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Database: UniProt
Entry: A0A674D5G1_SALTR
LinkDB: A0A674D5G1_SALTR
Original site: A0A674D5G1_SALTR 
ID   A0A674D5G1_SALTR        Unreviewed;       644 AA.
AC   A0A674D5G1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-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=LOC115167314 {ECO:0000313|Ensembl:ENSSTUP00000090869.1};
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000090869.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000090869.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- 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; A0A674D5G1; -.
DR   Ensembl; ENSSTUT00000096672.1; ENSSTUP00000090869.1; ENSSTUG00000038601.1.
DR   GeneTree; ENSGT00390000008859; -.
DR   InParanoid; A0A674D5G1; -.
DR   OrthoDB; 312683at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000472277; 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:UP000472277};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          156..488
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          523..641
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   644 AA;  70362 MW;  72E0339CBBC56407 CRC64;
     MAVVNGGFEG LMYSRSIRAH SLLHGCSSLD CVSCSTLSSL KRRFIPELRV GRRVTLPGVP
     ACPVSSAAVP AALCGDRGSH RLGILWRSVA ATFLYVPRRN RKVYWTSSNS AIMPGSKSQD
     MGSAFVQTQQ LGAAMADTFL EHMCLLDIDS EPTTARNTGI ICTIGPASRS VGMLKEMIKS
     GMNIARMNFS HGSHEYHCET IKNVREACES FEPGSIHYRP VAIALDTKGP EIRTGLIKGS
     GTSEVELKKG NMIKLTLDDA YQENCDEDNL WLDYKNITRV VEQGSKIYID DGLVSLQVKE
     IGGDYLMCEI ENGGTLGSKK GVNLPGAAVD LPAVSEKDIS DLTFGVEQGV DMVFASFIRK
     AADVHAVRKV LGEKGKNIKI ISKLENHEGV RRFDEIMEAS DGIMVARGDL GIEIPTEKVF
     LAQKMMIGRC NRAGKPITCA TQMLESMIKK PRPTRAEGSD VANAVLDGAD CIMLSGETAK
     GDYPLEAVRT QHMIAREAEA AMFHRQVFED LRRAAPHSTD PAEAIAIGAV EASFKILSSA
     FIVLTNSGRS AHLISRYRPR APIIAVTRNG QTARQAHLYR GIFPVFYNKP AHDVWAEDVD
     LRVNFAMEMG KERGFFKEGD VVIVLTGWRP GSGYTNTMRV VVVP
//
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