PFKA_MYCGE
ID PFKA_MYCGE Reviewed; 323 AA.
AC P47457;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MG215;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
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; L43967; AAC71434.1; -; Genomic_DNA.
DR PIR; G64223; G64223.
DR RefSeq; WP_010869375.1; NC_000908.2.
DR AlphaFoldDB; P47457; -.
DR SMR; P47457; -.
DR STRING; 243273.MG_215; -.
DR EnsemblBacteria; AAC71434; AAC71434; MG_215.
DR KEGG; mge:MG_215; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_14; -.
DR OMA; KFAVICV; -.
DR OrthoDB; 1421302at2; -.
DR BioCyc; MGEN243273:G1GJ2-251-MON; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
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..323
FT /note="Probable ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111963"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 72..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 125..127
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 162
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 169..171
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 221
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
FT BINDING 253..256
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A796"
SQ SEQUENCE 323 AA; 35641 MW; 67072AC3D5542E89 CRC64;
MDKIAILTSG GDASGMNATI AYLTKYAIAK QLEVFYVKNG YYGLYHNHFI TSKELDLTDF
FFMGGTVIGS SRFKQFQDPS LRKQAVLNLK KRGINNLVVI GGDGSYMGAK ALSELGLNCF
CLPGTIDNDV NSSEFTIGFW TALEAIRVNV EAIYHTTKSH NRLAIIEVMG RDCSDLTIFG
GLATNASFVV TSKNSLDLNG FEKAVRKVLQ FQNYCVVLVS ENIYGKNGLP SLEMVKEHFE
NNAIKCNLVS LGHTQRGFSP NSIELFQISL MAKHTIDLVV NNANSQVIGM KNNQAVNYDF
NTAFNLPKAD RTKLLNQVNT AII
