ID Q31QP5_SYNE7 Unreviewed; 360 AA.
AC Q31QP5;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=6-phosphofructokinase {ECO:0000313|EMBL:ABB56624.1};
DE EC=2.7.1.11 {ECO:0000313|EMBL:ABB56624.1};
GN OrderedLocusNames=Synpcc7942_0592 {ECO:0000313|EMBL:ABB56624.1};
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56624.1, ECO:0000313|Proteomes:UP000889800};
RN [1] {ECO:0000313|Proteomes:UP000889800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC {ECO:0000313|Proteomes:UP000889800};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004679}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC {ECO:0000256|ARBA:ARBA00038478}.
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DR EMBL; CP000100; ABB56624.1; -; Genomic_DNA.
DR RefSeq; WP_011377635.1; NZ_JACJTX010000006.1.
DR AlphaFoldDB; Q31QP5; -.
DR STRING; 1140.Synpcc7942_0592; -.
DR PaxDb; 1140-Synpcc7942_0592; -.
DR GeneID; 76399341; -.
DR KEGG; syf:Synpcc7942_0592; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_0_3; -.
DR OrthoDB; 9802503at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0592-MONOMER; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000889800; 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: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 Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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; IPR035966; PKF_sf.
DR PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000889800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABB56624.1}.
FT DOMAIN 5..294
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 360 AA; 38021 MW; F221D8011165123A CRC64;
MAVRKLGVLT SGGDCPGLNA VIRAIARHAV GNYGWELWGI AYATQGLLKR QAIALSPHHF
DRQSLDPLLC SGGTILGSIN RGDTLAHQAE ILAGYQELGL DALIGIGGDG SLAILRQLAE
AGRWQFIGIP KTIDNDVALT ERAIGFDTAI HTVAEALLSL GSTAASHDRI MIAEVMGRQS
GHLALQGGIA GGADVILLPE IPYRLLELCH YLQQLRDRWQ RRYAVIAIAE GTHHPPEVTQ
GPGSLGEQLV QAITAQDPTL DARVTVLGHV QRGGNPVASD RLLATQMGYA AVERLAAGAS
GEMMAWQGGR VVSVPLEAVC LQSPTLVDPH SPLVDTAAGL GIFLGDRSLT PWRGSACPTH
//
