(data stored in SCRATCH zone)

SWISSPROT: D1YV03_METPS

ID   D1YV03_METPS            Unreviewed;       345 AA.
AC   D1YV03;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 61.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976,
GN   ECO:0000313|EMBL:BAI60275.1};
GN   OrderedLocusNames=MCP_0203 {ECO:0000313|EMBL:BAI60275.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60275.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC       first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC       phosphoryl donor instead of ATP like common ATP-dependent
CC       phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC       and can thus function both in glycolysis and gluconeogenesis.
CC       Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC       PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC       {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01976}.
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_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}.
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DR   EMBL; AP011532; BAI60275.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0203; -.
DR   EnsemblBacteria; BAI60275; BAI60275; MCP_0203.
DR   KEGG; mpd:MCP_0203; -.
DR   PATRIC; fig|304371.9.peg.210; -.
DR   eggNOG; arCOG03641; Archaea.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248869; -.
DR   KO; K21071; -.
DR   OMA; ARGKKFA; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001882; Chromosome.
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:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV03.
DR   SWISS-2DPAGE; D1YV03.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000313|EMBL:BAI60275.1}.
FT   DOMAIN          6..301
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   REGION          128..130
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          172..174
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          275..278
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   METAL           106
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         14
FT                   /note="Diphosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         165
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         225
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         269
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   SITE            107
FT                   /note="Important for catalytic activity and substrate
FT                   specificity; stabilizes the transition state when the
FT                   phosphoryl donor is PPi; prevents ATP from binding by
FT                   mimicking the alpha-phosphate group of ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   SITE            127
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
SQ   SEQUENCE   345 AA;  36943 MW;  12D9C8F368566230 CRC64;
     MADIKKIGIL TGGGDCPGLN AVIRAVVFKA GEYGWQVLGV KYGWKGMLNA DAIPLTRNDV
     KDILPLGGTI LKTSRTNPYK VEGGEAKVLE NAKKMGIDCL VAVGGEDTLG VANKLTKAGL
     RCVGVPKTID NDLGATDYTF GYQTAVQIAS DAMDRLHTTA KSHDRVLVCE VMGRHAGWMT
     VDAGMSASAH WIYTPEAKGS VEDCCKMLKE RYARGDKYGI VAVAEGAEFS DLDVKAASQT
     TDSFGHVKLG GVAETLAKEI EKRTGLETRH VVLGHTQRGG SPLAYDRILG TRLGNKAAEM
     IKNGQFAMMA SLRGENVEAV PIEEAVKTLK TVPPQYYDVA KTFFG
//

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