» ]
    3O8N X-ray 3.20 A/B 1-762 [» ]
    ProteinModelPortali P00511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000014991.

    Chemistry

    ChEMBLi CHEMBL1075312.

    Proteomic databases

    PRIDEi P00511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK P00511.

    Miscellaneous databases

    EvolutionaryTracei P00511.

    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 rabbit muscle phosphofructokinase gene. Implications for protein structure, function, and tissue specificity."
      Lee C.P., Kao M.C., French B.A., Putney S.D., Chang S.H.
      J. Biol. Chem. 262:4195-4199(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Muscle.
    2. "Evolution of phosphofructokinase -- gene duplication and creation of new effector sites."
      Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.
      Nature 309:467-469(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-780, ACETYLATION AT THR-2.
    3. "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase."
      Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.
      Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 768-780, PHOSPHORYLATION AT SER-775.
    4. "The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
      Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
      J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959.

    Entry informationi

    Entry nameiPFKAM_RABIT
    AccessioniPrimary (citable) accession number: P00511
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3