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Database: UniProt/SWISS-PROT
Entry: PFKA_DICDI
LinkDB: PFKA_DICDI
Original site: PFKA_DICDI 
ID   PFKA_DICDI              Reviewed;         834 AA.
AC   P90521; Q555B1; Q86HR6; Q95023;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   13-FEB-2019, entry version 118.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=pfkA; Synonyms=pfk; ORFNames=DDB_G0274111;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=9030771; DOI=10.1111/j.1432-1033.1997.0442a.x;
RA   Estevez A.M., Martinez-Costa O.H., Sanchez V., Aragon J.J.;
RT   "Cloning, sequencing and developmental expression of
RT   phosphofructokinase from Dictyostelium discoideum.";
RL   Eur. J. Biochem. 243:442-451(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   AND COFACTOR.
RX   PubMed=7813455; DOI=10.1111/j.1432-1033.1994.01007.x;
RA   Martinez-Costa O.H., Estevez A.M., Sanchez V., Aragon J.J.;
RT   "Purification and properties of phosphofructokinase from Dictyostelium
RT   discoideum.";
RL   Eur. J. Biochem. 226:1007-1017(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=22530721; DOI=10.1042/BJ20120173;
RA   Martinez-Costa O.H., Sanchez V., Lazaro A., Hernandez E.D.,
RA   Tornheim K., Aragon J.J.;
RT   "Distinct functional roles of the two terminal halves of eukaryotic
RT   phosphofructokinase.";
RL   Biochem. J. 445:213-218(2012).
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       ECO:0000269|PubMed:22530721, ECO:0000269|PubMed:7813455}.
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         ECO:0000269|PubMed:7813455};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184,
CC         ECO:0000269|PubMed:7813455};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for ATP {ECO:0000269|PubMed:7813455};
CC         KM=22 uM for fructose 6-phosphate {ECO:0000269|PubMed:7813455};
CC         Vmax=89 umol/min/mg enzyme {ECO:0000269|PubMed:7813455};
CC       pH dependence:
CC         Optimum pH is 7.6. {ECO:0000269|PubMed:7813455};
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: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000269|PubMed:7813455}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PTM: The N-terminus is blocked.
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; X89039; CAA61438.2; -; mRNA.
DR   EMBL; X94340; CAA64065.1; -; mRNA.
DR   EMBL; AAFI02000012; EAL69948.1; -; Genomic_DNA.
DR   RefSeq; XP_644162.1; XM_639070.1.
DR   ProteinModelPortal; P90521; -.
DR   SMR; P90521; -.
DR   STRING; 44689.DDB0191364; -.
DR   PaxDb; P90521; -.
DR   PRIDE; P90521; -.
DR   EnsemblProtists; EAL69948; EAL69948; DDB_G0274111.
DR   GeneID; 8619591; -.
DR   KEGG; ddi:DDB_G0274111; -.
DR   dictyBase; DDB_G0274111; pfkA.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   InParanoid; P90521; -.
DR   KO; K00850; -.
DR   OMA; KQYDELC; -.
DR   PhylomeDB; P90521; -.
DR   BRENDA; 2.7.1.11; 1939.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-70171; Glycolysis.
DR   SABIO-RK; P90521; -.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:P90521; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IDA:dictyBase.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:dictyBase.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IPI:dictyBase.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:dictyBase.
DR   GO; GO:0006007; P:glucose catabolic process; IGI:dictyBase.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:dictyBase.
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   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    834       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000112030.
FT   NP_BIND     123    124       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     153    156       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    426       N-terminal catalytic PFK domain 1.
FT   REGION      199    201       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      243    245       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      332    335       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      427    437       Interdomain linker.
FT   REGION      438    834       C-terminal regulatory PFK domain 2.
FT   REGION      566    570       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      610    612       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      698    701       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    201    201       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       154    154       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      62     62       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     236    236       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     299    299       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     326    326       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     507    507       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     603    603       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     666    666       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     692    692       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     764    764       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   CONFLICT    110    112       GII -> WLY (in Ref. 1; CAA61438/
FT                                CAA64065). {ECO:0000305}.
FT   CONFLICT    302    303       ID -> MH (in Ref. 1; CAA64065).
FT                                {ECO:0000305}.
SQ   SEQUENCE   834 AA;  92235 MW;  F9E4F2DF798FE78B CRC64;
     MTTTSKIIND GEGEDVKGNK NINKKSLIDE NRLDEKKDLL SDKVESKTHC SVKRMAVLTS
     GGDSSGMNPA IRAFARQVML KGAKVFAVRE GYNGLVNDSI VPLNWGSVAG IISRGGTIIG
     TARSAEFRTR EGRKRAVFNL VKNRIDNLLV IGGDGSLTGA NLLRTEWCSL LEELVKDGKL
     TLDVMEHFPI LSIAGIVGSI DNDMCGTDLT VGADTATKRI LEAIDSILST AVSHQRSFVI
     EVMGRNCGWL ALASGVATGA DYILIPESPP DDGWEQTMAD NLERGRLSGR RCSLVIVSEG
     AIDRQGKPIT SAYVRQFLED KGHDARITIL GHVQRGGTPT FLDRYIATRM GIEAANYFYD
     STIEQLKQPV LIGMSGMDTI RSPLMECVQK TQSIASLIKE RRFNEVVDVR GGMFKEFYEI
     FIACSNLHRR KVESKGMGVL ILHSGGPSPG MNPCVRAFTR LGIDHGYTMY GCFNGFGGLA
     LGEIEQLHWM TVNGWSVMGG AELGTNRSIP NDSNIEAIIA TLERFKINAI LMFGGFNGYL
     GIAKLYEYRE KYQQLKRISI IGAPGTIANN VPGTNISIGS DTSLNNTLDA LDKIKQSAVA
     SRRLFVVEVM GAHCGYLAAM SSLTSGAERS YIMERGITLN TLTKDLEMFV ERFKREHRIG
     LIIKSELASN TYSTHFIYSL FKEEGKHLFD VRESILGHLQ QGGTPSAIDR IFSTRLMNHY
     YQFLENDLKE HGHLQMNGCI GFIDGGIHYT PMQEMIEEMS DKFRRPRSQW WMDLVETSQN
     ISVFPLDDPS STNFEGCNSN LSEQDRPIKK SDISSPTSYS QKTFDPNVNP QFTL
//
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