ID A0A1L8H000_XENLA Unreviewed; 527 AA.
AC A0A1L8H000;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN Name=pkm.L {ECO:0000313|RefSeq:XP_018106217.1,
GN ECO:0000313|Xenbase:XB-GENE-17331006};
GN Synonyms=cthbp {ECO:0000313|RefSeq:XP_018106217.1}, pk
GN {ECO:0000313|RefSeq:XP_018106217.1}, pk3
GN {ECO:0000313|RefSeq:XP_018106217.1}, pkm
GN {ECO:0000313|RefSeq:XP_018106217.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018106217.1};
RN [1] {ECO:0000313|RefSeq:XP_018106217.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018106217.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018106217.1};
RG RefSeq;
RL Submitted (SEP-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 -!- 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}.
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DR RefSeq; XP_018106217.1; XM_018250728.2.
DR AlphaFoldDB; A0A1L8H000; -.
DR SMR; A0A1L8H000; -.
DR GeneID; 380274; -.
DR CTD; 380274; -.
DR Xenbase; XB-GENE-17331006; pkm.L.
DR OMA; SHEDHRK; -.
DR OrthoDB; 312683at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 380274; Expressed in muscle tissue and 19 other cell types or tissues.
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; 2.
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:SF101; PYRUVATE KINASE PKM; 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,
KW ECO:0000313|RefSeq:XP_018106217.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 39..371
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 406..524
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 527 AA; 57326 MW; 2E08F0C168E3352B CRC64;
MSEAGSAFIQ TQQLHAAMAD TFLEHMCRLD IDSEPIVARN TGIICTIGPA SCSVEMLKEM
IKSGMNVARL NFSHGTHEYH AGTIKNVREA TESFASNPIH YRPVAVALDT KGPEIRTGLI
KGSGTAEVEL KKGATMRITL DDAFQEKCDE NVLWLDYKNL PKVVKPGSKI YVDDGLISLL
VKDIGPDFCV TEVENGGMLG SKKGVNLPGA AVDLPAVSPK DIQDLQFGVE QDVDMVFASF
IRKAADVHAV RKVLGEKGKN IKIISKIENH EGVRRFDEIL EASDGIMVAR GDLGIEIPAE
KVFLAQKMMI GRCNRAGKPI ICATQMLESM IKKPRPTRAE GSDVANAVLD GADCIMLSGE
TAKGDYPLEA VRMQHAIARE AEAAIYHRQL FEELRRVSPL TSDPTEAAAV GAVEASFKCS
SGAIIVLTKS GRSAHLVSRY RPRAPIISVT RNGQTARQAH LYRGIFPVIY REAVHEAWAE
DVDGRVNFAM DIGKARGFFK SGDVVIVLTG WRPGSGFTNT MRVVPVP
//