PGAM1_PONAB
ID PGAM1_PONAB Reviewed; 254 AA.
AC Q5RFB8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phosphoglycerate mutase 1 {ECO:0000250|UniProtKB:P18669};
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:0000250|UniProtKB:P18669};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR857242; CAH89539.1; -; mRNA.
DR RefSeq; NP_001127164.1; NM_001133692.2.
DR AlphaFoldDB; Q5RFB8; -.
DR SMR; Q5RFB8; -.
DR STRING; 9601.ENSPPYP00000002936; -.
DR GeneID; 100174215; -.
DR KEGG; pon:100174215; -.
DR CTD; 5223; -.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; Q5RFB8; -.
DR OrthoDB; 804949at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Phosphoglycerate mutase 1"
FT /id="PRO_0000179827"
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:0000250|UniProtKB:P18669"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
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:0000250|UniProtKB:Q9DBJ1"
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"
SQ SEQUENCE 254 AA; 28778 MW; E650852BEBB23AF8 CRC64;
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNSKPIKPM QFLGDEETVR
KAMEAVAAQG KAKK
