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   16-JUN-2009, entry version 24.
DE   RecName: Full=Bisphosphoglycerate mutase;
DE            Short=BPGM;
DE            EC=5.4.2.4;
DE   AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE   AltName: Full=2,3-bisphosphoglycerate synthase;
DE            EC=5.4.2.1;
DE            EC=3.1.3.13;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; 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
CC       affinity as a consequence of controlling 2,3-BPG concentration.
CC       Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC
CC       3.1.3.13 (phosphatase), but with a reduced activity (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
CC       bisphospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H(2)O = 3-
CC       phospho-D-glycerate + phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; AB169166; BAE01258.1; -; mRNA.
DR   SMR; Q4R6L7; 2-256.
DR   HOVERGEN; Q4R6L7; -.
DR   BRENDA; 3.1.3.13; 3438.
DR   BRENDA; 5.4.2.1; 3438.
DR   BRENDA; 5.4.2.4; 3438.
DR   GO; GO:0004083; F:2,3-bisphospho-D-glycerate 2-phosphohydrola...; IEA:EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Hydrolase; Isomerase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    259       Bisphosphoglycerate mutase.
FT                                /FTId=PRO_0000268184.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    188    188       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
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
//