ID A0A2P6RQY0_ROSCH Unreviewed; 335 AA.
AC A0A2P6RQY0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=RchiOBHm_Chr2g0115141 {ECO:0000313|EMBL:PRQ48834.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ48834.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ48834.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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:PRQ48834.1}.
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DR EMBL; PDCK01000040; PRQ48834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6RQY0; -.
DR STRING; 74649.A0A2P6RQY0; -.
DR EnsemblPlants; PRQ48834; PRQ48834; RchiOBHm_Chr2g0115141.
DR Gramene; PRQ48834; PRQ48834; RchiOBHm_Chr2g0115141.
DR OMA; EASVCAY; -.
DR Proteomes; UP000238479; Chromosome 2.
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, ECO:0000313|EMBL:PRQ48834.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479}.
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; 37524 MW; 4BBAA2EAC773CC1B CRC64;
MVAAAFRHPV GIIQLHGSLS DAGSASKCGH SSFRFISKNF AVDVALLGKG HCSYRQGQQH
VVRALSSQAQ TTCPSSSSSH VESALILIRH GESMWNEKNL FTGCVDVPLT KRGVDEAIEA
GKRISNIPVD MIYTSSLIRA QMTAMLTMTQ HHCKKVPIIM HNENRQAKSW SQIYSEDTEK
QSIPVITAWQ LNERMYGELQ GLNKLETAER YGKEQVHEWR RSYNSPPPNG ESLEMCSHRA
VAYFKDHIQP QLQSGRHVMV AAHGNSLRSI IMYLENLTSL EVVNLELPTG LPLLYIYKEG
KFMRRGSPVG PTEAGVYAYT ESLALYKQTL DEKLY
//
