ID G5SVX4_9BACT Unreviewed; 545 AA.
AC G5SVX4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01980};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01980};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01980};
GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01980};
GN ORFNames=HMPREF9441_03545 {ECO:0000313|EMBL:EHG98439.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG98439.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG98439.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG98439.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) 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_01980}.
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_01980};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01980};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01980}.
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_01980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}.
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_01980}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01980}.
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:EHG98439.1}.
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DR EMBL; AFFY01000074; EHG98439.1; -; Genomic_DNA.
DR RefSeq; WP_008622743.1; NZ_JH376642.1.
DR AlphaFoldDB; G5SVX4; -.
DR STRING; 762968.HMPREF9441_03545; -.
DR GeneID; 78584274; -.
DR PATRIC; fig|762968.3.peg.3107; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_022288_0_1_10; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000003598; 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_01980};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01980};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01980};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01980};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01980};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01980}.
FT DOMAIN 69..311
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 77
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 199..201
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 238..239
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 246..248
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 307
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 418..421
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT SITE 172
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_01980"
FT SITE 198
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
SQ SEQUENCE 545 AA; 59451 MW; 0D2B566B3A5110AB CRC64;
MEKSALQIAR AAYQPKLPKG LQGNVSVKEG VPTQSVADQE EIKKLFPNTY GMPLIEFVPG
EAQSYAPFNV GVILSGGQAP GGHNVICGLF DGIKRLNPES KLYGFILGPG GLVDHKYMEL
TADIIDQYRN TGGFDMIGSG RTKLEKEEQF EKGLEIIKEL GIKAIVIIGG DDSNTNACVL
AEYYAAKKCG VQVIGCPKTI DGDLKNEQIE TSFGFDTACK TYAEVIGNIQ RDANSARKYW
HFIKLMGRSA SHIALECALQ CQPNVCIVSE EVEAKNQTLD DIVTYIAQVV ADRAADGNNF
GTVLIPEGLI EFIPAMKALI AELNDLLATP EGAALAKDQQ REWILNKLSA ANKAVYESLP
LGVAAQLTME RDPHGNVQVS LIETEKLLSE MVANKLAAWK KEGKFNGKFS ALHHFFGYEG
RCAAPSNYDA DYCYALGTSA AMLMANGKTG YMAIVKNTTA PAAEWIAGGV PITMMMNMEK
RNGEMKPVIK KALVRLDGAP FKEFASRRNQ WARETCFVYP GPIQYFGPTE VCDQATKTLQ
LEQAK
//
