PFPA_SOLTU
ID PFPA_SOLTU Reviewed; 616 AA.
AC P21342; M1AMC7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 110.
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};
GN ORFNames=PGSC0003DMG400010007;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 277-295.
RC STRAIN=cv. Kennebec;
RX PubMed=2170409; DOI=10.1016/s0021-9258(17)44761-2;
RA Carlisle S.M., Blakeley S.D., Hemmingsen S.M., Trevanion S.J., Hiyoshi T.,
RA Kruger N.J., Dennis D.T.;
RT "Pyrophosphate-dependent phosphofructokinase. Conservation of protein
RT sequence between the alpha- and beta-subunits and with the ATP-dependent
RT phosphofructokinase.";
RL J. Biol. Chem. 265:18366-18371(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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; M55190; AAA63451.1; -; mRNA.
DR PIR; A36094; A36094.
DR RefSeq; NP_001275358.1; NM_001288429.1.
DR AlphaFoldDB; P21342; -.
DR SMR; P21342; -.
DR STRING; 4113.PGSC0003DMT400025919; -.
DR PRIDE; P21342; -.
DR EnsemblPlants; PGSC0003DMT400025919; PGSC0003DMT400025919; PGSC0003DMG400010007.
DR GeneID; 102577617; -.
DR Gramene; PGSC0003DMT400025919; PGSC0003DMT400025919; PGSC0003DMG400010007.
DR KEGG; sot:102577617; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_2_0_1; -.
DR OMA; NKWHCGA; -.
DR OrthoDB; 347054at2759; -.
DR SABIO-RK; P21342; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P21342; baseline.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
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 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..616
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit alpha"
FT /id="PRO_0000112048"
FT CONFLICT 48
FT /note="S -> A (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="E -> D (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> S (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="V -> G (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="C -> V (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="Q -> A (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="R -> A (in Ref. 1; AAA63451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 67359 MW; EF19B3A063C1A19D CRC64;
MDADYGIPRE LSDLQKLRSH YHPELPPCLQ GTTVRVELRD ATTAADPSGE HTIKRFFPHT
YGQPLAHFLR ATAKVPDAQI ITEHPAIRVG VLFCGRQSPG GHNVIWGLHD ALKVHNPKNI
LLGFLGGSEG LFAQKTLEIT DDVLATYKNQ GGYDMLGRTK DQIRTTEQVN AAMAACKALK
LDGLVIIGGV TSNTDAAHLA EKFAETKCLT KVVGVPVTLN GDLKNQFVEA NVGFDTICKV
NSQLISNVCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILGEE VAASKLTIFD
ITQQICDAVQ ARAEHDKNHG VILLPEGLIE SIPEVYALLQ EIHGLLRQGV SADKISSQLS
PWASALFEFL PHFIRKQLLL HPESDDSAQL SQIETEKLIA HLVETEMNKR LKEGTYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH VCYHILAAGL NGYMATITNL KNPANKWHCG
ASPISAMMTV KRYGRGPGKA SIGVPALHPA TVDLRGKSYE LLSQNATKFL LDDVYRNPGP
LQFDGPGADA KAVSLCVEDQ DYIGRIKKLQ EYLDKVRTIV KPGCSQDVLK AALSAMASVT
DILSVISSPS SVSTPF
