ID A0A2Z3I7K2_9GAMM Unreviewed; 476 AA.
AC A0A2Z3I7K2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:AWM81661.1};
GN ORFNames=DKL61_01775 {ECO:0000313|EMBL:AWM81661.1};
OS Gammaproteobacteria bacterium ESL0073.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=2070539 {ECO:0000313|EMBL:AWM81661.1, ECO:0000313|Proteomes:UP000246096};
RN [1] {ECO:0000313|EMBL:AWM81661.1, ECO:0000313|Proteomes:UP000246096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESL0073 {ECO:0000313|EMBL:AWM81661.1,
RC ECO:0000313|Proteomes:UP000246096};
RA Ellegaard K.M.;
RT "Reference genomes for bee gut microbiota database.";
RL Submitted (MAY-2018) 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 -!- 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; CP029478; AWM81661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3I7K2; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000246096; 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:AWM81661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246096};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 2..323
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 51439 MW; A91D644B09AEF828 CRC64;
MMKKTKIVCT LGPATDSPDT LDQLLINGMN VARFNFSHGT HADHQARIAA IRESSKRLGI
PVAIMLDTKG PEMRLGCFIN GKVTLHKGQQ FILTTEDRLG DETIASINHQ NLPQEVQVGN
KILLADGLIE LTIQSIQKNH IITIVENTGG ISDRKRIAAP GVSLGLPPVS EKDIEDILFG
IEQDIDFIAA SFIQRASDVQ LIKKILNDHN ASIQIISKIE NAEGVKNMTE ILEVSDGLMV
ARGDLGVEIP AEEVPLIQKE MIKLCNKLGK PVITATQMLE SMISNPRPTR AEASDVANAI
LDGTDAIMLS GETASGQYPV EAVKTMSLLA KRTEQAIDCE TALIHSGFKR TNTTDAISHA
CVQIAVELNI KGIIIPTESG FTAQMVSRYK PQPFIFAVTP HEKTVRRLQL IWGVIALQGN
QSSNTDSMTK EAIQCCLNTG HIKVGDLVEV TAGIPIGTQG STNMIQVHIA GNSLGS
//