ID   K0PSX6_9RHIZ            Unreviewed;       403 AA.
AC   K0PSX6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAY-2015, entry version 16.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01977};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01977};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01977,
GN   ECO:0000313|EMBL:CCM76968.1};
GN   ORFNames=BN77_4011 {ECO:0000313|EMBL:CCM76968.1};
OS   Rhizobium mesoamericanum STM3625.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1211777 {ECO:0000313|EMBL:CCM76968.1};
RN   [1] {ECO:0000313|EMBL:CCM76968.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=STM3625 {ECO:0000313|EMBL:CCM76968.1};
RA   Genoscope - CEA;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCM76968.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=STM3625 {ECO:0000313|EMBL:CCM76968.1};
RA   Moulin L., Mornico D., Melkonian R., Klonowska A.;
RT   "Draft Genome Sequence of Rhizobium mesoamericanum STM3625, a
RT   Nitrogen-Fixing Symbiont of Mimosa pudica Isolated in French Guiana
RT   (South America).";
RL   Genome Announc. 1:e00066-e00112(2013).
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_01977}.
CC   -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
CC       phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01977}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01977};
CC   -!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
CC       Rule:MF_01977}.
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_01977}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_01977}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. PPi-dependent PFK group II subfamily. Clade "P" sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01977}.
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:CCM76968.1}.
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DR   EMBL; CANI01000028; CCM76968.1; -; Genomic_DNA.
DR   RefSeq; WP_007534747.1; NZ_HF536772.1.
DR   EnsemblBacteria; CCM76968; CCM76968; BN77_4011.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP.
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   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR011405; PPi-PFK_SMc01852.
DR   PANTHER; PTHR13697:SF16; PTHR13697:SF16; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01977,
KW   ECO:0000313|EMBL:CCM76968.1}.
FT   REGION      150    152       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01977}.
FT   REGION      195    197       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01977}.
FT   REGION      324    327       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01977}.
FT   ACT_SITE    152    152       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01977}.
FT   METAL       122    122       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01977}.
FT   BINDING      13     13       Diphosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01977}.
FT   BINDING     267    267       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01977}.
FT   SITE        123    123       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_01977}.
FT   SITE        149    149       Important for catalytic activity;
FT                                stabilizes the transition state when the
FT                                phosphoryl donor is PPi.
FT                                {ECO:0000256|HAMAP-Rule:MF_01977}.
SQ   SEQUENCE   403 AA;  43227 MW;  1DA92E679949581F CRC64;
     MAKQKVAMLT AGGLAPCLSS AVGGLIERYS DVAPDIELIA YRSGYQGVLL GDSITITADM
     REKAPLLHRY GGSPIGNSRV KLTNAADCVK RGLVKEGENP LRVAAERLAN DGVNILHTIG
     GDDTNTTAAD LAAYLAANGY NLTVVGLPKT VDNDVVPIRQ SLGAWTAAEV GAHFFDNVSN
     EQTAAPRTLI IHEVMGRHCG WLTAATARAY LQRTKSYEYV DGLMTNAKMK SIDAVYLPEM
     AFDLDAEAAR LKDVMDRTGH ATVFVSEGAC LDAIVEEREA AGETIKRDAF GHVKIDTINV
     GGWFQKQFAG LISAERSLVQ KSGYFARSAP ANGDDLRLIQ SMTDLAVESA LNKVSGVTGH
     DEAQNGKLRT IEFPRIKGGK AFDISTTWFG EVMDTIGQKY PAA
//