ID A0A2U1KBF3_ARTAN Unreviewed; 614 AA.
AC A0A2U1KBF3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CTI12_AA622500 {ECO:0000313|EMBL:PWA34088.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA34088.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA34088.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA34088.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA34088.1}.
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DR EMBL; PKPP01023879; PWA34088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1KBF3; -.
DR STRING; 35608.A0A2U1KBF3; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000245207; 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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF15; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT ALPHA; 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:UP000245207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 88..451
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 614 AA; 67292 MW; 414B1CD1D4EB1032 CRC64;
MESDYGVKRE LSDLQKQRSL YQPDLPPCLQ GTTVRVEFGD RTTVSDSSGA HAISQSFPHT
YGQRLLHFLR ATAKVPGAHI INDHPALRVG LVFCGRQSPG GHNVVWGLHE ALKIHNPKST
LLGFLGGSEG LFAQKTLEIT DDVLATYKNQ GGYDLLGRTK DQIRTTEQVN ATMAACNDLK
LDGLVIVGGV TSNSDAAQLA ETFAEAKCVT KVVGVPVTLN GDLKNQFVEA NVGFDTICKV
NSQLIGNVCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILGEE VAASKLTIFD
LTKQICDAIQ ARAEQEKYHG VILLPEGLIE SIPEFYALLQ EIHSLLRQGV SADKISTQLS
PWAFALFEFL PPFIRKQLLL YPESDDLAQL SQIETEKLLA ELVEAEMNKR QKEGSYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATVTNL KSPSNKWRCG
AAPITAMLSV KHGGHGSGAM KIGKPFVHPA TVDLRGKVYE LLRENARQLL LDDIYRNPGP
LQFDGPGADS RVMSLCVEDL DYMGRIKKLN EYLEKVRAMV KPGCSQDVVK AALSAMSSIT
DILSVMSSPS NGTT
//
