ID Q6YQT6_ONYPE Unreviewed; 446 AA.
AC Q6YQT6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=pykF {ECO:0000313|EMBL:BAD04372.1};
GN OrderedLocusNames=PAM_287 {ECO:0000313|EMBL:BAD04372.1};
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=262768 {ECO:0000313|EMBL:BAD04372.1, ECO:0000313|Proteomes:UP000002523};
RN [1] {ECO:0000313|EMBL:BAD04372.1, ECO:0000313|Proteomes:UP000002523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M {ECO:0000313|Proteomes:UP000002523};
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04372.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQT6; -.
DR STRING; 262768.PAM_287; -.
DR KEGG; poy:PAM_287; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_0_14; -.
DR BioCyc; OYEL262768:G1G26-345-MONOMER; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002523; 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:BAD04372.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 2..324
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..430
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 446 AA; 50088 MW; 748E3520F812FF58 CRC64;
MNKTKIICTL GPASYDKNIL QALIQTGLNV ARFNFSHAQY EQTKLLMKTI KTISDKLDKN
TGLMLDTKGP EIRTHEFDGV VTIQKDSEVK ISMTEVLGNA KLFSVSYSNL YNELKVGDMV
NIDDGYLSLE VVGKDEAKQQ LVTKAKNTHS IKSRRGVNVP KVNLEMDFIS PKDYQDIVFA
AQQDFDYIAA SFVRRAQDVK DIRKILQEQG NSNIQIISKI ENQEGVDNLE EIIQESDGIM
VARGDLGIEV DGELVPLYQT RMITKCLEYG KPVVVATQML ESMQRNPRPT KAETSDVFNA
VREGTTFTML SGESASGEYP VEAVTYMKKI NYQAEKVVNY QALSQVYQPK NSKENLLLSA
VELALRTDVK AIVVYDLKDA YNVSKFHPSV PVLALVKTEQ EARRLVLNFG VCPFVSETKL
QTKLEELTQN QSSNCLVVKD GMLYFK
//
