ID K9YHQ2_CYASC Unreviewed; 592 AA.
AC K9YHQ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN OrderedLocusNames=Cyast_0517 {ECO:0000313|EMBL:AFZ46496.1};
OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ46496.1, ECO:0000313|Proteomes:UP000010483};
RN [1] {ECO:0000313|Proteomes:UP000010483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00006237}.
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DR EMBL; CP003940; AFZ46496.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YHQ2; -.
DR STRING; 292563.Cyast_0517; -.
DR KEGG; csn:Cyast_0517; -.
DR PATRIC; fig|292563.3.peg.538; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_3; -.
DR BioCyc; CSTA292563:G1353-521-MONOMER; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000010483; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AFZ46496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010483};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AFZ46496.1}.
FT DOMAIN 7..329
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 361..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 507..578
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 592 AA; 64294 MW; 4E3EDAD239804FC6 CRC64;
MSEKFSRRTK IVATVGPGCA NPETLRKMIL AGANTFRLNF SHGTHEVHQS SIRMIRQVEN
ELNRPIGILQ DLQGPKIRLG KYECGSIELH EGDRYVLTSR DVKCDEKIAC ISYEYLAEEV
PLNARILLDD GRVEMVVKEI DKENKDLHCQ VVVGGVLSSN KGVNFPNVYL SVKALTEKDK
KDLMFGLDQR VDWVALSFVR NPQDVLEIKD LIASAGKSTP VIAKIEKHEA IEQMEEILSL
CDGVMVARGD LGVELPAEDV PILQKRLIRT ANRLGIPIIT ATQMLDSMAN SPSPTRAEVS
DVANAILDGT DAVMLSNETA VGKYPVQAVA TMAKIARRTE EERDSIAPHL LSPMDNQNIP
NAISGAVGQI AKQLKASAIM TLTKTGATAR NVSKFRPKTP ILAITPHVSV SRQLQLVWGV
KPLLLLDMPG LKQVFSSAIE LAREEELLED GNLVVMTAGT LQGVAGSTDL IKVEIVKGLL
SEGLGIGQGI ITGRTKVVYD INNLTNFNQG DILVAKSTDN NYVDAMRLAS GIITEEGGVR
SHAAQIGMRL GIPVIVGVKD ATRIIRDASF VTMKIEQGLV YLGTDGSQDG VD
//
