ID A0A5J5B3D0_9ASTE Unreviewed; 579 AA.
AC A0A5J5B3D0;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, 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 ORFNames=F0562_028775 {ECO:0000313|EMBL:KAA8536297.1};
OS Nyssa sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Cornales; Nyssaceae; Nyssa.
OX NCBI_TaxID=561372 {ECO:0000313|EMBL:KAA8536297.1, ECO:0000313|Proteomes:UP000325577};
RN [1] {ECO:0000313|EMBL:KAA8536297.1, ECO:0000313|Proteomes:UP000325577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J267 {ECO:0000313|EMBL:KAA8536297.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA8536297.1};
RA Yang X., Kang M., Yang Y., Xiong H., Wang M., Zhang Z., Wang Z., Wu H.,
RA Ma T., Liu J., Xi Z.;
RT "A chromosome-level genome assembly of the Chinese tupelo Nyssa sinensis.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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; CM018039; KAA8536297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5B3D0; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000325577; Miscellaneous, Linkage group lg16.
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 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:SF21; 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:UP000325577};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 94..422
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 461..560
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 579 AA; 63884 MW; E52AFC8688C70CC2 CRC64;
MAVAGDSVLM CRQINAKKPN VHLKNRVFGV SVCPRRVCFN AGKLKGNKVR IGVRSAIEMD
DKEGLHLLKS FNGSLGFDVV SEGELRKKGF LGLRKTKLVC TIGPACCSLE ELEKLALGGM
NVARLNMCHN TREWHQDVIR RIKRLNEEKG FCVSVMIDTE GSQIQVVDHG APSSVKAEDG
SIWFFTTEKF EGSRPFTVQS NYESFSEGIK LGDELVIDGG MASFEVIEKI GNDLRCKCTD
PGLLLPRAKL SFWRDGKLVG KNDELPTLST KDWSDIEFGI TEGVDFIAMS FVNDADAVKH
LKNYLSTKSA GSIRVLAKIE SLEALQKLEE IVEASDGIMV ARGDLGVEIP LEQIPTVQEK
ITHVCRQLNK PVIIASQLLE SMVEYPTPTR AEVADVSEAV RQYADALMLS GESAIGSYGH
KALSVLRMTS SRMELWSHEE NRQSVLHQRQ LGVSLPDQIA EQICNCAVEM ANNLGVDAIF
VYTKHGRMAS LLSRNRPYPP IFAFTNENST RMALNLQWGV IPLFVDLSDD MEGNISKSID
LMKTKGIMKQ GDAVLVISDV IPSDATPTVF QSIQVKTIA
//
