ID A0A5J9WCZ0_9POAL Unreviewed; 616 AA.
AC A0A5J9WCZ0;
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};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
DE Flags: Fragment;
GN ORFNames=EJB05_05268 {ECO:0000313|EMBL:TVU45767.1};
OS Eragrostis curvula (weeping love grass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis.
OX NCBI_TaxID=38414 {ECO:0000313|EMBL:TVU45767.1, ECO:0000313|Proteomes:UP000324897};
RN [1] {ECO:0000313|EMBL:TVU45767.1, ECO:0000313|Proteomes:UP000324897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Victoria {ECO:0000313|Proteomes:UP000324897};
RC TISSUE=Leaf {ECO:0000313|EMBL:TVU45767.1};
RX PubMed=31308395; DOI=.1038/s41598-019-46610-0;
RA Carballo J., Santos B.A.C.M., Zappacosta D., Garbus I., Selva J.P.,
RA Gallo C.A., Diaz A., Albertini E., Caccamo M., Echenique V.;
RT "A high-quality genome of Eragrostis curvula grass provides insights into
RT Poaceae evolution and supports new strategies to enhance forage quality.";
RL Sci. Rep. 9:10250-10250(2019).
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 -!- 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 -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TVU45767.1}.
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DR EMBL; RWGY01000004; TVU45767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J9WCZ0; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000324897; Chromosome 5.
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 GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
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:SF21; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 2.
DR Pfam; PF02887; PK_C; 1.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000324897};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 95..180
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 212..457
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 496..595
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:TVU45767.1"
SQ SEQUENCE 616 AA; 67224 MW; 7B34EFAB83230F2B CRC64;
LGPYVIAQQA VATTRRAPAS HHPPTTFAVS AAQSLNLMAA PSGAAKSSFP HLVAASPAAR
RHGTALRIRA STGTGEAAMD VVSEAELREK GFMGMRKTKL VCTVGPSCVE ALPVLARGGM
GVARVNLCHG GREWHRAAMH AVRKLNEEEG FCVSLMVDTE GSQLLVADHG GATSVKAVVG
HSWPLCSRLL VELLPRVIVS IRCLDCSKND MYQDGSEWLF TSKKTYEAHP FTMHVNFDKF
SEGILVGDEL VIDGGMATFQ VTEKTGNDLR CTCTDPGLLL PRAKLSFWRN GKLVERNFGL
PTLSAKDWAD IEFGIAEGVD CIALSFVKDA NDIKHLKAYL SRRSLEHIKI FAKIESLESL
KNLKEIIEAS DGVMVARGDL GVQIPLEQIP AIQESIVKLC RHLNKPVIVA SQLLESMVEY
PTPTRAEVAD ISEAVRQYAD AVMLSAESAI GAYPQKALSV LRATSERIES WSREENMQKL
LPQYPLAIAL PDQISEQICN SAVEMANNLA VDAIFVYTKH GHMASLLSRN RPNPPIFAFT
DNANSRKSMN FFWGVIPLQL PLSNNMEDNF KTTISLMKSK GSVKSGDTVL VVSDSDLNRP
CAETSVFQSI QVRLVE
//
