ID   A0A087HIX1_ARAAL        Unreviewed;       617 AA.
AC   A0A087HIX1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   29-MAY-2024, entry version 46.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_03185};
DE            Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185};
DE   AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185};
GN   Name=PFP-ALPHA {ECO:0000256|HAMAP-Rule:MF_03185};
GN   OrderedLocusNames=AALP_Aa2g207700 {ECO:0000313|EMBL:KFK42073.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42073.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
CC   -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC       phosphotransferase. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC         Evidence={ECO:0000256|ARBA:ARBA00000628};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC       bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC       chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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DR   EMBL; CM002870; KFK42073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087HIX1; -.
DR   EnsemblPlants; KFK42073; KFK42073; AALP_AA2G207700.
DR   Gramene; KFK42073; KFK42073; AALP_AA2G207700.
DR   eggNOG; KOG2440; Eukaryota.
DR   OMA; NKWHCGA; -.
DR   OrthoDB; 197423at2759; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000029120; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:EnsemblPlants.
DR   GO; GO:0009749; P:response to glucose; IEA:TreeGrafter.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR011183; PfpB_PPi_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02477; PFKA_PPi; 1.
DR   PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR43650:SF23; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT ALPHA 2; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03185}; Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03185}.
FT   DOMAIN          88..450
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   617 AA;  67435 MW;  70EB47E66A9999ED CRC64;
     MDSDFGIPRE LSPLQQLRSQ YQPLLPPCLQ GTTVRVELGD GTTGAKAGDA HIIARAFPHT
     LGQPLAHFLR ANAKVVDAQI ITEHPAIRVG IVFSGRQAPG GHNVIWGLYE ALKVHNAKNT
     LLGFLGGSEG LFAQKTVEIT DDVLQTYKNQ GGFDLLGRTK DQIRTTEQVN AALKACTDLK
     LDGLVIIGGV TSNTDAGHLA EFFAETKCPT KVVGVPVTIN GDLKNQFVEA NVGFDTICKV
     NSQLISNVCT DALSAEKYYY FIRLMGRKHS HVALECTLQS HPNMVILGEE VAASKLTIFD
     IAKQICDAVQ ARAEQDKNHG VILIPEGLVE SIPELFALLK EIHGLLKEGV DADKISTKLS
     PWSFALFEFL PPFMKKQLLL HPESDDSAQL SQIETEKLLA YLVETEMNKR MKVGTYKGKK
     FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATVTNL KSPVNKWKCG
     AAPITAMMTV KRWSQNAGST SIGRPVIHPA TVDLKGKAYD LLRQNAQKFL MEDMYRNPGP
     LQYDGPGADA KAVSLCVEDQ DYMGRIKKLQ EYLDQVRTIV KPGCSQDVLK AALSVMASVT
     DVLSTISSSS TSGQQFA
//