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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//