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Database: UniProt
Entry: A0A2I4FX27_JUGRE
LinkDB: A0A2I4FX27_JUGRE
Original site: A0A2I4FX27_JUGRE 
ID   A0A2I4FX27_JUGRE        Unreviewed;       527 AA.
AC   A0A2I4FX27;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=LOC109002762 {ECO:0000313|RefSeq:XP_018836195.1};
GN   ORFNames=F2P56_010225 {ECO:0000313|EMBL:KAF5473625.1};
OS   Juglans regia (English walnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Juglans.
OX   NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018836195.1};
RN   [1] {ECO:0000313|EMBL:KAF5473625.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5473625.1};
RA   Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA   Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA   Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA   Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA   Wegrzyn J.L., Langley C.H., Neale D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF5473625.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5473625.1};
RA   Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA   Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA   Salzberg S.L., Neale D.B.;
RT   "Walnut 2.0.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_018836195.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaves {ECO:0000313|RefSeq:XP_018836195.1};
RG   RefSeq;
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|ARBA:ARBA00001174,
CC         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; LIHL02000004; KAF5473625.1; -; Genomic_DNA.
DR   RefSeq; XP_018836195.1; XM_018980650.2.
DR   STRING; 51240.A0A2I4FX27; -.
DR   EnsemblPlants; Jr04_22260_p1; cds.Jr04_22260_p1; Jr04_22260.
DR   GeneID; 109002762; -.
DR   Gramene; Jr04_22260_p1; cds.Jr04_22260_p1; Jr04_22260.
DR   KEGG; jre:109002762; -.
DR   OrthoDB; 5483908at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000235220; Chromosome 4.
DR   Proteomes; UP000619265; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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:SF4; 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.
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   ECO:0000313|RefSeq:XP_018836195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          30..360
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          395..515
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   527 AA;  57337 MW;  AF0C04FD46C16F9E CRC64;
     MHSNHLLLEE PIRMATVLEP SKATFFPAMT KIVGTLGPKS RSVEVLSGCL KAGMSVARFD
     FSWGDPKYHQ ETLENLRAAV KTTKKLCAVM LDTVGPELQA VNKSGKSISL LMDASVVLTP
     NQDLEASSDV LPINFDGLSK AVKKGDTIFM GQYLFTGSET TSVWLEVSEV NGEDVVCIIK
     NSATLSGSLF TLHASQICIE LPTLSDQDKE VISTWGVQNK IDFLSLSYTR HAEDVRQARE
     LLSKLGELSQ TQIFAKIENI EGLTHFDEIL QEADGIILSR GNLGIDLPPE KVFLFQKAAL
     YKCNMAGKPA VLTRVVDSMT DNLRPTRAEA TDVANAVLDG SDAILLGAET LRGLYPVETI
     SIVGKISAEA EKVFNQDLYF KKTVKYVGEP MTHLESIASS AVRAAIKVKA SAIICFTSSG
     RAARLIAKYR PTMPVLSVVI PRLKTNQLKW SFSGAFEARQ SLIVRGLFPM LADPRHPAES
     TSATNESVLK VALDHGKTAG VIKSHDRVVV CQKVGDASVV KIIELED
//
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