ID T0S876_LACLC Unreviewed; 502 AA.
AC T0S876;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=LLT6_03520 {ECO:0000313|EMBL:EQC54696.1};
OS Lactococcus cremoris subsp. cremoris TIFN6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234876 {ECO:0000313|EMBL:EQC54696.1, ECO:0000313|Proteomes:UP000015854};
RN [1] {ECO:0000313|EMBL:EQC54696.1, ECO:0000313|Proteomes:UP000015854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN6 {ECO:0000313|EMBL:EQC54696.1,
RC ECO:0000313|Proteomes:UP000015854};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(2013).
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQC54696.1}.
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DR EMBL; ATBB01000537; EQC54696.1; -; Genomic_DNA.
DR AlphaFoldDB; T0S876; -.
DR PATRIC; fig|1234876.3.peg.2221; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000015854; Unassembled WGS sequence.
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 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:EQC54696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015854};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..355
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 388..498
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 502 AA; 54334 MW; 7FEFA426C5F2F333 CRC64;
MNKRVKIVST LGPAVEIRGG KKFGESGYWG ESLDVEASAK NIAALIEEGA NVFRFNFSHG
DHPEQGARMA TVHRAEEIAG HKVGFLLDTK GPEMRTELFT DGADSISVVT GDKFRVATKQ
GLKSTPELIA LNVAGGLDIF DDVEIGQTIL IDDGKLGLSL TGKDAATREF EVEAQNDGVI
GKQKGVNIPN TKIPFPALAE RDDADIRFGL SQPGGINFIA ISFVRTANDV KEVRRICEET
GNPHVQLLAK IENQQGIENL DEIIEAADGI MIARGDMGIE VPFEMVPVYQ KLIISKVNKA
GKIVVTATNM LESMTYNPRA TRSEISDVFN AVIDGTDATM LSGESANGKY PRESVRTMAT
VNKNAQTMLK EYGRLHPERY DKSTVTEVVA ASVKNAAEAM DVKLIVALTE SGNTARLISK
HRPDADILAI TFDEKVERGL MINWGVIPMM TEKPASTDDM FEVAEKFALA SGLVEAGDNI
IIVAGVPVGT GRTNTMRIRT VK
//
