ID A0A0K1NCQ8_9BURK Unreviewed; 493 AA.
AC A0A0K1NCQ8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=ADJ79_05830 {ECO:0000313|EMBL:AKU66864.1};
OS Ottowia sp. oral taxon 894.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU66864.1, ECO:0000313|Proteomes:UP000056623};
RN [1] {ECO:0000313|Proteomes:UP000056623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-2015) 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=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; CP012073; AKU66864.1; -; Genomic_DNA.
DR RefSeq; WP_050715172.1; NZ_CP012073.1.
DR AlphaFoldDB; A0A0K1NCQ8; -.
DR STRING; 1658672.ADJ79_05830; -.
DR KEGG; oto:ADJ79_05830; -.
DR PATRIC; fig|1658672.3.peg.1545; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000056623; 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; 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.
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:AKU66864.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 20..344
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 377..489
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 493 AA; 52230 MW; 15F04CC266F82141 CRC64;
MPVSSAAASV LTGNPIVDQA TKIVATLGPA SSDAQVIESM IRAGLDVVRL NFSHGNAQDH
IARAQRVREA SRRVGREVAI MADLQGPKIR VGKFAQGKVQ LREGAPFILD AARQEPGDEH
AVGLDYKELP GDVKAGDVLL LNDGLIVLDV QRVAGDAVHT VVRVGGELSD NKGINKQGGG
LTAAALTAKD MEDIKTAIGL QADYVAVSFP KSGTDMEMAR QLCNVAAAGQ RHRPGLIAKI
ERAEAIANLK EILLASDGIM VARGDLAVEV GHAAVPALQK RMIRLAREHD RLIITATQMM
ESMINNPVPT RAEVSDVANA VLDGTDAVML SAETAAGRYP LETVQAMASV CEEAEKHMAA
SDHEYDGSHS HLPRIDQAIA ASALHAAALV GAKAIVALTD SGSTALWMSR RRIGIPIYAL
TPRVATQRKM ALYRNVIPML MDTSADRDEA LRQAESCLLR HGVMSQGDIY AITCGEPMGA
PGGTNMLKIS RVG
//
