ID   PMGE_RABIT              Reviewed;         259 AA.
AC   P07952;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 73.
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;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87055234; PubMed=3023182; DOI=10.1016/0378-1119(86)90181-2;
RA   Yanagawa S., Hitomi K., Sasaki R., Chiba H.;
RT   "Isolation and characterization of cDNA encoding rabbit reticulocyte
RT   2,3-bisphosphoglycerate synthase.";
RL   Gene 44:185-191(1986).
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.
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.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; M15884; AAA31240.1; -; mRNA.
DR   PIR; A24973; PMRBBM.
DR   RefSeq; NP_001075738.1; -.
DR   UniGene; Ocu.1868; -.
DR   HSSP; P31217; 1E58.
DR   SMR; P07952; 2-256.
DR   Ensembl; ENSOCUG00000003144; Oryctolagus cuniculus.
DR   GeneID; 100009096; -.
DR   HOVERGEN; P07952; -.
DR   BRENDA; 3.1.3.13; 255.
DR   BRENDA; 5.4.2.1; 255.
DR   BRENDA; 5.4.2.4; 255.
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_0000179836.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate.
FT   ACT_SITE    188    188
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates.
SQ   SEQUENCE   259 AA;  30030 MW;  350A0290D24AE528 CRC64;
     MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
     NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EKMALNHGEE QVRIWRRSYN
     VTPPPIEESH PYYHEIYSDR RYRVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
     KTVLISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
     IQAAIKKVED QGKVKRAEK
//