ID   PFKA_UREPA              Reviewed;         321 AA.
AC   Q9PQV8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
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; OrderedLocusNames=UU185;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30592.1; -; Genomic_DNA.
DR   RefSeq; WP_006689121.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQV8; -.
DR   SMR; Q9PQV8; -.
DR   STRING; 273119.UU185; -.
DR   EnsemblBacteria; AAF30592; AAF30592; UU185.
DR   GeneID; 29672722; -.
DR   KEGG; uur:UU185; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_0_1_14; -.
DR   OMA; MNTIMEC; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000423; 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; 3.40.50.460; -; 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..321
FT                   /note="Probable ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000112004"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         82..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         136..138
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         180..182
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   BINDING         265..268
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
SQ   SEQUENCE   321 AA;  36542 MW;  3087C6061E9F546C CRC64;
     MNQVNFLNLD KNILIITSGG DAPGMNASLI SLIHRLMNNN FNVFIGIEGL LGLYNNLIEP
     IKDKRVFDVY FNEQGTVIKT SRFIKLDIND KKTQIIKDNL LSHNIQKIII LGGQGSMQAG
     LVLTKMGFEV FGILHTIDND FSETQMCIGA LSAASFNQKL LKCLNYTAKA HCAFNLVELM
     GRECSWLVNN SVGKLKPILM LTNQDNKYTV DEVIDLIKDK INSIKEYDPL IIVQELIYDQ
     KWYELLVKTF EQKLHKSLRI TILNYLQRGA PVSDFDLQLA KDSANVLVDF IVNQNDIKNT
     NNMYVVINKF DNKLEVIKFN K