ID A0A0D5M3C1_9GAMM Unreviewed; 419 AA.
AC A0A0D5M3C1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=KO116_02409 {ECO:0000313|EMBL:AJY50884.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY50884.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY50884.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY50884.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP011052; AJY50884.1; -; Genomic_DNA.
DR RefSeq; WP_035558614.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M3C1; -.
DR STRING; 1504981.KO116_02409; -.
DR KEGG; hak:KO116_02409; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_6; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000028645; Chromosome.
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|HAMAP-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..302
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 419 AA; 45322 MW; 71297AA26C8186C2 CRC64;
MAQHNAFYAQ SGGVTAVINA SACGVIEACR QAPDQIGKVY AGHNGIIGAL TEDLIDVTQE
SDEAIAALRH TPGGAFGSCR YKLKDIDTHR AQYERLIEVF KAHDIRYFFY NGGGDSADTC
LKVSQLSEKL GYPLTAIHVP KTVDNDLPIT DNSPGFGSVA KYIATSTLEA SLDIASMCAT
STKVFVLEVM GRHAGWIAAA GGLAGEGEGE PPHMIIFPEI AFNRKAAMAR VEESVKQYGY
CVIVVSEGAR YEDGTFLADA GNTDAFGHRQ LGGVAPTLAG MIKQDLGYKY HWAVADYLQR
AARHLASKTD VEQAYAVGRE AVTLALAGKN AMMPAIRRIS QSPYQWDVIS APLSQVANKE
KFMPRDFISD NGFAITQTCR DYLSPLIQGE DFPPFENGLP KVAKLKLAKA ERKLPTFTL
//
