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Database: UniProt
Entry: J7LBW0_NOCAA
LinkDB: J7LBW0_NOCAA
Original site: J7LBW0_NOCAA 
ID   J7LBW0_NOCAA            Unreviewed;       452 AA.
AC   J7LBW0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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:AFR08895.1};
GN   OrderedLocusNames=B005_3866 {ECO:0000313|EMBL:AFR08895.1};
OS   Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR08895.1, ECO:0000313|Proteomes:UP000003779};
RN   [1] {ECO:0000313|EMBL:AFR08895.1, ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX   PubMed=23105086; DOI=10.1128/JB.01522-12;
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT   Associated with Honeybees.";
RL   J. Bacteriol. 194:6358-6359(2012).
RN   [2] {ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT   with honeybees.";
RL   Submitted (AUG-2012) 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}.
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DR   EMBL; CP003788; AFR08895.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7LBW0; -.
DR   STRING; 1205910.B005_3866; -.
DR   KEGG; nal:B005_3866; -.
DR   PATRIC; fig|1205910.3.peg.3661; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_0_2_11; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000003779; 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; 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:AFR08895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003779};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AFR08895.1}.
FT   DOMAIN          2..299
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          330..442
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   452 AA;  48220 MW;  14A02FFF70A70414 CRC64;
     MDAGLDVARL NLSHGTHDDH LAGLTNLRQA AKDAGRAVGV LADLQGPKIR VGTFPDGPIE
     LAEGDEFTIT TEDVPGDSTR VSTTYKGLPG DVRPGDRVLI DDGRVVLECT KTTSTDVQTR
     VIFGGPVSNH KGLNLPGVAV SVPALTDKDE EDLRWALHQG VDMVALSFVR SPADAEECHR
     IMDEEGITVP LIAKIEKPQA VERLHDIIEV FDGVMVARGD LGVELPLENV PMVQKRAIER
     CRDKAKPVIV ATQMLESMIG APRPTRAEAS DVANAVLDGA DAVMLSGETS VGKYPIETVE
     TMARIVGAAE QESLRASHIL NRVPETTGGA IARAAAEIGA TVGAKALVAF TMSGETARRL
     ARYRSPIPLL AFTTEASTRG RLSLTWGAET NLVPWVDNTD DMVRQVESEL LRLGDYNKGD
     KIVIVAGSPP GTPGSTNFLR VHRLGDTVSL SS
//
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