ID   R0ABP2_9FIRM            Unreviewed;       412 AA.
AC   R0ABP2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   08-MAY-2019, entry version 30.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01978};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01978};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01978};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01978};
GN   ORFNames=HMPREF1097_04386 {ECO:0000313|EMBL:ENZ33818.1};
OS   [Clostridium] bolteae 90B8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=997897 {ECO:0000313|EMBL:ENZ33818.1, ECO:0000313|Proteomes:UP000013041};
RN   [1] {ECO:0000313|EMBL:ENZ33818.1, ECO:0000313|Proteomes:UP000013041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90B8 {ECO:0000313|EMBL:ENZ33818.1,
RC   ECO:0000313|Proteomes:UP000013041};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium bolteae 90B8.";
RL   Submitted (JAN-2013) 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_01978}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-
CC         fructose 1,6-bisphosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634;
CC         EC=2.7.1.90; Evidence={ECO:0000256|HAMAP-Rule:MF_01978};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01978};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
CC       Rule:MF_01978}.
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_01978}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. PPi-dependent PFK group II subfamily. Clade "B2" sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENZ33818.1}.
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DR   EMBL; AGYG01000029; ENZ33818.1; -; Genomic_DNA.
DR   RefSeq; WP_002567258.1; NZ_KB851157.1.
DR   EnsemblBacteria; ENZ33818; ENZ33818; HMPREF1097_04386.
DR   PATRIC; fig|997897.5.peg.4609; -.
DR   BioCyc; GCF_000371645-HMP:HMPREF1097_RS26805-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000013041; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
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_01978; Phosphofructokinase_II_B2; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   InterPro; IPR011404; PPi-PFK_XF0274.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF036483; PFK_XF0274; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000013041};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01978, ECO:0000313|EMBL:ENZ33818.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01978}.
FT   DOMAIN        7    328       PFK. {ECO:0000259|Pfam:PF00365}.
FT   REGION      143    145       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01978}.
FT   REGION      191    193       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01978}.
FT   ACT_SITE    145    145       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01978}.
FT   METAL       115    115       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01978}.
FT   BINDING      14     14       Diphosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01978}.
FT   BINDING     248    248       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01978}.
FT   SITE        116    116       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_01978}.
FT   SITE        142    142       Important for catalytic activity;
FT                                stabilizes the transition state when the
FT                                phosphoryl donor is PPi.
FT                                {ECO:0000256|HAMAP-Rule:MF_01978}.
SQ   SEQUENCE   412 AA;  45173 MW;  79A093163F54FB4C CRC64;
     MGKKRNIIVG QSGGPTSVIN SSLAGVYKTA KERGFHKVYG MLHGIEGLLD EMYVDLSTQI
     HSDMDIELLK RTPSAFLGSC RYKLPDIHEN PAFYEKIFAI LDKLDIEVFI YIGGNDSMDT
     IKKLSDYAIV KGHGQKFLGV PKTIDNDLAL TDHTPGFGSA AKYIATSTKE VIRDAMGLSY
     RRKTITIMEC MGRNAGWLTG STALARTEDC CGPDLIYLPE IPFDIDKFLK KCKDLIQKKP
     SIVIAVSEGI KVPDGRYVCQ LSGGSDYVDA FGHKQLAGTA DYLAGFLAGE LGCKTRSVEL
     STLQRSASHV ASRVDINEAF MVGGAAVKAA DEGDTGKMVV IDRVSDDPYM SAAGIYDVHK
     IANNEKTVPR SWVNKDGSYV TQEFVNYVEP LIQGDYQPFM VNGLPQHLVL KR
//