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Database: UniProt
Entry: B2V7W7
LinkDB: B2V7W7
Original site: B2V7W7 
ID   PFKA_SULSY              Reviewed;         324 AA.
AC   B2V7W7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   07-NOV-2018, entry version 68.
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=SYO3AOP1_0397;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD66040.1; -; Genomic_DNA.
DR   RefSeq; WP_012459122.1; NC_010730.1.
DR   ProteinModelPortal; B2V7W7; -.
DR   SMR; B2V7W7; -.
DR   STRING; 436114.SYO3AOP1_0397; -.
DR   EnsemblBacteria; ACD66040; ACD66040; SYO3AOP1_0397.
DR   KEGG; sul:SYO3AOP1_0397; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   OrthoDB; POG091H01AC; -.
DR   BioCyc; SSP436114:G1GC2-423-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001201; 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; 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.
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    324       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_1000133289.
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      126    128       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      170    172       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      186    188       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      254    257       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    128    128       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     155    155       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     163    163       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING     248    248       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   324 AA;  36049 MW;  AFFFE32028C29772 CRC64;
     MKKIGLLTSG GDCPGLNACI RAVVRTANYY NIEVVAFKRG FKGLIENDFT TLDYKSVAGI
     LQKGGTILLT AREPRFKDYN FRKIAYENIQ KHNIEALFVI GGNGSFQGAY LLQKDFGLNI
     IGIPKTIDND IYGTDYAIGF DTAVNNAMEA IDKIKDTTMS HERIFIVEVM GRDNGFIALE
     VGIAVGAELT LIPEYPFPLH VIEETILKAK EMGKNFAIIV LAEGVASAKE LSEILNERLK
     DKDVGEIRYQ VLGYIQRGGS PSAYDRVMAS KFGVFAVEKF VQGEKNFMVA YENGKLLTKP
     LEISFNKVRI PNLEEYQINN ILSM
//
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