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Database: UniProt/SWISS-PROT
Entry: PFKA_BACVZ
LinkDB: PFKA_BACVZ
Original site: PFKA_BACVZ 
ID   PFKA_BACVZ              Reviewed;         319 AA.
AC   A7Z7K6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   18-JUL-2018, entry version 80.
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=RBAM_026240;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus
OS   amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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   -!- ENZYME 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; CP000560; ABS74982.1; -; Genomic_DNA.
DR   RefSeq; WP_007408068.1; NC_009725.1.
DR   ProteinModelPortal; A7Z7K6; -.
DR   SMR; A7Z7K6; -.
DR   EnsemblBacteria; ABS74982; ABS74982; RBAM_026240.
DR   KEGG; bay:RBAM_026240; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001120; 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   CDD; cd00763; Bacterial_PFK; 1.
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   Reference proteome; Transferase.
FT   CHAIN         1    319       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_1000059737.
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      213    215       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      249    252       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     211    211       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     222    222       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING     243    243       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   319 AA;  34261 MW;  461E8A30F03C6206 CRC64;
     MKRIGVLTSG GDSPGMNAAV RAVVRKAIYH DVEVYGIYNG YSGLISGKIE KLELGSVGDI
     IHRGGTKLYT ARCPEFKTVE GREKGIENLK KLGIEGLVVI GGDGSYMGAK KLTEHGFPCV
     GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA
     GLAGGAESIL IPEADYDMQE IIGRLKRGHD RGKKHSIIIV AEGVGSGVEF GKRIEEETNL
     ETRVSVLGHI QRGGSPSASD RVLASRLGAY AVELLLKGKG GRCVGIQNNK LVDHDIIEIL
     ESKHTVEPNM YQLSKELSI
//
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