ID A0A176TE57_9FLAO Unreviewed; 405 AA.
AC A0A176TE57;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=6-phosphofructokinase {ECO:0000313|EMBL:OAD46049.1};
GN ORFNames=LPB303_03800 {ECO:0000313|EMBL:OAD46049.1};
OS Polaribacter atrinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1333662 {ECO:0000313|EMBL:OAD46049.1, ECO:0000313|Proteomes:UP000076923};
RN [1] {ECO:0000313|EMBL:OAD46049.1, ECO:0000313|Proteomes:UP000076923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 17473 {ECO:0000313|EMBL:OAD46049.1,
RC ECO:0000313|Proteomes:UP000076923};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Polaribacter atrinae KACC17473.";
RL Submitted (FEB-2016) 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:OAD46049.1}.
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DR EMBL; LVWE01000005; OAD46049.1; -; Genomic_DNA.
DR RefSeq; WP_068448281.1; NZ_LVWE01000005.1.
DR AlphaFoldDB; A0A176TE57; -.
DR STRING; 1333662.LPB303_03800; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000076923; 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:OAD46049.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..319
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 405 AA; 45349 MW; 77DA61FCCFAD7052 CRC64;
MKKSVAIMCG GGPAPGINTV ISTVAKTFMK DGYEVIGVHH GYQGLLSENP VLEIFDFHRA
DRIFSRGGSS PIMSRFKPKD SDFKVDFFKK NNVKLLVTIG GDDTASTANR LTKYLKSEAL
DVRHIHVPKT IDNDLPLPDR NPTFGFHTAK DEGVRIGNTV YEDARTSENW FVMSAMGRSA
GHLAFGIASA CHFQMVIIPE MFNKTTITFE KLTNMIISSI IKCKIMGLEY GVALISEGVF
HFMEEEEIIN SGINFTYDDH GHPELGNVSK SHIFNYLLQI KLKEIGLDIK SRPVELGYEL
RCCNPIAFDL TLCTLLGIGV KKLFDQGATG CIVSANSRGD ITPLYLKDFE DENGKIPPRL
VDINSDMAQL FIENLFFLKE KDYENAKKYV TNPEAYDFKK ILNWS
//
