PMGE_MACFA
ID PMGE_MACFA Reviewed; 259 AA.
AC Q4R6L7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Bisphosphoglycerate mutase;
DE Short=BPGM;
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE AltName: Full=2,3-bisphosphoglycerate synthase;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=BPG-dependent PGAM;
GN Name=BPGM; ORFNames=QtsA-17708;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity
CC by controlling the levels of its allosteric effector 2,3-
CC bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11)
CC activity. {ECO:0000250|UniProtKB:P07738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P07738};
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:0000250|UniProtKB:P07738};
CC -!- ACTIVITY REGULATION: At alkaline pH BPGM favors the synthase reaction;
CC however, at lower pH the phosphatase reaction is dominant. Inhibited by
CC citrate. {ECO:0000250|UniProtKB:P07738}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07738}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; AB169166; BAE01258.1; -; mRNA.
DR RefSeq; NP_001272064.1; NM_001285135.1.
DR RefSeq; XP_005550884.1; XM_005550827.2.
DR AlphaFoldDB; Q4R6L7; -.
DR SMR; Q4R6L7; -.
DR STRING; 9541.XP_005550883.1; -.
DR GeneID; 101925598; -.
DR KEGG; mcf:101925598; -.
DR CTD; 669; -.
DR VEuPathDB; HostDB:ENSMFAG00000046266; -.
DR eggNOG; KOG0235; Eukaryota.
DR OMA; ITESHPY; -.
DR OrthoDB; 1112626at2759; -.
DR Proteomes; UP000233100; Chromosome 3.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 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; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT CHAIN 2..259
FT /note="Bisphosphoglycerate mutase"
FT /id="PRO_0000268184"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
SQ SEQUENCE 259 AA; 30014 MW; 4E7F13B7C99330B4 CRC64;
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN
ITPPPIEESH PYYHEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
KTVLISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
IQAAIKKVED QGKVKQAKK
