PFP_HALED
ID PFP_HALED Reviewed; 419 AA.
AC E1VB09;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01978};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:28081159};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01978};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01978};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000303|PubMed:28081159};
GN Synonyms=pfkA {ECO:0000312|EMBL:CBV42070.1};
GN OrderedLocusNames=HELO_2186 {ECO:0000312|EMBL:CBV42070.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA Kunte H.J.;
RT "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT study for integrative systems biology.";
RL PLoS ONE 12:E0168818-E0168818(2017).
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:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:28081159}.
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:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:28081159};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01978}.
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DR EMBL; FN869568; CBV42070.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VB09; -.
DR SMR; E1VB09; -.
DR STRING; 768066.HELO_2186; -.
DR EnsemblBacteria; CBV42070; CBV42070; HELO_2186.
DR KEGG; hel:HELO_2186; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_6; -.
DR OMA; AHDIGYF; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008707; 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; 3.40.50.460; -; 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_XF0274.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036483; PFK_XF0274; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000439536"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 13
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01978"
SQ SEQUENCE 419 AA; 45705 MW; 82077517AE634675 CRC64;
MAQHNAFYAQ SGGVTAVINA SACGVIEACR RHDDRIGKVY AGHNGIIGAL TEDLIDVSQE
SDEAIAALRH TPAGAFGSCR YKLKDIETHR TQYERLIEVF RAHDIRYFFY NGGGDSADTC
LKVSQLSEKM GYPLTAIHVP KTVDNDLPIT DNSPGFGSVA KYIATSTLEA SLDIASMCAT
STKVFVLEVM GRHAGWIAAA GALAGQGEGD PPHLVIFPEI DFDRAAVMAR VEESVKKCGY
CVIVVSEGAR YEDGTFLADS GNTDAFGHRQ LGGVAPTLAG MIKQDLGYKY HWAVADYLQR
AARHLASKTD VDQAYAVGEK AVELALDGQN AKMPAIKRIS DEPYAWTVEA APLADVANRE
KFMPRDFIRE DGFGITEQCR RYLAPLIQGE DFPPFENGLP KVAKLAKHRV ERKLPEFKL
