PFKA_MYCPN
ID PFKA_MYCPN Reviewed; 328 AA.
AC P75476;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable ATP-dependent 6-phosphofructokinase;
DE Short=ATP-PFK;
DE Short=Phosphofructokinase;
DE EC=2.7.1.11;
DE AltName: Full=Phosphohexokinase;
GN Name=pfkA; Synonyms=pfk; OrderedLocusNames=MPN_302; ORFNames=MP534;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000250|UniProtKB:P0A796}.
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:0000250|UniProtKB:P0A796};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A796};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000250|UniProtKB:P0A796}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC {ECO:0000305}.
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DR EMBL; U00089; AAB96182.1; -; Genomic_DNA.
DR PIR; S73860; S73860.
DR RefSeq; NP_109990.1; NC_000912.1.
DR RefSeq; WP_010874659.1; NC_000912.1.
DR AlphaFoldDB; P75476; -.
DR SMR; P75476; -.
DR IntAct; P75476; 2.
DR STRING; 272634.MPN_302; -.
DR EnsemblBacteria; AAB96182; AAB96182; MPN_302.
DR GeneID; 66609051; -.
DR KEGG; mpn:MPN_302; -.
DR PATRIC; fig|272634.6.peg.326; -.
DR HOGENOM; CLU_020655_0_1_14; -.
DR OMA; KFAVICV; -.
DR BioCyc; MetaCyc:MON-545; -.
DR BioCyc; MPNE272634:G1GJ3-472-MON; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
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; 3.40.50.460; -; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..328
FT /note="Probable ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111965"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 77..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 107..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 130..132
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 167
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 174..176
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 226
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 258..261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
SQ SEQUENCE 328 AA; 35989 MW; E29C9F0536766321 CRC64;
MSPKTTKKIA ILTSGGDAPG MNATLVYLTR YATSSEIEVF FVKNGYYGLY HDELVPAHQL
DLSNSLFSAG TVIGSKRFVE FKELKVREQA AQNLKKRQID YLVVIGGDGS YMGAKLLSEL
GVNCYCLPGT IDNDINSSEF TIGFLTALES IKVNVQAVYH TTKSHERVAI VEVMGRHCGD
LAIFGALATN ADFVVTPSNK MDLKQLESAV KKILQHQNHC VVIVSENIYG FDGYPSLTAI
KQHFDANNMK CNLVSLGHTQ RGFAPTSLEL VQISLMAQHT INLIGQNKVN QVIGNKANVP
VNYDFDQAFN MPPVDRSALI AVINKNII
