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Database: UniProt/TrEMBL
Entry: B3S470_TRIAD
LinkDB: B3S470_TRIAD
Original site: B3S470_TRIAD 
ID   B3S470_TRIAD            Unreviewed;       782 AA.
AC   B3S470;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE            EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|PIRNR:PIRNR000533};
GN   ORFNames=TRIADDRAFT_28803 {ECO:0000313|EMBL:EDV22403.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22403.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV22403.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22403.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432,
CC         ECO:0000256|PIRNR:PIRNR000533};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|PIRNR:PIRNR000533}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E"
CC       sub-subfamily. {ECO:0000256|PIRNR:PIRNR000533}.
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DR   EMBL; DS985249; EDV22403.1; -; Genomic_DNA.
DR   RefSeq; XP_002114947.1; XM_002114911.1.
DR   AlphaFoldDB; B3S470; -.
DR   STRING; 10228.B3S470; -.
DR   EnsemblMetazoa; TriadT28803; TriadP28803; TriadG28803.
DR   GeneID; 6756350; -.
DR   KEGG; tad:TRIADDRAFT_28803; -.
DR   CTD; 6756350; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   HOGENOM; CLU_011053_0_0_1; -.
DR   InParanoid; B3S470; -.
DR   OMA; EWQDQMC; -.
DR   OrthoDB; 374214at2759; -.
DR   PhylomeDB; B3S470; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000533};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PIRNR:PIRNR000533};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000533};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT   DOMAIN          26..330
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   DOMAIN          408..696
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   782 AA;  86220 MW;  65D4C69C0B7CD37F CRC64;
     MESKETREDQ QQCDHGTKSN APTKCIAVIT SGGDAQGMNA AVRAAVRMAI YNDARVFAVH
     EGYQGLVEGE DFIKEMTWSN FLIVLILKGG TIIGTARCQE FRAKEGRIKA AKNLVGRGIS
     NLMVIGGDGS LTGANLFRRE WTELLTILIE RGEIPENSLI EYPVLNIVGL VGSIDNDFCG
     TKMTIGADSA LHRILECANA IITTASSHRR TFVLEVMGRR CGYLALISGL AIGADWIFIP
     EVPPEDGWEE RMCAQLKAAR NVGNRLNIIV LAEGAVDIHG NAITAEQVKQ ILVKYAQQDT
     RITVLGHVQR GGSPSAFDRI LGCRMGAEAV LSLLESTVDT TPFVIGLQGN DMIRVPLMEC
     VEKTRNLAKA MDEHNFEAAL DLRNFGNTLS IFKGCNYYSP IPCDQKFRIC IMAVGAPAAG
     MNAAIRSVTR LSINQGHEVF CIRDGFEGLL SDTDNVQKME WVTVHDWIAK GGCDIGTKRT
     LPSVNMEKIA AGFKKYKFHG LVIIGGFEAF KSATQLLEAR NTFEAFAIPI IVIPATLSNN
     VPGTDYSLGT DTSLNVIVEV CYHRIRQSAT AANHRVFVVE TMGGNCGYLA TMAGLASGAD
     AAYIFEEKYN INDLQGDVAH MIAKFKQDKI HRGLLLTNEF CSRNYDTDFI TRLFADEGKE
     YFTTRKNVLG HVQQGGYPSP FDRVLSSRFA YAATSFLIRE IKNNIRGDGV MNASHPSTVA
     LVGSQNRSLR ISPVTDLMAV ADFDKRIPKQ QWWMRLRPLM RILAHHKQTF QRELRPENAD
     TE
//
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