ID   PGAM1_BOVIN             Reviewed;         254 AA.
AC   Q3SZ62;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Phosphoglycerate mutase 1;
DE            EC=5.4.2.1;
DE            EC=5.4.2.4;
DE            EC=3.1.3.13;
DE   AltName: Full=Phosphoglycerate mutase isozyme B;
DE            Short=PGAM-B;
DE   AltName: Full=BPG-dependent PGAM 1;
GN   Name=PGAM1;
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=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC       bisphosphoglycerate as the primer of the reaction. Can also
CC       catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13
CC       (phosphatase), but with a reduced activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
CC       bisphospho-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; BC103115; AAI03116.1; -; mRNA.
DR   IPI; IPI00698589; -.
DR   RefSeq; NP_001029226.1; -.
DR   UniGene; Bt.15319; -.
DR   SMR; Q3SZ62; 1-245, 2-246.
DR   PRIDE; Q3SZ62; -.
DR   Ensembl; ENSBTAG00000012697; Bos taurus.
DR   GeneID; 404148; -.
DR   KEGG; bta:404148; -.
DR   HOVERGEN; Q3SZ62; -.
DR   OMA; Q3SZ62; FMLWRRS.
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   Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    254       Phosphoglycerate mutase 1.
FT                                /FTId=PRO_0000246079.
FT   COMPBIAS    122    131       Pro-rich.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    186    186       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      26     26       Phosphotyrosine (By similarity).
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
SQ   SEQUENCE   254 AA;  28852 MW;  233E2F8EEBB222A1 CRC64;
     MAAYKLVLIR HGESTWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ
     KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
     VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR
     VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPMVYEL DKNLKPIKPM QFLGDEETVR
     KAMEAVAAQG KAKK
//