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 03-AUG-2022, entry version 128.
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 iPTMnet; P47859; -.
DR PRIDE; P47859; -.
DR GeneID; 100009526; -.
DR KEGG; ocu:100009526; -.
DR CTD; 5214; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; P47859; -.
DR OrthoDB; 172878at2759; -.
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; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
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
