ID   PMGE_BOVIN              Reviewed;         259 AA.
AC   Q3T014;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 29.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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.
CC   -!- CAUTION: Gln-187 is present instead of the conserved His which is
CC       expected to be an active site residue.
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DR   EMBL; BC102611; AAI02612.1; -; mRNA.
DR   IPI; IPI00706349; -.
DR   RefSeq; NP_001030479.1; -.
DR   UniGene; Bt.89285; -.
DR   SMR; Q3T014; 2-255.
DR   Ensembl; ENSBTAG00000008895; Bos taurus.
DR   GeneID; 533785; -.
DR   KEGG; bta:533785; -.
DR   HOVERGEN; Q3T014; -.
DR   BRENDA; 3.1.3.13; 251.
DR   BRENDA; 5.4.2.1; 251.
DR   BRENDA; 5.4.2.4; 251.
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_0000268183.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
SQ   SEQUENCE   259 AA;  30061 MW;  DE633B744A3C0250 CRC64;
     MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSDGLQEARN CGKQLKALNF EFDLVFTSIL
     NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALISLNR EQMALNHGEE QVRLWRRSYN
     VTPPPIEESH PYYHEIYNDR KYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
     KTVLISAQGN SCRALLKYLE GISDEEIINI TLPTGVPILL ELDENLRTVG PHQFLGDQEA
     IQAAIKKVDD QGKVKRADK
//