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Database: UniProt
Entry: K9SQ21_9SYNE
LinkDB: K9SQ21_9SYNE
Original site: K9SQ21_9SYNE 
ID   K9SQ21_9SYNE            Unreviewed;       813 AA.
AC   K9SQ21;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE            Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN   ORFNames=Syn7502_00090 {ECO:0000313|EMBL:AFY72263.1};
OS   Synechococcus sp. PCC 7502.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72263.1, ECO:0000313|Proteomes:UP000010385};
RN   [1] {ECO:0000313|EMBL:AFY72263.1, ECO:0000313|Proteomes:UP000010385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72263.1,
RC   ECO:0000313|Proteomes:UP000010385};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC       ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001518,
CC         ECO:0000256|PIRNR:PIRNR000854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR   EMBL; CP003594; AFY72263.1; -; Genomic_DNA.
DR   RefSeq; WP_015166922.1; NC_019702.1.
DR   AlphaFoldDB; K9SQ21; -.
DR   STRING; 1173263.Syn7502_00090; -.
DR   KEGG; synp:Syn7502_00090; -.
DR   PATRIC; fig|1173263.3.peg.92; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_007308_6_2_3; -.
DR   OrthoDB; 9765468at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000010385; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01418; PEP_synth; 1.
DR   PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   PIRSF; PIRSF000854; PEP_synthase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000854};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:AFY72263.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010385};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          33..363
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          404..475
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          498..809
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   813 AA;  89002 MW;  85149AA4C8E14411 CRC64;
     MTCTDILGRK GGTDCKEDAF VLWFDQVGIA DIPLVGGKNA SLGEMIRELK VKGVSVPNGF
     ATTAHAYRYF IQASGIDDKL RQLFAMLDVE NINSLRCVGK QARSLILNTP MPIVIQEAIG
     RAYAQLCGEY GVETDVAVRS SATAEDLPDA SFAGQQETYL NVHGLSTVLM ACQKCFASIF
     TDRAISYRTI KGFDHFSIAL SVGVQKMVRS DLATSGVMFS IDTETGFRNA ALVTAAYGLG
     ENVVQGAVNP DEYLVFKPTL KQGFRPIISK RMGSKEIKMI YDLGGSKLTK NVSVPTSEQN
     CFALSDDEIL QLAKWAVIIE DHYSLVRGQD SPMDIEWAKD GETGKLFIVQ ARPETVESQK
     SQSVLRNYHL QEQSKVLTTG RAVGAMIGQG KARIILDAPN LDQFQAGEVL VTNKTDPDWE
     PIMKKASAIV TNQGGRTCHA AIIARELGIP AIVGCGDASS AIANGQAITV SCAEGEEGRV
     YTGLLPFEIE ETNLDHLPRT RTKILMNVGN PEVAFGLSAI PCDGVGLARF EFIIANHIKA
     HPLALIHFDQ LKDFFEKQQI ARLTVGYPHK PDFFVDKLTS GVAMIAAAFY PKPVVVRMSD
     FKSNEYANLL GGKQFEPSEE NPMIGWRGAS RYYDPKYSEA YGLECQAIKR VRDQMGLTNV
     IPMIPFCRTP DEGRKVLAEM EKHGLKRGEN GLQVYVMCEI PSNVILAEQF SEVFDGFSIG
     SNDLTQLTLG LDRDSALIAH IFDERNEAVK QMISMVIAKV KECDRKIGIC GQAPSDYPEF
     ARFLVKEGID SISLNPDSLL KTMLAIAAAE SGQ
//
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