PFPA_RICCO
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 03-AUG-2022, entry version 99.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_03185};
GN Name=PFP-ALPHA {ECO:0000255|HAMAP-Rule:MF_03185};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 castor
RT pyrophosphate-dependent phosphofructokinase.";
RL Gene 152:181-186(1995).
CC -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC bisphosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC chains. {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_03185}.
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DR EMBL; Z32849; CAA83682.1; -; Genomic_DNA.
DR PIR; T10102; T10102.
DR AlphaFoldDB; Q41140; -.
DR SMR; Q41140; -.
DR STRING; 3988.XP_002510738.1; -.
DR PRIDE; Q41140; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; Q41140; -.
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 Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
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 SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..617
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit alpha"
FT /id="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