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Database: UniProt
Entry: A0A0R2UCR8_9GAMM
LinkDB: A0A0R2UCR8_9GAMM
Original site: A0A0R2UCR8_9GAMM 
ID   A0A0R2UCR8_9GAMM        Unreviewed;       420 AA.
AC   A0A0R2UCR8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ABS24_03870 {ECO:0000313|EMBL:KRO95163.1};
OS   SAR92 bacterium BACL26 MAG-121220-bin70.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO95163.1, ECO:0000313|Proteomes:UP000051213};
RN   [1] {ECO:0000313|EMBL:KRO95163.1, ECO:0000313|Proteomes:UP000051213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO95163.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01978}.
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|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC         Rule:MF_01978};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01978};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-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) family.
CC       PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO95163.1}.
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DR   EMBL; LICA01000103; KRO95163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2UCR8; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000051213; 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   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
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.
DR   PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF036483; PFK_XF0274; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01978};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01978};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01978};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01978};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01978}.
FT   DOMAIN          9..294
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         13
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         142..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         190..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         297..300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   SITE            115
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_01978"
FT   SITE            141
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
SQ   SEQUENCE   420 AA;  45142 MW;  90D6C350453D66B7 CRC64;
     MDKKNAFYAQ SGGVTAVINA SAAGVIEAAR ENKAIIGKLY AGLNGIVGAL QEELVDTSKE
     SSSAIAALRH TPGGAFGSCR YKMKNYQDSP AEYERLIAVF KAHNIGYFFY NGGGDSADTC
     LKVSQISEKM GYPIQAIHIP KTIDNDLPLT DCSPGFGSVA KYIATSTKEA SLDIESMCGS
     STKVFILEVM GRHAGWIAAS SGLAGEQAGD PPHIILFPEI PFSRENFIAK VEKTINEKGY
     CVIVASEGAQ YSDGAHISGS INKDAFGHQQ LGGVAPALAS MIKQSTGYKY HWAMADYLQR
     SARHIASKTD VDQAYAVGRA AVEMAVQGKS SVMVSIERGA GKKYSWSLGE VPLADVANME
     KKMPRSFITE DGYGITQKAR DYLEPLIAGE DYPPFKGGIP SYVRLKKILV PKKLMSDFKV
//
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