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Database: UniProt/SWISS-PROT
Entry: PFKA_CALS4
LinkDB: PFKA_CALS4
Original site: PFKA_CALS4 
ID   PFKA_CALS4              Reviewed;         321 AA.
AC   Q8R914;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   07-JUN-2017, entry version 93.
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=TTE1816;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 /
OS   JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM25008.1; -; Genomic_DNA.
DR   RefSeq; WP_011026004.1; NC_003869.1.
DR   ProteinModelPortal; Q8R914; -.
DR   SMR; Q8R914; -.
DR   STRING; 273068.TTE1816; -.
DR   PRIDE; Q8R914; -.
DR   EnsemblBacteria; AAM25008; AAM25008; TTE1816.
DR   KEGG; tte:TTE1816; -.
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; UP000000555; 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    321       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000112003.
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      251    254       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     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   321 AA;  35176 MW;  46EE37FB657E8D12 CRC64;
     MKTIGILTSG GDAPGMNAAI RAVVRTGIYY GLKVKGIMRG FAGLVEDEVI DLGLSSVGDI
     IQKGGTILRT ARCEEFKQKE VRKKAYETLQ KHGIEGLVVI GGDGSFRGAQ LLSEEWNVNT
     ICIPGTIDND IPCTDYTIGF DTACNTVIDA INKIRDTATS HERANIIEVM GRNSGYIALY
     AGVAGGAEMI ILPEVEWSID ELCDKITYGI KRGKLHHIIV LAEGVMSAPE LAKMIKERLP
     KLDLRYTILG HIQRGGAPTV MDRVLASQMG ARAVELLLEN KTKRVISIRN NQIVDDDIDE
     ALSMKKEFNR KLYELSKILS I
//
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