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Entry: I4EZK0_9ACTN
LinkDB: I4EZK0_9ACTN
Original site: I4EZK0_9ACTN 
ID   I4EZK0_9ACTN            Unreviewed;       471 AA.
AC   I4EZK0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE            EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN   Name=pyk {ECO:0000313|EMBL:CCH88813.1};
GN   OrderedLocusNames=MODMU_3401 {ECO:0000313|EMBL:CCH88813.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88813.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH88813.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH88813.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
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; FO203431; CCH88813.1; -; Genomic_DNA.
DR   RefSeq; WP_014741397.1; NC_017955.1.
DR   AlphaFoldDB; I4EZK0; -.
DR   STRING; 477641.MODMU_3401; -.
DR   KEGG; mmar:MODMU_3401; -.
DR   PATRIC; fig|477641.3.peg.3219; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_0_2_11; -.
DR   OMA; RVHHIGE; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000006461; 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; 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:CCH88813.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:CCH88813.1}.
FT   DOMAIN          3..323
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          353..465
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   471 AA;  50195 MW;  51CE2C024C1814BE CRC64;
     MSRRAKIVCT LGPATGSLEQ ITALVEAGMD VARLNFSHGK HADHETAYRN VRAASDTVGR
     AVAVLADLQG PKIRLGTFAD GPVVWETGSR VCITVEDVPG TADRVSTTYK DLANDARVGD
     RLLVDDGKLA LTVVDVTGPD VFCLVLEGGP VSNNKGLSLP GVAVSVPAMS EKDAEDLRFA
     LSLGVDFVAL SFVRHARDVE LVREIMRQED VEVPVIAKLE KPEAVENLDA IVKAFDGIMV
     ARGDLGVELP LEQVPLVQKR AVQAARERNK PVIVATQMLE SMIENSRPTR AEASDVANAV
     LDGADAVMLS GETSVGKYPI VAVKTMERII DAVETDEVRV PELSRPRNNR SGAIVRAAKD
     IGEALDVSAL AAFTLTGKTA QLLAALHTRL PILAFTTDPA VRSRLALSWG VETFLVPEVT
     HTDDMVGQVD FSLMSIGRLR EGDKVVVVAG SPPNTAGSTN LVRVHEVGTE A
//
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