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Database: UniProt/SWISS-PROT
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   10-APR-2019, entry version 116.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=8119919;
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
RT   phosphofructo-1-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
RT   by cyclic AMP-dependent protein kinase.";
RL   Biochim. Biophys. Acta 995:187-194(1989).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to 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
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       {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   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
DR   EMBL; U01154; AAA17707.1; -; mRNA.
DR   PIR; A53206; A53206.
DR   RefSeq; NP_001076217.1; NM_001082748.1.
DR   UniGene; Ocu.6209; -.
DR   ProteinModelPortal; 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   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P47859; -.
DR   KO; K00850; -.
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   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
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; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Glycoprotein;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN         1    791       ATP-dependent 6-phosphofructokinase,
FT                                platelet type.
FT                                /FTId=PRO_0000112026.
FT   NP_BIND      97     98       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     127    130       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    399       N-terminal catalytic PFK domain 1.
FT   REGION      173    175       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      217    219       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      307    310       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      400    411       Interdomain linker.
FT   REGION      412    791       C-terminal regulatory PFK domain 2.
FT   REGION      538    542       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      583    585       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      671    674       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      34     34       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     210    210       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     273    273       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     301    301       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     481    481       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     576    576       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     639    639       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     665    665       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     744    744       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES      12     12       Phosphoserine; by PKA.
FT                                {ECO:0000269|PubMed:2539199}.
FT   MOD_RES      21     21       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     142    142       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47860}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     395    395       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     486    486       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     651    651       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     688    688       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   CARBOHYD    540    540       O-linked (GlcNAc) serine. {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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