PGAM2_RAT
ID PGAM2_RAT Reviewed; 253 AA.
AC P16290;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Phosphoglycerate mutase 2;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
DE AltName: Full=BPG-dependent PGAM 2;
DE AltName: Full=Muscle-specific phosphoglycerate mutase;
DE AltName: Full=Phosphoglycerate mutase isozyme M;
DE Short=PGAM-M;
GN Name=Pgam2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2558656; DOI=10.1016/0006-291x(89)92751-4;
RA Castella-Escola J., Montoliu L., Pons G., Puigdomenech P., Cohen-Solal M.,
RA Carreras J., Rigau J., Climent F.;
RT "Sequence of rat skeletal muscle phosphoglycerate mutase cDNA.";
RL Biochem. Biophys. Res. Commun. 165:1345-1351(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926808; DOI=10.1016/0378-1119(94)90074-4;
RA Ruiz-Lozano P., de Lecea L., Buesa C., Perez de la Osa P., Lepage D.,
RA Gualberto A., Walsh K., Pons G.;
RT "The gene encoding rat phosphoglycerate mutase subunit M: cloning and
RT promoter analysis in skeletal muscle cells.";
RL Gene 147:243-248(1994).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-14; SER-15; SER-118;
RP THR-121; TYR-132; TYR-133; SER-135 AND THR-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC bisphosphoglycerate as the primer of the reaction. Can also catalyze
CC the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
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:P18669};
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:P18669};
CC -!- SUBUNIT: Homodimer. Interacts with ENO1. {ECO:0000250|UniProtKB:O70250,
CC ECO:0000250|UniProtKB:P18669}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; M31835; AAA41835.1; -; mRNA.
DR EMBL; Z17319; CAA78967.1; -; Genomic_DNA.
DR PIR; A33793; PMRTYM.
DR RefSeq; NP_059024.1; NM_017328.2.
DR AlphaFoldDB; P16290; -.
DR SMR; P16290; -.
DR BioGRID; 247059; 1.
DR IntAct; P16290; 8.
DR MINT; P16290; -.
DR STRING; 10116.ENSRNOP00000018227; -.
DR iPTMnet; P16290; -.
DR PhosphoSitePlus; P16290; -.
DR jPOST; P16290; -.
DR PaxDb; P16290; -.
DR PRIDE; P16290; -.
DR Ensembl; ENSRNOT00000018227; ENSRNOP00000018227; ENSRNOG00000013532.
DR GeneID; 24959; -.
DR KEGG; rno:24959; -.
DR UCSC; RGD:3313; rat.
DR CTD; 5224; -.
DR RGD; 3313; Pgam2.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P16290; -.
DR OMA; MATHRVV; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; P16290; -.
DR TreeFam; TF300007; -.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P16290; -.
DR PRO; PR:P16290; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000013532; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P16290; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IDA:RGD.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:RGD.
DR GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR GO; GO:0006096; P:glycolytic process; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IMP:RGD.
DR GO; GO:0046689; P:response to mercury ion; IMP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
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 1: Evidence at protein level;
KW Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..253
FT /note="Phosphoglycerate mutase 2"
FT /id="PRO_0000179831"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 253 AA; 28755 MW; 73F6118A1C73D545 CRC64;
MATHRLVMVR HGESSWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL
KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
TPPPPMDEKH NYYASISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGKR
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NQELKPTKPM RFLGDEETVR
KAMEAVAAQG KAK
