ID R7JH63_9BACT Unreviewed; 418 AA.
AC R7JH63;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphofructokinase {ECO:0000313|EMBL:CDE62953.1};
GN ORFNames=BN752_01693 {ECO:0000313|EMBL:CDE62953.1};
OS Alistipes putredinis CAG:67.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE62953.1, ECO:0000313|Proteomes:UP000018026};
RN [1] {ECO:0000313|EMBL:CDE62953.1, ECO:0000313|Proteomes:UP000018026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC {ECO:0000256|ARBA:ARBA00038478}.
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:CDE62953.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBJI010000012; CDE62953.1; -; Genomic_DNA.
DR AlphaFoldDB; R7JH63; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000018026; Unassembled WGS sequence.
DR GO; GO:0003872; F:6-phosphofructokinase activity; 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 InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
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; PIRSF036482; PPi_PFK_TM0289; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDE62953.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..329
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 418 AA; 46249 MW; 3DE060988218775C CRC64;
MTKRNEAIAI LTGGGPAPGM NTVVGSVAKT FLQKGYSVIG LHKGFTGLFR EAPATENITF
LKADEIFNLA GSFLRMSRFK PSDEDFEKRF NWQFFTENNI KLLVTIGGDD TASTANRVAK
FLEEKRHPIA NIHVPKTIDN DLPLPDCAPT FGYESAKDKG AVIARAVYVD ARTSGNWFVM
SAMGRSAGHL AFGIGEACHY PMIVIPEMFN KTPITIDKII RLMVSSIVKR RIVSMDYGAA
VISEGVFHEL SEAELSSCGI HFTYDAHGHP ELGKVSKACF FSMLLDQRLA ELKLNVQTRP
VELGYEIRGQ TPVAYDLTYC SELGIGVYKL FSEGKTGCMV YVDGCGNVEP LYLKDLQDPA
TGKILPRMVD ISSDRFKAVV DNILMAITPP DYEAARQYLS NPEEYDFCKI LGWDETDL
//
