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Database: UniProt
Entry: B4U2M2
LinkDB: B4U2M2
Original site: B4U2M2 
ID   PFKA_STREM              Reviewed;         337 AA.
AC   B4U2M2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   10-OCT-2018, entry version 59.
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=Sez_0881;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F.,
RA   Deleo F.R., Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus
RT   strain causing epidemic nephritis: new information about an old
RT   disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {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; CP001129; ACG62239.1; -; Genomic_DNA.
DR   RefSeq; WP_012515510.1; NC_011134.1.
DR   ProteinModelPortal; B4U2M2; -.
DR   SMR; B4U2M2; -.
DR   EnsemblBacteria; ACG62239; ACG62239; Sez_0881.
DR   KEGG; sez:Sez_0881; -.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001873; 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_1000120059.
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;  35670 MW;  1D4667FB04FF5AB9 CRC64;
     MKRIAVLTSG GDAPGMNAAI RAVVRKAISE GMEVYGINRG YAGMVDGDIF PLGSKEVGDK
     ISRGGTFLYS ARYPEFAQLE GQLAGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAV
     GIPGTIDNDI AGTDYTIGFD TAVNTAVEAI DKLRDTSSSH GRTFVVEVMG RNAGDIALWA
     GIASGADQII VPEEEFDIHK VVSTIKDDFE NRGKNHHIIV LAEGVMSGEA FAQQLKEAGD
     ESDLRVTNLG HILRGGSPTA RDRVIASWMG AHAVELLKEG KGGLAVGIHN EELVESPILG
     SAEDGALFSL TDEGNIVVNN PHKARLDYAA LNRSLAQ
//
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