ID A0A1B8P3S1_HALEL Unreviewed; 241 AA.
AC A0A1B8P3S1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=6-phosphofructokinase 1 {ECO:0000313|EMBL:OBX36901.1};
DE EC=2.7.1.11 {ECO:0000313|EMBL:OBX36901.1};
GN Name=pfkA1 {ECO:0000313|EMBL:OBX36901.1};
GN ORFNames=A8U91_01248 {ECO:0000313|EMBL:OBX36901.1};
OS Halomonas elongata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2746 {ECO:0000313|EMBL:OBX36901.1, ECO:0000313|Proteomes:UP000092504};
RN [1] {ECO:0000313|EMBL:OBX36901.1, ECO:0000313|Proteomes:UP000092504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HEK1 {ECO:0000313|EMBL:OBX36901.1,
RC ECO:0000313|Proteomes:UP000092504};
RA Gaba S., Singh R.N., Abrol S., Kaushik R., Saxena A.K.;
RT "Genome sequence of halotolerant plant growth promoting strain of Halomonas
RT elongata HEK1 isolated from salterns of Rann of Kutch, Gujarat, India.";
RL Submitted (JUN-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:OBX36901.1}.
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DR EMBL; MAJD01000001; OBX36901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8P3S1; -.
DR PATRIC; fig|2746.7.peg.1288; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000092504; Unassembled WGS sequence.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
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 InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBX36901.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OBX36901.1}.
FT DOMAIN 9..206
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 219..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 25773 MW; 796578D935D02FC9 CRC64;
MAQHNAFYAQ SGGVTAVINA SACGVIEACR RHDDRIGKVY AGHNGIIGAL TEDLIDVSQE
SDEAIAALRH TPAGAFGSCR YKLKDIETHR TQYERLIEVF RAHDIRYFFY NGGGDSADTC
LKVSQLSEKM GYPLTAIHVP KTVDNDLPIT DNSPGFGSVA KYIATSTLEA SLDIASMCAT
STKVFVLEVM GRHAGWIAAA GALAGQGEGD PPHLVIFPRS TSTAPRSWPA SRSRSRSAVT
A
//
