ID KPYK_CORGL Reviewed; 475 AA.
AC Q46078;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=Cgl2089, cg2291;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=8074528; DOI=10.1128/aem.60.7.2501-2507.1994;
RA Jetten M.S., Gubler M.E., Lee S.H., Sinskey A.J.;
RT "Structural and functional analysis of pyruvate kinase from Corynebacterium
RT glutamicum.";
RL Appl. Environ. Microbiol. 60:2501-2507(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF20425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L27126; AAA56793.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99482.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20425.1; ALT_INIT; Genomic_DNA.
DR PIR; I40840; I40840.
DR RefSeq; NP_601288.2; NC_003450.3.
DR RefSeq; WP_011014873.1; NC_006958.1.
DR AlphaFoldDB; Q46078; -.
DR SMR; Q46078; -.
DR STRING; 196627.cg2291; -.
DR World-2DPAGE; 0001:Q46078; -.
DR KEGG; cgb:cg2291; -.
DR KEGG; cgl:Cgl2089; -.
DR PATRIC; fig|196627.13.peg.2025; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_11; -.
DR OrthoDB; 9812123at2; -.
DR BioCyc; CORYNE:G18NG-11681-MONOMER; -.
DR BRENDA; 2.7.1.40; 960.
DR SABIO-RK; Q46078; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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 1: Evidence at protein level;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..475
FT /note="Pyruvate kinase"
FT /id="PRO_0000112068"
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 475 AA; 51471 MW; 4E56A16C570A5386 CRC64;
MDRRTKIVCT LGPAVASADG ILRLVEDGMD VARLNFSHGD HPDHEQNYKW VREAAEKTGR
AVGILADLQG PKIRLGRFTD GATVWENGET IRITVDDVEG THDRVSTTYK NLAKDAKPGD
RLLVDDGKVG LVCVSVEGND VICEVVEGGP VSNNKGVSLP GMDISVPALS EKDIRDLRFA
LKLGVDFIAL SFVRSPADAE LVHKIMDEEG RRVPVIAKLE KPEAVTSLEP IVLAFDAVMV
ARGDLGVEVP LEEVPLVQKR AIQIARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV
LDGADAVMLS GETSVGKDPH NVVRTMSRIV RFAETDGRVP DLTHIPRTKR GVISYSARDI
AERLNARALV AFTTSGDTAK RVARLHSHLP LLVFTPNEAV RSELALTWGA TTFLCPPVSD
TDDMMREVDR ALLAMPEYNK GDMMVVVAGS PPGVTGNTNM IHVHLLGDDT RIAKL
//
