ID A0A059BLH0_EUCGR Unreviewed; 344 AA.
AC A0A059BLH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=EUGRSUZ_F00493 {ECO:0000313|EMBL:KCW66736.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW66736.1};
RN [1] {ECO:0000313|EMBL:KCW66736.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW66736.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380};
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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DR EMBL; KK198758; KCW66736.1; -; Genomic_DNA.
DR RefSeq; XP_010060165.1; XM_010061863.2.
DR RefSeq; XP_010060166.1; XM_010061864.2.
DR AlphaFoldDB; A0A059BLH0; -.
DR STRING; 71139.A0A059BLH0; -.
DR EnsemblPlants; KCW66736; KCW66736; EUGRSUZ_F00493.
DR GeneID; 104448078; -.
DR Gramene; KCW66736; KCW66736; EUGRSUZ_F00493.
DR KEGG; egr:104448078; -.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; A0A059BLH0; -.
DR OMA; PMESDHD; -.
DR OrthoDB; 1008469at2759; -.
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:SF0; PHOSPHOGLYCERATE MUTASE; 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}.
FT ACT_SITE 99
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 202
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 98..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 111..112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 202..205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 272
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 344 AA; 38341 MW; 256B61A1CD42FB54 CRC64;
MAAAVFNQAS GIVQPHGCLN KSSNHQELGS VSFRFSQKVL NFEASQSMRG TRASDVTNSS
AARVSGQAPV LDPVIIPSKS DSTEPKKKSS EAALILIRHG ESLWNEKNLF TGCVDVPLTN
KGIEEAIHAG QRISNIPVDM IFTSALIRAQ MTAMLAMTQH RCKKVPIILH DGSEQARLWS
EIFSEDTKEQ SISVITAWQL NERMYGELQG LNKQETAERY GKEQVHEWRR SYDIPPPNGE
SLEMCAERAV AYFRDKIEPQ LLAGKNVMIA AHGNSLRSII MYLDKLTSQE VISLELSTGV
PMLYIFKEGK FIRRGSPSAP TDVGVYAYTK SLAKYRQKLD EMFQ
//
