ID A0A085G0B7_9ENTR Unreviewed; 326 AA.
AC A0A085G0B7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN ORFNames=GBAG_3895 {ECO:0000313|EMBL:KFC77162.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC77162.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC77162.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC77162.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000432};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004679}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KFC77162.1}.
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DR EMBL; JMPI01000068; KFC77162.1; -; Genomic_DNA.
DR RefSeq; WP_034499293.1; NZ_JMPI01000068.1.
DR AlphaFoldDB; A0A085G0B7; -.
DR STRING; 1006004.GBAG_3895; -.
DR eggNOG; COG0205; Bacteria.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000028653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFC77162.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFC77162.1}.
FT DOMAIN 2..280
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 326 AA; 35580 MW; 67EF043A0B8B600B CRC64;
MRIGMVISGG DVTGINNFVF QISRLAQAEI VLFNGGIPGL LQNNHQAISA RDLVDFSVAA
IPIMSSGRTH RKLMGSEYET IAKQLKTLHI DVLIMAGGDG SLQFLNNLSE YGVNCFGVGM
TIDNDVYGSD YTIGFSTACE QVIKEVGKLR NTGRALPGRV FMVELLGGYC GELTLQSAIK
SNADFALIPE CQQSLSELAH KISARLETQN SVVILCSEGY TKEYSPGFQG AIDTMIKQLE
PKIGVRIRKS IIGYSLRNGD PTCEEIYQGT IMAGEVVRCI QSGMRNKAII INSSNKPIPI
DLISMQKRLV DTEGHHYKLA KQLNII
//
