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Database: UniProt/SWISS-PROT
Entry: PFKA_NATTJ
LinkDB: PFKA_NATTJ
Original site: PFKA_NATTJ 
ID   PFKA_NATTJ              Reviewed;         319 AA.
AC   B2A6Y0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 66.
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=Nther_2004;
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-
RT   WN-LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001034; ACB85571.1; -; Genomic_DNA.
DR   RefSeq; WP_012448428.1; NC_010718.1.
DR   ProteinModelPortal; B2A6Y0; -.
DR   SMR; B2A6Y0; -.
DR   STRING; 457570.Nther_2004; -.
DR   EnsemblBacteria; ACB85571; ACB85571; Nther_2004.
DR   KEGG; nth:Nther_2004; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   OrthoDB; POG091H01AC; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001683; 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   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_1000120049.
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;  34618 MW;  B6E5099360197187 CRC64;
     MKKIGVLTSG GDSPGMNATI RAVVRRGIYM GLDIYGIYYG FSGLINGNIE KLEIGSVGDI
     IHRGGTILHT SRSEEFKTEM GQQKGFDNLK ELGIEGLIVI GGDGSFKGAE KLSQMGLPVI
     GVPGTIDNDI PETEMSIGFD TALNTVIEAI DRIRDTATSH ERIFVIEVMG RDCGNLALWS
     GLAGGAESVL IPEIDYDMEK VIERLKHGYK RGKKHSIIIV AEGVKPGAEI GKEIKERAGL
     DNRVTVLGHV QRGGTPTAYD RMLGSRLGAK AVDLLVAGES DKMIGMRDYK LVPVQFKDVF
     SKIEEPDYDI YELSQSLSI
//
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