ID A0A061FEW0_THECC Unreviewed; 617 AA.
AC A0A061FEW0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=TCM_034805 {ECO:0000313|EMBL:EOY15865.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY15865.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY15865.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(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; CM001886; EOY15865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FEW0; -.
DR STRING; 3641.A0A061FEW0; -.
DR EnsemblPlants; EOY15865; EOY15865; TCM_034805.
DR Gramene; EOY15865; EOY15865; TCM_034805.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_2_0_1; -.
DR InParanoid; A0A061FEW0; -.
DR OMA; SYTTLEC; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000026915; Chromosome 8.
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:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 88..452
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 617 AA; 67396 MW; CDACCE0FB7B9A35B CRC64;
MDSDFGIPRE LSDLQKLRSQ YQPGLPPCLE GTTVRVEFGD ATTALDPADA HTISRAFPHT
YGQPLAHFLR ATAKVPDAQI ITEHPAMRVG LVFCGRQSPG GHNVIWGLHK ALKIHNPNST
LLGFLGGTQG LFAQKTLEIT DDILSTYKNQ GGYDLLGRTQ DQIRTTEQVN AALTACNDLK
LDGLVIIGGV TSNTDAAQLA ETFAEAKCQT KVVGVPVTLN GDLKNQFVEA NVGFDTICKV
NSQLISNVCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILGEE VAASKLTLFD
ITKQICDAVQ ARAEQDKNHG VILLPEGLIE SIPEVYALLK EIHSLLRQGV SAEKISSQLS
PWASALFEFL PPFIRRQLLL HPESDDSAQL SQIETEKLLA HLVETEINKR LKAGTYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATITNL KNPVNKWRCG
AAPIAAMMSV KRWSQNPNAL SIGKPAIHPA TVDLKGKAYE LLRQNAARFL LDDIYRNPGP
LQFDGPGADA KAVTLCVEDQ DYMGRIKKLQ EYLEKVRTIV KPGCSQEVLK AALSVMASVT
EVLSVMSSSS SGGQTTL
//
