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Database: UniProt
Entry: Q2FXM8
LinkDB: Q2FXM8
Original site: Q2FXM8 
ID   PFKA_STAA8              Reviewed;         322 AA.
AC   Q2FXM8;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 2.
DT   12-SEP-2018, entry version 94.
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=SAOUHSC_01807;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL   Washington D.C. (2006).
RN   [2]
RP   INTERACTION WITH CSHA, AND SUBUNIT.
RC   STRAIN=UAMS-1;
RX   PubMed=21764917; DOI=10.1128/JB.05485-11;
RA   Roux C.M., DeMuth J.P., Dunman P.M.;
RT   "Characterization of components of the Staphylococcus aureus mRNA
RT   degradosome holoenzyme-like complex.";
RL   J. Bacteriol. 193:5520-5526(2011).
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: Subject to allosteric activation by ADP and
CC       other diphosphonucleosides, and inhibition by phosphoenolpyruvate.
CC       {ECO:0000250}.
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 (By similarity). Component of a possible RNA
CC       degradosome complex composed of cshA, eno, pfkA, pnp, rnjA, rnjB,
CC       rnpA and rny. Interacts specifically with RNA helicase CshA.
CC       {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:21764917}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD30875.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; CP000253; ABD30875.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_500312.1; NC_007795.1.
DR   PDB; 5XOE; X-ray; 2.98 A; A=1-322.
DR   PDBsum; 5XOE; -.
DR   ProteinModelPortal; Q2FXM8; -.
DR   SMR; Q2FXM8; -.
DR   STRING; 93061.SAOUHSC_01807; -.
DR   EnsemblBacteria; ABD30875; ABD30875; SAOUHSC_01807.
DR   GeneID; 3919277; -.
DR   KEGG; sao:SAOUHSC_01807; -.
DR   PATRIC; fig|93061.5.peg.1647; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000008816; 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   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   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    322       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000430112.
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      127    129       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      171    173       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      187    189       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      215    217       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    129    129       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     156    156       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     164    164       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     213    213       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     224    224       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   322 AA;  34840 MW;  1FAE41C0BA7CA7F1 CRC64;
     MKKIAVLTSG GDSPGMNAAV RAVVRTAIYN EIEVYGVYHG YQGLLNDDIH KLELGSVGDT
     IQRGGTFLYS ARCPEFKEQE VRKVAIENLR KRGIEGLVVI GGDGSYRGAQ RISEECKEIQ
     TIGIPGTIDN DINGTDFTIG FDTALNTIIG LVDKIRDTAS SHARTFIIEA MGRDCGDLAL
     WAGLSVGAET IVVPEVKTDI KEIADKIEQG IKRGKKHSIV LVAEGCMTAQ DCQKELSQYI
     NVDNRVSVLG HVQRGGSPTG ADRVLASRLG GYAVDLLMQG ETAKGVGIKN NKIVATSFDE
     IFDGKDHKFD YSLYELANKL SI
//
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