ID Q6YQU2_ONYPE Unreviewed; 332 AA.
AC Q6YQU2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN Name=pfkA {ECO:0000313|EMBL:BAD04366.1};
GN OrderedLocusNames=PAM_281 {ECO:0000313|EMBL:BAD04366.1};
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=262768 {ECO:0000313|EMBL:BAD04366.1, ECO:0000313|Proteomes:UP000002523};
RN [1] {ECO:0000313|EMBL:BAD04366.1, ECO:0000313|Proteomes:UP000002523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M {ECO:0000313|Proteomes:UP000002523};
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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}.
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DR EMBL; AP006628; BAD04366.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQU2; -.
DR STRING; 262768.PAM_281; -.
DR KEGG; poy:PAM_281; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_14; -.
DR BioCyc; OYEL262768:G1G26-339-MONOMER; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002523; Chromosome.
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: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; IPR015912; Phosphofructokinase_CS.
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.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..290
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 332 AA; 36218 MW; E30FF999504BF32E CRC64;
MKNENQKAKT KTKENKKIAV LTSGGDAPGM NAAIRALVFE SAKQGFEVFG VKDGYLGLFN
NQIEILNPQT FPRVLNVSGT FLGTSRFLDF QNNLDVRKQC AQNLKTLGID KLVVIGGDGS
YKGASKLHEL GIKCVGLPAT IDNDICATDF TIGFSTALNN IVDAIEKLRD TSVSHNRCSI
IEVMGRHKGD LALFGGLAAG ADVIVTRENL LSQKTICQKI KSLRQANQRH AIVVVTEHIF
DVASLAKEVE NYSGFETRAQ VLGHIQRGGK PTAEDLVLAF RMGSYAVSLL QQNIFNCAVG
TCGLNLHYTT FGDLFEKTYE KNELFNVVAK LL
//
