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Database: UniProt
Entry: A0A2G2VHZ9_CAPBA
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ID   A0A2G2VHZ9_CAPBA        Unreviewed;       617 AA.
AC   A0A2G2VHZ9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=CQW23_28934 {ECO:0000313|EMBL:PHT32597.1};
OS   Capsicum baccatum (Peruvian pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT32597.1, ECO:0000313|Proteomes:UP000224567};
RN   [1] {ECO:0000313|EMBL:PHT32597.1, ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHT32597.1};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [2] {ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA   Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA   Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA   Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA   Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA   Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA   Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT   "Multiple reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease resistance genes by retroduplication.";
RL   J. Anim. Genet. bioRxivorg:115410-115410(2017).
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:PHT32597.1}.
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DR   EMBL; MLFT02000012; PHT32597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2VHZ9; -.
DR   STRING; 33114.A0A2G2VHZ9; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000224567; Chromosome 12.
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: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:UP000224567};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03185}.
FT   DOMAIN          88..454
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   617 AA;  67033 MW;  03BE3E98CC444092 CRC64;
     MDADYGIARE LSDLQKLRSH YQPELPPCLQ GTTVRVELGD ATTAADPSGA HVISRSFPHT
     YGQPLAHFLR ATAKVTGAQI ITEHPAKRVG VVFCGRQSPG GHNVIWGIHD ALKIHNPNST
     LLGFLGGSEG LFAQKTLEIT NDVLATYKNQ GGYDILGRTK DQIRTTEQVN AAMAACKSLK
     LDALIIIGGV TSNTDAAQLA ETFAEAKCQT KVVGVPVTLN GDLKNQFVEA NVGFDTICKV
     NSQLISNMCT DALSAEKYYY FIRLMGRKAS HVALECTLQS HPNMVILGEE VAASKLTLFD
     ITHKICDAVQ ARAEQDKNHG VILLPEGLIE SIPEVYALLQ EIHGLLTQGV SADKISSQLS
     PWASALFEFL PPFIKKQLLL HPESDDSAQL SQIETEKLLA HLVENEMNKR VKEGTYKGKK
     FNAICHFFGY QARGSLPSKF DCDYAYVLGH VCYHILAAGL NGYMATLTNL KNPVNKWRCG
     AAPITAMMTV KRYGRGPGKA SIGKPALHPA TVDLKGKAYE LLSQNASKFL LDDVYRNPGP
     LQFDGPGADA KAVTLCVEDQ DYMGRIKKLQ EYLDKVRTIV KPGCSQDVLK AALSAMSSVT
     DILSVMASPS SNANTPF
//
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