PGAM1_RAT
ID PGAM1_RAT Reviewed; 254 AA.
AC P25113; Q6P0K6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Phosphoglycerate mutase 1 {ECO:0000305};
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 1;
DE AltName: Full=Phosphoglycerate mutase isozyme B;
DE Short=PGAM-B;
GN Name=Pgam1 {ECO:0000312|RGD:3312};
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].
RX PubMed=1533381; DOI=10.1016/0378-1119(92)90408-h;
RA Urena J.M., Grana X., de Lecea L., Ruiz P., Castella J., Carreras J.,
RA Pons G., Climent F.;
RT "Isolation and sequencing of a cDNA encoding the B isozyme of rat
RT phosphoglycerate mutase.";
RL Gene 113:281-282(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1832843; DOI=10.1016/0003-9861(91)90235-b;
RA Uchida K.;
RT "cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation
RT and nucleotide sequence.";
RL Arch. Biochem. Biophys. 288:558-561(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 11-39; 47-62; 163-176 AND 222-240, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; TYR-26 AND
RP SER-118, AND IDENTIFICATION BY MASS 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: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglyceratea crucial step in glycolysis, by using 2,3-
CC bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-
CC bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.
CC {ECO:0000250|UniProtKB:P18669}.
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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903;
CC 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. {ECO:0000250|UniProtKB:P18669}.
CC -!- PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose
CC condition. Acetylation increases catalytic activity. Under glucose
CC restriction SIRT1 levels dramatically increase and it deacetylates the
CC enzyme (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M76591; AAA41834.1; -; mRNA.
DR EMBL; S63233; AAB19888.2; -; mRNA.
DR EMBL; BC065582; AAH65582.1; -; mRNA.
DR RefSeq; NP_445742.2; NM_053290.2.
DR AlphaFoldDB; P25113; -.
DR SMR; P25113; -.
DR BioGRID; 246778; 3.
DR IntAct; P25113; 1.
DR STRING; 10116.ENSRNOP00000065690; -.
DR CarbonylDB; P25113; -.
DR iPTMnet; P25113; -.
DR PhosphoSitePlus; P25113; -.
DR SwissPalm; P25113; -.
DR World-2DPAGE; 0004:P25113; -.
DR jPOST; P25113; -.
DR PaxDb; P25113; -.
DR PRIDE; P25113; -.
DR Ensembl; ENSRNOT00000071965; ENSRNOP00000065690; ENSRNOG00000050585.
DR GeneID; 24642; -.
DR KEGG; rno:24642; -.
DR CTD; 5223; -.
DR RGD; 3312; Pgam1.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P25113; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; P25113; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR PRO; PR:P25113; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000050585; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P25113; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; ISS:UniProtKB.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; ISO:RGD.
DR GO; GO:0006110; P:regulation of glycolytic process; ISO:RGD.
DR GO; GO:0043456; P:regulation of pentose-phosphate shunt; ISO:RGD.
DR GO; GO:0045730; P:respiratory burst; 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 Acetylation; Direct protein sequencing; Glycolysis; Hydrolase; Isomerase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..254
FT /note="Phosphoglycerate mutase 1"
FT /id="PRO_0000179828"
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 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 251
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 251
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT CONFLICT 55
FT /note="C -> V (in Ref. 1; AAA41834)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> K (in Ref. 2; AAB19888)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="R -> G (in Ref. 1; AAA41834)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> P (in Ref. 1; AAA41834)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="LR -> YG (in Ref. 1; AAA41834)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="F -> S (in Ref. 1; AAA41834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 28832 MW; 6DC09A3BEBB22409 CRC64;
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR
KAMEAVAAQG KVKK
