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Q03216

- PFKA2_KLULA

UniProt

Q03216 - PFKA2_KLULA

Protein

ATP-dependent 6-phosphofructokinase subunit beta

Gene

PFK2

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (27 Sep 2004)
      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.

    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 sitei185 – 1851ATP; via amide nitrogenUniRule annotation
    Metal bindingi280 – 2801Magnesium; catalyticUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Binding sitei362 – 3621Substrate; shared with subunit alphaUniRule annotation
    Binding sitei426 – 4261SubstrateUniRule annotation
    Binding sitei454 – 4541Substrate; shared with subunit alphaUniRule annotation
    Binding sitei637 – 6371Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei733 – 7331Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei826 – 8261Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei915 – 9151Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi249 – 2502ATPUniRule annotation
    Nucleotide bindingi279 – 2824ATPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. fructose 6-phosphate metabolic process Source: InterPro
    2. 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-RKQ03216.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase subunit betaUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFK 2UniRule annotation
    Short name:
    Phosphofructokinase 2UniRule annotation
    Alternative name(s):
    Phosphohexokinase 2UniRule annotation
    Gene namesi
    Name:PFK2
    Ordered Locus Names:KLLA0F06248g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome F

    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
    Chaini1 – 938938ATP-dependent 6-phosphofructokinase subunit betaPRO_0000112041Add
    BLAST

    Interactioni

    Subunit structurei

    Heterooctamer of 4 alpha and 4 beta chains.

    Protein-protein interaction databases

    STRINGi28985.Q03216.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03216.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 552552N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni325 – 3273Substrate bindingUniRule annotation
    Regioni369 – 3713Substrate bindingUniRule annotation
    Regioni460 – 4634Substrate bindingUniRule annotation
    Regioni553 – 56614Interdomain linkerAdd
    BLAST
    Regioni567 – 938372C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni695 – 6995Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni740 – 7423Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni832 – 8354Allosteric 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.
    KOiK00850.
    OMAiHKPYAIY.
    OrthoDBiEOG7Q5HPV.

    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.

    Q03216-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQSLPLLNG TEAYKLVTTQ GLYDKTVKFY EKYLQLVHDK RVGTLTNSLI    50
    TLKLVVDNSF KPLDVVNDKD WRAIVSSALV FSCTNIQHFR DLAAGETIQA 100
    YPNETNPIEI YLKDPNGYII GITETKNAIS IKPTLPKQSV EASLISSRSS 150
    RIDIASSGVS TDSSYPAIPK TAKAQKSIAV MTSGGDAPGM NANVRAIVRT 200
    AIFKGCNAFV VMEGYEGLVK GGPNYIKQVY WETVRNWSCE GGTNIGTARC 250
    KEFREREGRL LGALHLIEAG VDALIVCGGD GSLTGADLFR SEWPSLIREL 300
    LDQGRINKVQ FDRYQHLNIC GTVGSIDNDM STTDATIGAY SALDRICQAI 350
    DYIEATANSH SRAFVVEVMG RNCGWLALLA GISTSADYIL IPEKPASSRE 400
    WQDQMCDIIS KHRSRGKRTT IVIVAEGAIS ADLTPISSKD VHKVLVDRLG 450
    LDCRITTLGH VQRGGTAVAY DRILATLQGV EAVNAVLEST PDTPSPLIAI 500
    NENKITRKPL VESVQLTKSV AEAIHSKDFK KAMQLRDSEF VEHLDNFMAI 550
    NSADHIEPKL PEHTHMKIAI VNVGAPAGGM NSAVYSMATY CMSQGHKPYA 600
    IYNGWTGLTR HESVRSLNWK DLLGWQSRGG SEIGTNRHTP EEADIGLIAY 650
    YFQKYGFDGI IIVGGFEAFV SLHQLERARE NYTAFRIPMV LIPATLSNNV 700
    PGTEYSLGSD TALNSLMQYC DIIKQSAAST RGRVFVVDVQ GGNSGYLATH 750
    AAVAVGAQVS YVPEEGISLE QLTQDIENLT ESFSEAEGRG KFGQLILKST 800
    NASKVLTPEV LAEVITQEAE GHFDAKCAIP GHVQQGGLPS PIDRTRGTRF 850
    AIRAVGFIES QHKVLAAEAN LDDDDFDFDT PKIIATASVL GVKGSDIVFS 900
    SIRQLYDFET ELNKRTPKTI HWQSTRTIAD HLVGRKKL 938
    Length:938
    Mass (Da):102,477
    Last modified:September 27, 2004 - v2
    Checksum:iCE9C56DD7588C955
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti523 – 5231Missing in CAA78964. (PubMed:8326866)Curated
    Sequence conflicti554 – 5541D → H in CAA78964. (PubMed:8326866)Curated
    Sequence conflicti783 – 7842FS → LR in CAA78964. (PubMed:8326866)Curated
    Sequence conflicti927 – 93812TIADH…GRKKL → PLRTICRKEKTYEIKNVSAS SKFPLKWMYIIM in CAA78964. (PubMed:8326866)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17316 Genomic DNA. Translation: CAA78964.1.
    CR382126 Genomic DNA. Translation: CAG98071.1.
    PIRiS32903.
    RefSeqiXP_455363.1. XM_455363.1.

    Genome annotation databases

    GeneIDi2894998.
    KEGGikla:KLLA0F06248g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17316 Genomic DNA. Translation: CAA78964.1 .
    CR382126 Genomic DNA. Translation: CAG98071.1 .
    PIRi S32903.
    RefSeqi XP_455363.1. XM_455363.1.

    3D structure databases

    ProteinModelPortali Q03216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.Q03216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2894998.
    KEGGi kla:KLLA0F06248g.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    KOi K00850.
    OMAi HKPYAIY.
    OrthoDBi EOG7Q5HPV.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK Q03216.

    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. "Molecular genetics of phosphofructokinase in the yeast Kluyveromyces lactis."
      Heinisch J.J., Kirchrath L., Liesen T., Vogelsang K., Hollenberg C.P.
      Mol. Microbiol. 8:559-570(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiPFKA2_KLULA
    AccessioniPrimary (citable) accession number: Q03216
    Secondary accession number(s): Q6CL26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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