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Database: UniProt
Entry: P72830
LinkDB: P72830
Original site: P72830 
ID   PFKA1_SYNY3             Reviewed;         361 AA.
AC   P72830;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   31-JAN-2018, entry version 123.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA1 {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfkA;
GN   OrderedLocusNames=sll1196;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA16845.1; -; Genomic_DNA.
DR   PIR; S74694; S74694.
DR   ProteinModelPortal; P72830; -.
DR   SMR; P72830; -.
DR   IntAct; P72830; 1.
DR   STRING; 1148.SYNGTS_0269; -.
DR   PaxDb; P72830; -.
DR   PRIDE; P72830; -.
DR   EnsemblBacteria; BAA16845; BAA16845; BAA16845.
DR   KEGG; syn:sll1196; -.
DR   HOGENOM; HOG000248869; -.
DR   InParanoid; P72830; -.
DR   KO; K21071; -.
DR   OMA; GKLHSII; -.
DR   PhylomeDB; P72830; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001425; 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   TIGRFAMs; TIGR02483; PFK_mixed; 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    361       ATP-dependent 6-phosphofructokinase 1.
FT                                /FTId=PRO_0000111998.
FT   NP_BIND      79     80       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   NP_BIND     116    119       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   REGION      140    142       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      184    186       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      284    287       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    142    142       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   METAL       117    117       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      14     14       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     177    177       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     237    237       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING     278    278       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   SITE        118    118       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   361 AA;  38588 MW;  96A83E05F318552C CRC64;
     MGEIKRIGIL TSGGDCAGLN AVIRSVVHHA IGTYGWEVIG IQEATQGLME NPSKAIALHR
     DNIDHLLMMG GTFLGTTNKG NPFAFPMADG TVRDRTEDII AGYRQLGLDA LIGIGGDGSL
     AILRRIAQQG GINLVGIPKT IDNDVGATEI SIGFDTATNI ATEALDRLHF TAASHNRVMV
     LEVMGRDAGH IALAAGIGGG ADIILIPEIP YRIQSVCNKI RQRQAEGKNF CLVMVSEAVR
     TELGDQVKQI QQFGEDRYGG IGKYIAEQIA QRTGAETRVT VLGHIQRGGI PSPFDRLLGS
     VFGVAAVDLI AEGKFDHMVA WRNRQTISVP IEEAIQTYQT VQLDGTLVKT ARGLGICLGN
     D
//
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