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Database: UniProt
Entry: M5W014_PRUPE
LinkDB: M5W014_PRUPE
Original site: M5W014_PRUPE 
ID   M5W014_PRUPE            Unreviewed;       335 AA.
AC   M5W014;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0000256|ARBA:ARBA00012028};
DE            EC=5.4.2.11 {ECO:0000256|ARBA:ARBA00012028};
GN   ORFNames=PRUPE_6G181400 {ECO:0000313|EMBL:ONI02178.1};
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:ONI02178.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI02178.1, 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).
RN   [2] {ECO:0000313|EMBL:ONI02178.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Verde I., Jenkins J., Dondini L., Micali S., Pagliarani G., Vendramin E.,
RA   Paris R., Aramini V., Gazza L., Rossini L., Bassi D., Troggio M., Shu S.,
RA   Grimwood J.H., Tartarini S., Dettori M.T., Schmutz J.;
RT   "WGS assembly of Prunus persica.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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DR   EMBL; CM007656; ONI02177.1; -; Genomic_DNA.
DR   EMBL; CM007656; ONI02178.1; -; Genomic_DNA.
DR   RefSeq; XP_007205512.1; XM_007205450.1.
DR   AlphaFoldDB; M5W014; -.
DR   EnsemblPlants; ONI02177; ONI02177; PRUPE_6G181400.
DR   EnsemblPlants; ONI02178; ONI02178; PRUPE_6G181400.
DR   GeneID; 18773279; -.
DR   Gramene; ONI02177; ONI02177; PRUPE_6G181400.
DR   Gramene; ONI02178; ONI02178; PRUPE_6G181400.
DR   KEGG; pper:18773279; -.
DR   HOGENOM; CLU_033323_1_2_1; -.
DR   OMA; PMESDHD; -.
DR   OrthoDB; 1008469at2759; -.
DR   Proteomes; UP000006882; Chromosome g6.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF16; PHOSPHOGLYCERATE MUTASE (2,3-DIPHOSPHOGLYCERATE-DEPENDENT); 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT   ACT_SITE        90
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        193
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         89..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         193..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         264..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            263
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   335 AA;  37652 MW;  0DA2AD0816E51E57 CRC64;
     MVANAFRHPV GVIQLHGSVG DSGSMSKCRQ MSFRFISKNF AVDVGLLRKG QCGSRQCKLQ
     VIRASSSQTS TTDPILSTSK AESALILIRH GESLWNEKNL FTGCVDVPLT KRGVDEAIEA
     GKRISNIPID MIFTSSLIRA QMTAMLAMTQ HRRKKVPIIT HNESRQAKTW SQIYSGDTKK
     QSIPVVTAWQ LNERMYGELQ GLNKLETAER YGKEKVHEWR RSYDIPPPSG ESLEMCSQRA
     VAYFKEHIEP KLQSGKNVLV AAHGNSLRSI IMYLERLTSQ EVISLELSTG VPLLYIHKEE
     KFMRRGSPVG PTEPGVYAYT KSLALYRQEL DKKSH
//
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