ID F9U818_9GAMM Unreviewed; 480 AA.
AC F9U818;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ORFNames=ThimaDRAFT_1244 {ECO:0000313|EMBL:EGV19798.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV19798.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV19798.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV19798.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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=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 -!- 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; AFWV01000003; EGV19798.1; -; Genomic_DNA.
DR RefSeq; WP_007192121.1; NZ_AFWV01000003.1.
DR AlphaFoldDB; F9U818; -.
DR STRING; 768671.ThimaDRAFT_1244; -.
DR PATRIC; fig|768671.3.peg.1330; -.
DR eggNOG; COG0469; Bacteria.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000005459; Unassembled WGS sequence.
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:SF125; PYRUVATE KINASE II; 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:EGV19798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EGV19798.1}.
FT DOMAIN 3..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..469
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 480 AA; 52076 MW; B1DEF1F8FFB1BE7D CRC64;
MPRRTKIVAT LGPATDPVSV MDEIIAAGVD VVRLNLSHDT HDRHRERAEA IRERAAAAGR
EIAILMDLQG PKIRIGKFAD GPIRLERGEH FAIDADCPLH AGDRNRVGTT YPELVDDVRH
GDTLLLDDGA IELWVEAVDG GRINCKVVVG GALSNNKGIN KKGGGLSAPA LTEKDQEDIR
FAAEIDADYL AVSFVRNGDD VRLARELFHE AGGHGGIVAK IERAESLRAI DDIINAADVI
MVARGDLGVE IGDAELPAAQ KNLISRAREL NSVVITATQM MQSMIENPIP TRAEVFDVAN
AVLDGTDAVM LSAESSIGKN PAKVVEALDR ICLEAEKHVT RSGHRIDSVF GRVDEAIAMA
AMYTANHLGV KAIAALTETG STVKWMSRIR SGIPIYAITR SAPTRRKVRV FRGVYPVSFD
VSSTDIHEVN REVIEELMRR GTVRDGDLVI ITKGDRSGVE GQTNILKIMR VGEHKLLTKD
//
