ID A0A143YMT5_9LACT Unreviewed; 476 AA.
AC A0A143YMT5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=Tpal_1548 {ECO:0000313|EMBL:CZQ92817.1};
OS Trichococcus palustris.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=140314 {ECO:0000313|EMBL:CZQ92817.1, ECO:0000313|Proteomes:UP000242754};
RN [1] {ECO:0000313|EMBL:CZQ92817.1, ECO:0000313|Proteomes:UP000242754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus palustris {ECO:0000313|EMBL:CZQ92817.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; FJNE01000004; CZQ92817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143YMT5; -.
DR STRING; 140314.SAMN04488076_11654; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000242754; 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; 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; 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:CZQ92817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242754};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 51131 MW; F5D31125A40D3089 CRC64;
MVKKTKIVCT IGPASDSIDT LVKMINNGMN VARLNFSHGE HETHLGSLNN VREAARQANQ
VVGIMLDIQG QKIRTHKMTD DAVTLTTGDT VRISMDQVLG TKDKFSVTYP TLIDDVTIGM
HILIDDGLLV LQITDIDYET KEIIAVVQTG GVLKNSKGIN VPEAKFSMPG LTEKDAADIR
FGAEHGVDYI AASFVRKPSD ILEIIAILEE MDAADTQIIA KIENQEGVQN AEAILSVCSG
LMVARGDLGV EINGGDVPIV QKDLIRKCNI AGKQVITATQ MLDSMQWNPR PTRAEASDVA
NAIFDGTDAV MLSGESAVGK YPVETVAMMA RIAVRAEEAL DVNGGHLTMS DLFEKDSVTE
AISQAAAQTV KNLSIKTVVA ATSSGHTARM ISKYRPKANI LAATYSERVQ RGLSLVWGVQ
AFVIDIPRNV DDMLEKVTAL AVEKGFAQKG DAIVITAGTP ILESGTTNLM KIEKIG
//
