ID A0A1U7SFF9_CARSF Unreviewed; 531 AA.
AC A0A1U7SFF9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN Name=PKM {ECO:0000313|RefSeq:XP_008046614.1,
GN ECO:0000313|RefSeq:XP_021563376.1};
OS Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC Carlito.
OX NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_008046614.1};
RN [1] {ECO:0000313|RefSeq:XP_008046614.1, ECO:0000313|RefSeq:XP_021563376.1}
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 -!- 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_008046614.1; XM_008048423.1.
DR RefSeq; XP_021563376.1; XM_021707701.1.
DR Ensembl; ENSTSYT00000043040; ENSTSYP00000027312; ENSTSYG00000031545.
DR GeneID; 103249802; -.
DR KEGG; csyr:103249802; -.
DR CTD; 5315; -.
DR OMA; RVHHIGE; -.
DR OrthoDB; 312683at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000189704; 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: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 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_008046614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189704};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 43..375
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 410..528
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 531 AA; 58048 MW; 69E5FEA5A2374C32 CRC64;
MAKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVDM
LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS DPILYRPVAV ALDTKGPEIR
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICRVVEV GSKIYVDDGL
ISLLVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDVQDLK FGVEQDVDMV
FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM
LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR ASSHSTDLME AMAMGSVEAS
YKCLAAALIV LTESGRSAHQ VSRYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE
AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
//