ID A0A5N5HJ18_9ROSA Unreviewed; 584 AA.
AC A0A5N5HJ18;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, 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=D8674_017150 {ECO:0000313|EMBL:KAB2625490.1};
OS Pyrus ussuriensis x Pyrus communis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=2448454 {ECO:0000313|EMBL:KAB2625490.1, ECO:0000313|Proteomes:UP000327157};
RN [1] {ECO:0000313|EMBL:KAB2625490.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2625490.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2625490.1};
RA Ou C.;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAB2625490.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2625490.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2625490.1};
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (NOV-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}.
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:KAB2625490.1}.
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DR EMBL; SMOL01000160; KAB2625490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5HJ18; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000327157; Chromosome 16.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF14; PLASTIDIAL PYRUVATE KINASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; 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, ECO:0000313|EMBL:KAB2625490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000327157};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 105..436
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 475..574
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64066 MW; 9384E8902BFE0612 CRC64;
MSQSVHLLTP SNLAIPKHHS SFLSTFNRRL PVTTTTTTAS PFFPKLSIRA SSSDRKPSVL
VTDNGTSSSG LQSSTSHADH ALSSSIEVDA VTEAELRENG FRSTRRTKLV CTIGPATSGF
DQLESLAVGG MNVARINMCH GTREWHREVI QRVRRLNVDK GYAVAIMMDT EGSEIHMGDL
GGASSAKAED GEVWTFSVRA FGSTLPQNTI NVNYEGFAED VKVGDELLVD GGMVRFEVIE
KLGPDVKCKC TDPGLLLPRA NLTFWRDGSL VRERNAMLPT ISSKDWLDID FGIAEGVDFI
AVSFVKSAEV INHLKSYIAA RSRDSDVAVI AKIESIDSLK NLEEIIQASD GAMVARGDLG
AQIPLEQVPA AQQKIVQVCR QLNKPVIVAS QLLESMIEYP TPTRAEVADV SEAVRQRADA
LMLSGESAMG QFPEKSLAVL RSVSLRIERW WREEKRHEAM ELPAIGTSFS DSISEEICIS
AAKMANNLEV DALFVYTKTG HMASLLSRCR PDCPIFAFTN TTSVRRRLNL QWGLIPFRVS
FSDDMESNLN KTFSLLKARN LIKSGDLVIA VSDVLQCIQV MNVP
//
