ID A0A6J3RHI9_TURTR Unreviewed; 510 AA.
AC A0A6J3RHI9;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=PKLR {ECO:0000313|RefSeq:XP_033713433.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033713433.1};
RN [1] {ECO:0000313|RefSeq:XP_033713433.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033713433.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_033713433.1; XM_033857542.1.
DR AlphaFoldDB; A0A6J3RHI9; -.
DR InParanoid; A0A6J3RHI9; -.
DR OrthoDB; 312683at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000245320; Chromosome 1.
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 CDD; cd00288; Pyruvate_Kinase; 1.
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:SF31; PYRUVATE KINASE PKLR; 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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,
KW ECO:0000313|RefSeq:XP_033713433.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 22..354
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 391..507
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 510 AA; 54929 MW; E4DAE86532BF412E CRC64;
MADTFLEHLC LLDIDSEPVA ARSTSIIATI GPASRSVERL KEMIRAGMNI ARLNFSHGSH
EYHAESIANV REAVESIATS PLSYRPVAIA LDTKGPEIRT GILQGGPESE VELVKGSQVL
VTVDPAFRTR GDANTVWVDY ANIVQVVPVG GRIYIDDGLI SLEVTKIGPE GLETHVENGG
VLGSRKGVNL PGAQVDLPGL SEQDVQDLRF GVEHGVDIVF ASFVRRASDV AAVRAALGPE
GQGIKIISKI ENHEGVKKFD EILEVSDGIM VARGDLGIEI PAEKVFLAQK MMIGRCNLAG
KPVVCATQML ESMITKPRPT RAETSDVANA VLDGADCIML SGETAKGNFP VEAVKMQHAI
AREAEAAVYH RQLFEELRRA APLSRDPTEV TAIGAVEAAF KCCAAAIIVL TTTGRSAQLL
SRYRPRAAVI AVTRSAQAAR QAHLCRGVFP VLYREPPEAI WADDVDRRVQ FGIESGKLRG
FLRFGDLVIV VTGWRPGSGY TNIMRVLSVT
//
