ID A0A022R8L1_ERYGU Unreviewed; 616 AA.
AC A0A022R8L1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=MIMGU_mgv1a003013mg {ECO:0000313|EMBL:EYU36601.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU36601.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU36601.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI630592; EYU36601.1; -; Genomic_DNA.
DR RefSeq; XP_012838997.1; XM_012983543.1.
DR AlphaFoldDB; A0A022R8L1; -.
DR STRING; 4155.A0A022R8L1; -.
DR GeneID; 105959440; -.
DR KEGG; egt:105959440; -.
DR eggNOG; KOG2440; Eukaryota.
DR OMA; NKWHCGA; -.
DR OrthoDB; 197423at2759; -.
DR PhylomeDB; A0A022R8L1; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000030748; 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:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 88..449
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 616 AA; 67113 MW; FD596DB0EB80FC34 CRC64;
MDSDYGIARE LSDLQKLRSH YQPELPPCLQ GTTVRVHFGD ATAAADPTGA HTISRSFPLT
YGQPLAHFLR STAKVPDAQI ITEHAAVRVG VVFCGRQSPG GHNVIWGLHE ALKVHNPKSV
LLGFLGGSDG LFAQKTLEVT DEVLATYKNQ GGYDLLGRTK DQIRTIEQVN AALNACTALK
LDALVIIGGV TSNTDAAQLA ETFAERKCPT KVVGIPVTLN GDLRNQFVET NVGFDTICKV
NSQLISNVCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILAEE VAASKLTIFD
ITNQICDAVQ ARAEQDKYHG VILLPEGLIE SFPEVFALLQ EIHALLRQGV SADNISAQLS
PWASALFEFL PPFIRKQLLL HPESDDSAQL SQIETEKLLA HLVEAEMNKR TKEGTYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH IGYHIIAAGL NGYMATLTNL KNPVNKWRCA
AAPITAMMTV KRYGRGHGAS ILGKPALHPA TVDLKGKSYE LLRQNSTKFL MDDVYRNPGP
LQYDGPGADA KAVTLCVEDQ DYMGRIKLLQ EHLDKVRSIV KPGCSQDVLK AALSAMASVT
EILSVMSAAS GGSTPF
//
