ID V6LN73_9EUKA Unreviewed; 543 AA.
AC V6LN73;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185};
GN ORFNames=SS50377_14240 {ECO:0000313|EMBL:EST45668.1}, SS50377_22171
GN {ECO:0000313|EMBL:KAH0576607.1};
OS Spironucleus salmonicida.
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Hexamitinae;
OC Spironucleus.
OX NCBI_TaxID=348837 {ECO:0000313|EMBL:EST45668.1};
RN [1] {ECO:0000313|EMBL:KAH0576607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0576607.1};
RX PubMed=24516394;
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 10:E1004053-E1004053(2014).
RN [2] {ECO:0000313|EMBL:EST45668.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu F., Jerlstrom-Hultqvist J., Einarsson E., Astvaldsson A., Svard S.G.,
RA Andersson J.O.;
RT "The Genome of Spironucleus salmonicida Highlights a Fish Pathogen Adapted
RT to Fluctuating Environments.";
RL PLoS Genet. 0:0-0(2014).
RN [3] {ECO:0000313|EMBL:KAH0576607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50377 {ECO:0000313|EMBL:KAH0576607.1};
RA Xu F., Kurt Z., Jimenez-Gonzalez A., Astvaldsson A., Andersson J.O.,
RA Svard S.G.;
RT "New Spironucleus salmonicida genome in near-complete chromosomes.";
RL Submitted (DEC-2020) 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|HAMAP-Rule:MF_03185}.
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_03185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_03185}.
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_03185}.
CC -!- SUBUNIT: Homodimer or monomer. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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DR EMBL; KI546089; EST45668.1; -; Genomic_DNA.
DR EMBL; AUWU02000002; KAH0576607.1; -; Genomic_DNA.
DR AlphaFoldDB; V6LN73; -.
DR EnsemblProtists; EST45668; EST45668; SS50377_14240.
DR VEuPathDB; GiardiaDB:SS50377_22171; -.
DR OrthoDB; 197423at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000018208; 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:0005524; F:ATP binding; IEA:InterPro.
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_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02477; PFKA_PPi; 1.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03185}; Reference proteome {ECO:0000313|Proteomes:UP000018208};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 71..316
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 78
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 200..202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 240..241
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 412..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT SITE 173
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_03185"
FT SITE 199
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
SQ SEQUENCE 543 AA; 59901 MW; FC614C8F2F3E402E CRC64;
MSQFEIYRRK HTPVLPESIR GTSYSIHEGE KSVPISDAAE IAKTFTKTTY LPIIDIKAET
THATQLPPQT IGVIFSGGQA PGGHNVLCGL YDKLQQIAPG STLLGFLDGP AGLMKNRHIT
LTKEYLEQYR NMGGFHAIGS GRDKIASQEQ FDAAAKTSQD LNLDGLVIIG GDDSNTNACV
LAEDFLTRGI KTNIVGVPKT IDRDLISKKG IETSFGFDST TKVYSELIGN LCFDALSAKK
YWHFVRLMGR SASHITLECG LQTHPNICLI GEEILEKKLT SKQVFEMIAD IIDNRAKSGK
NYGIALIPEG LIEFIPENNK LFDYLNNTLL PHWTGELNPE VVAAKLPADL RATFESIPRN
IRFQLLLDRD PHGNIAISQI ETEKFLVAGV KEVLEARKSV AKFNPLYHFF GYEGRCCPPS
NFDSSYCYGL GSVASILLAN GKTGYMASLK NLSKPPQDWI PVGLPLTCLM NVEMRHGKPT
PVIQKQMVDL VGKPMKMLID NRDSWATEDH YVQPGSLQLI DATDAEAIAL AARPTITLIE
EYK
//
