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Database: UniProt
Entry: A0A3Q3F5R0_9LABR
LinkDB: A0A3Q3F5R0_9LABR
Original site: A0A3Q3F5R0_9LABR 
ID   A0A3Q3F5R0_9LABR        Unreviewed;       532 AA.
AC   A0A3Q3F5R0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000014182.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000014182.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q3F5R0; -.
DR   Ensembl; ENSLBET00000015001.1; ENSLBEP00000014182.1; ENSLBEG00000010965.1.
DR   GeneTree; ENSGT00390000008859; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000261660; Unplaced.
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:SF115; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          44..376
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          411..529
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   532 AA;  58084 MW;  695AB7C5DD223150 CRC64;
     MPHPKVPDMG SAFIQTQQLN AAMADTFLEH MCLLDIDSEP TTARNTGIIC TIGPASRSVD
     ILKEMIKSGM NIARMNFSHG THEYHADTIK NVREACESFE PGSIQYRPIG IALDTKGPEI
     RTGLIQGSGT AEVELKKGNT IKITVDDAHQ DNCSDELLWL DYKNISKVVE VGSKIYIDDG
     LISLQVTEIV SDNLICEIEN GGTLGSKKGV NLPGAAVDLP AVSEKDIKDL QFGVQHGVDM
     VFASFIRKAA DVHAVRAVLG EKGKDIKIIS KLENHEGVRR FDEIMEASDG IMVARGDLGI
     EIPTEKVFLA QKMMIGRCNR AGKPITCATQ MLESMIKKPR PTRAEGSDVA NAVLDGADCI
     MLSGETAKGD YPLEAVRTQH MIAREAEAAM FHRQVFEDLR RSTPYCKDPA EAIAIGAVEA
     SFKSLASGII VLTGSGRSAH LLSRYRPRAP IIAVTRNAQT ARQAHLYRGI FPVLYTKPSH
     DVWAEDVDMR VNFAMDMGKA RGFFKEGDVV IVLTGWRPGS GYTNTMRVVL VA
//
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