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Database: UniProt
Entry: Q8DJB1
LinkDB: Q8DJB1
Original site: Q8DJB1 
ID   PFKA_THEEB              Reviewed;         369 AA.
AC   Q8DJB1;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   28-FEB-2018, entry version 92.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01976};
GN   OrderedLocusNames=tll1316;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(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_01976}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
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_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01976}.
DR   EMBL; BA000039; BAC08868.1; -; Genomic_DNA.
DR   RefSeq; NP_682106.1; NC_004113.1.
DR   RefSeq; WP_011057156.1; NC_004113.1.
DR   ProteinModelPortal; Q8DJB1; -.
DR   SMR; Q8DJB1; -.
DR   STRING; 197221.tll1316; -.
DR   EnsemblBacteria; BAC08868; BAC08868; BAC08868.
DR   GeneID; 1012416; -.
DR   KEGG; tel:tll1316; -.
DR   PATRIC; fig|197221.4.peg.1384; -.
DR   eggNOG; ENOG4107R1X; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248869; -.
DR   KO; K21071; -.
DR   OMA; RDGWRGP; -.
DR   OrthoDB; POG091H01AC; -.
DR   BioCyc; TELO197221:G1G3I-1340-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000440; 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
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_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
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   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    369       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000111997.
FT   NP_BIND      81     82       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   NP_BIND     108    111       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   REGION      132    134       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      176    178       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      272    275       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    134    134       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   METAL       109    109       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      15     15       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     169    169       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     230    230       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING     266    266       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   SITE        110    110       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   369 AA;  39271 MW;  2FE4A8C249105916 CRC64;
     MSSSRKRLGV FTSGGDCPGL NTAIRAIVAH ATLSYGWEVL GILHATQGLI ERKAIPLNAE
     GLGGMDVLLN MGGTILGAIN KGDTLGHADE VIAGYYELGL DALIAICGDG SLRILHQLAQ
     KGNWNFLAIP KTIDNDVALT DRAIGFDTAV NTVVEALNRI TSTAASHDRV FVVEVMGRTA
     GHLALYSGIA GGADIILIPE IPYSIEGICQ HLQKLRDRWG RQFALIVVAE GSKQLEEDAN
     HPRHCSIGQY IADKIAQHSP IPIELRVSVL GHIQRGGAPM AMDRLLAAGM GNTAVDLAAQ
     GTFGRMVAWQ AGQVVTVPIA DVVAKCPRHV DPNSFLIRTA QGLGIYVGDK PMLPYVDPTL
     CRDQVICAI
//
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