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Database: UniProt
Entry: A0A368S1T3_SETIT
LinkDB: A0A368S1T3_SETIT
Original site: A0A368S1T3_SETIT 
ID   A0A368S1T3_SETIT        Unreviewed;       195 AA.
AC   A0A368S1T3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Phosphoglycerate mutase-like protein 4 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SETIT_7G315100v2 {ECO:0000313|EMBL:RCV36392.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV36392.1};
RN   [1] {ECO:0000313|EMBL:RCV36392.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV36392.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV36392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV36392.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000256|ARBA:ARBA00038362}.
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DR   EMBL; CM003534; RCV36392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368S1T3; -.
DR   STRING; 4555.A0A368S1T3; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF29; OS11G0138600 PROTEIN; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
FT   ACT_SITE        19
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        80
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         18..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   195 AA;  21259 MW;  D9B3C5E46CC07765 CRC64;
     MSPASPHGEH FTEVVVVRHG ETSWNASRII QGQMDPELNE TEAKPAAVYS SDLKRAAETA
     QTIATACHVS NLVFDQSLRE RHMGDLHGLK FDDAGGGESL DQLSERCVSY LNTIADKHKG
     ERVVVVSHGA AIEEICRHAD PTMTLVRRRI PNTSISVIHI SGENRHWILE KLGDVGHLDE
     DGFLQSAFGG DGASV
//
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