ID C6DK89_PECCP Unreviewed; 470 AA.
AC C6DK89;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN OrderedLocusNames=PC1_2441 {ECO:0000313|EMBL:ACT13472.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13472.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT13472.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT13472.1,
RC ECO:0000313|Proteomes:UP000002736};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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}.
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DR EMBL; CP001657; ACT13472.1; -; Genomic_DNA.
DR RefSeq; WP_015840654.1; NC_012917.1.
DR AlphaFoldDB; C6DK89; -.
DR STRING; 561230.PC1_2441; -.
DR KEGG; pct:PC1_2441; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_0_6; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002736; 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 CDD; cd00288; Pyruvate_Kinase; 1.
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; IPR018209; Pyrv_Knase_AS.
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; 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.
DR PROSITE; PS00110; PYRUVATE_KINASE; 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:ACT13472.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ACT13472.1}.
FT DOMAIN 1..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 470 AA; 50413 MW; AA668A47B2F40E04 CRC64;
MKKTKIVCTI GPKTESEEML GNLLSAGMNV MRLNFSHGDY AEHGQRIKNL RAVTEKTGKK
AAILLDTKGP EIRTMKLENG ADVTLTAGQT FTFTTDQSIV GNKDRVAVTY AGFTEDLSVG
NTVLVDDGLI GMQVTAINGN DVVCKVLNNG DLGENKGVNL PGVSIQLPAL AEKDKRDLIF
GCEQGVDFVA ASFIRKRSDV EEIRAHLKAH GGEHIQIISK IENQEGLNNF DEILEASDGI
MVARGDLGVE IPVEEVIFAQ KMMIEKCNLA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
AIIDGTDAVM LSGESAKGKY PLESVTIMAT ICQRTDSVMK SRLDTIKTPG VLRITEAVCR
GAVETAEKLD APLIVVATSG GKSAKSIRKY FPNARILALT TNEVTARQLL LSKGIDTLLV
KEIASTDDFY RIGKEAALNS GYAQAGDVVV MVSGALVSSG TTNTSSVHRL
//
