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Database: UniProt
Entry: A0A067HBR1_CITSI
LinkDB: A0A067HBR1_CITSI
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ID   A0A067HBR1_CITSI        Unreviewed;       623 AA.
AC   A0A067HBR1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=CISIN_1g006964mg {ECO:0000313|EMBL:KDO85267.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO85267.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO85267.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC       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 (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; KK784874; KDO85267.1; -; Genomic_DNA.
DR   EMBL; KK784874; KDO85268.1; -; Genomic_DNA.
DR   STRING; 2711.A0A067HBR1; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
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:0015979; P:photosynthesis; IBA:GO_Central.
DR   GO; GO:0009749; P:response to glucose; IBA:GO_Central.
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; 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:SF17; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT ALPHA 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
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:UP000027120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03185}.
FT   DOMAIN          96..459
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   623 AA;  68497 MW;  A7B883F1789CF1E4 CRC64;
     MLFFFLFNPS DPQSFHFWDI ALLAIYLLQM FSFNANMQGT TVRVEFGDST TTADPADTHS
     ISRSFPHTYG QPLAHFLRAT AKVPDAQIIT EHPAIRVGIV FCGRQSPGGH NVVWGLYDAL
     KLHNPKSTLL GFLGGSEGLF AQKTLEVTKE ILSTYKNQGG YDMLGRTKDQ IRTTEQVNAA
     LTACKNLNLD GLVIIGGVTS NTDAAYLAET FAEAKCPTKV VGVPVTLNGD LKNQFVETNV
     GFDTICKVNS QLISNVCTDA LSAEKYYYFI RLMGRRASHV ALECTLQSHP NMVILGEEVA
     ASKLTLFDLT KQICDAVQAR AEQDKNHGVI LLPEGLIESI PEVYALLKEI HSLLRQGVPV
     DNISSQLSPW ASALFEFLPP FIKKQLLLQP ESDDSAQLSQ IETEKLLAHL VEVEMNKRLK
     EGTYKGKKFN AICHFFGYQA RGSLPSKFDC DYAYVLGHIC YHILAAGLNG YMATVTNLKN
     PANKWRCGAA PITSMMTVKR WSQNPGASSI GRPAINPATV DMRGKAYELL RQNATRFLLD
     DLYRNPGPVQ FDGPGADAKA VTLCVEDRDY MGRIKELQKY LDEVRTIVKP GCSQEVLKAA
     LSVMASVTEV LSAMSASGGQ TTL
//
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