KPYK_COREF
ID KPYK_COREF Reviewed; 474 AA.
AC Q8FP04;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=CE1989;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC18799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18799.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006767987.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FP04; -.
DR SMR; Q8FP04; -.
DR STRING; 196164.23493830; -.
DR PRIDE; Q8FP04; -.
DR EnsemblBacteria; BAC18799; BAC18799; BAC18799.
DR KEGG; cef:CE1989; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_11; -.
DR OrthoDB; 1098983at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001409; 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 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; IPR015795; Pyrv_Knase_C.
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 Pfam; PF02887; PK_C; 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 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..474
FT /note="Pyruvate kinase"
FT /id="PRO_0000112067"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 35..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 35
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 218
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 51504 MW; AC0E634D219A5BCE CRC64;
MERRTKIVCT LGPAVASADG ILRLVQDGMD VARLNFSHGD HPDHEQNYKW VREATDKTGR
AVGILADLQG PKIRLGRFKE GSTVWETGET VRITVDDVEG THDRVSTTYK NLAKDARPGD
RLLVDDGKVG LVCVSVEGND VICEVTEGGP VSNNKGVSLP GMDISVPALS EKDIKDLRFA
LKLGVDFIAL SFVRSPADVE LVHAIMDEEG RRVPVIAKLE KPEAVAALES IVLAFDAIMV
ARGDLGVEVP LEEVPLVQKR AIQIARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV
LDGADAVMLS GETSVGKDPH NVVRTMSRIV RFAETDGRVP DLTHIPRTKR GVISYSARDI
AERLNARALV AFTTSGDTAK RLARLHSHLP LLVFTPDPSV RSQLALTWGA QTFLCPKVDD
TDGMMREVDR ALLAMDEYQK DDMMVVVAGS PPGVTGNTNM IHVHLLGEDT RIPK
