ID PGAM2_BOVIN Reviewed; 253 AA.
AC Q32KV0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 97.
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;
GN Name=PGAM2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 (NOV-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 catalyze
CC the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; BC109918; AAI09919.1; -; mRNA.
DR RefSeq; NP_001033200.1; NM_001038111.2.
DR AlphaFoldDB; Q32KV0; -.
DR SMR; Q32KV0; -.
DR STRING; 9913.ENSBTAP00000019336; -.
DR PaxDb; 9913-ENSBTAP00000019336; -.
DR PeptideAtlas; Q32KV0; -.
DR GeneID; 515067; -.
DR KEGG; bta:515067; -.
DR CTD; 5224; -.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; Q32KV0; -.
DR OrthoDB; 1008469at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
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; Phosphoglycerate mutase-like; 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 NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF8; PHOSPHOGLYCERATE MUTASE 2; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..253
FT /note="Phosphoglycerate mutase 2"
FT /id="PRO_0000282827"
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:0000250|UniProtKB:P16290"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70250"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
SQ SEQUENCE 253 AA; 28685 MW; 13DF4728D4D9D17D CRC64;
MSTHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGAEEAKK AAQAIKDAKM EFDICYTSVL
KRAIRTLWTI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
IPPPPMDEKH PYYKSISKER RYAGLKAGEL PTCESLKDTI ARALPFWNDE IAPQIKAGKR
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL DQALKPTKPM RFLGDEETVR
KAMEAVAAQG KAK
//
