ID A0A251NUL8_PRUPE Unreviewed; 653 AA.
AC A0A251NUL8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN ORFNames=PRUPE_6G232800 {ECO:0000313|EMBL:ONI03003.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI03003.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI03003.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000256|RuleBase:RU000532};
CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR EMBL; CM007656; ONI03003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251NUL8; -.
DR STRING; 3760.A0A251NUL8; -.
DR EnsemblPlants; ONI03003; ONI03003; PRUPE_6G232800.
DR Gramene; ONI03003; ONI03003; PRUPE_6G232800.
DR eggNOG; KOG1367; Eukaryota.
DR eggNOG; KOG3115; Eukaryota.
DR OrthoDB; 446644at2759; -.
DR Proteomes; UP000006882; Chromosome g6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF32; PHOSPHOGLYCERATE KINASE; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
SQ SEQUENCE 653 AA; 73307 MW; 7D9D1C160C5B4388 CRC64;
MGHLVNLLQL QTTLFFSNSP TCSSIALKPH TFEYLKANVL TSKCKAFGGG EMDALPHLQT
LRKFPREELV AKVVLVRFDS TLLLREQGEE QRFQPNALFT IKYLHQSGAK VVLVSDWSVK
TNPRLFVAQS VAEFLSSLLE YKVVPVQCIS QNVVSKREGF EKGDILLLEN LSAFRGEVAN
CSKFSQALSS GVDIFVNDYF SRSHKILAST CGVTRFCYAN LAGFHFEESL SQLRRATESN
TKPHVAIIGG GNLFDKAAAL HSLTSRCDGL VFVGMMSFQI MHALGLPVPL NLVEHGVLKE
ALDIVQVAHI RNVQILYPKD FWCKNDHLPK QLEIFRAHRI LDGWVPVDIG PASFVEMKFM
LSRCKKVTWI GPVKFRTSNC TKGDSELAQM LNQLSQSNCN ITVVGNKACE AMVKESNFTF
NFTMIKDASV VWEFLKGRKL PGVMALDRAY PFDIDWSDAY SDPAQPLVVD IGSGNGMFLL
GMAKTRKYLN FLGLEINKKL VKRCLDSVHW RGIRNGYFIA TNATSTFRSI ISSYPGKLVL
VSIQCPNPDF NEPDHRWSML QRSLVEAVAD LLTANGRVFL QSDIEAVSLR MKEQFQRYGK
GKLTVVHEQS FAITNSGWLK DNPFGVRSDW EQHVLARGDP MYRLLLCKST TTE
//
