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Database: UniProt
Entry: B5DGU1_SALSA
LinkDB: B5DGU1_SALSA
Original site: B5DGU1_SALSA 
ID   B5DGU1_SALSA            Unreviewed;       530 AA.
AC   B5DGU1;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=pk {ECO:0000313|EMBL:ACH70965.1,
GN   ECO:0000313|RefSeq:NP_001135175.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACH70965.1};
RN   [1] {ECO:0000313|EMBL:ACH70965.1, ECO:0000313|RefSeq:NP_001135175.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=White muscle {ECO:0000313|EMBL:ACH70965.1};
RX   PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA   Andreassen R., Lunner S., Hoyheim B.;
RT   "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT   Atlantic salmon (Salmo salar).";
RL   BMC Genomics 10:502-502(2009).
RN   [2] {ECO:0000313|RefSeq:NP_001135175.1}
RP   IDENTIFICATION.
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   EMBL; BT043850; ACH70965.1; -; mRNA.
DR   EMBL; BT043851; ACH70966.1; -; mRNA.
DR   RefSeq; NP_001135175.1; NM_001141703.1.
DR   STRING; 8030.ENSSSAP00000051465; -.
DR   Allergome; 12331; Sal s 9.
DR   Allergome; 12332; Sal s 9.0101.
DR   PaxDb; 8030-ENSSSAP00000051465; -.
DR   Ensembl; ENSSSAT00000079809; ENSSSAP00000051295; ENSSSAG00000050952.
DR   GeneID; 100196674; -.
DR   KEGG; sasa:100196674; -.
DR   CTD; 18745; -.
DR   OrthoDB; 312683at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000087266; Chromosome ssa10.
DR   Bgee; ENSSSAG00000050952; Expressed in muscle tissue and 14 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:SF129; 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   2: Evidence at transcript level;
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:ACH70965.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          42..374
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          409..527
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   530 AA;  58332 MW;  CC894B1AB52600F9 CRC64;
     MSKGKDMGSA FIQTQQLHAA MADTFLEHMC LLDIDSEPAV ARNTGIICTI GPASRSVNMA
     KEMIKSGMNI ARMNFSHGTH EYHAETIKNV REATESFGPG TIEYRPVAIA LDTKGPEIRT
     GLIKGSGEAE VELKKGAHIK LTLDDKYKDN CDEKHLWLDY KNITKILKVG GHVYIDDGLM
     SLKVKEVGAD FLDCEIENGG TLGSKKGVNL PGAAVDLPAV SEKDIQDLQF GVEQGVDMVF
     ASFIRKAADV HAVRKVLGEK GKNIKIISKL ENHEGVRRFD EILEASDGIM VARGDLGIEI
     PTEKVFIAQK MMTGRCNRIG KPITCATQML ESMIKKPRPT RAEGSDVANA VLDGNDCIML
     SGETAKGDYP LEAVRTQHKI AREAEAAMYH RQMFEEIRRT SHLTRDPTES VAIGAVEASF
     KCCASAIIVL TKTGRSAHLL SRYRPRAPII AVTRCGQTAR QAHLYRGIYP VLYTKPANDV
     WAEDVDLRVN FALEMGKHRH FFKSGDVIIV VTGWRPGPGY TNTMRVVLVP
//
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