ID F7WZD1_9GAMM Unreviewed; 460 AA.
AC F7WZD1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pykA {ECO:0000313|EMBL:AEH39793.1};
GN ORFNames=BCTU_208 {ECO:0000313|EMBL:AEH39793.1};
OS Buchnera aphidicola (Cinara tujafilina).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=261317 {ECO:0000313|EMBL:AEH39793.1, ECO:0000313|Proteomes:UP000006811};
RN [1] {ECO:0000313|EMBL:AEH39793.1, ECO:0000313|Proteomes:UP000006811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cinara tujafilina {ECO:0000313|Proteomes:UP000006811};
RX PubMed=21571878; DOI=10.1128/AEM.00141-11;
RA Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT "The genome of Buchnera aphidicola from the aphid Cinara tujafilina
RT provides new clues about the evolutionary history of metabolic losses in
RT bacterial endosymbionts.";
RL Appl. Environ. Microbiol. 77:4446-4454(2011).
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; CP001817; AEH39793.1; -; Genomic_DNA.
DR AlphaFoldDB; F7WZD1; -.
DR STRING; 261317.BCTU_208; -.
DR KEGG; baj:BCTU_208; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_8_0_6; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000006811; 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:SF125; PYRUVATE KINASE II; 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:AEH39793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006811};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 7..331
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 363..454
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 460 AA; 50865 MW; 14C417D553CFD43C CRC64;
MHNDICRTKI VSTLGPSTNS KSIIKKLIQS GSKILRLNFS HGTAEEHKKR VKSIREITKK
YGYSVAIIGD LQGPKIRISS FKNKKIFLDV GDTFLLDHTI PKFHGNKKKV GISYKNLPFE
VVVNDLILLD DGKIQLKVLE IDNNKIYTKV VIGGTLTDNK GLNKLGGGLS AKALTKKDKE
DIKLASKLGI DYLAVSFPRS AADIQEARTL MKNAGSNAQI IAKIERAEAV MSDIVIKEII
LAADAIMIAR GDLGVEIGDD KLIGVQKHLI QLARQLNRTV ITATQMMESM IDNPFPTRAE
VMDVANAVID GTDAVMLSAE TASGHFPINT VQSVLKICQG AEKLPCMHIS KHRLGLKFYN
ISETLAMSIM YAANHLKNVS AILIYTDSLD IALLTSRITS RIPIFYFSYC QKNLNLSTLY
KGVIPIYIEK KQMELNNIDD AISIIKEKKG VQKKMIISLL
//
