ID A0A2Y9ETZ0_PHYMC Unreviewed; 573 AA.
AC A0A2Y9ETZ0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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_007108925.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007108925.1};
RN [1] {ECO:0000313|RefSeq:XP_007108925.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007108925.1};
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_007108925.1; XM_007108863.1.
DR AlphaFoldDB; A0A2Y9ETZ0; -.
DR STRING; 9755.ENSPCTP00005027516; -.
DR Ensembl; ENSPCTT00005030291; ENSPCTP00005027516; ENSPCTG00005019603.
DR GeneID; 102982777; -.
DR KEGG; pcad:102982777; -.
DR CTD; 5313; -.
DR InParanoid; A0A2Y9ETZ0; -.
DR OrthoDB; 312683at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000248484; 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; 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_007108925.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 85..417
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 454..570
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 573 AA; 61896 MW; 0DF15DEDB49A83B3 CRC64;
MSVQDNMRPM WLWSWISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE LGTSFFQQQL
PAAMADTFLE HLCLLDIDSE PVAARSTSII ATIGPASRSV ERLKEMIRAG MNIARLNFSH
GSHEYHAESI ANVREAVESF ATSPLSYRPV AIALDTKGPE IRTGILQGGP ASEVELVKGS
QVLVTVDPAF RTRGDANTVW VDYPNIVQVV PVGGRIYIDD GLISLEVTKI GPEGLETQVE
NGGVLGSRKG VNLPGAQVDL PGLSEQDVQD LRFGVEHGVD IIFASFVRRA SDVAAVRAAL
GPEGQGIKII SKIENHEGVK KFDEILEVSD GIMVARGDLG IEIPAEKVFL AQKMMIGRCN
LAGKPVVCAT QMLESMITKP RPTRAETSDV ANAVLDGADC IMLSGETAKG NFPVEAVKMQ
HAIAREAEAA VYHRQLFEEL RRAAPLSRDP TEVTAIGAVE AAFKCCAAAI IVLTTTGRSA
QLLSQYRPRA AVIAVTRSAQ AARQAHLCRG VFPVLYREPP EAIWADDVDR RVQFGIESGK
LRGFLRFGDL VIVVTGWRPG SGYTNIMRVL SIT
//
