ID F6IRP2_LACPE Unreviewed; 586 AA.
AC F6IRP2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=LPE_00199 {ECO:0000313|EMBL:CCB81192.1};
OS Lactiplantibacillus pentosus MP-10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1028490 {ECO:0000313|EMBL:CCB81192.1};
RN [1] {ECO:0000313|EMBL:CCB81192.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP-10 {ECO:0000313|EMBL:CCB81192.1};
RX PubMed=21705590; DOI=10.1128/JB.05171-11;
RA Abriouel H., Benomar N., Perez Pulido R., Canamero M.M., Galvez A.;
RT "Annotated genome sequence of Lactobacillus pentosus MP-10, which has
RT probiotic potential, from naturally fermented Alorena green table olives.";
RL J. Bacteriol. 193:4559-4560(2011).
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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00006237}.
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DR EMBL; FR871761; CCB81192.1; -; Genomic_DNA.
DR RefSeq; WP_050338583.1; NZ_FLYG01000003.1.
DR AlphaFoldDB; F6IRP2; -.
DR GeneID; 49394120; -.
DR UniPathway; UPA00109; UER00188.
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; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom.
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; 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; PF00391; PEP-utilizers; 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.
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:CCB81192.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:CCB81192.1}.
FT DOMAIN 1..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 358..470
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT DOMAIN 507..576
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 586 AA; 62855 MW; 024AA879A5D3F942 CRC64;
MKKTKIVSTL GPASTDTDTI VKLIEAGANI FRFNFSHGDH EEHLDRLNKV HEAEKITGKT
VGIMLDTKGA EIRTTVQANG KSEYKIGDKV RISMDESLDT THDKIAVTYK NLYDDVHVGG
HVLFDDGLLD MKIDEKDEAN RELVTTVQNA GVLGSRKGVN APGVSINLPG ITEKDSSDIR
FGLDHEINYI AASFVRKPQD VLDIRELLEE KHMEHVQIFP KIESQEGIDN ADEILKVCDG
LMVARGDMGV EIPAENVPLV QKSLIKKCNA LGMPVITATQ MLDSMQENPR PTRAEASDVA
NAVFDGTDAT MLSGESANGL YPVESVAMMA KIDEKAENTL AENGSLQLNR FDKTSVTETI
GIAIARAAKN LNIKTIVAAT ESGYTAKMIS KYRPNADILA ITFDERTQRG LMVNWGVQPI
VADKPETTDD MFDLAASKAV ELGFAKEGDL ILITAGVPVG ERGTTNIMKI QLIGSKLADG
QGVGDETVIG KAVIATSAQE AIDKAVEGGV LVTKTTDKDY LPAIEKSSAL VVENGGLTSH
AAVVGISMGI PVIVGVKDAT SVISDGQLIT VDSRRGLVYR GASNAL
//
