ID   A0A087HIX1_ARAAL        Unreviewed;       617 AA.
AC   A0A087HIX1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-MAY-2019, entry version 26.
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   ORFNames=AALP_AA2G207700 {ECO:0000313|EMBL:KFK42073.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Arabideae;
OC   Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42073.1};
RN   [1] {ECO:0000313|EMBL:KFK42073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KFK42073.1};
RA   Willing E.-M.;
RT   "The reference genome of Arabis alpina.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-
CC       phosphate 1-phosphotransferase. {ECO:0000256|HAMAP-Rule:MF_03185}.
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
CC       (catalytic) 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)
CC       family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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DR   EMBL; CM002870; KFK42073.1; -; Genomic_DNA.
DR   STRING; 50452.A0A087HIX1; -.
DR   OMA; IKAHNAN; -.
DR   OrthoDB; 347054at2759; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
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_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   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02477; PFKA_PPi; 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|HAMAP-Rule:MF_03185};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03185};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03185}.
FT   DOMAIN       88    393       PFK. {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
//