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Database: UniProt
Entry: F6FG41_MYCHI
LinkDB: F6FG41_MYCHI
Original site: F6FG41_MYCHI 
ID   F6FG41_MYCHI            Unreviewed;        60 AA.
AC   F6FG41;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE            EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN   OrderedLocusNames=MHF_1303 {ECO:0000313|EMBL:AEG73539.1};
OS   Mycoplasma haemofelis (strain Ohio2).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=859194 {ECO:0000313|EMBL:AEG73539.1, ECO:0000313|Proteomes:UP000007952};
RN   [1] {ECO:0000313|EMBL:AEG73539.1, ECO:0000313|Proteomes:UP000007952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ohio2 {ECO:0000313|EMBL:AEG73539.1,
RC   ECO:0000313|Proteomes:UP000007952};
RX   PubMed=21317328; DOI=10.1128/JB.00133-11;
RA   Messick J.B., Santos A.P., Guimaraes A.M.;
RT   "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT   haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL   J. Bacteriol. 193:2068-2069(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ohio2;
RA   Santos A.P., Guimaraes A.M.S., SanMiguel P.J., Martin S.W., Messick J.B.;
RT   "The Genome of Mycoplasma haemofelis Strain Ohio2, a pathogenic hemoplasma
RT   of the cat.";
RL   Submitted (MAY-2011) 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}.
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DR   EMBL; CP002808; AEG73539.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6FG41; -.
DR   STRING; 859194.MHF_1303; -.
DR   KEGG; mhf:MHF_1303; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_209770_0_0_14; -.
DR   BioCyc; MHAE859194:G1GR7-1298-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000007952; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
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   InterPro; IPR022953; ATP_PFK.
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   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};
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          5..56
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   60 AA;  6361 MW;  3709CEB47B693B8A CRC64;
     MENKKIAVLT SGGDSPAMNA TICSFVASAR SCGWDVYGVI DGYKGLIESN FSKLDSDLKV
//
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