ID   PFPA_RICCO              Reviewed;         617 AA.
AC   Q41140;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha;
DE            Short=PFP;
DE            EC=2.7.1.90;
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
DE   AltName: Full=PPi-PFK;
GN   Name=PFP-ALPHA;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC   Acalypheae; Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95137384; PubMed=7835697; DOI=10.1016/0378-1119(94)00646-A;
RA   Todd J.F., Blakeley S.D., Dennis D.T.;
RT   "Structure of the genes encoding the alpha- and beta-subunits of
RT   castor pyrophosphate-dependent phosphofructokinase.";
RL   Gene 152:181-186(1995).
CC   -!- FUNCTION: The alpha subunit may be involved in the regulation of
CC       PFP by Fru-2,6-P (By similarity).
CC   -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
CC       phosphate + D-fructose 1,6-bisphosphate.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains (By
CC       similarity).
CC   -!- MISCELLANEOUS: The active site might be on the beta subunit.
CC   -!- SIMILARITY: Belongs to the pyrophosphate-dependent
CC       phosphofructokinase family.
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DR   EMBL; Z32849; CAA83682.1; -; Genomic_DNA.
DR   PIR; T10102; T10102.
DR   HSSP; P70826; 1KZH.
DR   BRENDA; 2.7.1.90; 816.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphot...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011183; PfpB_PPi_PFK.
DR   InterPro; IPR000023; Phosphofructokinase.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR   ProDom; PD000707; Ppfruckinase; 1.
DR   TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    617       Pyrophosphate--fructose 6-phosphate 1-
FT                                phosphotransferase subunit alpha.
FT                                /FTId=PRO_0000112047.
SQ   SEQUENCE   617 AA;  67361 MW;  1C9B2A0AF11FF3F0 CRC64;
     MDSDFGIPRE LSDLQKLRSL YKPELPPCLQ GTTVRVELGD GTTACSEAGA HTISRSFPHT
     YGQPLAHFLR ATAKVADAHI ISEHPAMRVG VVFCGRQSPG GHNVVWGLHN ALKIHNPNST
     LLGFLGGSEG LFAQKTLEVT DDILSTYKNQ GGYDLLGRTK DQIRTTEQVH AALTTCKNLK
     LDGLVIIGGV TSNTDAAQLA ETFAEAKCPT KVVGVPVTLN GDLKNQFVET NVGFDTICKV
     NSQLISNVCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILGEE VAASKLTLFD
     LTKQVCDAVQ ARAEQDKYHG VILLPEGLIE SIPEVYALLK EIHGLLRQGV SPNNISSQLS
     PWASALFEFL PPFIKKQLLL YPESDDSAQL SQIETEKLLA HLVEAEMNKR LKEGTYKGKK
     FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHVLAAGL NGYMATATNL KNPVNKWRCG
     AAPIAAMMTV KRWAQNPGAT SIGKPAIHPA AVDLKGKAYE LLRLNAVKFL MDDLYRNPGP
     LQFEGPGADA KPITLCVEDQ DYMGRIKKLQ EYLDKVRTIV KPGCSQEVLK AALSVMASVT
     DVLLTMSSTS LDGQKPL
//