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Database: UniProt/TrEMBL
Entry: F8B656_FRADG
LinkDB: F8B656_FRADG
Original site: F8B656_FRADG 
ID   F8B656_FRADG            Unreviewed;       341 AA.
AC   F8B656;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   29-APR-2015, entry version 28.
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   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976};
GN   OrderedLocusNames=FsymDg_3146 {ECO:0000313|EMBL:AEH10455.1};
OS   Frankia symbiont subsp. Datisca glomerata.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=656024 {ECO:0000313|EMBL:AEH10455.1, ECO:0000313|Proteomes:UP000001549};
RN   [1] {ECO:0000313|EMBL:AEH10455.1, ECO:0000313|Proteomes:UP000001549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4085684 {ECO:0000313|EMBL:AEH10455.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A.,
RA   Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.;
RT   "Complete sequence of chromosome of Frankia symbiont of Datisca
RT   glomerata.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate,
CC       the first committing step of glycolysis. Uses inorganic phosphate
CC       (PPi) as phosphoryl donor instead of ATP like common ATP-dependent
CC       phosphofructokinases (ATP-PFKs), which renders the reaction
CC       reversible, and can thus function both in glycolysis and
CC       gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of
CC       both the forward (ATP-PFK) and reverse (fructose-bisphosphatase
CC       (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
CC       phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01976};
CC   -!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
CC       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, ECO:0000256|SAAS:SAAS00041065}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
CC       ECO:0000256|SAAS:SAAS00054613}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01976}.
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DR   EMBL; CP002801; AEH10455.1; -; Genomic_DNA.
DR   RefSeq; WP_013874350.1; NC_015656.1.
DR   RefSeq; YP_004584376.1; NC_015656.1.
DR   ProteinModelPortal; F8B656; -.
DR   EnsemblBacteria; AEH10455; AEH10455; FsymDg_3146.
DR   KEGG; fsy:FsymDg_3146; -.
DR   KO; K00850; -.
DR   OMA; ESHHRVL; -.
DR   BioCyc; FSYM656024:GHLT-3170-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001549; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   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;
KW   ATP-binding {ECO:0000256|RuleBase:RU004092};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001549};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041050};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041074};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041077};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041029};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001549};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092}.
FT   REGION      125    127       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      169    171       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      271    274       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    127    127       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       103    103       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      10     10       Diphosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     162    162       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     265    265       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        104    104       Important for catalytic activity and
FT                                substrate specificity; stabilizes the
FT                                transition state when the phosphoryl
FT                                donor is PPi; prevents ATP from binding
FT                                by mimicking the alpha-phosphate group of
FT                                ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        124    124       Important for catalytic activity;
FT                                stabilizes the transition state when the
FT                                phosphoryl donor is PPi.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   341 AA;  36406 MW;  CB2CD4D2CD29C6DA CRC64;
     MRIGVLTGGG DCPGLNAVIR AVVRKGTDVY GYSFVGFRDG WRGPLENATV PLGVEAVRGI
     LPRGGTILGS SRTNPYKEDG GVARIRQTLA AHGVDALIAI GGEDTLGVAA RLHDEGIPVV
     GVPKTIDNDL SATDYTFGFD TAVNIAMEAI DRLHTTAESH HRVLIVEVMG RHAGWIALHS
     GLAGGANVIL LPERPFDIDK VCAFVEHRFA SHYAPIIVVA EGAVPVAGSL VVKDGELDAF
     GHVRLQGIAT VLETEIRGRT GRESRATVLG HVQRGGTPTA FDRWLATRFG LHVIDAAHDG
     DWGTMVALHG TRIDRVPLEE ATRELKLVPE ELYAEAEVFF G
//
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