ID B0JGV0_MICAN Unreviewed; 473 AA.
AC B0JGV0;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=MAE_55440 {ECO:0000313|EMBL:BAG05366.1};
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG05366.1, ECO:0000313|Proteomes:UP000001510};
RN [1] {ECO:0000313|EMBL:BAG05366.1, ECO:0000313|Proteomes:UP000001510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 {ECO:0000313|EMBL:BAG05366.1,
RC ECO:0000313|Proteomes:UP000001510};
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; AP009552; BAG05366.1; -; Genomic_DNA.
DR RefSeq; WP_002758171.1; NC_010296.1.
DR AlphaFoldDB; B0JGV0; -.
DR STRING; 449447.MAE_55440; -.
DR PaxDb; 449447-MAE_55440; -.
DR EnsemblBacteria; BAG05366; BAG05366; MAE_55440.
DR GeneID; 66705877; -.
DR KEGG; mar:MAE_55440; -.
DR PATRIC; fig|449447.4.peg.5059; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_3; -.
DR BioCyc; MAER449447:MAE_RS24100-MONOMER; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001510; 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; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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; 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 Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:BAG05366.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 6..328
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 357..470
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 473 AA; 52046 MW; 4A0A4523D6363CAD CRC64;
MSIITHRTKI VATIGPASNS PEVLKQMIGA GMNVARLNFS HGSYEDHARV VTLLRQISQE
LDNPITLLQD LQGPKIRVGN LPNGSITIND GDYLTLVPMD EYRGEANTVS IDYPYLAEEA
KLGEQILLDD GLLELKIVEI NGKDLKCQVL EGGILKSRKG VNLPRLNLRL PSMTEKDKQD
LEFGLSQGVD WVSLSFVRKG EDIKAIKAFL AERNHADMPV MAKIEKPQAI ENLESIIEEC
DGIMVARGDL GVELSPEKVP MLQKRIIKLC NMKTIPVITA TQMLESMINN PRPTRAEASD
VANAIIDGTD AVMLSGESAV GDFPVKAVAM LAKIAHDVEA DVKFDNAPPN QSDETHALSE
ALVAIDQTLD LRYIVTFTTS GYTSLLASKE RPSVPVIAMT PNKRVYHRLN LVWGVIPILL
DHQVSVFEDV LKQTESILLQ KNLAQSGDKI LIMAGIPMQK TKGTNFLKIH RIP
//
