ID   A0A6L8PCL3_BACAN        Unreviewed;       352 AA.
AC   A0A6L8PCL3; A0A2B6C9J6; E9QRA9; E9QRB0; Q6HW95; Q6KQE6; Q81N35;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=pykA1 {ECO:0000313|EMBL:AAT32490.1};
GN   OrderedLocusNames=GBAA_3382 {ECO:0000313|EMBL:AAT32490.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT32490.1, ECO:0000313|Proteomes:UP000000594};
RN   [1] {ECO:0000313|EMBL:AAT32490.1, ECO:0000313|Proteomes:UP000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017334; AAT32490.1; -; Genomic_DNA.
DR   RefSeq; WP_000151131.1; NZ_WXXJ01000007.1.
DR   AlphaFoldDB; A0A6L8PCL3; -.
DR   GeneID; 45023138; -.
DR   KEGG; bar:GBAA_3382; -.
DR   PATRIC; fig|1392.230.peg.3332; -.
DR   OMA; DGPFAMK; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000000594; 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   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; 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   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel 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:AAT32490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AAT32490.1}.
FT   DOMAIN          6..318
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
SQ   SEQUENCE   352 AA;  38860 MW;  94A73CAB2AB03E85 CRC64;
     MTIDRVCTIG PASNNKETLA KLINNGMKIV RLNLSHGTHE SHKDIIRLVK SLDDSIKILG
     DVQGPKIRLG EIKGEQITLQ AGDSFMLRTQ PVTGSSTEAS VDYEGIANDV KVGSRILMND
     GEVELIVEKV STDKIETKVK TGGNISSHKG VNLPGAIVSL PAITEKDKKD IQFLLEEDVD
     FIACSFVRKP SHIKEIRDFI QQYKETSPNL IAKIETMEAI ENFQDICKEA DGIMIARGDL
     GVELPYQFIP LLQKMMIQEC NRTNTYVITA TQMLQSMVDH SIPTRAEVTD VFQAVLDGTN
     AVMLSAESAS GEHPVESVST LRLVSEFAEH VKKDGPFVMK DVLELLHKSL DE
//