KPYK_MYCPN
ID KPYK_MYCPN Reviewed; 508 AA.
AC P78031;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=MPN_303; ORFNames=MP533;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- ACTIVITY REGULATION: Regulated by phosphoenolpyruvate substrate and is
CC allosterically activated by ribose-5-phosphate, AMP and other
CC nucleoside monophosphates but not by fructose-1,6-bisphosphate.
CC {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INTERACTION:
CC P78031; P02788: LTF; Xeno; NbExp=3; IntAct=EBI-2259473, EBI-1058602;
CC P78031; P04004: VTN; Xeno; NbExp=3; IntAct=EBI-2259473, EBI-1036653;
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; U00089; AAB96181.1; -; Genomic_DNA.
DR PIR; S73859; S73859.
DR RefSeq; NP_109991.1; NC_000912.1.
DR RefSeq; WP_010874660.1; NC_000912.1.
DR AlphaFoldDB; P78031; -.
DR SMR; P78031; -.
DR IntAct; P78031; 5.
DR STRING; 272634.MPN_303; -.
DR PRIDE; P78031; -.
DR EnsemblBacteria; AAB96181; AAB96181; MPN_303.
DR GeneID; 66609050; -.
DR KEGG; mpn:MPN_303; -.
DR PATRIC; fig|272634.6.peg.327; -.
DR HOGENOM; CLU_015439_0_2_14; -.
DR OMA; QVPIVQK; -.
DR BioCyc; MPNE272634:G1GJ3-473-MON; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
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:0031639; P:plasminogen activation; IDA:AgBase.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..508
FT /note="Pyruvate kinase"
FT /id="PRO_0000112081"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 58..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 58
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 249
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 57268 MW; 011D97377F8BB527 CRC64;
MIHHLKRTKI IATCGPALTK KLWTLAMLDD PAYAAMKAEA YANIENIIKN GVTVIRLNFS
HGNHEEQAVR IKIVRDVAKK LNLPVSIMLD TNGPEIRVFE TAPEGLKILK DSEVVINTTT
KEVAKNNQFS VSDASGTYNM VNDVKVGQKI LVDDGKLSLV VKRIDTKNNQ VICVAQNDHT
IFTKKRLNLP NADYSIPFLS AKDLRDIDFG LTHQIDYIAA SFVNTTENIK QLRDYLASKN
AKHVKLIAKI ESNHALNNID GIIKASDGIM VARGDLGLEI PYYKVPYWQR YMIKACRFFN
KRVITATQML DSLEKNIQPT RAEVTDVYFA VDRGNDATML SGETANGAFP LNAVYVMKMI
DKQSETFFDY QYNLNYYMAN SKARHSEFWK QVVLPLAQKT APKRKLINSD FKYDFVVHAT
NNLNEIYALS NARLAAAVII LTNDPQVYTG HGVDYGIFPY LIDQKPQSLS KAEFKSLANV
AIKHYQQHGE ISQLKQCLGV FHNKIISL
