ID PFKA_STRPM Reviewed; 337 AA.
AC Q48T86;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 05-DEC-2018, entry version 85.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
GN OrderedLocusNames=M28_Spy0961;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D.,
RA Beres S.B., Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC to fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC diphosphonucleosides, and allosterically inhibited by
CC phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC family. ATP-dependent PFK group I subfamily. Prokaryotic clade
CC "B1" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}.
DR EMBL; CP000056; AAX72074.1; -; Genomic_DNA.
DR RefSeq; WP_002984444.1; NC_007296.1.
DR ProteinModelPortal; Q48T86; -.
DR SMR; Q48T86; -.
DR EnsemblBacteria; AAX72074; AAX72074; M28_Spy0961.
DR KEGG; spb:M28_Spy0961; -.
DR HOGENOM; HOG000248870; -.
DR KO; K00850; -.
DR OMA; GKLHSII; -.
DR BioCyc; SPYO319701:G1G4H-994-MONOMER; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000009292; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR012828; PFKA_ATP_prok.
DR InterPro; IPR015912; Phosphofructokinase_CS.
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.
DR TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1 337 ATP-dependent 6-phosphofructokinase.
FT /FTId=PRO_1000059800.
FT NP_BIND 72 73 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT NP_BIND 102 105 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT REGION 21 25 Allosteric activator ADP binding; shared
FT with dimeric partner. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT REGION 125 127 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT REGION 169 171 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT REGION 185 187 Allosteric activator ADP binding.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT REGION 214 216 Allosteric activator ADP binding.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT REGION 251 254 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT ACT_SITE 127 127 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT METAL 103 103 Magnesium; catalytic. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT BINDING 11 11 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT BINDING 154 154 Allosteric activator ADP.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT BINDING 162 162 Substrate; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT BINDING 212 212 Allosteric activator ADP.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
FT BINDING 223 223 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00339}.
FT BINDING 245 245 Substrate; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_00339}.
SQ SEQUENCE 337 AA; 35762 MW; DA99570A8BF391FF CRC64;
MKRIAVLTSG GDAPGMNAAI RAVVRKAISE GMEVYGINRG YAGMVDGDIF PLGSKEVGDK
ISRGGTFLYS ARYPEFAQLE GQLAGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAV
GIPGTIDNDI AGTDYTIGFD TAVNTAVEAI DKLRDTSSSH GRTFVVEVMG RNAGDIALWA
GIASGADQII VPEEEFDIEK VASTIQYDFE HKGKNHHIIV LAEGVMSGEA FAQKLKEAGD
KSDLRVTNLG HILRGGSPTA RDRVIASWMG SHAVELLKEG KGGLAVGIHN EELVESPILG
TAEEGALFSL TEEGKIIVNN PHKARLDFAA LNRSLSQ
//
