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Database: UniProt
Entry: A0A073AYU2_9PSEU
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ID   A0A073AYU2_9PSEU        Unreviewed;       473 AA.
AC   A0A073AYU2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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   ORFNames=GU90_10060 {ECO:0000313|EMBL:KEI44501.1};
OS   Saccharopolyspora rectivirgula.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI44501.1, ECO:0000313|Proteomes:UP000031419};
RN   [1] {ECO:0000313|EMBL:KEI44501.1, ECO:0000313|Proteomes:UP000031419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI44501.1,
RC   ECO:0000313|Proteomes:UP000031419};
RA   Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT   "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL   Submitted (JUN-2014) 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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEI44501.1}.
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DR   EMBL; JNVU01000025; KEI44501.1; -; Genomic_DNA.
DR   RefSeq; WP_029719440.1; NZ_JNVU01000025.1.
DR   AlphaFoldDB; A0A073AYU2; -.
DR   STRING; 28042.GU90_10060; -.
DR   eggNOG; COG0469; Bacteria.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000031419; 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; 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; 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.
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:KEI44501.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031419};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KEI44501.1}.
FT   DOMAIN          3..323
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          354..465
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   473 AA;  50935 MW;  E879BF3F40A35041 CRC64;
     MSRRAKIVCT MGPATATPEK VAELVSSGMN VARLNFSHGS HEDHRQVYEM VRAAAKESGR
     AVGILADLQG PKIRLGKFAA GPVEWRTGDV VRITVDDVQG THDRVSTTYK GLANDAKPGD
     SLLVDDGKVG LVVREVDGND VVCEVVEGGP VSDHKGLSMP GMDISVPALS EKDVEDLEFA
     LELGVDFIAL SFVRSPADID VVHQVMDRVG RRAPVIAKLE KPEAVENLEA IVLAFDGIMV
     ARGDLGVELP LEHVPLVQKK AIRIARENAK PIIVATQMLD SMINNSRPTR AEASDVANAV
     LDGTDAVMLS GETSVGRYPV ETVQTMARIV EAVEAGSTTP PPLSHVPRTK RGVISYAARD
     IGERLNAKAL VAFTQSGDTV RRLARLHTRL PLLAFTPEES VRSQLALTWG TETFLVPKVD
     TTDQMVRQVD QAMLSLGRYQ RGDMVVIVAG SPPGTVGSTN LIRVHRLGEE DHV
//
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