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Database: UniProt
Entry: PFKAP_RABIT
LinkDB: PFKAP_RABIT
Original site: PFKAP_RABIT 
ID   PFKAP_RABIT             Reviewed;         791 AA.
AC   P47859;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-NOV-2023, entry version 132.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase, platelet type {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=PFK-P;
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=6-phosphofructokinase type C;
DE   AltName: Full=Phosphofructo-1-kinase isozyme C;
DE            Short=PFK-C;
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=PFKP;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=8119919; DOI=10.1016/s0021-9258(17)37530-0;
RA   Li Y., Valaitis A.P., Latshaw S.P., Kwiatkowska D., Tripathi R.L.,
RA   Campbell M.C., Kemp R.G.;
RT   "Structure and expression of the cDNA for the C isozyme of phosphofructo-1-
RT   kinase from rabbit brain.";
RL   J. Biol. Chem. 269:5781-5787(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 5-17, AND PHOSPHORYLATION AT SER-12.
RX   PubMed=2539199; DOI=10.1016/0167-4838(89)90079-4;
RA   Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.;
RT   "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by
RT   cyclic AMP-dependent protein kinase.";
RL   Biochim. Biophys. Acta 995:187-194(1989).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC       (PFK) enzyme functions as a tetramer composed of different combinations
CC       of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC       composition of the PFK tetramer differs according to the tissue type it
CC       is present in. The kinetic and regulatory properties of the tetrameric
CC       enzyme are dependent on the subunit composition, hence can vary across
CC       tissues (Probable). Interacts with ATG4B; promoting phosphorylation of
CC       ATG4B. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-386 promotes interaction with ATG4B.
CC       {ECO:0000250|UniProtKB:Q01813}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC       sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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DR   EMBL; U01154; AAA17707.1; -; mRNA.
DR   PIR; A53206; A53206.
DR   RefSeq; NP_001076217.1; NM_001082748.1.
DR   AlphaFoldDB; P47859; -.
DR   SMR; P47859; -.
DR   STRING; 9986.ENSOCUP00000026775; -.
DR   GlyCosmos; P47859; 1 site, No reported glycans.
DR   iPTMnet; P47859; -.
DR   PaxDb; 9986-ENSOCUP00000026775; -.
DR   GeneID; 100009526; -.
DR   KEGG; ocu:100009526; -.
DR   CTD; 5214; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   InParanoid; P47859; -.
DR   OrthoDB; 374214at2759; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00764; Eukaryotic_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR041914; PFK_vert-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF5; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, PLATELET TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Glycoprotein; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..791
FT                   /note="ATP-dependent 6-phosphofructokinase, platelet type"
FT                   /id="PRO_0000112026"
FT   REGION          1..399
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          400..411
FT                   /note="Interdomain linker"
FT   REGION          412..791
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         97..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         127..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         173..175
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         307..310
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         481
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         538..542
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         576
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         583..585
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         639
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         665
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         671..674
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         744
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         12
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:2539199"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47860"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         395
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         486
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         651
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   MOD_RES         688
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01813"
FT   CARBOHYD        540
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   791 AA;  86350 MW;  3C10A36F229FD8E8 CRC64;
     MDNKVSASPR GSYRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI
     YEGYQGMVDG GSNIVEANWE SVSSILQVGG TIIGSARSKA FRTREGRLKA ACNLIHRGIT
     NLCVIGGSGS LTGANIFRME WSGLLEELAQ DGKIDNEAVQ KYAYLNVVGM VGSIDNDFCG
     TDMTIGTDSA CHRIIEVIDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP
     ESPPEEGWEE QMCVKLSENR AQKKRLNIII VAEGAIDTLN RPITSEKIKE LVVTQLGYDT
     RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLSGN HAVRLPLVEC
     VQMTQEVQKA MDERRFKDAV QLRGRSFENN LNTYKRLAIK LPDDKIQKSN CNVAVINVGA
     PAAGMNAAVR SAVRVGIADG HKMFAVYDGF DGFAKGQIKE IRWGDVGGWT GQGGSILGTK
     RILPGKYLEE IATQIRTHNI NAILIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS
     NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
     DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGRG
     VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMQWITTK LKESPGKGKR FVSDDSICVL
     GISKRNVLFQ PVAELKNETD FEHRIPKEQW WLKLRPLMKI LAKYKTSYDV SDSGQLVPVR
     HRGGPEEPAA I
//
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